diff --git a/.claude/commands/curate.md b/.claude/commands/curate.md
index ac34147..f80a370 100644
--- a/.claude/commands/curate.md
+++ b/.claude/commands/curate.md
@@ -73,7 +73,8 @@ See AGENTS.md §4.4 for the `...`/`[...]` operators and the read-the-context gua
 - Walk through 2–6 intermediate biological entities (proteins, pathways, processes, phenotypes) toward the disease node (`label: Disease`, prefix `MESH`).
 - **One connected chain — no shortcut/bypass edge** (AGENTS.md §0). The path is a single chain drug→…→disease. **Do not** add an edge straight from the drug to the disease, and **do not** add an edge from the drug (or any node) to a node already reached through intermediate steps. End the chain at the disease with a mechanistic/causal predicate (`causes`, `contributes to`, …), **never** with a clinical-outcome predicate (`treats`, `prevents`, `ameliorates`, …). Those are reserved for the no-mechanism stub. If you worked out a mechanism, curate *only* that chain — never also append a `Drug —treats→ Disease` edge. (This is the `clinical_shortcut` / `short_circuit` HARD error; the semantic critic checks for it too.)
 - Each edge:
-  - `key`: pick from the canonical 67 in `src/drugmechdb/schema/biolink_predicates.yaml`.
+  - `key`: pick one marked `status: current` in `src/drugmechdb/schema/biolink_predicate_status.yaml` (47 of the 70 enum values; the other 23 are legacy-only and Layer 3 will reject them).
+  - `object_aspect_qualifier` / `object_direction_qualifier`: **required** where the predicate carries no polarity of its own — `affects` needs both, `regulates` needs a direction. This is where `decreases activity of` went: `key: affects` + `object_aspect_qualifier: activity` + `object_direction_qualifier: decreased`. See AGENTS.md §3.0.
   - `evidence`: ≥1 `EvidenceItem` with:
     - `reference: PMID:xxxxxxxx`
     - `snippet:` **verbatim** substring of the cached source (abstract, or full text if you escalated) — copy/paste from `references_cache/`, never typed from memory.
diff --git a/AGENTS.md b/AGENTS.md
index 36a2bd6..97d9132 100644
--- a/AGENTS.md
+++ b/AGENTS.md
@@ -111,21 +111,47 @@ The CURIE prefix of every node `id` **must** match the canonical ontology for th
 
 ## 3. Predicate vocabulary
 
-Every edge `key` must be an **exact** member of the `BiolinkPredicate` enum in `src/drugmechdb/schema/biolink_predicates.yaml` (67 predicates as of May 2026). The list includes the high-frequency ones the agent will reach for first:
+Every edge `key` must be an **exact** member of the `BiolinkPredicate` enum in `src/drugmechdb/schema/biolink_predicates.yaml`. That enum spans two eras — it still accepts the v1.3.0-era vocabulary the 4,846 legacy records are written in — so membership alone is not enough. **New curation must use only the predicates marked `status: current` in `src/drugmechdb/schema/biolink_predicate_status.yaml`** (47 of 70, pinned to Biolink 4.4.4). QC Layer 3 enforces this for any record carrying evidence.
+
+The high-frequency ones you will reach for:
 
 ```
-positively regulates    negatively regulates    decreases activity of    increases activity of
-positively correlated with    negatively correlated with    causes    contributes to
-participates in    occurs in    located in    part of    manifestation of    in taxon
-treats    prevents    has metabolite    binds    affects    disrupts    affects risk for
-…
+regulates    affects    causes    contributes to    treats    prevents
+positively correlated with    negatively correlated with    manifestation of
+participates in    occurs in    located in    part of    in taxon
+has metabolite    directly physically interacts with    disrupts
 ```
 
-Read the file; the descriptions distinguish near-synonyms (e.g. `regulates` vs `positively regulates`, `correlated with` vs `causes`).
+### 3.0 Polarity lives in qualifiers, not in the predicate name
+
+Biolink's v2→v4 refactor removed `positively regulates`, `decreases activity of`, and the whole
+`increases/decreases <aspect> of` family. **Do not use them** — they are `status: legacy_only`.
+Say the same thing with a canonical predicate plus qualifiers on the edge:
+
+```yaml
+  - key: affects                              # was: decreases activity of
+    object_aspect_qualifier: activity         # activity | abundance | expression | synthesis | ...
+    object_direction_qualifier: decreased     # increased | decreased | upregulated | downregulated
+    source: MESH:D000068877
+    target: UniProt:A9UF07
+
+  - key: regulates                            # was: positively regulates
+    object_direction_qualifier: increased
+    source: UniProt:A9UF07
+    target: GO:0008283
+```
+
+`affects` requires **both** qualifiers; `regulates` requires `object_direction_qualifier`. Bare, they
+assert almost nothing, so Layer 3 rejects them without direction. The permissible values are the
+`ObjectAspectEnum` / `ObjectDirectionEnum` enums in `src/drugmechdb/schema/drugmechdb.yaml`, and
+`biolink_predicate_status.yaml` gives the exact replacement for every removed predicate.
+
+Read the enum file; the descriptions distinguish near-synonyms (e.g. `regulates` vs `affects`,
+`correlated with` vs `causes`).
 
 **You may emit predicates in casual surface forms** — `positively_regulates`, `biolink:positively_regulates`, `Positively Regulates` — and `scripts/canonicalize_predicates.py --write` will normalize them. But the **final** YAML must use the canonical form (lowercase, spaces, no prefix). Always canonicalize before validation.
 
-**You may NOT invent new predicates.** If no canonical predicate fits, escalate per PRD §7 Open Q #3 (adding to the enum requires curator approval + Biolink Model citation).
+**You may NOT invent new predicates.** If no canonical predicate fits, escalate per PRD §7 Open Q #3 (adding to the enum requires curator approval + Biolink Model citation). "Valid in Biolink" is not sufficient on its own — the predicate has to be in *our* enum and marked `current`.
 
 ### 3.1 Predicate domain/range
 
@@ -134,15 +160,15 @@ Some predicates only make sense between certain node types. Apply each predicate
 | Predicate(s) | Subject (`source`) label | Object (`target`) label |
 |---|---|---|
 | `treats`, `prevents`, `ameliorates`, `exacerbates`, `contraindicated for` | `Drug`, `ChemicalSubstance` | `Disease`, `PhenotypicFeature` |
-| `decreases activity of`, `increases activity of` | any | `Protein`, `GeneFamily`, `MacromolecularComplex`, `MolecularActivity`, `Pathway`, `BiologicalProcess` |
-| `decreases abundance of`, `increases abundance of`, `increases degradation of`, `decreases synthesis of` | any | `Protein`, `GeneFamily`, `MacromolecularComplex`, `ChemicalSubstance`, `MolecularActivity` |
-| `increases expression of`, `decreases expression of` | any | `Protein`, `GeneFamily`, `MacromolecularComplex`, `ChemicalSubstance` |
+| `affects` + aspect `activity` | any | `Protein`, `GeneFamily`, `MacromolecularComplex`, `MolecularActivity`, `Pathway`, `BiologicalProcess` |
+| `affects` + aspect `abundance`, `degradation`, `synthesis`, `stability`, `transport`, `uptake` | any | `Protein`, `GeneFamily`, `MacromolecularComplex`, `ChemicalSubstance`, `MolecularActivity` |
+| `affects` + aspect `expression` | any | `Protein`, `GeneFamily`, `MacromolecularComplex`, `ChemicalSubstance` |
 | `has metabolite` | `Drug`, `ChemicalSubstance` | `ChemicalSubstance`, `Drug` |
 | `has phenotype` | any | `PhenotypicFeature` |
 | `in taxon` | any | `OrganismTaxon` |
 | `occurs in`, `located in`, `expressed in` | any | `CellularComponent`, `GrossAnatomicalStructure`, `Cell`, `OrganismTaxon`, `Pathway` |
 
-The activity / abundance / expression / degradation / synthesis predicates (rows 2–4) never take a `Disease` or `PhenotypicFeature` object — reach the disease with a mechanistic/causal predicate (e.g. `causes`, `contributes to`) instead, per §0.
+Since Biolink 4.4.4 the object constraint follows the **aspect**, not the predicate name, so the lexicon keys those rows `affects|<aspect>` (the legacy `decreases activity of`-style keys are kept for the legacy corpus). An `affects` edge never takes a `Disease` or `PhenotypicFeature` object — reach the disease with a mechanistic/causal predicate (e.g. `causes`, `contributes to`) instead, per §0.
 
 The gate enforces these: an edge whose known endpoint types fall outside the allowed set is flagged as a SOFT `type_violation` and routed to the semantic critic (§5 step 8), so a mis-typed edge is surfaced and returned for correction rather than passing silently. Getting the types right here keeps the edge from bouncing.
 
diff --git a/CLAUDE.md b/CLAUDE.md
index 0ac2943..3be78ec 100644
--- a/CLAUDE.md
+++ b/CLAUDE.md
@@ -21,8 +21,11 @@ new ones) — keys: `directed`, `multigraph`, `graph`
 Edges may carry per-edge `evidence` (an `EvidenceItem` with a verbatim PubMed `snippet`).
 `_index.yaml` is a **generated** aggregate — don't hand-edit it.
 
-Full structure, the 14 node types, the 67-predicate vocabulary, and the path-quality
+Full structure, the 14 node types, the predicate vocabulary, and the path-quality
 conventions are in **`AGENTS.md`** and **`CurationGuide.md`**. Read those before curating.
+The predicate enum spans two Biolink eras — new curation uses only the `status: current`
+values in `src/drugmechdb/schema/biolink_predicate_status.yaml` (pinned to Biolink 4.4.4),
+with polarity carried in edge qualifiers. See **AGENTS.md §3.0**.
 
 ## The QC gate (`scripts/qc.py`)
 
@@ -35,7 +38,8 @@ and runs the matching layers:
 | `ai_curated` | any edge has `evidence:`      | 1, 2, 3, 4  |
 
 1. **schema** (LinkML `MechanisticPath`) · 2. **node ontology** (prefix↔label) ·
-3. **predicate enum** (67 Biolink predicates) · 4. **reference** (snippet verbatim in source).
+3. **predicate enum** (era-aware: `ai_curated` records must use current-Biolink predicates)
+· 4. **reference** (snippet verbatim in source).
 
 ```bash
 just qc                       # whole corpus, auto profile
diff --git a/CurationGuide.md b/CurationGuide.md
index 9654c48..826c6c3 100644
--- a/CurationGuide.md
+++ b/CurationGuide.md
@@ -218,6 +218,15 @@ to one of the predicates previously used, if a relationship found in the process
 any of these types listed below, a predicate may be selected
 from the [full set of biolink predicates](https://biolink.github.io/biolink-model/docs/predicates.html).
 
+> **Biolink 4.4.4 note (2026-09).** The list below is the vocabulary *found in the legacy
+> corpus* — it is v1.3.0-era, and 23 of these predicates no longer exist in Biolink. It stays
+> here because `kb/paths/` is still written in it. **New curation must not use them.** Pick a
+> predicate marked `status: current` in `src/drugmechdb/schema/biolink_predicate_status.yaml`,
+> and carry polarity in the edge's `object_aspect_qualifier` / `object_direction_qualifier`
+> rather than in the predicate name — `decreases activity of` is now
+> `affects` + `activity` + `decreased`. See AGENTS.md §3.0 for the contract and
+> `docs/biolink_version_decision.md` for why.
+
 The predicates currently found within DrugMechDB are as follows:
 
 [affects risk for](https://biolink.github.io/biolink-model/docs/affects_risk_for.html)  
diff --git a/README.md b/README.md
index 6fc901d..7f5dc5e 100644
--- a/README.md
+++ b/README.md
@@ -77,8 +77,9 @@ profile per file and runs the matching layers:
 | `ai_curated` | any edge has `evidence:` | 1, 2, 3, 4 |
 
 1. **schema** (LinkML `MechanisticPath`) · 2. **node ontology** (CURIE prefix ↔ label,
-plus an invisible/whitespace-character guard) · 3. **predicate enum** (67 Biolink
-predicates) · 4. **reference** (every snippet is verbatim in its cited source).
+plus an invisible/whitespace-character guard) · 3. **predicate enum** (Biolink predicates,
+era-aware — newly curated records must use the pinned current release) · 4. **reference**
+(every snippet is verbatim in its cited source).
 
 ```bash
 just qc                       # whole corpus
diff --git a/docs/biolink_drift_monitor.md b/docs/biolink_drift_monitor.md
index 763841c..90b9f0f 100644
--- a/docs/biolink_drift_monitor.md
+++ b/docs/biolink_drift_monitor.md
@@ -12,7 +12,8 @@
 ## 1. Why this exists
 
 The corpus stores edges keyed by a fixed vocabulary of Biolink predicates
-(`src/drugmechdb/schema/biolink_predicates.yaml`, 67 predicates), each also assigned a
+(`src/drugmechdb/schema/biolink_predicates.yaml`; `biolink_predicate_status.yaml` records
+which of them the pinned Biolink release still defines), each also assigned a
 direction-of-influence sign in `scripts/quality/predicate_polarity.yaml`. Biolink evolves
 independently — the v2→v4 **qualifier refactor** already folded many of our high-frequency
 predicates (`positively regulates`, `increases activity of`, …) into `regulates`/`affects`
diff --git a/docs/biolink_version_decision.md b/docs/biolink_version_decision.md
index 7864df9..e691a44 100644
--- a/docs/biolink_version_decision.md
+++ b/docs/biolink_version_decision.md
@@ -1,44 +1,68 @@
 # Biolink-version strategy
 
-> **Decision:** the corpus is **re-curated from scratch in the latest Biolink version**
-> (forwardfill). There is **no legacy vocabulary to preserve or to translate** — the
-> re-curated records are written directly in current Biolink, so storage *is* the current
-> vocabulary. Recorded here as the single source of truth; the publish layer references this.
+> **Decision:** DrugMechDB targets a **pinned current Biolink release** — **4.4.4** — and
+> AI-curated records are written in it, qualifiers and all. The legacy corpus stays in its
+> own vocabulary until forwardfill replaces it. Recorded here as the single source of truth;
+> the publish layer references this.
 
 ## The choice
 
 The drift audit (`docs/biolink_ontology_drift_report.md`) framed three options: **(A)** pin the old
 version, **(B)** migrate stored records, **(C)** keep legacy in storage and translate at publish.
-Its leaning was **C** (translate-at-publish), which minimizes churn *when the legacy corpus is kept*.
 
-That premise no longer holds. Because the corpus is **forwardfilled** — every record re-curated from
-scratch by the AI curator — the output is authored directly in the **latest Biolink version**. This
-is effectively a clean rewrite, not a migration of existing records. So:
+An earlier revision of this document recorded the strategy as *"re-curated from scratch in the latest
+Biolink version, so storage **is** the current vocabulary"* and closed #19 and #54 as moot on that
+basis. **That premise did not hold.** The curator was handed the legacy 67-predicate enum
+(`AGENTS.md` §3, `.claude/commands/curate.md`) and QC Layer 3 enforced it, so forwardfilled records
+came out in the *legacy* vocabulary: measured against Biolink 4.4.4, **323 of 558 edges (58%)** in
+the 135 AI-curated records used predicates Biolink had already removed. Writing "latest Biolink" in
+a policy document does not make the gate produce it.
 
-- **No version pin to an old Biolink** (rejects A).
-- **No record migration** of legacy vocabulary (B is moot — there is no legacy vocabulary in the
-  re-curated corpus to migrate).
-- **No publish-time translation layer** (C is moot — storage already holds current Biolink; there is
-  nothing to translate at export).
+The corrected strategy is **B, scoped to the AI-curated corpus**:
 
-## Consequences (issues closed as moot)
+- **Pin the Biolink release** (4.4.4) in `src/drugmechdb/schema/biolink_predicate_status.yaml`,
+  rather than tracking a moving `master`.
+- **The enum spans both eras.** `biolink_predicates.yaml` still accepts the v1.3.0-era vocabulary,
+  because the 4,846 legacy records in `kb/paths/` are written in it and are not being rewritten.
+- **The gate decides per profile.** Layer 3 permits any enum member for `legacy` records and only
+  `status: current` members for `ai_curated` ones. This is what actually holds new curation to
+  current Biolink — the contract text alone did not.
+- **Records already curated were migrated**, not re-curated, by `scripts/migrate_predicates.py`
+  (a deterministic transform driven by the same status file the gate reads).
 
-- **#19 (publish-time translation to current Biolink)** — moot. Storage is already current Biolink;
-  the export layer emits it directly, with no qualifier remap.
-- **#54 (predicate→qualifier remap rules)** — moot. The ~20 deterministic remap rules were only
-  needed to translate *legacy* predicates at publish; the forwardfilled corpus never uses them.
+## Consequences
 
-*Transition caveat:* until forwardfill completes, the stored corpus is still legacy vocabulary. If a
-publish of the **legacy** corpus is ever needed **before** forwardfill finishes, #19/#54 can be
-reopened for that interim need. The target state (forwardfilled) needs neither.
+- **#19 (publish-time translation to current Biolink)** — still moot *for AI-curated records*
+  (they are stored in current Biolink, so the exporter emits it directly), but **live again for the
+  legacy corpus**: publishing `kb/paths/` as current Biolink needs the translation, because those
+  records keep the legacy vocabulary until forwardfill reaches them.
+- **#54 (predicate→qualifier remap rules)** — **not moot.** The rules are implemented as
+  `scripts/migrate_predicates.py` + the `replacement:` blocks in
+  `src/drugmechdb/schema/biolink_predicate_status.yaml`. They were used to migrate the AI-curated
+  corpus and are what a legacy publish would reuse.
+
+## What has no mechanical answer
+
+Three removed predicates have no faithful qualifier form and are never rewritten automatically —
+they carry `needs_human_decision: true` in the status file:
+
+| Predicate | Why |
+|---|---|
+| `affects risk for` | Direction is unspecified; 4.4.4 splits it into `associated with increased likelihood of` / `associated with decreased likelihood of`. Needs a per-edge reading of the evidence. |
+| `increases response to` / `decreases response to` | Biolink 4.4.4 has no `response` aspect in `GeneOrGeneProductOrChemicalEntityAspectEnum`. |
+
+These appear only in the legacy corpus (1–82 edges each), never in the AI-curated records.
 
 ## Going forward
 
-Keeping the schema aligned with future Biolink releases is handled by the **Biolink-drift monitor**
-(`docs/biolink_drift_monitor.md`, `scripts/check_biolink_drift.py`): it detects predicate drift and
-opens a human-reviewed draft PR — it never auto-applies a schema change and never auto-assigns a
-polarity sign.
+Keeping the pin current is handled by the **Biolink-drift monitor**
+(`docs/biolink_drift_monitor.md`, `scripts/check_biolink_drift.py`): it compares the committed enum
+against a Biolink ref and reports the delta for a human-reviewed draft PR — it never auto-applies a
+schema change and never auto-assigns a polarity sign. When a release moves the pin, update
+`biolink_predicate_status.yaml` and re-run `scripts/migrate_predicates.py --check`.
 
 ### See also
 - `docs/biolink_ontology_drift_report.md` — the drift audit that framed the options.
 - `docs/biolink_drift_monitor.md` — how future Biolink releases are tracked.
+- `src/drugmechdb/schema/biolink_predicate_status.yaml` — the pin, the per-predicate status, and the
+  replacement each removed predicate maps to.
diff --git a/experiments/opus_vs_sonnet/opus/outputs/P01.yaml b/experiments/opus_vs_sonnet/opus/outputs/P01.yaml
index 21c7341..a3fbec3 100644
--- a/experiments/opus_vs_sonnet/opus/outputs/P01.yaml
+++ b/experiments/opus_vs_sonnet/opus/outputs/P01.yaml
@@ -24,7 +24,9 @@ nodes:
     name: Myocardial infarction
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:D001241
     target: UniProt:P23219
     evidence:
@@ -37,7 +39,8 @@ links:
         snippet: "the acetylation of platelet cyclooxygenase (COX)-1 at serine-529 is the direct mechanism of action of low-dose aspirin"
         supports: SUPPORT
         evidence_source: HUMAN_CLINICAL
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P23219
     target: CHEBI:50124
     evidence:
@@ -46,7 +49,8 @@ links:
         supports: SUPPORT
         evidence_source: HUMAN_CLINICAL
         explanation: "COX-1 activity drives thromboxane A2 formation; inhibiting COX-1 reduces thromboxane A2."
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: CHEBI:50124
     target: GO:0070527
     evidence:
diff --git a/experiments/opus_vs_sonnet/opus/outputs/P02.yaml b/experiments/opus_vs_sonnet/opus/outputs/P02.yaml
index f0e0d1b..ffd3e33 100644
--- a/experiments/opus_vs_sonnet/opus/outputs/P02.yaml
+++ b/experiments/opus_vs_sonnet/opus/outputs/P02.yaml
@@ -27,7 +27,9 @@ nodes:
     name: Hypercholesterolemia
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:D000069059
     target: UniProt:P04035
     evidence:
@@ -43,7 +45,8 @@ links:
         snippet: "their ability to inhibit HMG-CoA reductase, the rate-limiting enzyme of de novo cholesterol synthesis"
         supports: SUPPORT
         evidence_source: IN_VITRO
-  - key: negatively regulates
+  - key: regulates
+    object_direction_qualifier: decreased
     source: UniProt:P04035
     target: UniProt:P01130
     evidence:
@@ -52,7 +55,9 @@ links:
         supports: SUPPORT
         evidence_source: HUMAN_CLINICAL
         explanation: "Inhibiting HMG-CoA reductase leads to upregulation of LDL receptors, i.e. the enzyme's activity negatively regulates LDL receptor expression."
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: UniProt:P01130
     target: MESH:D008078
     evidence:
diff --git a/experiments/opus_vs_sonnet/opus/outputs/P03.yaml b/experiments/opus_vs_sonnet/opus/outputs/P03.yaml
index cf11ae7..255e37c 100644
--- a/experiments/opus_vs_sonnet/opus/outputs/P03.yaml
+++ b/experiments/opus_vs_sonnet/opus/outputs/P03.yaml
@@ -27,7 +27,9 @@ nodes:
     name: Hypertension
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:D017706
     target: UniProt:P12821
     evidence:
@@ -36,7 +38,8 @@ links:
         supports: SUPPORT
         evidence_source: HUMAN_CLINICAL
         explanation: "Lisinopril is identified as an angiotensin-converting enzyme inhibitor, i.e. it decreases ACE activity."
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P12821
     target: MESH:D000804
     evidence:
@@ -45,7 +48,9 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: "ACE converts angiotensin-I into angiotensin-II, increasing angiotensin II formation."
-  - key: increases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: increased
     source: MESH:D000804
     target: UniProt:P30556
     evidence:
@@ -54,7 +59,8 @@ links:
         supports: SUPPORT
         evidence_source: OTHER
         explanation: "Angiotensin II acts on AT1 receptors (AT1R), activating the receptor."
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P30556
     target: GO:0042310
     evidence:
diff --git a/experiments/opus_vs_sonnet/opus/outputs/P04.yaml b/experiments/opus_vs_sonnet/opus/outputs/P04.yaml
index 3b51df8..1cd43fd 100644
--- a/experiments/opus_vs_sonnet/opus/outputs/P04.yaml
+++ b/experiments/opus_vs_sonnet/opus/outputs/P04.yaml
@@ -21,7 +21,9 @@ nodes:
     name: Heart failure
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: DB:DB00264
     target: UniProt:P08588
     evidence:
@@ -30,7 +32,8 @@ links:
         supports: SUPPORT
         evidence_source: MODEL_ORGANISM
         explanation: "Metoprolol is described as a β1-adrenergic receptor blocker, i.e. it decreases the activity of the β1-adrenergic receptor."
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P08588
     target: GO:0010659
     evidence:
diff --git a/experiments/opus_vs_sonnet/opus/outputs/P05.yaml b/experiments/opus_vs_sonnet/opus/outputs/P05.yaml
index e7ff0ed..b3fa4a2 100644
--- a/experiments/opus_vs_sonnet/opus/outputs/P05.yaml
+++ b/experiments/opus_vs_sonnet/opus/outputs/P05.yaml
@@ -27,7 +27,9 @@ nodes:
     name: Stroke
     label: Disease
 links:
-  - key: increases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: increased
     source: UniProt:P33261
     target: DB:DB00758
     evidence:
@@ -36,7 +38,9 @@ links:
         supports: SUPPORT
         evidence_source: HUMAN_CLINICAL
         explanation: CYP2C19 activates the clopidogrel prodrug to its active metabolite.
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: DB:DB00758
     target: UniProt:Q9H244
     evidence:
@@ -54,7 +58,8 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: The P2Y12 receptor mediates platelet aggregation.
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: GO:0070527
     target: GO:0007596
     evidence:
diff --git a/experiments/opus_vs_sonnet/opus/outputs/P06.yaml b/experiments/opus_vs_sonnet/opus/outputs/P06.yaml
index 84a4497..e6c59c2 100644
--- a/experiments/opus_vs_sonnet/opus/outputs/P06.yaml
+++ b/experiments/opus_vs_sonnet/opus/outputs/P06.yaml
@@ -33,7 +33,9 @@ links:
         supports: SUPPORT
         evidence_source: OTHER
         explanation: "Tamoxifen is metabolized by CYP enzymes to its active metabolite endoxifen."
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: CHEBI:71176
     target: UniProt:P03372
     evidence:
@@ -42,7 +44,8 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: "Endoxifen is a potent antiestrogen that blocks ERalpha transcriptional activity and targets it for degradation, after binding the receptor with high affinity."
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P03372
     target: GO:0008283
     evidence:
diff --git a/experiments/opus_vs_sonnet/opus/outputs/P07.yaml b/experiments/opus_vs_sonnet/opus/outputs/P07.yaml
index 62ecbea..4c57d66 100644
--- a/experiments/opus_vs_sonnet/opus/outputs/P07.yaml
+++ b/experiments/opus_vs_sonnet/opus/outputs/P07.yaml
@@ -18,7 +18,9 @@ nodes:
     name: Chronic Myeloid Leukemia
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: DB:DB00619
     target: UniProt:P00519
     evidence:
diff --git a/experiments/opus_vs_sonnet/opus/outputs/P08.yaml b/experiments/opus_vs_sonnet/opus/outputs/P08.yaml
index b1cc231..5e1d045 100644
--- a/experiments/opus_vs_sonnet/opus/outputs/P08.yaml
+++ b/experiments/opus_vs_sonnet/opus/outputs/P08.yaml
@@ -33,7 +33,9 @@ links:
         supports: SUPPORT
         evidence_source: OTHER
         explanation: "Cetuximab is an antibody directed against the extracellular ligand-binding domain of EGFR."
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: DB:DB00002
     target: UniProt:P00533
     evidence:
@@ -42,7 +44,8 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: "Cetuximab produces EGFR blockade affecting downstream signalling pathways in colon cancer cell lines."
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P00533
     target: GO:0000165
     evidence:
@@ -51,7 +54,8 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: "EGFR activation drives the downstream RAS-MAPK signaling pathway in colorectal cancer cells."
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: GO:0000165
     target: GO:0008283
     evidence:
diff --git a/experiments/opus_vs_sonnet/opus/outputs/P09.yaml b/experiments/opus_vs_sonnet/opus/outputs/P09.yaml
index f9b02c3..cef2cba 100644
--- a/experiments/opus_vs_sonnet/opus/outputs/P09.yaml
+++ b/experiments/opus_vs_sonnet/opus/outputs/P09.yaml
@@ -30,7 +30,9 @@ nodes:
     name: Acute lymphoblastic leukemia
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: DB:DB00563
     target: UniProt:P00374
     evidence:
@@ -47,7 +49,8 @@ links:
         snippet: "MTX competitively inhibits dihydrofolate reductase (DHFR), an enzyme that participates in the tetrahydrofolate synthesis so as to inhibit purine synthesis."
         supports: SUPPORT
         evidence_source: OTHER
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: GO:0046654
     target: GO:0006164
     evidence:
@@ -56,7 +59,8 @@ links:
         supports: SUPPORT
         explanation: "Tetrahydrofolate synthesis is required for purine synthesis; inhibiting DHFR (and thus tetrahydrofolate synthesis) inhibits purine synthesis."
         evidence_source: OTHER
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: GO:0006164
     target: GO:0071897
     evidence:
@@ -65,7 +69,9 @@ links:
         supports: SUPPORT
         explanation: "Purine synthesis supplies nucleotides for DNA synthesis; MTX-mediated inhibition of purine synthesis contributes to inhibition of DNA synthesis."
         evidence_source: OTHER
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: DB:DB00563
     target: UniProt:P04818
     evidence:
@@ -73,7 +79,8 @@ links:
         snippet: "its downstream metabolite methotrexate polyglutamates (MTX-PGs) inhibit the thymidylate synthase (TS)."
         supports: SUPPORT
         evidence_source: OTHER
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P04818
     target: GO:0071897
     evidence:
diff --git a/experiments/opus_vs_sonnet/opus/outputs/P10.yaml b/experiments/opus_vs_sonnet/opus/outputs/P10.yaml
index b83d43b..a7a74f0 100644
--- a/experiments/opus_vs_sonnet/opus/outputs/P10.yaml
+++ b/experiments/opus_vs_sonnet/opus/outputs/P10.yaml
@@ -24,7 +24,9 @@ nodes:
     name: HER2-positive Breast Cancer
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: DB:DB00072
     target: UniProt:P04626
     evidence:
@@ -33,7 +35,8 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: "Trastuzumab, directed against the HER2 extracellular domain (PMID:24462377), down-regulates HER2 and reduces downstream phosphorylation."
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P04626
     target: GO:0043491
     evidence:
@@ -42,7 +45,9 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: "High HER2 increases phosphorylation of downstream Akt, indicating HER2 positively regulates PI3K/Akt signaling."
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: DB:DB00072
     target: GO:0043491
     evidence:
@@ -51,7 +56,8 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: "Trastuzumab reduces Akt phosphorylation, decreasing PI3K/Akt signal transduction."
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: GO:0043491
     target: GO:0008283
     evidence:
@@ -60,7 +66,8 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: "PI3K-AKT signaling promotes DNA synthesis and proliferation of breast cancer cells."
-  - key: negatively regulates
+  - key: regulates
+    object_direction_qualifier: decreased
     source: DB:DB00072
     target: GO:0008283
     evidence:
diff --git a/experiments/opus_vs_sonnet/opus/outputs/P11.yaml b/experiments/opus_vs_sonnet/opus/outputs/P11.yaml
index c5d3ada..6fca0b6 100644
--- a/experiments/opus_vs_sonnet/opus/outputs/P11.yaml
+++ b/experiments/opus_vs_sonnet/opus/outputs/P11.yaml
@@ -24,7 +24,9 @@ nodes:
     name: Pulmonary Tuberculosis
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: DB:DB01045
     target: UniProt:P9WGY9
     evidence:
@@ -33,7 +35,9 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: "Rifampin binds the RpoB beta subunit, inhibiting the RNA polymerase enzyme."
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: DB:DB01045
     target: GO:0006351
     evidence:
@@ -50,7 +54,8 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: "RpoB-containing RNA polymerase performs DNA-templated transcription in M. tuberculosis."
-  - key: negatively regulates
+  - key: regulates
+    object_direction_qualifier: decreased
     source: DB:DB01045
     target: NCBITaxon:1773
     evidence:
diff --git a/experiments/opus_vs_sonnet/opus/outputs/P12.yaml b/experiments/opus_vs_sonnet/opus/outputs/P12.yaml
index 108218f..7706339 100644
--- a/experiments/opus_vs_sonnet/opus/outputs/P12.yaml
+++ b/experiments/opus_vs_sonnet/opus/outputs/P12.yaml
@@ -24,7 +24,9 @@ nodes:
     name: Pulmonary Tuberculosis
     label: Disease
 links:
-  - key: increases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: increased
     source: MESH:D007538
     target: UniProt:P9WIE5
     evidence:
@@ -33,7 +35,9 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: "KatG activates the isoniazid prodrug into its reactive species."
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:D007538
     target: UniProt:P9WGR1
     evidence:
diff --git a/experiments/opus_vs_sonnet/opus/outputs/P14.yaml b/experiments/opus_vs_sonnet/opus/outputs/P14.yaml
index 19d5f35..6a40320 100644
--- a/experiments/opus_vs_sonnet/opus/outputs/P14.yaml
+++ b/experiments/opus_vs_sonnet/opus/outputs/P14.yaml
@@ -32,7 +32,9 @@ links:
         snippet: "Oseltamivir is a prodrug for the active carboxylate metabolite."
         supports: SUPPORT
         evidence_source: HUMAN_CLINICAL
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:C111791
     target: UniProt:P03468
     evidence:
diff --git a/experiments/opus_vs_sonnet/opus/outputs/P15.yaml b/experiments/opus_vs_sonnet/opus/outputs/P15.yaml
index 986192b..67f10eb 100644
--- a/experiments/opus_vs_sonnet/opus/outputs/P15.yaml
+++ b/experiments/opus_vs_sonnet/opus/outputs/P15.yaml
@@ -46,7 +46,9 @@ links:
         snippet: "This selectivity is due to the initial activation of the drug by phosphorylation by a herpes virus-specified thymidine kinase."
         supports: SUPPORT
         evidence_source: IN_VITRO
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:C025643
     target: UniProt:P04293
     evidence:
diff --git a/experiments/opus_vs_sonnet/opus/outputs/P17.yaml b/experiments/opus_vs_sonnet/opus/outputs/P17.yaml
index 5d06877..8f3e161 100644
--- a/experiments/opus_vs_sonnet/opus/outputs/P17.yaml
+++ b/experiments/opus_vs_sonnet/opus/outputs/P17.yaml
@@ -21,7 +21,9 @@ nodes:
     name: Major Depressive Disorder
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: DB:DB00472
     target: UniProt:P31645
     evidence:
@@ -30,7 +32,8 @@ links:
         supports: SUPPORT
         evidence_source: MODEL_ORGANISM
         explanation: "Fluoxetine inhibits (decreases the activity of) the serotonin transporter SERT."
-  - key: negatively regulates
+  - key: regulates
+    object_direction_qualifier: decreased
     source: UniProt:P31645
     target: MESH:D012701
     evidence:
diff --git a/experiments/opus_vs_sonnet/opus/outputs/P18.yaml b/experiments/opus_vs_sonnet/opus/outputs/P18.yaml
index bf7141f..c456859 100644
--- a/experiments/opus_vs_sonnet/opus/outputs/P18.yaml
+++ b/experiments/opus_vs_sonnet/opus/outputs/P18.yaml
@@ -24,7 +24,9 @@ nodes:
     name: Bipolar Disorder
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: DB:DB01356
     target: UniProt:P49841
     evidence:
@@ -38,7 +40,8 @@ links:
         supports: SUPPORT
         evidence_source: HUMAN_CLINICAL
         explanation: "Review identifying direct GSK-3 beta inhibition as a mechanism of lithium in bipolar disorder."
-  - key: negatively regulates
+  - key: regulates
+    object_direction_qualifier: decreased
     source: UniProt:P49841
     target: UniProt:P35222
     evidence:
@@ -52,7 +55,8 @@ links:
         supports: SUPPORT
         evidence_source: MODEL_ORGANISM
         explanation: "GSK-3 beta inhibition by lithium stabilizes beta-catenin."
-  - key: negatively regulates
+  - key: regulates
+    object_direction_qualifier: decreased
     source: UniProt:P35222
     target: GO:0006915
     evidence:
diff --git a/experiments/opus_vs_sonnet/opus/outputs/P19.yaml b/experiments/opus_vs_sonnet/opus/outputs/P19.yaml
index f3fac1c..8e8e11c 100644
--- a/experiments/opus_vs_sonnet/opus/outputs/P19.yaml
+++ b/experiments/opus_vs_sonnet/opus/outputs/P19.yaml
@@ -24,7 +24,9 @@ nodes:
     name: Epilepsy
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: DB:DB00996
     target: UniProt:P54289
     evidence:
@@ -36,7 +38,8 @@ links:
         snippet: "Binding of these ligands to the alpha2delta subunit is considered to explain their usefulness in treating several clinical disorders, including epilepsy"
         supports: SUPPORT
         evidence_source: OTHER
-  - key: negatively regulates
+  - key: regulates
+    object_direction_qualifier: decreased
     source: UniProt:P54289
     target: GO:0070509
     evidence:
@@ -44,7 +47,8 @@ links:
         snippet: "they exhibit a high affinity for the α2δ-1 and α2δ-2 subunits of voltage-activated calcium channels, wherein binding of gabapentinoids inhibits cellular calcium influx and attenuates neurotransmission"
         supports: SUPPORT
         evidence_source: OTHER
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: GO:0070509
     target: GO:0007269
     evidence:
diff --git a/experiments/opus_vs_sonnet/opus/outputs/P20.yaml b/experiments/opus_vs_sonnet/opus/outputs/P20.yaml
index f08713e..7a5c670 100644
--- a/experiments/opus_vs_sonnet/opus/outputs/P20.yaml
+++ b/experiments/opus_vs_sonnet/opus/outputs/P20.yaml
@@ -24,7 +24,9 @@ nodes:
     name: Alzheimer's Disease
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: DB:DB00843
     target: UniProt:P22303
     evidence:
@@ -33,7 +35,8 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: "Donepezil is a reversible acetylcholinesterase inhibitor, decreasing the enzyme's activity."
-  - key: negatively regulates
+  - key: regulates
+    object_direction_qualifier: decreased
     source: UniProt:P22303
     target: MESH:D000109
     evidence:
@@ -42,7 +45,8 @@ links:
         supports: SUPPORT
         evidence_source: OTHER
         explanation: "Acetylcholinesterase hydrolyzes acetylcholine; its inhibition by donepezil therefore raises acetylcholine levels."
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: MESH:D000109
     target: GO:0007268
     evidence:
diff --git a/experiments/opus_vs_sonnet/opus/outputs/P21.yaml b/experiments/opus_vs_sonnet/opus/outputs/P21.yaml
index a55273b..4e2f4d5 100644
--- a/experiments/opus_vs_sonnet/opus/outputs/P21.yaml
+++ b/experiments/opus_vs_sonnet/opus/outputs/P21.yaml
@@ -27,7 +27,9 @@ nodes:
     name: Rheumatoid Arthritis
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:D008727
     target: UniProt:P31939
     evidence:
@@ -36,7 +38,8 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: "Methotrexate (as polyglutamates) inhibits ATIC enzymatic activity."
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P31939
     target: CHEBI:16335
     evidence:
@@ -45,7 +48,9 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: "Inhibition of ATIC promotes release of adenosine; ATIC inhibition is the upstream driver of adenosine accumulation."
-  - key: increases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: increased
     source: CHEBI:16335
     target: UniProt:P29274
     evidence:
@@ -54,7 +59,9 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: "Adenosine activates A2A adenosine receptor signaling in rheumatoid synoviocytes."
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: UniProt:P29274
     target: UniProt:P08254
     evidence:
diff --git a/experiments/opus_vs_sonnet/opus/outputs/P22.yaml b/experiments/opus_vs_sonnet/opus/outputs/P22.yaml
index 9e1b2f9..b4d94c2 100644
--- a/experiments/opus_vs_sonnet/opus/outputs/P22.yaml
+++ b/experiments/opus_vs_sonnet/opus/outputs/P22.yaml
@@ -21,7 +21,9 @@ nodes:
     name: Crohn's Disease
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: DB:DB00065
     target: UniProt:P01375
     evidence:
@@ -35,7 +37,8 @@ links:
         supports: SUPPORT
         evidence_source: OTHER
         explanation: "Infliximab is named among these anti-TNF drugs that block TNF from interacting with its receptors, i.e. neutralize its activity."
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P01375
     target: GO:0006954
     evidence:
diff --git a/experiments/opus_vs_sonnet/opus/outputs/P23.yaml b/experiments/opus_vs_sonnet/opus/outputs/P23.yaml
index 35e4d05..066dc69 100644
--- a/experiments/opus_vs_sonnet/opus/outputs/P23.yaml
+++ b/experiments/opus_vs_sonnet/opus/outputs/P23.yaml
@@ -21,7 +21,9 @@ nodes:
     name: Systemic Lupus Erythematosus
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: DB:DB01611
     target: UniProt:Q9NYK1
     evidence:
@@ -30,7 +32,8 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: "Hydroxychloroquine inhibits the proteolytic maturation of TLR7 and thereby reduces TLR7-driven activation."
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:Q9NYK1
     target: GO:0032606
     evidence:
diff --git a/experiments/opus_vs_sonnet/opus/outputs/P24.yaml b/experiments/opus_vs_sonnet/opus/outputs/P24.yaml
index 92d6c30..87350a7 100644
--- a/experiments/opus_vs_sonnet/opus/outputs/P24.yaml
+++ b/experiments/opus_vs_sonnet/opus/outputs/P24.yaml
@@ -36,7 +36,9 @@ links:
         supports: SUPPORT
         evidence_source: OTHER
         explanation: "MMF is hydrolyzed to release the active metabolite mycophenolic acid."
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:D015232
     target: UniProt:P12268
     evidence:
@@ -52,7 +54,8 @@ links:
         snippet: "an inhibitor of inosine monophosphate dehydrogenase (IMPDH). This is the rate-limiting enzyme in de novo synthesis of guanosine nucleotides."
         supports: SUPPORT
         evidence_source: OTHER
-  - key: negatively regulates
+  - key: regulates
+    object_direction_qualifier: decreased
     source: MESH:D015232
     target: GO:0046651
     evidence:
diff --git a/experiments/opus_vs_sonnet/opus/outputs/P25.yaml b/experiments/opus_vs_sonnet/opus/outputs/P25.yaml
index eeea7c7..39e9607 100644
--- a/experiments/opus_vs_sonnet/opus/outputs/P25.yaml
+++ b/experiments/opus_vs_sonnet/opus/outputs/P25.yaml
@@ -21,7 +21,9 @@ nodes:
     name: Psoriasis
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: DB:DB00051
     target: UniProt:P01375
     evidence:
diff --git a/experiments/opus_vs_sonnet/opus/outputs/P26.yaml b/experiments/opus_vs_sonnet/opus/outputs/P26.yaml
index ccda886..359ac43 100644
--- a/experiments/opus_vs_sonnet/opus/outputs/P26.yaml
+++ b/experiments/opus_vs_sonnet/opus/outputs/P26.yaml
@@ -24,7 +24,9 @@ nodes:
     name: Type 2 Diabetes Mellitus
     label: Disease
 links:
-  - key: increases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: increased
     source: MESH:D008687
     target: UniProt:Q13131
     evidence:
@@ -33,7 +35,9 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: Metformin directly activates AMP-activated protein kinase in hepatocytes.
-  - key: increases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: increased
     source: UniProt:Q15831
     target: UniProt:Q13131
     evidence:
@@ -42,7 +46,8 @@ links:
         supports: SUPPORT
         evidence_source: MODEL_ORGANISM
         explanation: LKB1 is the upstream kinase that phosphorylates and activates AMPK in the liver, mediating the therapeutic effect of metformin.
-  - key: negatively regulates
+  - key: regulates
+    object_direction_qualifier: decreased
     source: UniProt:Q13131
     target: GO:0006094
     evidence:
diff --git a/experiments/opus_vs_sonnet/opus/outputs/P27.yaml b/experiments/opus_vs_sonnet/opus/outputs/P27.yaml
index c87b27c..3eb0c55 100644
--- a/experiments/opus_vs_sonnet/opus/outputs/P27.yaml
+++ b/experiments/opus_vs_sonnet/opus/outputs/P27.yaml
@@ -27,7 +27,9 @@ nodes:
     name: Type 1 Diabetes Mellitus
     label: Disease
 links:
-  - key: increases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: increased
     source: MESH:D007328
     target: UniProt:P06213
     evidence:
@@ -36,7 +38,8 @@ links:
         supports: SUPPORT
         evidence_source: OTHER
         explanation: "Insulin binds the insulin receptor and triggers its autophosphorylation/activation."
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P06213
     target: UniProt:P14672
     evidence:
@@ -54,7 +57,8 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: "GLUT4 at the plasma membrane mediates insulin-stimulated glucose uptake/import."
-  - key: negatively regulates
+  - key: regulates
+    object_direction_qualifier: decreased
     source: GO:0046323
     target: HP:0003074
     evidence:
diff --git a/experiments/opus_vs_sonnet/opus/outputs/P28.yaml b/experiments/opus_vs_sonnet/opus/outputs/P28.yaml
index 05b87be..76559df 100644
--- a/experiments/opus_vs_sonnet/opus/outputs/P28.yaml
+++ b/experiments/opus_vs_sonnet/opus/outputs/P28.yaml
@@ -33,7 +33,9 @@ links:
         supports: SUPPORT
         evidence_source: HUMAN_CLINICAL
         explanation: "Levothyroxine (LT4) is converted to the active hormone triiodothyronine (T3)."
-  - key: increases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: increased
     source: MESH:D014284
     target: UniProt:P10828
     evidence:
diff --git a/experiments/opus_vs_sonnet/opus/outputs/P29.yaml b/experiments/opus_vs_sonnet/opus/outputs/P29.yaml
index 676f867..73df87f 100644
--- a/experiments/opus_vs_sonnet/opus/outputs/P29.yaml
+++ b/experiments/opus_vs_sonnet/opus/outputs/P29.yaml
@@ -24,7 +24,9 @@ nodes:
     name: Gout
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: DB:DB00437
     target: UniProt:P47989
     evidence:
@@ -33,7 +35,8 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: "Allopurinol is metabolized by xanthine oxidoreductase to oxypurinol, which inhibits the enzyme's active center."
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P47989
     target: MESH:D014527
     evidence:
@@ -42,7 +45,9 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: "Xanthine oxidoreductase produces uric acid as the final step of purine metabolism."
-  - key: increases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: increased
     source: MESH:D014527
     target: UniProt:Q96P20
     evidence:
diff --git a/experiments/opus_vs_sonnet/opus/outputs/P30.yaml b/experiments/opus_vs_sonnet/opus/outputs/P30.yaml
index 54f0044..992ae2f 100644
--- a/experiments/opus_vs_sonnet/opus/outputs/P30.yaml
+++ b/experiments/opus_vs_sonnet/opus/outputs/P30.yaml
@@ -27,7 +27,9 @@ nodes:
     name: Type 2 Diabetes Mellitus
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: DB:DB09038
     target: UniProt:P31639
     evidence:
@@ -45,7 +47,8 @@ links:
         supports: SUPPORT
         evidence_source: COMPUTATIONAL
         explanation: "SGLT2 mediates renal glucose reabsorption; inhibiting SGLT2 reduces this process."
-  - key: negatively regulates
+  - key: regulates
+    object_direction_qualifier: decreased
     source: GO:0035623
     target: HP:0003076
     evidence:
diff --git a/experiments/opus_vs_sonnet/opus/outputs/P31.yaml b/experiments/opus_vs_sonnet/opus/outputs/P31.yaml
index 6849e15..2b81864 100644
--- a/experiments/opus_vs_sonnet/opus/outputs/P31.yaml
+++ b/experiments/opus_vs_sonnet/opus/outputs/P31.yaml
@@ -27,7 +27,9 @@ nodes:
     name: Hemophilia A
     label: Disease
 links:
-  - key: increases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: increased
     source: DB:DB00067
     target: UniProt:P30518
     evidence:
@@ -36,7 +38,8 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: "DDAVP (desmopressin), a vasopressin analogue, acts as a specific agonist at the vasopressin V2 receptor."
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P30518
     target: GO:0061156
     evidence:
@@ -45,7 +48,8 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: "V2 receptor activation drives cAMP-mediated von Willebrand factor secretion from endothelial cells."
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: GO:0061156
     target: UniProt:P04275
     evidence:
@@ -54,7 +58,9 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: "Secretion of von Willebrand factor from endothelial stores raises circulating plasma vWF levels."
-  - key: increases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: increased
     source: UniProt:P04275
     target: UniProt:P00451
     evidence:
diff --git a/experiments/opus_vs_sonnet/opus/outputs/P32.yaml b/experiments/opus_vs_sonnet/opus/outputs/P32.yaml
index ef5a121..5c6e806 100644
--- a/experiments/opus_vs_sonnet/opus/outputs/P32.yaml
+++ b/experiments/opus_vs_sonnet/opus/outputs/P32.yaml
@@ -21,7 +21,8 @@ nodes:
     name: Ascorbic acid deficiency
     label: Disease
 links:
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: MESH:D001205
     target: UniProt:P13674
     evidence:
diff --git a/experiments/opus_vs_sonnet/opus/outputs/P33.yaml b/experiments/opus_vs_sonnet/opus/outputs/P33.yaml
index cbb5d18..e01bb69 100644
--- a/experiments/opus_vs_sonnet/opus/outputs/P33.yaml
+++ b/experiments/opus_vs_sonnet/opus/outputs/P33.yaml
@@ -27,7 +27,9 @@ nodes:
     name: Relapsing-remitting multiple sclerosis
     label: Disease
 links:
-  - key: increases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: increased
     source: DB:DB00068
     target: UniProt:P17181
     evidence:
@@ -44,7 +46,8 @@ links:
         snippet: "IFNß exerts its activity through the interaction with IFNAR, through activation of the JAK/STAT pathway."
         supports: SUPPORT
         evidence_source: HUMAN_CLINICAL
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: DB:DB00068
     target: UniProt:Q8NEV9
     evidence:
@@ -52,7 +55,8 @@ links:
         snippet: "IFN-β induced IL-27 expression by DC, and neutralisation of IL-27 abrogated the suppressive effects of IFN-β on zymosan-induced IL-1 and IL-23 production and the generation of Th17 cells in vitro."
         supports: SUPPORT
         evidence_source: HUMAN_CLINICAL
-  - key: negatively regulates
+  - key: regulates
+    object_direction_qualifier: decreased
     source: UniProt:Q8NEV9
     target: CL:0000899
     evidence:
diff --git a/experiments/opus_vs_sonnet/opus/outputs/P34.yaml b/experiments/opus_vs_sonnet/opus/outputs/P34.yaml
index bcbfa28..1a9d50c 100644
--- a/experiments/opus_vs_sonnet/opus/outputs/P34.yaml
+++ b/experiments/opus_vs_sonnet/opus/outputs/P34.yaml
@@ -27,7 +27,9 @@ nodes:
     name: Primary cutaneous T-cell lymphoma
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: DB:DB00004
     target: UniProt:P01589
     evidence:
@@ -36,7 +38,8 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: "Denileukin diftitox (the monovalent human IL-2 fusion toxin, Ontak) binds CD25 (IL-2R alpha) and blocks IL-2 binding to the receptor."
-  - key: negatively regulates
+  - key: regulates
+    object_direction_qualifier: decreased
     source: DB:DB00004
     target: GO:0006412
     evidence:
@@ -44,7 +47,8 @@ links:
         snippet: "The ADP-ribosyltransferase activity of diphtheria toxin is cleaved in the endosome and is translocated into the cytosol where it inhibits protein synthesis, leading to apoptosis."
         supports: SUPPORT
         evidence_source: OTHER
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: GO:0006412
     target: GO:0006915
     evidence:
diff --git a/experiments/opus_vs_sonnet/opus/outputs/P35.yaml b/experiments/opus_vs_sonnet/opus/outputs/P35.yaml
index 90bafec..66c4d2b 100644
--- a/experiments/opus_vs_sonnet/opus/outputs/P35.yaml
+++ b/experiments/opus_vs_sonnet/opus/outputs/P35.yaml
@@ -30,7 +30,9 @@ nodes:
     name: Chronic hepatitis C
     label: Disease
 links:
-  - key: increases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: increased
     source: DB:DB00008
     target: UniProt:P48551
     evidence:
@@ -40,7 +42,9 @@ links:
         evidence_source: IN_VITRO
         explanation: Peginterferon alfa-2a is a pegylated interferon alpha-2 that binds and activates the type I interferon receptor (IFNAR).
         source_tier: FULL_TEXT
-  - key: increases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: increased
     source: UniProt:P48551
     target: UniProt:P29597
     evidence:
@@ -49,7 +53,9 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         source_tier: FULL_TEXT
-  - key: increases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: increased
     source: UniProt:P29597
     target: UniProt:P42224
     evidence:
diff --git a/experiments/opus_vs_sonnet/opus/outputs/P36.yaml b/experiments/opus_vs_sonnet/opus/outputs/P36.yaml
index f2a87e4..015d387 100644
--- a/experiments/opus_vs_sonnet/opus/outputs/P36.yaml
+++ b/experiments/opus_vs_sonnet/opus/outputs/P36.yaml
@@ -33,7 +33,9 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: "Gramicidin is a channel-forming peptide that inserts into the membrane."
-  - key: increases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: increased
     source: MESH:D006096
     target: GO:0098655
     evidence:
diff --git a/experiments/opus_vs_sonnet/opus/outputs/P37.yaml b/experiments/opus_vs_sonnet/opus/outputs/P37.yaml
index da6cd44..dc569b0 100644
--- a/experiments/opus_vs_sonnet/opus/outputs/P37.yaml
+++ b/experiments/opus_vs_sonnet/opus/outputs/P37.yaml
@@ -24,7 +24,9 @@ nodes:
     name: Anxiety
     label: Disease
 links:
-  - key: increases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: increased
     source: DB:DB00186
     target: UniProt:P14867
     evidence:
@@ -33,7 +35,8 @@ links:
         supports: SUPPORT
         evidence_source: HUMAN_CLINICAL
         explanation: Lorazepam is a GABAA positive allosteric modulator, increasing GABAA receptor activity.
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P14867
     target: GO:1902476
     evidence:
diff --git a/experiments/opus_vs_sonnet/opus/outputs/P38.yaml b/experiments/opus_vs_sonnet/opus/outputs/P38.yaml
index 74048a4..bf0c94f 100644
--- a/experiments/opus_vs_sonnet/opus/outputs/P38.yaml
+++ b/experiments/opus_vs_sonnet/opus/outputs/P38.yaml
@@ -30,7 +30,9 @@ nodes:
     name: Hypercholesterolemia
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:D017035
     target: UniProt:P04035
     evidence:
@@ -46,7 +48,8 @@ links:
         snippet: "Statins have been widely used for the treatment of hypercholesterolemia due to their ability to inhibit HMG-CoA reductase, the rate-limiting enzyme of de novo cholesterol synthesis, via the so-called mevalonate pathway."
         supports: SUPPORT
         evidence_source: IN_VITRO
-  - key: negatively regulates
+  - key: regulates
+    object_direction_qualifier: decreased
     source: GO:0006695
     target: UniProt:Q12772
     evidence:
@@ -54,7 +57,8 @@ links:
         snippet: "The decrease of the hepatic intracellular cholesterol pool produced by these drugs upregulates the activity of the SREBP2 transcription factor, which subsequently stimulates the expression of the LDL receptor gene, an effect that is followed by an increase in the serum concentration of PCSK9."
         supports: SUPPORT
         evidence_source: OTHER
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:Q12772
     target: UniProt:P01130
     evidence:
diff --git a/experiments/opus_vs_sonnet/opus/outputs/P39.yaml b/experiments/opus_vs_sonnet/opus/outputs/P39.yaml
index 9193735..af8b9b8 100644
--- a/experiments/opus_vs_sonnet/opus/outputs/P39.yaml
+++ b/experiments/opus_vs_sonnet/opus/outputs/P39.yaml
@@ -24,7 +24,9 @@ nodes:
     name: Type 1 Diabetes Mellitus
     label: Disease
 links:
-  - key: increases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: increased
     source: DB:DB00046
     target: UniProt:P06213
     evidence:
@@ -38,7 +40,8 @@ links:
         supports: SUPPORT
         evidence_source: OTHER
         explanation: "Ligand binding to the insulin receptor alpha subunits triggers conformational changes that stimulate autophosphorylation and promote the receptor's kinase activity."
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P06213
     target: GO:0046323
     evidence:
@@ -52,7 +55,8 @@ links:
         supports: SUPPORT
         evidence_source: OTHER
         explanation: "Insulin receptor signaling increases glucose flux into cells via GLUT4 translocation."
-  - key: negatively regulates
+  - key: regulates
+    object_direction_qualifier: decreased
     source: GO:0046323
     target: HP:0003074
     evidence:
diff --git a/experiments/opus_vs_sonnet/opus/outputs/P40.yaml b/experiments/opus_vs_sonnet/opus/outputs/P40.yaml
index 632d830..24fc557 100644
--- a/experiments/opus_vs_sonnet/opus/outputs/P40.yaml
+++ b/experiments/opus_vs_sonnet/opus/outputs/P40.yaml
@@ -27,7 +27,9 @@ nodes:
     name: Asthma
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: DB:DB00043
     target: UniProt:P01854
     evidence:
@@ -36,7 +38,9 @@ links:
         supports: SUPPORT
         evidence_source: HUMAN_CLINICAL
         explanation: "Omalizumab binds and sequesters free IgE, neutralizing its function."
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: UniProt:P01854
     target: UniProt:P12319
     evidence:
@@ -53,7 +57,8 @@ links:
         snippet: "can block IgE's binding to high-affinity IgE Fc receptors (FcepsilonRI) on mast cells and basophils"
         supports: SUPPORT
         evidence_source: OTHER
-  - key: negatively regulates
+  - key: regulates
+    object_direction_qualifier: decreased
     source: UniProt:P12319
     target: GO:0043303
     evidence:
diff --git a/experiments/opus_vs_sonnet/sonnet/outputs/P01.yaml b/experiments/opus_vs_sonnet/sonnet/outputs/P01.yaml
index 22134f0..c8a9644 100644
--- a/experiments/opus_vs_sonnet/sonnet/outputs/P01.yaml
+++ b/experiments/opus_vs_sonnet/sonnet/outputs/P01.yaml
@@ -24,7 +24,9 @@ nodes:
     name: Myocardial Infarction
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:D001241
     target: UniProt:P23219
     evidence:
@@ -38,7 +40,8 @@ links:
         supports: SUPPORT
         evidence_source: HUMAN_CLINICAL
         explanation: States that aspirin inactivates COX-1, confirming decreases activity of relationship.
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P23219
     target: MESH:D013931
     evidence:
@@ -52,7 +55,8 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: States COX-1 is involved in platelet production of TXA2, supporting positive regulation.
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: MESH:D013931
     target: GO:0070527
     evidence:
diff --git a/experiments/opus_vs_sonnet/sonnet/outputs/P02.yaml b/experiments/opus_vs_sonnet/sonnet/outputs/P02.yaml
index bc57063..d8f4e35 100644
--- a/experiments/opus_vs_sonnet/sonnet/outputs/P02.yaml
+++ b/experiments/opus_vs_sonnet/sonnet/outputs/P02.yaml
@@ -24,7 +24,9 @@ nodes:
     name: Hypercholesterolemia
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:D000069059
     target: UniProt:P04035
     evidence:
@@ -47,7 +49,8 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: HMG-CoA reductase catalyzes the committed (rate-limiting) step in the cholesterol biosynthetic process.
-  - key: negatively regulates
+  - key: regulates
+    object_direction_qualifier: decreased
     source: GO:0006695
     target: UniProt:P01130
     evidence:
@@ -56,7 +59,8 @@ links:
         supports: SUPPORT
         evidence_source: HUMAN_CLINICAL
         explanation: Reduced cholesterol biosynthesis (via HMGCR inhibition) leads to LDL receptor upregulation, demonstrating that the cholesterol biosynthetic process negatively regulates LDL receptor expression.
-  - key: negatively regulates
+  - key: regulates
+    object_direction_qualifier: decreased
     source: UniProt:P01130
     target: MESH:D006937
     evidence:
diff --git a/experiments/opus_vs_sonnet/sonnet/outputs/P03.yaml b/experiments/opus_vs_sonnet/sonnet/outputs/P03.yaml
index 69eb7f0..0277610 100644
--- a/experiments/opus_vs_sonnet/sonnet/outputs/P03.yaml
+++ b/experiments/opus_vs_sonnet/sonnet/outputs/P03.yaml
@@ -24,7 +24,9 @@ nodes:
     name: Hypertension
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:D017706
     target: UniProt:P12821
     evidence:
@@ -37,7 +39,8 @@ links:
         snippet: Inhibition of the angiotensin-converting enzyme (ACE) protects against the progression of several cardiovascular diseases. Because of its dual role in regulating angiotensin II and bradykinin levels, the positive clinical effects of ACE inhibitors were thought to be the consequence of concomitant reductions in the production of angiotensin II
         supports: SUPPORT
         evidence_source: IN_VITRO
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P12821
     target: MESH:D000804
     evidence:
diff --git a/experiments/opus_vs_sonnet/sonnet/outputs/P04.yaml b/experiments/opus_vs_sonnet/sonnet/outputs/P04.yaml
index ec52de6..4c2e6c5 100644
--- a/experiments/opus_vs_sonnet/sonnet/outputs/P04.yaml
+++ b/experiments/opus_vs_sonnet/sonnet/outputs/P04.yaml
@@ -21,7 +21,9 @@ nodes:
     name: Heart Failure
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:D008790
     target: UniProt:P08588
     evidence:
@@ -35,7 +37,8 @@ links:
         supports: SUPPORT
         evidence_source: MODEL_ORGANISM
         explanation: Metoprolol is a beta-1 adrenergic receptor blocker, decreasing receptor activity.
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P08588
     target: GO:0006915
     evidence:
diff --git a/experiments/opus_vs_sonnet/sonnet/outputs/P05.yaml b/experiments/opus_vs_sonnet/sonnet/outputs/P05.yaml
index b1df0a2..60b414f 100644
--- a/experiments/opus_vs_sonnet/sonnet/outputs/P05.yaml
+++ b/experiments/opus_vs_sonnet/sonnet/outputs/P05.yaml
@@ -33,7 +33,9 @@ links:
         supports: SUPPORT
         evidence_source: HUMAN_CLINICAL
         explanation: Establishes that clopidogrel is a prodrug that generates an active metabolite responsible for its antiplatelet effect.
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: CHEBI:174738
     target: UniProt:Q9H244
     evidence:
@@ -46,7 +48,8 @@ links:
         snippet: Clopidogrel is an antithrombotic prodrug, whose active metabolite inhibits platelet function by irreversibly binding to the platelet receptor for adenosine diphosphate, P2Y(12).
         supports: SUPPORT
         evidence_source: HUMAN_CLINICAL
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:Q9H244
     target: GO:0070527
     evidence:
diff --git a/experiments/opus_vs_sonnet/sonnet/outputs/P06.yaml b/experiments/opus_vs_sonnet/sonnet/outputs/P06.yaml
index 1951b45..8afa120 100644
--- a/experiments/opus_vs_sonnet/sonnet/outputs/P06.yaml
+++ b/experiments/opus_vs_sonnet/sonnet/outputs/P06.yaml
@@ -33,7 +33,9 @@ links:
         supports: SUPPORT
         evidence_source: HUMAN_CLINICAL
         explanation: Tamoxifen is metabolised by CYP enzymes to form the active metabolite 4-hydroxytamoxifen.
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: CHEBI:44616
     target: UniProt:P03372
     evidence:
@@ -47,7 +49,8 @@ links:
         supports: SUPPORT
         evidence_source: HUMAN_CLINICAL
         explanation: Active tamoxifen metabolites including 4-hydroxytamoxifen have high affinity for the estrogen receptor and suppress its proliferative activity.
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P03372
     target: GO:0008283
     evidence:
diff --git a/experiments/opus_vs_sonnet/sonnet/outputs/P07.yaml b/experiments/opus_vs_sonnet/sonnet/outputs/P07.yaml
index ceb30c3..a866fb3 100644
--- a/experiments/opus_vs_sonnet/sonnet/outputs/P07.yaml
+++ b/experiments/opus_vs_sonnet/sonnet/outputs/P07.yaml
@@ -24,7 +24,9 @@ nodes:
     name: Chronic Myeloid Leukemia
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:D000068877
     target: UniProt:P00519
     evidence:
@@ -36,7 +38,8 @@ links:
         snippet: STI571 was shown to be a competitive inhibitor at the ATP-binding site of the Bcr-Abl tyrosine kinase
         supports: SUPPORT
         evidence_source: IN_VITRO
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P00519
     target: GO:0008283
     evidence:
@@ -48,7 +51,8 @@ links:
         snippet: Chronic myeloid leukaemia (CML) is a myeloproliferative neoplasm characterized by constitutive activity of the tyrosine kinase BCR-ABL1
         supports: PARTIAL
         evidence_source: HUMAN_CLINICAL
-  - key: negatively regulates
+  - key: regulates
+    object_direction_qualifier: decreased
     source: UniProt:P00519
     target: GO:0006915
     evidence:
diff --git a/experiments/opus_vs_sonnet/sonnet/outputs/P08.yaml b/experiments/opus_vs_sonnet/sonnet/outputs/P08.yaml
index e327040..edc2e16 100644
--- a/experiments/opus_vs_sonnet/sonnet/outputs/P08.yaml
+++ b/experiments/opus_vs_sonnet/sonnet/outputs/P08.yaml
@@ -21,7 +21,7 @@ nodes:
     name: Colorectal Cancer
     label: Disease
 links:
-  - key: molecularly interacts with
+  - key: directly physically interacts with
     source: MESH:D000068818
     target: UniProt:P00533
     evidence:
@@ -30,7 +30,9 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: Cetuximab binds specifically to the extracellular domain of EGFR (UniProt:P00533).
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:D000068818
     target: UniProt:P00533
     evidence:
@@ -39,7 +41,8 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: Cetuximab binding blocks EGFR phosphorylation and downstream kinase activation, thereby decreasing EGFR signaling activity.
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P00533
     target: GO:0008283
     evidence:
diff --git a/experiments/opus_vs_sonnet/sonnet/outputs/P09.yaml b/experiments/opus_vs_sonnet/sonnet/outputs/P09.yaml
index 3779c10..547efb1 100644
--- a/experiments/opus_vs_sonnet/sonnet/outputs/P09.yaml
+++ b/experiments/opus_vs_sonnet/sonnet/outputs/P09.yaml
@@ -24,7 +24,9 @@ nodes:
     name: Acute Lymphoblastic Leukemia
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:D008727
     target: UniProt:P00374
     evidence:
@@ -56,7 +58,8 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: dTMP biosynthesis is required for DNA synthesis; inhibiting dTMP synthesis directly inhibits DNA replication.
-  - key: negatively regulates
+  - key: regulates
+    object_direction_qualifier: decreased
     source: MESH:D008727
     target: GO:0071897
     evidence:
diff --git a/experiments/opus_vs_sonnet/sonnet/outputs/P10.yaml b/experiments/opus_vs_sonnet/sonnet/outputs/P10.yaml
index 9dd826d..5c557eb 100644
--- a/experiments/opus_vs_sonnet/sonnet/outputs/P10.yaml
+++ b/experiments/opus_vs_sonnet/sonnet/outputs/P10.yaml
@@ -24,7 +24,9 @@ nodes:
     name: HER2-positive Breast Cancer
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:D000068878
     target: UniProt:P04626
     evidence:
@@ -33,7 +35,8 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: Trastuzumab abrogates intracellular signaling downstream of HER2, effectively decreasing HER2-mediated signaling activity.
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P04626
     target: UniProt:P31749
     evidence:
@@ -42,7 +45,8 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: HER2 (ErbB2) activates the PI3K/AKT (protein kinase B) pathway, demonstrating HER2 positively regulates AKT1 signaling.
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P31749
     target: GO:0008283
     evidence:
diff --git a/experiments/opus_vs_sonnet/sonnet/outputs/P11.yaml b/experiments/opus_vs_sonnet/sonnet/outputs/P11.yaml
index e4a88fb..28a8b20 100644
--- a/experiments/opus_vs_sonnet/sonnet/outputs/P11.yaml
+++ b/experiments/opus_vs_sonnet/sonnet/outputs/P11.yaml
@@ -21,7 +21,9 @@ nodes:
     name: Pulmonary Tuberculosis
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:D012293
     target: UniProt:P9WKP4
     evidence:
@@ -49,7 +51,8 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: RpoB is the subunit through which RNA extension (transcription) occurs; rifampicin blocks this activity by steric occlusion.
-  - key: negatively regulates
+  - key: regulates
+    object_direction_qualifier: decreased
     source: MESH:D012293
     target: GO:0006351
     evidence:
diff --git a/experiments/opus_vs_sonnet/sonnet/outputs/P12.yaml b/experiments/opus_vs_sonnet/sonnet/outputs/P12.yaml
index 0100e18..b2565e4 100644
--- a/experiments/opus_vs_sonnet/sonnet/outputs/P12.yaml
+++ b/experiments/opus_vs_sonnet/sonnet/outputs/P12.yaml
@@ -24,7 +24,9 @@ nodes:
     name: Pulmonary Tuberculosis
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:D007538
     target: UniProt:P0A5Q9
     evidence:
diff --git a/experiments/opus_vs_sonnet/sonnet/outputs/P13.yaml b/experiments/opus_vs_sonnet/sonnet/outputs/P13.yaml
index f582b08..7d51ed3 100644
--- a/experiments/opus_vs_sonnet/sonnet/outputs/P13.yaml
+++ b/experiments/opus_vs_sonnet/sonnet/outputs/P13.yaml
@@ -24,7 +24,7 @@ nodes:
     name: MRSA Infection
     label: Disease
 links:
-  - key: binds
+  - key: directly physically interacts with
     source: MESH:D014640
     target: CHEBI:83419
     evidence:
@@ -33,7 +33,8 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: Vancomycin binds the D-Ala-D-Ala terminus of the peptidoglycan precursor lipid II.
-  - key: negatively regulates
+  - key: regulates
+    object_direction_qualifier: decreased
     source: CHEBI:83419
     target: GO:0009252
     evidence:
@@ -42,7 +43,8 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: Vancomycin binding to Lipid II interferes with peptidoglycan layer maturation (biosynthetic process).
-  - key: negatively regulates
+  - key: regulates
+    object_direction_qualifier: decreased
     source: GO:0009252
     target: NCBITaxon:1280
     evidence:
diff --git a/experiments/opus_vs_sonnet/sonnet/outputs/P14.yaml b/experiments/opus_vs_sonnet/sonnet/outputs/P14.yaml
index 9bba259..a2b1aa7 100644
--- a/experiments/opus_vs_sonnet/sonnet/outputs/P14.yaml
+++ b/experiments/opus_vs_sonnet/sonnet/outputs/P14.yaml
@@ -36,7 +36,9 @@ links:
         snippet: Oseltamivir, an inactive anti-influenza virus prodrug, is activated (hydrolysed) in vivo by carboxylesterase 1 (CES1) to its active metabolite oseltamivir carboxylate.
         supports: SUPPORT
         evidence_source: HUMAN_CLINICAL
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: CHEBI:67200
     target: UniProt:P03472
     evidence:
@@ -48,7 +50,8 @@ links:
         snippet: Anti influenza drugs such as Oseltamivir target a highly conserved active site of NA, which comprises of 8 functional residues (R118, D151, R152, R224, E276, R292, R371 and Y406) to restrict viral release from host cells, thus inhibiting its ability to cleave sialic acid residues on the cell membrane.
         supports: SUPPORT
         evidence_source: COMPUTATIONAL
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P03472
     target: GO:0019076
     evidence:
diff --git a/experiments/opus_vs_sonnet/sonnet/outputs/P15.yaml b/experiments/opus_vs_sonnet/sonnet/outputs/P15.yaml
index 63bfd69..518e978 100644
--- a/experiments/opus_vs_sonnet/sonnet/outputs/P15.yaml
+++ b/experiments/opus_vs_sonnet/sonnet/outputs/P15.yaml
@@ -33,7 +33,9 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: Acyclovir is phosphorylated by viral thymidine kinase to the monophosphate, which is then converted by cellular kinases to the active triphosphate metabolite.
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: CHEBI:16624
     target: UniProt:P04293
     evidence:
diff --git a/experiments/opus_vs_sonnet/sonnet/outputs/P16.yaml b/experiments/opus_vs_sonnet/sonnet/outputs/P16.yaml
index 4e3a12e..553a3f7 100644
--- a/experiments/opus_vs_sonnet/sonnet/outputs/P16.yaml
+++ b/experiments/opus_vs_sonnet/sonnet/outputs/P16.yaml
@@ -24,7 +24,9 @@ nodes:
     name: Parkinson's Disease
     label: Disease
 links:
-  - key: increases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: increased
     source: MESH:D007980
     target: UniProt:P20711
     evidence:
@@ -49,7 +51,9 @@ links:
         supports: SUPPORT
         evidence_source: MODEL_ORGANISM
         explanation: Confirms levodopa is a dopamine precursor and its conversion to dopamine is central to its therapeutic effect.
-  - key: increases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: increased
     source: MESH:D004298
     target: UniProt:P14416
     evidence:
diff --git a/experiments/opus_vs_sonnet/sonnet/outputs/P17.yaml b/experiments/opus_vs_sonnet/sonnet/outputs/P17.yaml
index 5ce54bc..7e9d4ba 100644
--- a/experiments/opus_vs_sonnet/sonnet/outputs/P17.yaml
+++ b/experiments/opus_vs_sonnet/sonnet/outputs/P17.yaml
@@ -24,7 +24,9 @@ nodes:
     name: Major Depressive Disorder
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:D005473
     target: UniProt:P31645
     evidence:
@@ -38,7 +40,8 @@ links:
         supports: SUPPORT
         evidence_source: HUMAN_CLINICAL
         explanation: SSRIs including fluoxetine inhibit presynaptic serotonin reuptake via SERT blockade.
-  - key: negatively regulates
+  - key: regulates
+    object_direction_qualifier: decreased
     source: UniProt:P31645
     target: MESH:D012701
     evidence:
@@ -47,7 +50,8 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: SERT normally removes serotonin from the synapse; its inhibition leads to increased extracellular serotonin.
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: MESH:D012701
     target: GO:0007210
     evidence:
@@ -56,7 +60,8 @@ links:
         supports: SUPPORT
         evidence_source: HUMAN_CLINICAL
         explanation: Increased synaptic serotonin activates postsynaptic receptors, enhancing serotonin receptor signaling.
-  - key: negatively regulates
+  - key: regulates
+    object_direction_qualifier: decreased
     source: GO:0007210
     target: MESH:D003865
     evidence:
diff --git a/experiments/opus_vs_sonnet/sonnet/outputs/P18.yaml b/experiments/opus_vs_sonnet/sonnet/outputs/P18.yaml
index 3e7c47a..b279bd5 100644
--- a/experiments/opus_vs_sonnet/sonnet/outputs/P18.yaml
+++ b/experiments/opus_vs_sonnet/sonnet/outputs/P18.yaml
@@ -21,7 +21,9 @@ nodes:
     name: Bipolar Disorder
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:D008094
     target: UniProt:P49841
     evidence:
@@ -35,7 +37,8 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: Lithium is hypothesized to exert its therapeutic effects through direct inhibition of GSK3.
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P49841
     target: GO:0006915
     evidence:
diff --git a/experiments/opus_vs_sonnet/sonnet/outputs/P19.yaml b/experiments/opus_vs_sonnet/sonnet/outputs/P19.yaml
index 6228eb8..9813d0a 100644
--- a/experiments/opus_vs_sonnet/sonnet/outputs/P19.yaml
+++ b/experiments/opus_vs_sonnet/sonnet/outputs/P19.yaml
@@ -24,7 +24,9 @@ nodes:
     name: Epilepsy
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:D000077306
     target: UniProt:P54289
     evidence:
@@ -37,7 +39,9 @@ links:
         snippet: binding to the alpha-2-delta protein subunit of voltage-gated calcium channels in the central nervous system, thereby blocking the excitatory influx of calcium
         supports: SUPPORT
         evidence_source: IN_VITRO
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: UniProt:P54289
     target: UniProt:O00555
     evidence:
@@ -46,7 +50,8 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: The alpha-2-delta subunit modulated by gabapentin decreases activity of the P/Q-type voltage-gated calcium channel, reducing Ca2+ influx.
-  - key: negatively regulates
+  - key: regulates
+    object_direction_qualifier: decreased
     source: UniProt:O00555
     target: GO:0007269
     evidence:
diff --git a/experiments/opus_vs_sonnet/sonnet/outputs/P20.yaml b/experiments/opus_vs_sonnet/sonnet/outputs/P20.yaml
index bc2407e..5bdd97b 100644
--- a/experiments/opus_vs_sonnet/sonnet/outputs/P20.yaml
+++ b/experiments/opus_vs_sonnet/sonnet/outputs/P20.yaml
@@ -24,7 +24,9 @@ nodes:
     name: Alzheimer's Disease
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:D000077856
     target: UniProt:P22303
     evidence:
@@ -33,7 +35,9 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: Donepezil acts by blocking AChE, increasing extracellular acetylcholine concentrations.
-  - key: decreases abundance of
+  - key: affects
+    object_aspect_qualifier: abundance
+    object_direction_qualifier: decreased
     source: UniProt:P22303
     target: MESH:D000109
     evidence:
@@ -42,7 +46,8 @@ links:
         supports: SUPPORT
         evidence_source: OTHER
         explanation: AChE hydrolyzes acetylcholine, thereby reducing its availability at the synapse.
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: MESH:D000109
     target: GO:0007271
     evidence:
diff --git a/experiments/opus_vs_sonnet/sonnet/outputs/P21.yaml b/experiments/opus_vs_sonnet/sonnet/outputs/P21.yaml
index 3430c53..8428817 100644
--- a/experiments/opus_vs_sonnet/sonnet/outputs/P21.yaml
+++ b/experiments/opus_vs_sonnet/sonnet/outputs/P21.yaml
@@ -27,7 +27,9 @@ nodes:
     name: Rheumatoid Arthritis
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:D008727
     target: UniProt:P00374
     evidence:
@@ -35,7 +37,9 @@ links:
         snippet: Methotrexate (MTX), a synthetic folate analog, is a tight-binding inhibitor of dihydrofolate reductase (DHFR), a key enzyme for the biosynthesis of purines, thymidylate, and several amino acids.
         supports: SUPPORT
         evidence_source: IN_VITRO
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:D008727
     target: UniProt:P31939
     evidence:
@@ -47,7 +51,8 @@ links:
         snippet: intracellular MTX polyglutamates inhibit AICAR transformylase (ATIC) activity and thereby promote adenosine release
         supports: SUPPORT
         evidence_source: IN_VITRO
-  - key: negatively regulates
+  - key: regulates
+    object_direction_qualifier: decreased
     source: UniProt:P31939
     target: MESH:D000241
     evidence:
@@ -61,7 +66,8 @@ links:
         supports: PARTIAL
         evidence_source: HUMAN_CLINICAL
         explanation: ATIC inhibition (blockade at AICA ribonucleotide transformylase step) leads to AICAR accumulation and adenosine release; this sentence describes the blockade and its clinical significance.
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: MESH:D000241
     target: UniProt:P29274
     evidence:
diff --git a/experiments/opus_vs_sonnet/sonnet/outputs/P23.yaml b/experiments/opus_vs_sonnet/sonnet/outputs/P23.yaml
index 006e6b9..ff2cbf6 100644
--- a/experiments/opus_vs_sonnet/sonnet/outputs/P23.yaml
+++ b/experiments/opus_vs_sonnet/sonnet/outputs/P23.yaml
@@ -26,7 +26,9 @@ nodes:
     label: Disease
 
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:D006886
     target: UniProt:Q9NYK1
     evidence:
@@ -40,7 +42,9 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
 
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:D006886
     target: UniProt:Q9NR96
     evidence:
@@ -54,7 +58,8 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
 
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:Q9NYK1
     target: GO:0032606
     evidence:
@@ -68,7 +73,8 @@ links:
         evidence_source: HUMAN_CLINICAL
         explanation: CpG-A stimulates TLR9 and R848/ssRNA stimulate TLR7/8; the pDC IFNα production is shown to be downstream of TLR activation.
 
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:Q9NR96
     target: GO:0032606
     evidence:
diff --git a/experiments/opus_vs_sonnet/sonnet/outputs/P24.yaml b/experiments/opus_vs_sonnet/sonnet/outputs/P24.yaml
index c8f52e9..d378aa3 100644
--- a/experiments/opus_vs_sonnet/sonnet/outputs/P24.yaml
+++ b/experiments/opus_vs_sonnet/sonnet/outputs/P24.yaml
@@ -33,7 +33,9 @@ links:
         supports: SUPPORT
         evidence_source: HUMAN_CLINICAL
         explanation: MMF is a prodrug that is completely hydrolyzed to the active metabolite mycophenolic acid (MPA) after oral administration.
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:D009173
     target: UniProt:P12268
     evidence:
@@ -46,7 +48,8 @@ links:
         snippet: Mycophenolic acid (MPA) is a highly selective, non-competitive and reversible inhibitor of the inosine monophosphate dehydrogenase (IMPDH), the rate-limiting enzyme in the de novo biosynthesis of guanosine nucleotides.
         supports: SUPPORT
         evidence_source: IN_VITRO
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P12268
     target: GO:0046651
     evidence:
diff --git a/experiments/opus_vs_sonnet/sonnet/outputs/P25.yaml b/experiments/opus_vs_sonnet/sonnet/outputs/P25.yaml
index 858b5f4..613b3a5 100644
--- a/experiments/opus_vs_sonnet/sonnet/outputs/P25.yaml
+++ b/experiments/opus_vs_sonnet/sonnet/outputs/P25.yaml
@@ -21,7 +21,7 @@ nodes:
     name: Psoriasis
     label: Disease
 links:
-  - key: molecularly interacts with
+  - key: directly physically interacts with
     source: MESH:D000068879
     target: UniProt:P01375
     evidence:
@@ -29,7 +29,9 @@ links:
         snippet: Adalimumab, a fully human monoclonal antibody, binds to and neutralizes tumor necrosis factor.
         supports: SUPPORT
         evidence_source: HUMAN_CLINICAL
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:D000068879
     target: UniProt:P01375
     evidence:
@@ -37,7 +39,8 @@ links:
         snippet: Adalimumab is a fully recombinant human immunoglobulin G1 monoclonal antibody that specifically binds with high affinity to human TNF-α and inhibits its binding to TNF receptors.
         supports: SUPPORT
         evidence_source: HUMAN_CLINICAL
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P01375
     target: GO:0007249
     evidence:
@@ -45,7 +48,8 @@ links:
         snippet: TNF-alpha and NF-kappaB expressions were significantly higher in psoriatic epidermis than in normal epidermis (p < 0.05).
         supports: SUPPORT
         evidence_source: HUMAN_CLINICAL
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: GO:0007249
     target: MESH:D011565
     evidence:
diff --git a/experiments/opus_vs_sonnet/sonnet/outputs/P26.yaml b/experiments/opus_vs_sonnet/sonnet/outputs/P26.yaml
index 24d0fad..5462a50 100644
--- a/experiments/opus_vs_sonnet/sonnet/outputs/P26.yaml
+++ b/experiments/opus_vs_sonnet/sonnet/outputs/P26.yaml
@@ -24,7 +24,9 @@ nodes:
     name: Diabetes Mellitus, Type 2
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:D008687
     target: UniProt:P03886
     evidence:
@@ -52,7 +54,8 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: Complex I inhibition by metformin raises AMP/ATP ratio and activates AMPK.
-  - key: negatively regulates
+  - key: regulates
+    object_direction_qualifier: decreased
     source: UniProt:Q13131
     target: GO:0006094
     evidence:
diff --git a/experiments/opus_vs_sonnet/sonnet/outputs/P29.yaml b/experiments/opus_vs_sonnet/sonnet/outputs/P29.yaml
index 4675722..4f25d3a 100644
--- a/experiments/opus_vs_sonnet/sonnet/outputs/P29.yaml
+++ b/experiments/opus_vs_sonnet/sonnet/outputs/P29.yaml
@@ -21,7 +21,9 @@ nodes:
     name: Gout
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:D000493
     target: UniProt:P47989
     evidence:
@@ -30,7 +32,8 @@ links:
         supports: SUPPORT
         evidence_source: HUMAN_CLINICAL
         explanation: Allopurinol directly inhibits xanthine oxidase, reducing urate production.
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P47989
     target: MESH:D014527
     evidence:
diff --git a/experiments/opus_vs_sonnet/sonnet/outputs/P30.yaml b/experiments/opus_vs_sonnet/sonnet/outputs/P30.yaml
index 0375c4b..fdcf75c 100644
--- a/experiments/opus_vs_sonnet/sonnet/outputs/P30.yaml
+++ b/experiments/opus_vs_sonnet/sonnet/outputs/P30.yaml
@@ -24,7 +24,9 @@ nodes:
     name: Type 2 Diabetes Mellitus
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:C000591311
     target: UniProt:P31639
     evidence:
@@ -38,7 +40,8 @@ links:
         supports: SUPPORT
         evidence_source: HUMAN_CLINICAL
         explanation: Confirms SGLT2 inhibition as the mechanism of action of empagliflozin.
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P31639
     target: GO:0070293
     evidence:
@@ -52,7 +55,8 @@ links:
         supports: SUPPORT
         evidence_source: HUMAN_CLINICAL
         explanation: SGLT2 is the primary transporter responsible for renal glucose reabsorption.
-  - key: negatively regulates
+  - key: regulates
+    object_direction_qualifier: decreased
     source: GO:0070293
     target: HP:0003074
     evidence:
diff --git a/experiments/opus_vs_sonnet/sonnet/outputs/P31.yaml b/experiments/opus_vs_sonnet/sonnet/outputs/P31.yaml
index 8a52ff3..92ee0ab 100644
--- a/experiments/opus_vs_sonnet/sonnet/outputs/P31.yaml
+++ b/experiments/opus_vs_sonnet/sonnet/outputs/P31.yaml
@@ -30,7 +30,9 @@ nodes:
     name: Hemophilia A
     label: Disease
 links:
-  - key: increases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: increased
     source: MESH:C016671
     target: UniProt:P30518
     evidence:
@@ -39,7 +41,9 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: DDAVP (the synthetic vasopressin analogue) activates the endothelial vasopressin V2 receptor (AVPR2), initiating cAMP-mediated signaling.
-  - key: increases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: increased
     source: UniProt:P30518
     target: GO:0019933
     evidence:
@@ -48,7 +52,8 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: Activation of the V2 receptor increases cAMP-mediated signaling, which drives Weibel-Palade body exocytosis.
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: GO:0019933
     target: GO:0099132
     evidence:
@@ -57,7 +62,8 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: cAMP-mediated signaling downstream of V2 receptor activation leads to exocytosis from Weibel-Palade bodies.
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: GO:0099132
     target: UniProt:P04275
     evidence:
@@ -70,7 +76,8 @@ links:
         snippet: DDAVP elicits the release of von Willebrand Factor (VWF) from endothelial cells, thereby increasing the levels of circulating VWF and coagulation factor (F)VIII.
         supports: SUPPORT
         evidence_source: HUMAN_CLINICAL
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P04275
     target: UniProt:P00451
     evidence:
diff --git a/experiments/opus_vs_sonnet/sonnet/outputs/P32.yaml b/experiments/opus_vs_sonnet/sonnet/outputs/P32.yaml
index 38a5000..1d8bc65 100644
--- a/experiments/opus_vs_sonnet/sonnet/outputs/P32.yaml
+++ b/experiments/opus_vs_sonnet/sonnet/outputs/P32.yaml
@@ -21,7 +21,9 @@ nodes:
     name: Ascorbic acid deficiency
     label: Disease
 links:
-  - key: increases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: increased
     source: MESH:D001205
     target: UniProt:P13674
     evidence:
diff --git a/experiments/opus_vs_sonnet/sonnet/outputs/P34.yaml b/experiments/opus_vs_sonnet/sonnet/outputs/P34.yaml
index 258c268..409c0c5 100644
--- a/experiments/opus_vs_sonnet/sonnet/outputs/P34.yaml
+++ b/experiments/opus_vs_sonnet/sonnet/outputs/P34.yaml
@@ -27,7 +27,8 @@ nodes:
     name: Primary cutaneous T-cell lymphoma
     label: Disease
 links:
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: MESH:C078456
     target: UniProt:P01589
     evidence:
@@ -39,7 +40,9 @@ links:
         snippet: DAB(389)IL-2 is internalized into IL-2 receptor-bearing cells by endocytosis.
         supports: SUPPORT
         evidence_source: IN_VITRO
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:C078456
     target: UniProt:P13639
     evidence:
@@ -48,7 +51,8 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         source_tier: FULL_TEXT
-  - key: negatively regulates
+  - key: regulates
+    object_direction_qualifier: decreased
     source: UniProt:P13639
     target: GO:0006412
     evidence:
@@ -56,7 +60,8 @@ links:
         snippet: ADP(R) of eEF2 resulted in a decrease in total protein synthesis consistent with a defect in translation elongation.
         supports: SUPPORT
         evidence_source: IN_VITRO
-  - key: negatively regulates
+  - key: regulates
+    object_direction_qualifier: decreased
     source: GO:0006412
     target: GO:0006915
     evidence:
diff --git a/experiments/opus_vs_sonnet/sonnet/outputs/P35.yaml b/experiments/opus_vs_sonnet/sonnet/outputs/P35.yaml
index 92b4204..500da7d 100644
--- a/experiments/opus_vs_sonnet/sonnet/outputs/P35.yaml
+++ b/experiments/opus_vs_sonnet/sonnet/outputs/P35.yaml
@@ -33,7 +33,9 @@ nodes:
     name: Chronic hepatitis C
     label: Disease
 links:
-  - key: increases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: increased
     source: MESH:C100416
     target: UniProt:P23458
     evidence:
@@ -42,7 +44,9 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: Peginterferon alfa-2a (an IFN-alpha) activates JAK1 through receptor engagement.
-  - key: increases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: increased
     source: MESH:C100416
     target: UniProt:P29597
     evidence:
@@ -51,7 +55,9 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: Peginterferon alfa-2a (an IFN-alpha) activates TYK2 through receptor engagement.
-  - key: increases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: increased
     source: UniProt:P23458
     target: UniProt:P42224
     evidence:
@@ -60,7 +66,9 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: Activated JAK1 phosphorylates STAT1 on conserved tyrosine residues.
-  - key: increases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: increased
     source: UniProt:P29597
     target: UniProt:P52630
     evidence:
@@ -69,7 +77,8 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: Activated TYK2 phosphorylates STAT2 on conserved tyrosine residues.
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P42224
     target: GO:0035458
     evidence:
@@ -78,7 +87,8 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: STAT1 forms ISGF3 complex that drives interferon-stimulated gene transcription, representing the cellular response to interferon.
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P52630
     target: GO:0035458
     evidence:
@@ -87,7 +97,8 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: STAT2 forms ISGF3 complex that drives interferon-stimulated gene transcription, representing the cellular response to interferon.
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: GO:0035458
     target: GO:0009615
     evidence:
@@ -96,7 +107,8 @@ links:
         supports: SUPPORT
         evidence_source: HUMAN_CLINICAL
         explanation: IFN-alpha-induced ISG expression (cellular interferon response) leads to an antiviral response against HCV.
-  - key: negatively regulates
+  - key: regulates
+    object_direction_qualifier: decreased
     source: GO:0009615
     target: MESH:D019698
     evidence:
diff --git a/experiments/opus_vs_sonnet/sonnet/outputs/P37.yaml b/experiments/opus_vs_sonnet/sonnet/outputs/P37.yaml
index c1c5a76..62bd5e9 100644
--- a/experiments/opus_vs_sonnet/sonnet/outputs/P37.yaml
+++ b/experiments/opus_vs_sonnet/sonnet/outputs/P37.yaml
@@ -24,7 +24,9 @@ nodes:
     name: Anxiety
     label: Disease
 links:
-  - key: increases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: increased
     source: MESH:D008140
     target: UniProt:P14867
     evidence:
@@ -33,7 +35,9 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: Lorazepam is a benzodiazepine that binds allosterically to the GABA-A receptor and increases its activity (chloride current).
-  - key: increases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: increased
     source: UniProt:P14867
     target: GO:0005254
     evidence:
@@ -51,7 +55,8 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: Chloride influx through the GABA-A channel causes membrane hyperpolarization of the postsynaptic neuron.
-  - key: negatively regulates
+  - key: regulates
+    object_direction_qualifier: decreased
     source: GO:0060081
     target: MESH:D001007
     evidence:
diff --git a/experiments/opus_vs_sonnet/sonnet/outputs/P38.yaml b/experiments/opus_vs_sonnet/sonnet/outputs/P38.yaml
index e0e424b..ed0aa01 100644
--- a/experiments/opus_vs_sonnet/sonnet/outputs/P38.yaml
+++ b/experiments/opus_vs_sonnet/sonnet/outputs/P38.yaml
@@ -27,7 +27,9 @@ nodes:
     name: Hypercholesterolemia
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:D017035
     target: UniProt:P04035
     evidence:
@@ -47,7 +49,8 @@ links:
         snippet: Statins have been widely used for the treatment of hypercholesterolemia due to their ability to inhibit HMG-CoA reductase, the rate-limiting enzyme of de novo cholesterol synthesis, via the so-called mevalonate pathway.
         supports: SUPPORT
         evidence_source: IN_VITRO
-  - key: negatively regulates
+  - key: regulates
+    object_direction_qualifier: decreased
     source: GO:0006695
     target: UniProt:P01130
     evidence:
@@ -56,7 +59,8 @@ links:
         supports: SUPPORT
         evidence_source: HUMAN_CLINICAL
         explanation: Inhibition of cholesterol biosynthesis (via reduced mevalonate synthesis) is linked to upregulation of LDL receptor expression, consistent with the negative feedback relationship between intracellular cholesterol levels and LDLR expression.
-  - key: negatively regulates
+  - key: regulates
+    object_direction_qualifier: decreased
     source: UniProt:P01130
     target: MESH:D008077
     evidence:
diff --git a/experiments/opus_vs_sonnet/sonnet/outputs/P40.yaml b/experiments/opus_vs_sonnet/sonnet/outputs/P40.yaml
index 597a574..17d2dc3 100644
--- a/experiments/opus_vs_sonnet/sonnet/outputs/P40.yaml
+++ b/experiments/opus_vs_sonnet/sonnet/outputs/P40.yaml
@@ -27,7 +27,9 @@ nodes:
     name: Asthma
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:D000069444
     target: UniProt:P01854
     evidence:
@@ -35,7 +37,8 @@ links:
         snippet: This non-anaphylactogenic anti-IgE monoclonal antibody (omalizumab) binds IgE at the same site as these antibodies bind FcepsilonRI and FcepsilonRII. Consequently, omalizumab inhibits IgE effector functions by blocking IgE binding to high-affinity receptors on IgE effector cells.
         supports: SUPPORT
         evidence_source: HUMAN_CLINICAL
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P01854
     target: UniProt:P12319
     evidence:
@@ -43,7 +46,8 @@ links:
         snippet: interaction with FcεRI on mast cells and basophils leads to immediate hypersensitivity reactions upon allergen challenge
         supports: SUPPORT
         evidence_source: IN_VITRO
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P12319
     target: GO:0043303
     evidence:
diff --git a/experiments/pilot/outputs/B02362_MESH_D003882_1.yaml b/experiments/pilot/outputs/B02362_MESH_D003882_1.yaml
index 8449169..e9dc400 100644
--- a/experiments/pilot/outputs/B02362_MESH_D003882_1.yaml
+++ b/experiments/pilot/outputs/B02362_MESH_D003882_1.yaml
@@ -18,7 +18,9 @@ nodes:
     name: Dermatomyositis
     label: Disease
 links:
-  - key: decreases abundance of
+  - key: affects
+    object_aspect_qualifier: abundance
+    object_direction_qualifier: decreased
     source: MESH:D010129
     target: MESH:D006025
     evidence:
diff --git a/experiments/pilot/outputs/B02362_MESH_D003882_1__r2.yaml b/experiments/pilot/outputs/B02362_MESH_D003882_1__r2.yaml
index 843384c..9c09db3 100644
--- a/experiments/pilot/outputs/B02362_MESH_D003882_1__r2.yaml
+++ b/experiments/pilot/outputs/B02362_MESH_D003882_1__r2.yaml
@@ -21,7 +21,8 @@ nodes:
     name: Dermatomyositis
     label: Disease
 links:
-  - key: negatively regulates
+  - key: regulates
+    object_direction_qualifier: decreased
     source: MESH:D010129
     target: GO:0009411
     evidence:
@@ -30,7 +31,8 @@ links:
         supports: SUPPORT
         evidence_source: MODEL_ORGANISM
         explanation: "para-aminobenzoic acid (aminobenzoic acid) is a UV absorber that, applied before UVB exposure, prevents the pathological skin changes caused by UVB, i.e. it blunts the skin's response to ultraviolet radiation."
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: GO:0009411
     target: GO:0006915
     evidence:
diff --git a/experiments/pilot/outputs/B02362_MESH_D003882_1__r3.yaml b/experiments/pilot/outputs/B02362_MESH_D003882_1__r3.yaml
index 0339fe2..71a4c66 100644
--- a/experiments/pilot/outputs/B02362_MESH_D003882_1__r3.yaml
+++ b/experiments/pilot/outputs/B02362_MESH_D003882_1__r3.yaml
@@ -18,7 +18,9 @@ nodes:
     name: Dermatomyositis
     label: Disease
 links:
-  - key: decreases abundance of
+  - key: affects
+    object_aspect_qualifier: abundance
+    object_direction_qualifier: decreased
     source: MESH:D010129
     target: MESH:D006025
     evidence:
diff --git a/experiments/pilot/outputs/DB00002_MESH_D003110_1.yaml b/experiments/pilot/outputs/DB00002_MESH_D003110_1.yaml
index 8d7967c..0c84ac1 100644
--- a/experiments/pilot/outputs/DB00002_MESH_D003110_1.yaml
+++ b/experiments/pilot/outputs/DB00002_MESH_D003110_1.yaml
@@ -21,7 +21,9 @@ nodes:
     name: Malignant tumor of colon
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:D000068818
     target: UniProt:P00533
     evidence:
@@ -30,7 +32,8 @@ links:
         supports: SUPPORT
         evidence_source: OTHER
         explanation: "Cetuximab binds the extracellular domain of EGFR and impairs EGFR-mediated signaling, i.e. decreases EGFR activity."
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P00533
     target: GO:0008283
     evidence:
diff --git a/experiments/pilot/outputs/DB00002_MESH_D003110_1__r2.yaml b/experiments/pilot/outputs/DB00002_MESH_D003110_1__r2.yaml
index 19fa753..168fb95 100644
--- a/experiments/pilot/outputs/DB00002_MESH_D003110_1__r2.yaml
+++ b/experiments/pilot/outputs/DB00002_MESH_D003110_1__r2.yaml
@@ -21,7 +21,9 @@ nodes:
     name: Malignant tumor of colon
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:D000068818
     target: UniProt:P00533
     evidence:
@@ -34,7 +36,8 @@ links:
         snippet: "Cetuximab binding to the EGFR blocks phosphorylation and activation of receptor-associated kinases and their associated downstream signalling (MAPK, PI3K/Akt, Jak/Stat pathways)"
         supports: SUPPORT
         evidence_source: OTHER
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P00533
     target: GO:0008283
     evidence:
diff --git a/experiments/pilot/outputs/DB00002_MESH_D003110_1__r3.yaml b/experiments/pilot/outputs/DB00002_MESH_D003110_1__r3.yaml
index 219afef..6a67023 100644
--- a/experiments/pilot/outputs/DB00002_MESH_D003110_1__r3.yaml
+++ b/experiments/pilot/outputs/DB00002_MESH_D003110_1__r3.yaml
@@ -21,7 +21,9 @@ nodes:
     name: Malignant tumor of colon
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: DB:DB00002
     target: UniProt:P00533
     evidence:
@@ -30,7 +32,8 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: "Cetuximab blocks ligand-dependent EGFR signaling, reducing EGFR activity."
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P00533
     target: GO:0008283
     evidence:
diff --git a/experiments/pilot/outputs/DB00005_MESH_D015535_1.yaml b/experiments/pilot/outputs/DB00005_MESH_D015535_1.yaml
index 00e520d..95b084b 100644
--- a/experiments/pilot/outputs/DB00005_MESH_D015535_1.yaml
+++ b/experiments/pilot/outputs/DB00005_MESH_D015535_1.yaml
@@ -21,7 +21,9 @@ nodes:
     name: Psoriasis with arthropathy
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: DB:DB00005
     target: UniProt:P01375
     evidence:
diff --git a/experiments/pilot/outputs/DB00009_MESH_D011655_1.yaml b/experiments/pilot/outputs/DB00009_MESH_D011655_1.yaml
index d414ac9..4e8b44f 100644
--- a/experiments/pilot/outputs/DB00009_MESH_D011655_1.yaml
+++ b/experiments/pilot/outputs/DB00009_MESH_D011655_1.yaml
@@ -21,7 +21,9 @@ nodes:
     name: Pulmonary embolism
     label: Disease
 links:
-  - key: increases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: increased
     source: DB:DB00009
     target: UniProt:P00747
     evidence:
@@ -30,7 +32,9 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: "Alteplase is recombinant human tissue-type plasminogen activator (t-PA), which activates the zymogen plasminogen."
-  - key: decreases abundance of
+  - key: affects
+    object_aspect_qualifier: abundance
+    object_direction_qualifier: decreased
     source: UniProt:P00747
     target: MESH:D005342
     evidence:
diff --git a/experiments/pilot/outputs/DB00009_MESH_D011655_1__r2.yaml b/experiments/pilot/outputs/DB00009_MESH_D011655_1__r2.yaml
index fca8a95..b3e288c 100644
--- a/experiments/pilot/outputs/DB00009_MESH_D011655_1__r2.yaml
+++ b/experiments/pilot/outputs/DB00009_MESH_D011655_1__r2.yaml
@@ -24,7 +24,9 @@ nodes:
     name: Pulmonary embolism
     label: Disease
 links:
-  - key: increases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: increased
     source: DB:DB00009
     target: UniProt:P00747
     evidence:
diff --git a/experiments/pilot/outputs/DB00009_MESH_D011655_1__r3.yaml b/experiments/pilot/outputs/DB00009_MESH_D011655_1__r3.yaml
index 5cd8af7..10ad45f 100644
--- a/experiments/pilot/outputs/DB00009_MESH_D011655_1__r3.yaml
+++ b/experiments/pilot/outputs/DB00009_MESH_D011655_1__r3.yaml
@@ -21,7 +21,9 @@ nodes:
     name: Pulmonary embolism
     label: Disease
 links:
-  - key: increases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: increased
     source: DB:DB00009
     target: UniProt:P00747
     evidence:
@@ -34,7 +36,9 @@ links:
         snippet: "The therapeutic action of tissue plasminogen activator (t-PA) is a two-step process: (1) binding to lysine-rich fibrin (Km event) and (2) converting local plasminogen into plasmin (Kcat event)."
         supports: SUPPORT
         evidence_source: IN_VITRO
-  - key: decreases abundance of
+  - key: affects
+    object_aspect_qualifier: abundance
+    object_direction_qualifier: decreased
     source: UniProt:P00747
     target: MESH:D005341
     evidence:
diff --git a/experiments/pilot/outputs/DB00010_MESH_D004393_1.yaml b/experiments/pilot/outputs/DB00010_MESH_D004393_1.yaml
index 96169f0..fee2fe4 100644
--- a/experiments/pilot/outputs/DB00010_MESH_D004393_1.yaml
+++ b/experiments/pilot/outputs/DB00010_MESH_D004393_1.yaml
@@ -21,7 +21,9 @@ nodes:
     name: Pituitary dwarfism
     label: Disease
 links:
-  - key: increases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: increased
     source: MESH:D017337
     target: UniProt:Q02643
     evidence:
@@ -35,7 +37,8 @@ links:
         supports: SUPPORT
         evidence_source: HUMAN_CLINICAL
         explanation: "Sermorelin (GHRH(1-29)NH2) is a full GHRH-receptor agonist, equipotent to full-length GHRH in stimulating GH release."
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:Q02643
     target: GO:0030252
     evidence:
@@ -49,7 +52,8 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: "Activation of the GHRH receptor drives the adenylyl-cyclase/cAMP pathway that stimulates GH secretion."
-  - key: negatively regulates
+  - key: regulates
+    object_direction_qualifier: decreased
     source: GO:0030252
     target: MESH:D004393
     evidence:
diff --git a/experiments/pilot/outputs/DB00013_MESH_D011655_1.yaml b/experiments/pilot/outputs/DB00013_MESH_D011655_1.yaml
index b2d2aa2..a4b8d15 100644
--- a/experiments/pilot/outputs/DB00013_MESH_D011655_1.yaml
+++ b/experiments/pilot/outputs/DB00013_MESH_D011655_1.yaml
@@ -23,7 +23,9 @@ nodes:
     name: Pulmonary embolism
     label: Disease
 links:
-  - key: increases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: increased
     source: MESH:D014568
     target: UniProt:P00747
     evidence:
@@ -32,7 +34,9 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: "Urokinase (u-PA) is a plasminogen activator that activates plasminogen, converting it to active plasmin."
-  - key: decreases abundance of
+  - key: affects
+    object_aspect_qualifier: abundance
+    object_direction_qualifier: decreased
     source: UniProt:P00747
     target: MESH:D005341
     evidence:
diff --git a/experiments/pilot/outputs/DB00026_MESH_D056587_1.yaml b/experiments/pilot/outputs/DB00026_MESH_D056587_1.yaml
index 8c300d1..da9f4fd 100644
--- a/experiments/pilot/outputs/DB00026_MESH_D056587_1.yaml
+++ b/experiments/pilot/outputs/DB00026_MESH_D056587_1.yaml
@@ -21,7 +21,9 @@ nodes:
     name: Cryopyrin-associated periodic syndrome
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: DB:DB00026
     target: UniProt:P14778
     evidence:
@@ -30,7 +32,8 @@ links:
         supports: SUPPORT
         evidence_source: OTHER
         explanation: "Anakinra competitively inhibits binding of IL-1 to the type 1 IL-1 receptor, decreasing the receptor's signaling activity."
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P14778
     target: GO:0006954
     evidence:
diff --git a/experiments/pilot/outputs/DB00030_MESH_D003922_1.yaml b/experiments/pilot/outputs/DB00030_MESH_D003922_1.yaml
index 5ad7ce5..7b7b63c 100644
--- a/experiments/pilot/outputs/DB00030_MESH_D003922_1.yaml
+++ b/experiments/pilot/outputs/DB00030_MESH_D003922_1.yaml
@@ -24,7 +24,9 @@ nodes:
     name: Diabetes Mellitus, Type 1
     label: Disease
 links:
-  - key: increases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: increased
     source: MESH:D007328
     target: UniProt:P06213
     evidence:
@@ -37,7 +39,8 @@ links:
         snippet: "Insulin action involves a series of signaling cascades initiated by insulin binding to its receptor, eliciting receptor autophosphorylation and activation of the receptor tyrosine kinase, resulting in tyrosine phosphorylation of insulin receptor substrates (IRSs)."
         supports: SUPPORT
         evidence_source: OTHER
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P06213
     target: GO:0046323
     evidence:
@@ -50,7 +53,8 @@ links:
         snippet: "is involved in several of the metabolic effects of the hormone, such as glucose transport, glycolysis and glycogen synthesis."
         supports: SUPPORT
         evidence_source: OTHER
-  - key: negatively regulates
+  - key: regulates
+    object_direction_qualifier: decreased
     source: GO:0046323
     target: HP:0003074
     evidence:
diff --git a/experiments/pilot/outputs/DB00035_MESH_D006467_1.yaml b/experiments/pilot/outputs/DB00035_MESH_D006467_1.yaml
index 79a14e4..e8e05b4 100644
--- a/experiments/pilot/outputs/DB00035_MESH_D006467_1.yaml
+++ b/experiments/pilot/outputs/DB00035_MESH_D006467_1.yaml
@@ -24,7 +24,9 @@ nodes:
     name: Hereditary factor VIII deficiency disease
     label: Disease
 links:
-  - key: increases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: increased
     source: MESH:D003894
     target: UniProt:P30518
     evidence:
@@ -38,7 +40,9 @@ links:
         supports: SUPPORT
         evidence_source: OTHER
         explanation: "DDAVP acts via activation of the endothelial vasopressin V2 receptor."
-  - key: increases abundance of
+  - key: affects
+    object_aspect_qualifier: abundance
+    object_direction_qualifier: increased
     source: UniProt:P30518
     target: UniProt:P04275
     evidence:
@@ -47,7 +51,9 @@ links:
         supports: SUPPORT
         evidence_source: OTHER
         explanation: "V2 receptor activation drives exocytosis of Weibel-Palade bodies, releasing stored von Willebrand factor and raising its plasma level."
-  - key: increases abundance of
+  - key: affects
+    object_aspect_qualifier: abundance
+    object_direction_qualifier: increased
     source: UniProt:P04275
     target: UniProt:P00451
     evidence:
diff --git a/experiments/pilot/outputs/DB00038_MESH_D013921_1.yaml b/experiments/pilot/outputs/DB00038_MESH_D013921_1.yaml
index 9faf198..7e35b18 100644
--- a/experiments/pilot/outputs/DB00038_MESH_D013921_1.yaml
+++ b/experiments/pilot/outputs/DB00038_MESH_D013921_1.yaml
@@ -24,7 +24,9 @@ nodes:
     name: Thrombocytopenic disorder
     label: Disease
 links:
-  - key: increases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: increased
     source: DB:DB00038
     target: UniProt:Q14626
     evidence:
@@ -37,7 +39,8 @@ links:
         snippet: "A pre-requisite for signal transduction is the initial binding of the cytokines to their unique α-receptors, IL-6R and IL-11R."
         supports: SUPPORT
         evidence_source: IN_VITRO
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:Q14626
     target: GO:0030219
     evidence:
@@ -51,7 +54,8 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: "Activation of IL-11 receptor signalling (gp130/STAT3) in megakaryocytes directly promotes megakaryocytopoiesis/megakaryocyte differentiation."
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: GO:0030219
     target: GO:0030220
     evidence:
diff --git a/experiments/pilot/outputs/DB00152_MESH_D001361_1__r2.yaml b/experiments/pilot/outputs/DB00152_MESH_D001361_1__r2.yaml
index f6a470f..e36f955 100644
--- a/experiments/pilot/outputs/DB00152_MESH_D001361_1__r2.yaml
+++ b/experiments/pilot/outputs/DB00152_MESH_D001361_1__r2.yaml
@@ -33,7 +33,9 @@ links:
         supports: SUPPORT
         evidence_source: OTHER
         explanation: "Thiamine is phosphorylated intracellularly and converted into its active metabolite, thiamine pyrophosphate."
-  - key: increases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: increased
     source: MESH:D013835
     target: UniProt:P29401
     evidence:
diff --git a/experiments/pilot/outputs/DB00152_MESH_D001361_1__r3.yaml b/experiments/pilot/outputs/DB00152_MESH_D001361_1__r3.yaml
index 5a5fc78..c2a49e7 100644
--- a/experiments/pilot/outputs/DB00152_MESH_D001361_1__r3.yaml
+++ b/experiments/pilot/outputs/DB00152_MESH_D001361_1__r3.yaml
@@ -30,7 +30,9 @@ links:
         supports: SUPPORT
         evidence_source: OTHER
         explanation: "Thiamine is the precursor metabolized to its active coenzyme form, thiamine pyrophosphate (TPP); repletion with thiamine raises TPP, the vitamin form whose depletion defines the thiamine-deficiency state."
-  - key: increases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: increased
     source: MESH:D013835
     target: GO:0004802
     evidence:
diff --git a/experiments/pilot/outputs/DB00258_MESH_D006996_1.yaml b/experiments/pilot/outputs/DB00258_MESH_D006996_1.yaml
index 3ea19d2..8f3cdcd 100644
--- a/experiments/pilot/outputs/DB00258_MESH_D006996_1.yaml
+++ b/experiments/pilot/outputs/DB00258_MESH_D006996_1.yaml
@@ -18,7 +18,9 @@ nodes:
     name: Hypocalcemia
     label: Disease
 links:
-  - key: increases abundance of
+  - key: affects
+    object_aspect_qualifier: abundance
+    object_direction_qualifier: increased
     source: MESH:C120662
     target: MESH:D002118
     evidence:
diff --git a/experiments/pilot/outputs/DB00290_MESH_D002294_1.yaml b/experiments/pilot/outputs/DB00290_MESH_D002294_1.yaml
index 76f4568..9db0368 100644
--- a/experiments/pilot/outputs/DB00290_MESH_D002294_1.yaml
+++ b/experiments/pilot/outputs/DB00290_MESH_D002294_1.yaml
@@ -24,7 +24,9 @@ nodes:
     name: Squamous cell carcinoma
     label: Disease
 links:
-  - key: increases abundance of
+  - key: affects
+    object_aspect_qualifier: abundance
+    object_direction_qualifier: increased
     source: MESH:D001761
     target: MESH:D017382
     evidence:
diff --git a/experiments/pilot/outputs/DB00619_MESH_D015464_1.yaml b/experiments/pilot/outputs/DB00619_MESH_D015464_1.yaml
index b7d9e9c..af6e358 100644
--- a/experiments/pilot/outputs/DB00619_MESH_D015464_1.yaml
+++ b/experiments/pilot/outputs/DB00619_MESH_D015464_1.yaml
@@ -21,7 +21,9 @@ nodes:
     name: Chronic myeloid leukemia
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:D000068877
     target: UniProt:A9UF07
     evidence:
@@ -30,7 +32,8 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: "Imatinib is a BCR-ABL1 tyrosine kinase inhibitor, i.e. it decreases the activity of the BCR-ABL fusion kinase."
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:A9UF07
     target: GO:0008283
     evidence:
diff --git a/experiments/pilot/outputs/DB00619_MESH_D015464_1__r2.yaml b/experiments/pilot/outputs/DB00619_MESH_D015464_1__r2.yaml
index 2a1bcfb..e32322c 100644
--- a/experiments/pilot/outputs/DB00619_MESH_D015464_1__r2.yaml
+++ b/experiments/pilot/outputs/DB00619_MESH_D015464_1__r2.yaml
@@ -18,7 +18,9 @@ nodes:
     name: Chronic myeloid leukemia, BCR-ABL positive
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:D000068877
     target: UniProt:A9UF07
     evidence:
diff --git a/experiments/pilot/outputs/DB00619_MESH_D015464_1__r3.yaml b/experiments/pilot/outputs/DB00619_MESH_D015464_1__r3.yaml
index ef15c6a..b2e560b 100644
--- a/experiments/pilot/outputs/DB00619_MESH_D015464_1__r3.yaml
+++ b/experiments/pilot/outputs/DB00619_MESH_D015464_1__r3.yaml
@@ -18,7 +18,9 @@ nodes:
     name: Leukemia, Myelogenous, Chronic, BCR-ABL Positive
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:D000068877
     target: UniProt:A9UF07
     evidence:
diff --git a/experiments/pilot/outputs/DB00843_MESH_D000544_1.yaml b/experiments/pilot/outputs/DB00843_MESH_D000544_1.yaml
index 9918ce3..7cc7e8a 100644
--- a/experiments/pilot/outputs/DB00843_MESH_D000544_1.yaml
+++ b/experiments/pilot/outputs/DB00843_MESH_D000544_1.yaml
@@ -21,7 +21,9 @@ nodes:
     name: Alzheimer's disease
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:C076946
     target: UniProt:P22303
     evidence:
@@ -34,7 +36,9 @@ links:
         snippet: "The most commonly used drug, donepezil, is a cholinesterase inhibitor."
         supports: SUPPORT
         evidence_source: IN_VITRO
-  - key: decreases abundance of
+  - key: affects
+    object_aspect_qualifier: abundance
+    object_direction_qualifier: decreased
     source: UniProt:P22303
     target: CHEBI:15355
     evidence:
diff --git a/experiments/pilot/outputs/DB00993_MESH_D001172_1.yaml b/experiments/pilot/outputs/DB00993_MESH_D001172_1.yaml
index f089a46..20fe7ea 100644
--- a/experiments/pilot/outputs/DB00993_MESH_D001172_1.yaml
+++ b/experiments/pilot/outputs/DB00993_MESH_D001172_1.yaml
@@ -37,7 +37,8 @@ links:
         snippet: "The thioguanine derivative, azathioprine, is a prodrug of 6-mercaptopurine that is further metabolized by various enzymes present in the liver and gut."
         supports: SUPPORT
         evidence_source: OTHER
-  - key: negatively regulates
+  - key: regulates
+    object_direction_qualifier: decreased
     source: MESH:D008774
     target: GO:0006164
     evidence:
@@ -55,7 +56,8 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: "6-Mercaptopurine is a purine synthesis inhibitor."
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: GO:0006164
     target: GO:0042098
     evidence:
diff --git a/experiments/pilot/outputs/DB01076_MESH_D006937_1.yaml b/experiments/pilot/outputs/DB01076_MESH_D006937_1.yaml
index 365a45e..627e557 100644
--- a/experiments/pilot/outputs/DB01076_MESH_D006937_1.yaml
+++ b/experiments/pilot/outputs/DB01076_MESH_D006937_1.yaml
@@ -27,7 +27,9 @@ nodes:
     name: Hypercholesterolemia
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:D000069059
     target: UniProt:P04035
     evidence:
@@ -36,7 +38,9 @@ links:
         supports: SUPPORT
         evidence_source: OTHER
         explanation: "Atorvastatin's mechanism of action is inhibition of HMG-CoA reductase."
-  - key: increases abundance of
+  - key: affects
+    object_aspect_qualifier: abundance
+    object_direction_qualifier: increased
     source: UniProt:P04035
     target: MESH:D002784
     evidence:
@@ -45,7 +49,8 @@ links:
         supports: SUPPORT
         evidence_source: OTHER
         explanation: "HMG-CoA reductase is the rate-limiting enzyme of cholesterol biosynthesis, so its activity increases cellular cholesterol."
-  - key: negatively regulates
+  - key: regulates
+    object_direction_qualifier: decreased
     source: MESH:D002784
     target: UniProt:P01130
     evidence:
@@ -54,7 +59,9 @@ links:
         supports: SUPPORT
         evidence_source: OTHER
         explanation: "Cellular cholesterol negatively feedback-regulates LDL receptor levels via SREBP-2; statin-lowered cholesterol therefore raises LDL receptor expression."
-  - key: decreases abundance of
+  - key: affects
+    object_aspect_qualifier: abundance
+    object_direction_qualifier: decreased
     source: UniProt:P01130
     target: MESH:D008078
     evidence:
diff --git a/experiments/pilot/outputs/DB01527_MESH_D000856_1.yaml b/experiments/pilot/outputs/DB01527_MESH_D000856_1.yaml
index c428013..5f39892 100644
--- a/experiments/pilot/outputs/DB01527_MESH_D000856_1.yaml
+++ b/experiments/pilot/outputs/DB01527_MESH_D000856_1.yaml
@@ -17,7 +17,8 @@ nodes:
     name: Anorexia
     label: Disease
 links:
-  - key: negatively regulates
+  - key: regulates
+    object_direction_qualifier: decreased
     source: DB:DB01527
     target: GO:0007631
     evidence:
diff --git a/experiments/pilot/outputs/DB09038_MESH_D003924_1.yaml b/experiments/pilot/outputs/DB09038_MESH_D003924_1.yaml
index dbb9355..bc0a570 100644
--- a/experiments/pilot/outputs/DB09038_MESH_D003924_1.yaml
+++ b/experiments/pilot/outputs/DB09038_MESH_D003924_1.yaml
@@ -27,7 +27,9 @@ nodes:
     name: Diabetes Mellitus, Type 2
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: DB:DB09038
     target: UniProt:P31639
     evidence:
@@ -35,7 +37,8 @@ links:
         snippet: "Empagliflozin is an orally available, potent and highly selective inhibitor of the sodium glucose cotransporter 2 (SGLT2)."
         supports: SUPPORT
         evidence_source: HUMAN_CLINICAL
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P31639
     target: GO:0035623
     evidence:
diff --git a/scripts/build_site_data.py b/scripts/build_site_data.py
new file mode 100644
index 0000000..99a4866
--- /dev/null
+++ b/scripts/build_site_data.py
@@ -0,0 +1,291 @@
+"""
+Build the static-site JSON (index + per-record) that web-revamp-mockup/ consumes
+in "live" mode, from the **agentically curated** path records.
+
+WHY THIS EXISTS
+The site's data layer (web-revamp-mockup/dmdb-data.js) has one documented swap
+point: flip SOURCE to "live" and the pages fetch the JSON files named in its
+ENDPOINTS map. This script emits exactly those shapes.
+
+WHAT IT READS
+Not kb/paths/ — those 4,846 records are the legacy corpus and carry no per-edge
+evidence. The AI-curated records produced by the harness live in the run output
+directories listed in RUNS below. The same (drug, disease) pair is often curated
+by several runs (model comparison, pilot repeats), so a record's site id is
+namespaced by run: "<run>__<file stem>". graph._id is kept as `record_id`.
+
+WHAT IT ADDS (join, not invention)
+  * `paper`       — title/authors/journal/year/doi for each cited PMID, read from
+                    reference's PMID_*.md frontmatter in any references_cache/.
+  * `source_type` — derived from the reference CURIE prefix (PMID -> pubmed, ...).
+  * `source_tier` — from the cache entry's content_type (abstract vs full text).
+  * `graph.summary` — the node chain along the record's longest path, joined with
+                    arrows. Generated for display; flagged as such in `site`.
+  * `area`        — a COARSE display-only bucket keyword-matched from the disease
+                    name. Not an ontology assertion; it exists to drive the
+                    browse facet and nothing else.
+
+Usage:
+    python scripts/build_site_data.py                # write web-revamp-mockup/data/
+    python scripts/build_site_data.py --out DIR      # write elsewhere
+"""
+
+from __future__ import annotations
+
+import argparse
+import json
+import re
+from pathlib import Path
+
+import yaml
+
+HERE = Path(__file__).resolve().parent
+REPO = HERE.parent
+# Every reference cache in the repo: the shared one plus the per-run caches the
+# model-eval runs wrote alongside their outputs.
+CACHE_DIRS = [
+    REPO / "references_cache",
+    REPO / "experiments" / "opus_vs_sonnet" / "opus" / "references_cache",
+    REPO / "experiments" / "opus_vs_sonnet" / "sonnet" / "references_cache",
+]
+DEFAULT_OUT = REPO / "web-revamp-mockup" / "data"
+
+# The agentic curation runs, in display order: (run key, label, glob).
+RUNS = [
+    ("pilot", "Pilot run", "experiments/pilot/outputs/*.yaml"),
+    ("opus", "Opus (model eval)", "experiments/opus_vs_sonnet/opus/outputs/*.yaml"),
+    ("sonnet", "Sonnet (model eval)", "experiments/opus_vs_sonnet/sonnet/outputs/*.yaml"),
+    ("phase3", "Phase-3 eval", "tests/phase3_eval_outputs/*.yaml"),
+]
+
+# Coarse display buckets for the browse facet. First match wins, so the more
+# specific patterns are listed first.
+AREA_RULES = [
+    ("Neoplasms", r"leukemia|leukaemia|lymphoma|neoplasm|carcinoma|tumor|tumour|myeloma|myelogenous|cancer"),
+    ("Immune", r"psoriasis|arthritis|arthropath|lupus|crohn|sclerosis|dermatomyositis|asthma|cryopyrin|periodic syndrome|colitis"),
+    ("Infectious disease", r"tuberculosis|influenza|herpes|hepatitis|conjunctivitis|staphylococc|infection|malaria|hiv"),
+    ("Cardiovascular", r"heart failure|hypertension|myocardial|stroke|thromb|embolism|angina|arrhythmia"),
+    ("Blood", r"hemophilia|haemophilia|factor viii|thrombocytopen|anemia|anaemia"),
+    ("Metabolic", r"cholesterol|diabetes|gout|avitaminosis|deficiency|hypocalcemia|obesity|anorexia|lipid"),
+    ("Endocrine", r"thyroid|dwarfism|acromegal|adrenal"),
+    ("Nervous system", r"alzheimer|parkinson|epilep|migraine|neuropath|pain"),
+    ("Mental health", r"depress|anxiety|bipolar|schizophren|psychos"),
+    ("Respiratory", r"pulmonary fibrosis|copd|bronch"),
+    ("Musculoskeletal", r"osteoarthritis|osteoporosis|myopath"),
+    ("Kidney", r"nephritis|nephropath|renal"),
+]
+
+TIER = {"abstract": "ABSTRACT", "full_text": "FULL_TEXT", "fulltext": "FULL_TEXT"}
+
+
+def area_for(disease: str) -> str:
+    d = (disease or "").lower()
+    for area, pattern in AREA_RULES:
+        if re.search(pattern, d):
+            return area
+    return "Other"
+
+
+def source_type_for(reference: str) -> str:
+    ref = (reference or "").upper()
+    if ref.startswith("PMID"):
+        return "pubmed"
+    if ref.startswith("PMC"):
+        return "pmc"
+    if ref.startswith("DB") or ref.startswith("DRUGBANK"):
+        return "drugbank"
+    if ref.startswith("DOI") or ref.startswith("10."):
+        return "doi"
+    return "other"
+
+
+def load_cache() -> dict[str, dict]:
+    """Map reference id -> paper credential block, from references_cache frontmatter."""
+    papers: dict[str, dict] = {}
+    for md in sorted(m for d in CACHE_DIRS if d.is_dir() for m in d.glob("*.md")):
+        text = md.read_text(encoding="utf-8", errors="replace")
+        if not text.startswith("---"):
+            continue
+        end = text.find("\n---", 3)
+        if end == -1:
+            continue
+        try:
+            fm = yaml.safe_load(text[3:end]) or {}
+        except yaml.YAMLError:
+            continue
+        ref = fm.get("reference_id")
+        if not ref:
+            continue
+        papers[str(ref)] = {
+            "title": fm.get("title"),
+            "authors": fm.get("authors") or [],
+            "journal": fm.get("journal"),
+            "year": str(fm.get("year")) if fm.get("year") is not None else None,
+            "doi": fm.get("doi"),
+            "pmcid": fm.get("pmcid"),
+            "license": fm.get("license"),
+            "_tier": TIER.get(str(fm.get("content_type") or "").lower()),
+        }
+    return papers
+
+
+def longest_chain(nodes: list[dict], links: list[dict]) -> list[str]:
+    """Node ids along a longest source->target chain (the record's 'spine')."""
+    incoming: dict[str, list[str]] = {n["id"]: [] for n in nodes}
+    for l in links:
+        if l.get("target") in incoming:
+            incoming[l["target"]].append(l.get("source"))
+
+    best: dict[str, list[str]] = {}
+    visiting: set[str] = set()
+
+    def chain(nid: str) -> list[str]:
+        if nid in best:
+            return best[nid]
+        if nid in visiting:                     # cycle guard
+            return [nid]
+        visiting.add(nid)
+        parents = [p for p in incoming.get(nid, []) if p in incoming]
+        longest: list[str] = []
+        for p in parents:
+            c = chain(p)
+            if len(c) > len(longest):
+                longest = c
+        visiting.discard(nid)
+        best[nid] = longest + [nid]
+        return best[nid]
+
+    return max((chain(n["id"]) for n in nodes), key=len, default=[])
+
+
+def build_record(path: Path, run: str, run_label: str, papers: dict[str, dict]) -> dict:
+    raw = yaml.safe_load(path.read_text(encoding="utf-8")) or {}
+    graph = dict(raw.get("graph") or {})
+    nodes = raw.get("nodes") or []
+    links = [dict(l) for l in (raw.get("links") or [])]
+    by_id = {n["id"]: n for n in nodes}
+
+    # enrich each EvidenceItem with its joined paper credential + derived fields
+    for link in links:
+        items = link.get("evidence")
+        if not isinstance(items, list):
+            continue
+        enriched = []
+        for item in items:
+            it = dict(item)
+            ref = it.get("reference")
+            it["source_type"] = source_type_for(ref)
+            paper = papers.get(str(ref))
+            if paper:
+                p = {k: v for k, v in paper.items() if k != "_tier"}
+                it["paper"] = p
+                it.setdefault("source_tier", paper.get("_tier") or "ABSTRACT")
+            else:
+                it["paper"] = None
+            enriched.append(it)
+        link["evidence"] = enriched
+
+    chain = longest_chain(nodes, links)
+    graph["summary"] = " → ".join(by_id[n]["name"] for n in chain if n in by_id)
+
+    # references ship as bare URL strings in the record files; the site wants
+    # {url, type, label} rows.
+    refs = []
+    for r in raw.get("references") or []:
+        if isinstance(r, dict):
+            refs.append(r)
+            continue
+        url = str(r)
+        host = re.sub(r"^https?://(www\.)?", "", url).split("/")[0]
+        kind = "drugbank" if "drugbank" in host else "wiki" if "wikipedia" in host else "other"
+        refs.append({"url": url, "type": kind, "label": f"{host} — record source"})
+
+    site_id = f"{run}__{path.stem}"
+    return {
+        "directed": raw.get("directed", True),
+        "multigraph": raw.get("multigraph", True),
+        "graph": graph,
+        "nodes": nodes,
+        "links": links,
+        "references": refs,
+        "site": {
+            "id": site_id,
+            "record_id": graph.get("_id"),
+            "run": run,
+            "run_label": run_label,
+            "source_file": str(path.relative_to(REPO)),
+            "summary_generated": True,
+        },
+    }
+
+
+def index_row(rec: dict) -> dict:
+    nodes, links = rec["nodes"], rec["links"]
+    types, seen = [], set()
+    for nid in longest_chain(nodes, links):
+        label = next((n["label"] for n in nodes if n["id"] == nid), None)
+        if label and label not in seen:
+            seen.add(label)
+            types.append(label)
+    for n in nodes:                             # types off the spine still matter to the facet
+        if n.get("label") and n["label"] not in seen:
+            seen.add(n["label"])
+            types.append(n["label"])
+
+    target = next((n["name"] for n in nodes if n.get("label") == "Protein"), None)
+    if not target:
+        target = next((n["name"] for n in nodes[1:]), "")
+
+    sourced = sum(1 for l in links if l.get("evidence"))
+    flagged = sum(
+        1 for l in links
+        if any((it.get("supports") or "SUPPORT") != "SUPPORT" for it in (l.get("evidence") or []))
+    )
+    return {
+        "id": rec["site"]["id"],
+        "record_id": rec["site"]["record_id"],
+        "run": rec["site"]["run_label"],
+        "drug": rec["graph"].get("drug") or "",
+        "disease": rec["graph"].get("disease") or "",
+        "area": area_for(rec["graph"].get("disease")),
+        "target": target or "",
+        "types": types,
+        "steps": max(len(longest_chain(nodes, links)) - 1, 0),
+        "edges": len(links),
+        "sourced": sourced,
+        "flagged": flagged,
+    }
+
+
+def main() -> int:
+    ap = argparse.ArgumentParser(
+        description=__doc__, formatter_class=argparse.RawDescriptionHelpFormatter)
+    ap.add_argument("--out", default=str(DEFAULT_OUT), help="output data directory")
+    args = ap.parse_args()
+
+    out = Path(args.out)
+    records_dir = out / "records"
+    records_dir.mkdir(parents=True, exist_ok=True)
+
+    papers = load_cache()
+    rows, written = [], 0
+    for run, run_label, pattern in RUNS:
+        for path in sorted(REPO.glob(pattern)):
+            rec = build_record(path, run, run_label, papers)
+            (records_dir / f"{rec['site']['id']}.json").write_text(
+                json.dumps(rec, indent=2, ensure_ascii=False) + "\n", encoding="utf-8")
+            rows.append(index_row(rec))
+            written += 1
+
+    rows.sort(key=lambda r: (r["drug"].lower(), r["disease"].lower(), r["id"]))
+    (out / "index.json").write_text(
+        json.dumps(rows, indent=2, ensure_ascii=False) + "\n", encoding="utf-8")
+
+    runs = {r["run"] for r in rows}
+    print(f"Wrote {written} records + index.json to {out} "
+          f"({len(runs)} runs, {len({r['record_id'] for r in rows})} distinct path ids).")
+    return 0
+
+
+if __name__ == "__main__":
+    raise SystemExit(main())
diff --git a/scripts/check_biolink_drift.py b/scripts/check_biolink_drift.py
index 22c7bd3..eebdce4 100644
--- a/scripts/check_biolink_drift.py
+++ b/scripts/check_biolink_drift.py
@@ -249,8 +249,11 @@ def render_report(drift: dict, meta: dict, *, show_added: bool) -> str:
         A("")
         A("These edges' keys are no longer valid in the current Biolink model (most were")
         A("folded into `regulates`/`affects` + qualifiers in the v2->v4 refactor). Removing")
-        A("them from the enum would break existing records, so this needs a human decision")
-        A("(the locked policy is to translate at the publish/export layer, not migrate data).")
+        A("them from the enum would break the legacy corpus, so this needs a human decision.")
+        A("Per docs/biolink_version_decision.md the enum deliberately spans both eras: QC")
+        A("Layer 3 allows these for `legacy` records and rejects them for `ai_curated` ones,")
+        A("and src/drugmechdb/schema/biolink_predicate_status.yaml records the replacement")
+        A("each one maps to.")
         A("")
         for r in drift["removed"]:
             A(f"  - {r['predicate']:<28} {r['meaning'] or '(no biolink mapping)'}")
diff --git a/scripts/migrate_predicates.py b/scripts/migrate_predicates.py
new file mode 100644
index 0000000..4f3dbea
--- /dev/null
+++ b/scripts/migrate_predicates.py
@@ -0,0 +1,159 @@
+"""
+Migrate a record's edge predicates from the legacy (v1.3.0-era) Biolink vocabulary
+to the pinned current release, using the qualifier model.
+
+WHAT IT DOES
+Biolink's v2->v4 refactor removed the `positively/negatively regulates` and
+`increases/decreases <aspect> of` predicate families, folding them into
+`regulates` / `affects` carried with `object_aspect_qualifier` +
+`object_direction_qualifier`. This script applies that mapping to a record:
+
+    - key: decreases activity of        - key: affects
+      source: MESH:D000068877     ->      object_aspect_qualifier: activity
+      target: UniProt:A9UF07              object_direction_qualifier: decreased
+                                          source: MESH:D000068877
+                                          target: UniProt:A9UF07
+
+The mapping is NOT defined here — it lives in
+`src/drugmechdb/schema/biolink_predicate_status.yaml`, the single source of truth
+shared with QC Layer 3 (scripts/validate_predicates.py). Predicates marked
+`needs_human_decision` are never rewritten; they are reported and left alone.
+
+WHY A LINE-BASED REWRITE
+Round-tripping these files through a YAML dumper would reformat every line and bury
+the change in noise. Every edge key in the corpus is written as `- key: <value>` on
+its own line, so the transform is applied textually: the record's formatting,
+comments, and quoting style survive untouched.
+
+Usage:
+    python scripts/migrate_predicates.py --check  DIR_OR_FILE...   # report only, exit 1 if stale
+    python scripts/migrate_predicates.py --write  DIR_OR_FILE...   # rewrite in place
+    python scripts/migrate_predicates.py --write --diff DIR...     # rewrite + print each change
+"""
+
+from __future__ import annotations
+
+import argparse
+import re
+import sys
+from pathlib import Path
+
+import yaml
+
+REPO = Path(__file__).resolve().parent.parent
+STATUS = REPO / "src" / "drugmechdb" / "schema" / "biolink_predicate_status.yaml"
+
+KEY_LINE = re.compile(r"^(?P<indent>\s*)- key:\s*(?P<key>.+?)\s*$")
+
+# Qualifier keys are emitted in this order, directly under the rewritten key.
+QUALIFIER_ORDER = ("object_aspect_qualifier", "object_direction_qualifier", "qualified_predicate")
+
+
+def load_status() -> dict:
+    doc = yaml.safe_load(STATUS.read_text(encoding="utf-8"))
+    return doc["predicates"]
+
+
+def rel(path: Path) -> str:
+    """Repo-relative when possible; the given path otherwise."""
+    try:
+        return str(path.resolve().relative_to(REPO))
+    except ValueError:
+        return str(path)
+
+
+def iter_files(targets: list[str]) -> list[Path]:
+    files: list[Path] = []
+    for t in targets:
+        p = Path(t)
+        if p.is_dir():
+            files.extend(sorted(q for q in p.glob("*.yaml") if q.name != "_index.yaml"))
+        elif p.is_file():
+            files.append(p)
+        else:
+            print(f"warning: {t} is not a file or directory", file=sys.stderr)
+    return files
+
+
+def migrate_text(text: str, status: dict) -> tuple[str, list[tuple[str, str]], list[str]]:
+    """Return (new_text, [(old_key, new_key)...], [blocked_predicates...])."""
+    out: list[str] = []
+    changed: list[tuple[str, str]] = []
+    blocked: list[str] = []
+
+    for line in text.splitlines(keepends=True):
+        m = KEY_LINE.match(line.rstrip("\n"))
+        if not m:
+            out.append(line)
+            continue
+        key = m.group("key").strip().strip("'\"")
+        entry = status.get(key)
+        if not entry or entry.get("status") == "current":
+            out.append(line)
+            continue
+        replacement = entry.get("replacement")
+        if not replacement:
+            blocked.append(key)                     # needs_human_decision — leave untouched
+            out.append(line)
+            continue
+
+        newline = "\n" if line.endswith("\n") else ""
+        indent = m.group("indent")
+        child = indent + "  "                       # align with `source:`/`target:`
+        out.append(f"{indent}- key: {replacement['key']}{newline}")
+        for q in QUALIFIER_ORDER:
+            if q in replacement:
+                out.append(f"{child}{q}: {replacement[q]}{newline}")
+        changed.append((key, replacement["key"]))
+
+    return "".join(out), changed, blocked
+
+
+def main() -> int:
+    ap = argparse.ArgumentParser(
+        description=__doc__, formatter_class=argparse.RawDescriptionHelpFormatter)
+    ap.add_argument("targets", nargs="+", help="Record files or directories to migrate.")
+    mode = ap.add_mutually_exclusive_group(required=True)
+    mode.add_argument("--check", action="store_true",
+                      help="Report what would change; exit 1 if anything is stale.")
+    mode.add_argument("--write", action="store_true", help="Rewrite the files in place.")
+    ap.add_argument("--diff", action="store_true", help="Print each predicate rewrite.")
+    args = ap.parse_args()
+
+    status = load_status()
+    files = iter_files(args.targets)
+    if not files:
+        print("no files matched", file=sys.stderr)
+        return 2
+
+    n_files = n_edges = 0
+    all_blocked: dict[str, int] = {}
+    for path in files:
+        text = path.read_text(encoding="utf-8")
+        new_text, changed, blocked = migrate_text(text, status)
+        for b in blocked:
+            all_blocked[b] = all_blocked.get(b, 0) + 1
+        if not changed:
+            continue
+        n_files += 1
+        n_edges += len(changed)
+        if args.diff or args.check:
+            print(rel(path))
+            for old, new in changed:
+                print(f"    {old}  ->  {new}")
+        if args.write:
+            path.write_text(new_text, encoding="utf-8")
+
+    verb = "would migrate" if args.check else "migrated"
+    print(f"\n{verb} {n_edges} edges across {n_files}/{len(files)} files.")
+    if all_blocked:
+        print("\nLEFT FOR A HUMAN (no mechanical replacement — see the `note` in "
+              f"{rel(STATUS)}):")
+        for k, n in sorted(all_blocked.items(), key=lambda kv: -kv[1]):
+            print(f"    {n:4d}  {k}")
+
+    return 1 if (args.check and n_edges) else 0
+
+
+if __name__ == "__main__":
+    raise SystemExit(main())
diff --git a/scripts/qc.py b/scripts/qc.py
index 6d33030..3c66a24 100644
--- a/scripts/qc.py
+++ b/scripts/qc.py
@@ -88,7 +88,8 @@ def iter_files(targets: Iterable[str]) -> list[Path]:
     return files
 
 
-def run_layer(layer: int, files: list[Path], json_out: bool, offline: bool = False) -> tuple[int, str]:
+def run_layer(layer: int, files: list[Path], json_out: bool, offline: bool = False,
+              profile: str = "auto") -> tuple[int, str]:
     """Invoke a layer script against a set of files. Returns (exit_code, stdout_or_json)."""
     cmd = [python_bin(), str(LAYER_SCRIPTS[layer])]
     if json_out:
@@ -97,6 +98,11 @@ def run_layer(layer: int, files: list[Path], json_out: bool, offline: bool = Fal
     # to the committed references_cache/ for deterministic CI / reproducible runs.
     if offline and layer == 4:
         cmd.append("--offline")
+    # Layer 3 applies a different predicate era per profile (legacy accepts the old
+    # vocabulary, ai_curated does not), so a forced --profile has to reach it too —
+    # otherwise it would re-detect and override the caller's choice.
+    if layer == 3 and profile != "auto":
+        cmd.extend(["--profile", profile])
     cmd.extend(str(f) for f in files)
     proc = subprocess.run(cmd, capture_output=True, text=True)
     return proc.returncode, proc.stdout + proc.stderr
@@ -182,7 +188,8 @@ def main() -> int:
             continue
         if not args.json:
             print(f"--- Layer {layer} ({LAYER_SCRIPTS[layer].name}) — {len(layer_files)} file(s) ---")
-        code, out = run_layer(layer, layer_files, json_out=args.json, offline=args.offline)
+        code, out = run_layer(layer, layer_files, json_out=args.json, offline=args.offline,
+                              profile=args.profile)
         results.append({"layer": layer, "files": len(layer_files), "exit_code": code, "output": out})
         if code != 0:
             overall_fail = True
diff --git a/scripts/quality/predicate_polarity.yaml b/scripts/quality/predicate_polarity.yaml
index 879dfe7..578a2b4 100644
--- a/scripts/quality/predicate_polarity.yaml
+++ b/scripts/quality/predicate_polarity.yaml
@@ -60,6 +60,14 @@ predicates:
   affects risk for:            {sign:  0, role: clinical_outcome, confidence: review, note: "direction unspecified"}
   predisposes:                 {sign: +1, role: clinical_outcome, confidence: review}
 
+  # Biolink 4.4.4 condition-scoped forms — same semantics, same signs as the removed
+  # bare verbs they replace (`prevents` -> `preventative for condition`, etc.).
+  preventative for condition:  {sign: -1, role: clinical_outcome, confidence: high}
+  ameliorates condition:       {sign: -1, role: clinical_outcome, confidence: high}
+  exacerbates condition:       {sign: +1, role: clinical_outcome, confidence: high}
+  predisposes to condition:    {sign: +1, role: clinical_outcome, confidence: review}
+  contraindicated in:          {sign:  0, role: clinical_outcome, confidence: review, note: "not a mechanistic step; flag if present"}
+
   # ── Neutral scaffolding (skipped in polarity; presence is fine) ─────────────
   participates in:             {sign: 0, role: contextual, confidence: high}
   occurs in:                   {sign: 0, role: contextual, confidence: high}
@@ -95,6 +103,15 @@ predicates:
   phenotype of:                {sign: +1, role: reverse, confidence: review}
   regulates:                   {sign: 0, role: regulatory, confidence: review, note: "direction unspecified; flag for tightening"}
 
+  # ── Biolink 4.4.4 canonical predicates (qualifier model) ────────────────────
+  # These carry NO polarity in the predicate name — it lives in the edge's
+  # `object_direction_qualifier`. structural_quality.py resolves the sign from
+  # that qualifier (see DIRECTION_SIGN there); the sign: 0 below is the fallback
+  # for an edge that omits it, which QC Layer 3 rejects for ai_curated records.
+  affects:                     {sign: 0, role: regulatory, confidence: review, note: "polarity is in object_direction_qualifier"}
+  directly physically interacts with: {sign: 0, role: contextual, confidence: high, note: "binding; no direction"}
+  binds:                       {sign: 0, role: contextual, confidence: high, note: "binding; no direction"}
+
   # ── Biochemical derivation / lineage ────────────────────────────────────────
   has metabolite:              {sign: +1, role: derivation, confidence: review}
   is metabolite of:            {sign: +1, role: reverse, confidence: review}
@@ -139,6 +156,11 @@ type_constraints:
   ameliorates:          {subj_in: CHEM,  obj_in: DISEASE_LIKE}
   exacerbates:          {subj_in: CHEM,  obj_in: DISEASE_LIKE}
   contraindicated for:  {subj_in: CHEM,  obj_in: DISEASE_LIKE}
+  preventative for condition: {subj_in: CHEM, obj_in: DISEASE_LIKE}
+  ameliorates condition:      {subj_in: CHEM, obj_in: DISEASE_LIKE}
+  exacerbates condition:      {subj_in: CHEM, obj_in: DISEASE_LIKE}
+  predisposes to condition:   {subj_in: CHEM, obj_in: DISEASE_LIKE}
+  contraindicated in:         {subj_in: CHEM, obj_in: DISEASE_LIKE}
   in taxon:             {obj_in: [OrganismTaxon]}
   decreases activity of: {obj_in: ACTIVITY_BEARING}
   increases activity of: {obj_in: ACTIVITY_BEARING}
@@ -153,3 +175,16 @@ type_constraints:
   occurs in:            {obj_in: LOCATION}
   located in:           {obj_in: LOCATION}
   expressed in:         {obj_in: LOCATION}
+
+  # ── Qualified forms (Biolink 4.4.4) ─────────────────────────────────────────
+  # After the qualifier refactor the aspect, not the predicate name, says what kind
+  # of thing the object must be. structural_quality.py looks up `<key>|<aspect>`
+  # first and falls back to the bare key, so these mirror the legacy rows above.
+  affects|activity:     {obj_in: ACTIVITY_BEARING}
+  affects|abundance:    {obj_in: MOLECULAR}
+  affects|degradation:  {obj_in: MOLECULAR}
+  affects|synthesis:    {obj_in: MOLECULAR}
+  affects|stability:    {obj_in: MOLECULAR}
+  affects|transport:    {obj_in: MOLECULAR}
+  affects|uptake:       {obj_in: MOLECULAR}
+  affects|expression:   {obj_in: GENE_PRODUCT}
diff --git a/scripts/quality/structural_quality.py b/scripts/quality/structural_quality.py
index 162c881..a841a43 100644
--- a/scripts/quality/structural_quality.py
+++ b/scripts/quality/structural_quality.py
@@ -100,6 +100,37 @@ def resolve(spec):
     return {"predicates": preds, "constraints": constraints}
 
 
+# Biolink 4.4.4 moved polarity out of the predicate name and into the edge's
+# `object_direction_qualifier`. `regulates`/`affects` are therefore sign-0 in the
+# lexicon, and the real sign is read from the qualifier here.
+DIRECTION_SIGN = {"increased": +1, "upregulated": +1, "decreased": -1, "downregulated": -1}
+
+
+def qualified_key(edge: dict, preds: dict) -> str:
+    """The lexicon key for this edge, folding in its direction qualifier.
+
+    An edge with a qualifier gets a synthetic `<predicate>|<direction>` entry
+    registered in this record's copy of the lexicon, so every downstream lookup
+    (polarity, duplicate detection) sees the qualified sign without any of them
+    needing to know about qualifiers.
+    """
+    key = edge.get("key")
+    direction = edge.get("object_direction_qualifier")
+    if not direction:
+        return key
+    qkey = f"{key}|{direction}"
+    if qkey not in preds:
+        sign = DIRECTION_SIGN.get(direction, 0)
+        base = preds.get(key) or {}
+        preds[qkey] = {
+            "sign": sign,
+            "role": base.get("role") or "regulatory",
+            "confidence": "high" if sign else "review",
+            "note": f"sign from object_direction_qualifier={direction!r}",
+        }
+    return qkey
+
+
 def orientation(entry: dict) -> str:
     """forward | reverse | neutral | opaque — derived from role + sign."""
     role, sign = entry.get("role"), entry.get("sign", 0)
@@ -177,7 +208,8 @@ def path_polarity(path_edges, preds):
 
 
 def analyze(path: Path, lex: dict) -> dict:
-    preds, constraints = lex["predicates"], lex["constraints"]
+    # local copy: qualified `<predicate>|<direction>` entries are synthesized per record
+    preds, constraints = dict(lex["predicates"]), lex["constraints"]
     doc = yaml.safe_load(path.read_text())
     graph = doc.get("graph", {}) or {}
     nodes = doc.get("nodes", []) or []
@@ -188,7 +220,8 @@ def analyze(path: Path, lex: dict) -> dict:
     indeg, outdeg = Counter(), Counter()
     edge_counts = Counter()
     for e in links:
-        s, t, k = e.get("source"), e.get("target"), e.get("key")
+        s, t = e.get("source"), e.get("target")
+        k = qualified_key(e, preds)
         adj[s].append((t, k)); outdeg[s] += 1; indeg[t] += 1
         edge_counts[(s, t, k)] += 1
 
@@ -218,7 +251,13 @@ def flag(sev, code, msg): flags.append({"severity": sev, "code": code, "msg": ms
 
     # predicate domain/range
     for e in links:
-        k = e.get("key"); c = constraints.get(k)
+        # Qualified edges constrain the object by ASPECT (`affects|activity`), so try
+        # that first and fall back to the bare predicate for unqualified/legacy edges.
+        k = e.get("key")
+        aspect = e.get("object_aspect_qualifier")
+        c = constraints.get(f"{k}|{aspect}") if aspect else None
+        if c is None:
+            c = constraints.get(k)
         if not c:
             continue
         ls, lo = label.get(e.get("source")), label.get(e.get("target"))
diff --git a/scripts/validate_predicates.py b/scripts/validate_predicates.py
index a3d6b93..4b309ff 100644
--- a/scripts/validate_predicates.py
+++ b/scripts/validate_predicates.py
@@ -5,6 +5,20 @@
 *exact* member of the BiolinkPredicate enum declared in
 src/drugmechdb/schema/biolink_predicates.yaml.
 
+The enum is deliberately era-spanning: it still accepts the v1.3.0-era vocabulary the
+4,846 legacy records are written in. Which era a given record MAY use is the second
+check, and it is profile-dependent (mirroring qc.py's own legacy/ai_curated split):
+
+  legacy      any enum member, current or not — these records are frozen history.
+  ai_curated  `status: current` members only. A record curated today must be written in
+              the pinned Biolink release, so the removed `positively regulates` /
+              `increases <aspect> of` families are rejected with the qualifier form that
+              replaces them (see src/drugmechdb/schema/biolink_predicate_status.yaml).
+
+For ai_curated records the qualifiers themselves are checked too: values must be in the
+schema's ObjectAspectEnum / ObjectDirectionEnum, and the canonical predicates that carry
+polarity (`affects`, `regulates`) must actually carry it.
+
 This script does NOT normalize surface forms. Whitespace, case, and CURIE
 drift produce failures. Run `scripts/canonicalize_predicates.py --write`
 first if needed; that is the data-rewrite path. Layer 3 is the final gate.
@@ -30,6 +44,13 @@
 REPO = Path(__file__).resolve().parent.parent
 PATHS_DIR = REPO / "kb" / "paths"
 SCHEMA = REPO / "src" / "drugmechdb" / "schema" / "biolink_predicates.yaml"
+STATUS = REPO / "src" / "drugmechdb" / "schema" / "biolink_predicate_status.yaml"
+MODEL = REPO / "src" / "drugmechdb" / "schema" / "drugmechdb.yaml"
+
+# Canonical predicates whose meaning lives in the qualifiers: bare, they assert almost
+# nothing, so an ai_curated edge using one must say which way it goes.
+NEEDS_DIRECTION = {"affects", "regulates"}
+NEEDS_ASPECT = {"affects"}
 
 
 def load_enum() -> set[str]:
@@ -38,6 +59,39 @@ def load_enum() -> set[str]:
     return set(doc["enums"]["BiolinkPredicate"]["permissible_values"].keys())
 
 
+def load_status() -> dict:
+    """predicate -> {status, replacement, ...} for the pinned Biolink release."""
+    with STATUS.open() as fh:
+        return yaml.safe_load(fh)["predicates"]
+
+
+def load_qualifier_values() -> tuple[set[str], set[str]]:
+    with MODEL.open() as fh:
+        enums = yaml.safe_load(fh)["enums"]
+    return (set(enums["ObjectAspectEnum"]["permissible_values"]),
+            set(enums["ObjectDirectionEnum"]["permissible_values"]))
+
+
+def detect_profile(doc: dict) -> str:
+    """Same rule qc.py uses: any per-edge evidence -> ai_curated."""
+    for link in doc.get("links") or []:
+        if isinstance(link, dict) and link.get("evidence"):
+            return "ai_curated"
+    return "legacy"
+
+
+def _replacement_hint(entry: dict) -> str:
+    why = {"legacy_only": "removed in current Biolink",
+           "deprecated": "deprecated in current Biolink"}.get(entry.get("status"),
+                                                              "not a current Biolink predicate")
+    r = entry.get("replacement")
+    if not r:
+        return (f"{why} and has no mechanical replacement "
+                f"({entry.get('note', 'needs a human decision')})")
+    bits = [f"key={r['key']!r}"] + [f"{k}={v!r}" for k, v in r.items() if k != "key"]
+    return f"{why} — use " + ", ".join(bits)
+
+
 def iter_files(targets: Iterable[str]) -> list[Path]:
     targets = list(targets)
     if not targets:
@@ -54,20 +108,47 @@ def iter_files(targets: Iterable[str]) -> list[Path]:
     return files
 
 
-def validate_file(path: Path, enum: set[str]) -> list[dict]:
+def validate_file(path: Path, enum: set[str], status: dict,
+                  aspects: set[str], directions: set[str],
+                  profile: str = "auto") -> list[dict]:
     """Return a list of failure dicts for this file (empty if all keys valid)."""
     with path.open() as fh:
         doc = yaml.safe_load(fh)
     if not isinstance(doc, dict):
         return [{"file": str(path), "edge_index": None, "key": None, "reason": "not a YAML mapping"}]
+
+    effective = detect_profile(doc) if profile == "auto" else profile
     failures = []
     for i, link in enumerate(doc.get("links") or []):
         if not isinstance(link, dict):
             failures.append({"file": str(path), "edge_index": i, "key": None, "reason": "edge is not a mapping"})
             continue
         key = link.get("key")
+        fail = lambda reason: failures.append(
+            {"file": str(path), "edge_index": i, "key": key, "profile": effective, "reason": reason})
+
         if key not in enum:
-            failures.append({"file": str(path), "edge_index": i, "key": key, "reason": "key not in BiolinkPredicate enum"})
+            fail("key not in BiolinkPredicate enum")
+            continue
+
+        aspect = link.get("object_aspect_qualifier")
+        direction = link.get("object_direction_qualifier")
+        if aspect is not None and aspect not in aspects:
+            fail(f"object_aspect_qualifier={aspect!r} not in ObjectAspectEnum")
+        if direction is not None and direction not in directions:
+            fail(f"object_direction_qualifier={direction!r} not in ObjectDirectionEnum")
+
+        if effective != "ai_curated":
+            continue                       # legacy records are frozen in their own era
+
+        entry = status.get(key) or {}
+        if entry.get("status") != "current":
+            fail(_replacement_hint(entry))
+            continue
+        if key in NEEDS_DIRECTION and direction is None:
+            fail(f"{key!r} carries its polarity in object_direction_qualifier, which is missing")
+        if key in NEEDS_ASPECT and aspect is None:
+            fail(f"{key!r} requires object_aspect_qualifier (which aspect of the target is affected)")
     return failures
 
 
@@ -75,18 +156,23 @@ def main() -> int:
     parser = argparse.ArgumentParser(description=__doc__)
     parser.add_argument("targets", nargs="*", help="Path files or directories. Defaults to kb/paths/.")
     parser.add_argument("--json", action="store_true", help="Output machine-readable JSON.")
+    parser.add_argument("--profile", choices=("auto", "legacy", "ai_curated"), default="auto",
+                        help="Validation profile. `auto` detects per file (default).")
     args = parser.parse_args()
 
     enum = load_enum()
+    status = load_status()
+    aspects, directions = load_qualifier_values()
     files = iter_files(args.targets)
 
     all_failures: list[dict] = []
     for path in files:
-        all_failures.extend(validate_file(path, enum))
+        all_failures.extend(validate_file(path, enum, status, aspects, directions, args.profile))
 
     summary = {
         "files_checked": len(files),
         "enum_size": len(enum),
+        "current_predicates": sum(1 for v in status.values() if v.get("status") == "current"),
         "failure_count": len(all_failures),
         "failures": all_failures,
     }
@@ -101,7 +187,9 @@ def main() -> int:
             if len(all_failures) > 50:
                 print(f"  …and {len(all_failures) - 50} more (re-run with --json for full list)")
         else:
-            print(f"Layer 3 PASS: {len(files)} files, every edge key is in BiolinkPredicate ({len(enum)} canonical predicates).")
+            n_current = summary["current_predicates"]
+            print(f"Layer 3 PASS: {len(files)} files — every edge key is in BiolinkPredicate "
+                  f"({len(enum)} accepted; {n_current} current in the pinned Biolink release).")
 
     return 0 if not all_failures else 1
 
diff --git a/src/drugmechdb/schema/biolink_predicate_status.yaml b/src/drugmechdb/schema/biolink_predicate_status.yaml
new file mode 100644
index 0000000..c004e24
--- /dev/null
+++ b/src/drugmechdb/schema/biolink_predicate_status.yaml
@@ -0,0 +1,235 @@
+# Biolink predicate status — which of our enum values are still current Biolink,
+# and what each removed one becomes.
+#
+# WHY THIS FILE EXISTS
+# `biolink_predicates.yaml` is the LinkML enum: the set of keys any record MAY use.
+# It must keep accepting the legacy vocabulary, because the 4,846 legacy records in
+# kb/paths/ are written in it. This file is the second axis — for each enum value,
+# whether Biolink still defines it, and if not, the qualifier form that replaces it.
+#
+# WHO READS IT
+#   * scripts/validate_predicates.py — QC Layer 3. `ai_curated` records may only use
+#     `status: current` keys; `legacy` records may use anything in the enum.
+#   * scripts/migrate_predicates.py  — applies `replacement` to rewrite a record.
+#
+# Verified against the pinned Biolink release below by scripts/check_biolink_drift.py.
+# When Biolink releases again, the drift monitor reports the delta; a human updates
+# this file — nothing here is auto-applied.
+
+biolink_version: 4.4.4
+biolink_source: https://raw.githubusercontent.com/biolink/biolink-model/v4.4.4/biolink-model.yaml
+verified_on: '2026-09-03'
+
+predicates:
+
+  # ── Removed in Biolink 4.4.4 — legacy records only ───────────────────────────
+  # The v2->v4 qualifier refactor folded these into `regulates` / `affects` plus
+  # object_aspect_qualifier + object_direction_qualifier.
+
+  ameliorates:
+    status: legacy_only
+    replacement:
+      key: ameliorates condition
+
+  contraindicated for:
+    status: legacy_only
+    replacement:
+      key: contraindicated in
+
+  decreases abundance of:
+    status: legacy_only
+    replacement:
+      key: affects
+      object_aspect_qualifier: abundance
+      object_direction_qualifier: decreased
+
+  decreases activity of:
+    status: legacy_only
+    replacement:
+      key: affects
+      object_aspect_qualifier: activity
+      object_direction_qualifier: decreased
+
+  decreases expression of:
+    status: legacy_only
+    replacement:
+      key: affects
+      object_aspect_qualifier: expression
+      object_direction_qualifier: decreased
+
+  decreases synthesis of:
+    status: legacy_only
+    replacement:
+      key: affects
+      object_aspect_qualifier: synthesis
+      object_direction_qualifier: decreased
+
+  decreases uptake of:
+    status: legacy_only
+    replacement:
+      key: affects
+      object_aspect_qualifier: uptake
+      object_direction_qualifier: decreased
+
+  directly interacts with:
+    status: legacy_only
+    replacement:
+      key: directly physically interacts with
+
+  exacerbates:
+    status: legacy_only
+    replacement:
+      key: exacerbates condition
+
+  increases abundance of:
+    status: legacy_only
+    replacement:
+      key: affects
+      object_aspect_qualifier: abundance
+      object_direction_qualifier: increased
+
+  increases activity of:
+    status: legacy_only
+    replacement:
+      key: affects
+      object_aspect_qualifier: activity
+      object_direction_qualifier: increased
+
+  increases degradation of:
+    status: legacy_only
+    replacement:
+      key: affects
+      object_aspect_qualifier: degradation
+      object_direction_qualifier: increased
+
+  increases expression of:
+    status: legacy_only
+    replacement:
+      key: affects
+      object_aspect_qualifier: expression
+      object_direction_qualifier: increased
+
+  increases stability of:
+    status: legacy_only
+    replacement:
+      key: affects
+      object_aspect_qualifier: stability
+      object_direction_qualifier: increased
+
+  increases transport of:
+    status: legacy_only
+    replacement:
+      key: affects
+      object_aspect_qualifier: transport
+      object_direction_qualifier: increased
+
+  molecularly interacts with:
+    status: legacy_only
+    replacement:
+      key: directly physically interacts with
+
+  negatively regulates:
+    status: legacy_only
+    replacement:
+      key: regulates
+      object_direction_qualifier: decreased
+
+  positively regulates:
+    status: legacy_only
+    replacement:
+      key: regulates
+      object_direction_qualifier: increased
+
+  predisposes:
+    status: legacy_only
+    replacement:
+      key: predisposes to condition
+
+  prevents:
+    status: legacy_only
+    replacement:
+      key: preventative for condition
+
+  # ── Deprecated upstream — present in Biolink 4.4.4 but flagged deprecated ────
+
+  binds:
+    status: deprecated
+    replacement:
+      key: directly physically interacts with
+
+  # ── Removed, and NO mechanical replacement — needs a human, per edge ─────────
+
+  affects risk for:
+    status: legacy_only
+    replacement: null
+    needs_human_decision: true
+    note: >-
+      Direction is unspecified in the legacy predicate; 4.4.4 splits it into `associated with increased likelihood of` / `associated with decreased likelihood of`. Requires a per-edge reading of the evidence.
+
+  decreases response to:
+    status: legacy_only
+    replacement: null
+    needs_human_decision: true
+    note: >-
+      Biolink 4.4.4 has no `response` aspect in GeneOrGeneProductOrChemicalEntityAspectEnum; no faithful qualifier form.
+
+  increases response to:
+    status: legacy_only
+    replacement: null
+    needs_human_decision: true
+    note: >-
+      Biolink 4.4.4 has no `response` aspect in GeneOrGeneProductOrChemicalEntityAspectEnum; no faithful qualifier form.
+
+  # ── Still current in Biolink 4.4.4 — usable by new curation ──────────────────
+
+  actively involved in: {status: current}
+  affected by: {status: current}
+  capable of: {status: current}
+  caused by: {status: current}
+  causes: {status: current}
+  chemically similar to: {status: current}
+  coexists with: {status: current}
+  contributes to: {status: current}
+  correlated with: {status: current}
+  derives from: {status: current}
+  derives into: {status: current}
+  disrupted by: {status: current}
+  disrupts: {status: current}
+  enables: {status: current}
+  expressed in: {status: current}
+  expresses: {status: current}
+  has active ingredient: {status: current}
+  has metabolite: {status: current}
+  has output: {status: current}
+  has part: {status: current}
+  has participant: {status: current}
+  has phenotype: {status: current}
+  in complex with: {status: current}
+  in taxon: {status: current}
+  interacts with: {status: current}
+  is metabolite of: {status: current}
+  located in: {status: current}
+  location of: {status: current}
+  manifestation of: {status: current}
+  negatively correlated with: {status: current}
+  occurs in: {status: current}
+  part of: {status: current}
+  participates in: {status: current}
+  phenotype of: {status: current}
+  physically interacts with: {status: current}
+  positively correlated with: {status: current}
+  precedes: {status: current}
+  produced by: {status: current}
+  produces: {status: current}
+  regulates: {status: current}
+  similar to: {status: current}
+  subclass of: {status: current}
+  superclass of: {status: current}
+  treats: {status: current}
+  affects: {status: current}
+  directly physically interacts with: {status: current}
+  preventative for condition: {status: current}
+  ameliorates condition: {status: current}
+  exacerbates condition: {status: current}
+  predisposes to condition: {status: current}
+  contraindicated in: {status: current}
diff --git a/src/drugmechdb/schema/biolink_predicates.yaml b/src/drugmechdb/schema/biolink_predicates.yaml
index 57d583d..41615f4 100644
--- a/src/drugmechdb/schema/biolink_predicates.yaml
+++ b/src/drugmechdb/schema/biolink_predicates.yaml
@@ -295,3 +295,53 @@ enums:
       decreases uptake of:            # 1 use
         meaning: biolink:decreases_uptake_of
         description: Subject decreases uptake of the object.
+
+      # ── Biolink 4.4.4 canonical predicates (added 2026-09) ─────────────────
+      # The qualifier refactor (v2->v4) removed the `increases/decreases <aspect>
+      # of` and `positively/negatively regulates` families. Their replacements are
+      # these canonical predicates carried with `object_aspect_qualifier` /
+      # `object_direction_qualifier` on the edge. See
+      # src/drugmechdb/schema/biolink_predicate_status.yaml for the per-predicate
+      # status and the replacement each legacy key maps to.
+
+      affects:                        # Biolink 4.4.4 canonical_predicate
+        meaning: biolink:affects
+        description: >-
+          Subject has an effect on the state or quality of the object. Carries
+          object_aspect_qualifier + object_direction_qualifier to express what
+          the legacy `increases/decreases <aspect> of` predicates asserted.
+
+      directly physically interacts with:   # Biolink 4.4.4 canonical_predicate
+        meaning: biolink:directly_physically_interacts_with
+        description: >-
+          Subject and object make direct physical contact. Replaces the removed
+          `molecularly interacts with` / `directly interacts with`.
+
+      binds:                          # Biolink 4.4.4
+        meaning: biolink:binds
+        description: >-
+          Subject binds the object through non-covalent interaction. A narrower
+          form of `directly physically interacts with`.
+
+      # Condition-scoped replacements for the removed clinical-outcome predicates.
+      # (`prevents` -> `preventative for condition`, and so on.)
+
+      preventative for condition:
+        meaning: biolink:preventative_for_condition
+        description: Subject is preventative for the object condition. Replaces the removed `prevents`.
+
+      ameliorates condition:
+        meaning: biolink:ameliorates_condition
+        description: Subject ameliorates the object condition. Replaces the removed `ameliorates`.
+
+      exacerbates condition:
+        meaning: biolink:exacerbates_condition
+        description: Subject exacerbates the object condition. Replaces the removed `exacerbates`.
+
+      predisposes to condition:
+        meaning: biolink:predisposes_to_condition
+        description: Subject predisposes to the object condition. Replaces the removed `predisposes`.
+
+      contraindicated in:
+        meaning: biolink:contraindicated_in
+        description: Subject is contraindicated in the object condition. Replaces the removed `contraindicated for`.
diff --git a/src/drugmechdb/schema/drugmechdb.yaml b/src/drugmechdb/schema/drugmechdb.yaml
index 1e6a746..6f10e63 100644
--- a/src/drugmechdb/schema/drugmechdb.yaml
+++ b/src/drugmechdb/schema/drugmechdb.yaml
@@ -78,6 +78,37 @@ types:
 # ── Enumerations ──────────────────────────────────────────────────────────────
 
 enums:
+  ObjectAspectEnum:
+    description: >-
+      The aspect of the object that an edge affects. Mirrors the Biolink 4.4.4
+      `GeneOrGeneProductOrChemicalEntityAspectEnum` values DrugMechDB uses; carried on
+      `object_aspect_qualifier`. Together with ObjectDirectionEnum this expresses what the
+      removed `increases/decreases <aspect> of` predicates asserted before the v2->v4
+      qualifier refactor.
+    permissible_values:
+      activity:
+      abundance:
+      expression:
+      synthesis:
+      degradation:
+      stability:
+      transport:
+      uptake:
+      localization:
+      secretion:
+      molecular_interaction:
+      activity_or_abundance:
+
+  ObjectDirectionEnum:
+    description: >-
+      Direction of the effect on the object's aspect. Mirrors the Biolink 4.4.4
+      `DirectionQualifierEnum`; carried on `object_direction_qualifier`.
+    permissible_values:
+      increased:
+      decreased:
+      upregulated:
+      downregulated:
+
   EvidenceSupportEnum:
     description: The level of support an evidence item provides for an edge claim.
     permissible_values:
@@ -308,6 +339,29 @@ slots:
       Biolink predicate describing the relationship from source to target.
       Must be a value from the BiolinkPredicate enum.
 
+  # Biolink 4.4.4 qualifiers. Optional and additive: legacy records carry none, and
+  # `key` alone remains a complete edge. New (ai_curated) records use them to express
+  # what the removed `increases/decreases <aspect> of` and `positively/negatively
+  # regulates` predicates asserted — see biolink_predicate_status.yaml for the mapping.
+
+  object_aspect_qualifier:
+    range: ObjectAspectEnum
+    description: >-
+      Which aspect of the target the edge affects (activity, abundance, expression, ...).
+      Set alongside object_direction_qualifier when `key` is `affects`.
+
+  object_direction_qualifier:
+    range: ObjectDirectionEnum
+    description: >-
+      Direction of the effect on the target — increased or decreased. Set when `key` is
+      `affects` or `regulates`; carries the polarity the legacy predicate name used to.
+
+  qualified_predicate:
+    range: uriorcurie
+    description: >-
+      The Biolink predicate the qualified statement resolves to (e.g. biolink:causes),
+      when the core `key` plus qualifiers needs an explicit causal reading.
+
   evidence:
     range: EvidenceItem
     multivalued: true
@@ -520,6 +574,9 @@ classes:
       - source
       - target
       - key
+      - object_aspect_qualifier
+      - object_direction_qualifier
+      - qualified_predicate
       - evidence
     slot_usage:
       source:
diff --git a/tests/fixtures/sample_ai_curated.yaml b/tests/fixtures/sample_ai_curated.yaml
index 69b7f03..914aa4e 100644
--- a/tests/fixtures/sample_ai_curated.yaml
+++ b/tests/fixtures/sample_ai_curated.yaml
@@ -21,7 +21,9 @@ nodes:
     name: Malignant tumor of colon
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:D000068818
     target: UniProt:P00533
     evidence:
diff --git a/tests/fixtures/sample_ai_curated_bad_snippet.yaml b/tests/fixtures/sample_ai_curated_bad_snippet.yaml
index b04291c..3532f14 100644
--- a/tests/fixtures/sample_ai_curated_bad_snippet.yaml
+++ b/tests/fixtures/sample_ai_curated_bad_snippet.yaml
@@ -17,7 +17,9 @@ nodes:
     name: Epidermal growth factor receptor
     label: Protein
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:D000068818
     target: UniProt:P00533
     evidence:
diff --git a/tests/phase3_eval_outputs/P01.yaml b/tests/phase3_eval_outputs/P01.yaml
index 8ec8bea..c8024e2 100644
--- a/tests/phase3_eval_outputs/P01.yaml
+++ b/tests/phase3_eval_outputs/P01.yaml
@@ -27,7 +27,9 @@ nodes:
     name: Myocardial Infarction
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:D001241
     target: UniProt:P23219
     evidence:
@@ -41,7 +43,8 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: "Quantitative proteomic confirmation that aspirin acetylates COX-1 at Ser529, the canonical mechanistic step."
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P23219
     target: GO:0001516
     evidence:
@@ -59,7 +62,8 @@ links:
         supports: SUPPORT
         evidence_source: HUMAN_CLINICAL
         explanation: "TXA2 is the platelet-specific prostanoid generated from arachidonic acid via COX-1 — i.e. it is an output of the prostaglandin biosynthetic process in platelets."
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: MESH:D013928
     target: GO:0070527
     evidence:
diff --git a/tests/phase3_eval_outputs/P01_no_provider.yaml b/tests/phase3_eval_outputs/P01_no_provider.yaml
index 9df099a..c10f549 100644
--- a/tests/phase3_eval_outputs/P01_no_provider.yaml
+++ b/tests/phase3_eval_outputs/P01_no_provider.yaml
@@ -30,7 +30,9 @@ nodes:
     name: Myocardial Infarction
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:D001241
     target: UniProt:P23219
     evidence:
@@ -39,7 +41,9 @@ links:
         supports: SUPPORT
         evidence_source: HUMAN_CLINICAL
         explanation: "Aspirin covalently acetylates Ser529 of platelet COX-1, irreversibly inhibiting its catalytic activity."
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:D001241
     target: UniProt:P35354
     evidence:
@@ -48,7 +52,8 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: "Aspirin (ASA) acetylates COX-2 at Serine 516, inhibiting its prostanoid-generating activity."
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P23219
     target: GO:0001516
     evidence:
@@ -57,7 +62,8 @@ links:
         supports: SUPPORT
         evidence_source: HUMAN_CLINICAL
         explanation: "Catalytically intact COX-1 drives platelet prostanoid biosynthesis; its acetylation by aspirin suppresses thromboxane A2 (a prostaglandin-class product) generation."
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P35354
     target: GO:0001516
     evidence:
@@ -75,7 +81,8 @@ links:
         supports: SUPPORT
         evidence_source: HUMAN_CLINICAL
         explanation: "TXA2 is the platelet-specific prostanoid output of COX-1-mediated arachidonic acid metabolism (the prostaglandin biosynthetic process)."
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: MESH:D013928
     target: GO:0070527
     evidence:
diff --git a/tests/phase3_eval_outputs/P02.yaml b/tests/phase3_eval_outputs/P02.yaml
index f51c7fa..661480d 100644
--- a/tests/phase3_eval_outputs/P02.yaml
+++ b/tests/phase3_eval_outputs/P02.yaml
@@ -24,7 +24,9 @@ nodes:
     name: Hypercholesterolemia
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:D000069059
     target: UniProt:P04035
     evidence:
@@ -38,7 +40,8 @@ links:
         supports: SUPPORT
         evidence_source: OTHER
         explanation: "Pharmacology review confirming atorvastatin acts by competitive and selective inhibition of HMG-CoA reductase, blocking conversion of its HMG-CoA substrate."
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P04035
     target: GO:0006695
     evidence:
@@ -52,7 +55,9 @@ links:
         supports: SUPPORT
         evidence_source: OTHER
         explanation: "HMG-CoA reductase is the rate-limiting enzyme of the mevalonate pathway (cholesterol biosynthesis); inhibiting it lowers cholesterol, confirming the enzyme positively regulates the biosynthetic process."
-  - key: increases abundance of
+  - key: affects
+    object_aspect_qualifier: abundance
+    object_direction_qualifier: increased
     source: GO:0006695
     target: MESH:D002784
     evidence:
diff --git a/tests/phase3_eval_outputs/P03.yaml b/tests/phase3_eval_outputs/P03.yaml
index 35436f3..b105935 100644
--- a/tests/phase3_eval_outputs/P03.yaml
+++ b/tests/phase3_eval_outputs/P03.yaml
@@ -21,7 +21,9 @@ nodes:
     name: Hypertension
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:D017706
     target: UniProt:P12821
     evidence:
diff --git a/tests/phase3_eval_outputs/P04.yaml b/tests/phase3_eval_outputs/P04.yaml
index d797965..fc3ca86 100644
--- a/tests/phase3_eval_outputs/P04.yaml
+++ b/tests/phase3_eval_outputs/P04.yaml
@@ -21,7 +21,9 @@ nodes:
     name: Heart failure
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:D008790
     target: UniProt:P08588
     evidence:
@@ -35,7 +37,8 @@ links:
         supports: SUPPORT
         evidence_source: OTHER
         explanation: "Confirms metoprolol's mechanism class as a β1-receptor blocker (antagonist), decreasing beta-1 adrenergic receptor activity."
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P08588
     target: GO:0003300
     evidence:
diff --git a/tests/phase3_eval_outputs/P05.yaml b/tests/phase3_eval_outputs/P05.yaml
index ed2dc2f..37e5f9f 100644
--- a/tests/phase3_eval_outputs/P05.yaml
+++ b/tests/phase3_eval_outputs/P05.yaml
@@ -21,7 +21,9 @@ nodes:
     name: Stroke
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:D000077144
     target: UniProt:Q9H244
     evidence:
@@ -35,7 +37,8 @@ links:
         supports: SUPPORT
         evidence_source: MODEL_ORGANISM
         explanation: "Clopidogrel's active metabolite forms disulfide bonds with platelet P2Y12 receptors, irreversibly inhibiting the receptor and thereby its downstream aggregation function."
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:Q9H244
     target: GO:0070527
     evidence:
diff --git a/tests/phase3_eval_outputs/P06.yaml b/tests/phase3_eval_outputs/P06.yaml
index 5c22be1..847b83e 100644
--- a/tests/phase3_eval_outputs/P06.yaml
+++ b/tests/phase3_eval_outputs/P06.yaml
@@ -21,7 +21,9 @@ nodes:
     name: Breast Neoplasms
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:D013629
     target: UniProt:P03372
     evidence:
@@ -35,7 +37,8 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: "Tamoxifen is an endocrine therapy that acts by disrupting estrogen signaling through the estrogen receptor, i.e. decreasing receptor activity."
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P03372
     target: GO:0008283
     evidence:
diff --git a/tests/phase3_eval_outputs/P07.yaml b/tests/phase3_eval_outputs/P07.yaml
index 6e9a8b2..01f5a86 100644
--- a/tests/phase3_eval_outputs/P07.yaml
+++ b/tests/phase3_eval_outputs/P07.yaml
@@ -21,7 +21,9 @@ nodes:
     name: Chronic Myeloid Leukemia
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:D000068877
     target: UniProt:P00519
     evidence:
@@ -35,7 +37,8 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: "Imatinib inhibits BCR-ABL1 kinase activity, abolishing its downstream tyrosine-phosphorylation activity in CML cells — direct support for the decreases-activity-of edge."
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P00519
     target: GO:0070661
     evidence:
diff --git a/tests/phase3_eval_outputs/P08.yaml b/tests/phase3_eval_outputs/P08.yaml
index 214ad0a..7be7256 100644
--- a/tests/phase3_eval_outputs/P08.yaml
+++ b/tests/phase3_eval_outputs/P08.yaml
@@ -24,7 +24,9 @@ nodes:
     name: Colorectal Neoplasms
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:D000068818
     target: UniProt:P00533
     evidence:
@@ -33,7 +35,8 @@ links:
         supports: SUPPORT
         evidence_source: HUMAN_CLINICAL
         explanation: Cetuximab is a monoclonal antibody that binds the EGFR extracellular domain, blocking ligand-induced receptor activation and thereby decreasing EGFR signaling activity.
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P00533
     target: GO:0000165
     evidence:
@@ -42,7 +45,8 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: Activated EGFR drives phosphorylation of ERK1/2 (the terminal kinases of the MAPK cascade), demonstrating that EGFR positively regulates the MAPK cascade in colorectal cancer cells.
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: GO:0000165
     target: GO:0008283
     evidence:
diff --git a/tests/phase3_eval_outputs/P09.yaml b/tests/phase3_eval_outputs/P09.yaml
index 1ea5d4e..4c9f505 100644
--- a/tests/phase3_eval_outputs/P09.yaml
+++ b/tests/phase3_eval_outputs/P09.yaml
@@ -27,7 +27,9 @@ nodes:
     name: Acute Lymphoblastic Leukemia
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:D008727
     target: UniProt:P00374
     evidence:
@@ -41,7 +43,8 @@ links:
         supports: SUPPORT
         evidence_source: OTHER
         explanation: Confirms competitive inhibition of DHFR by MTX, reducing the enzyme's activity in tetrahydrofolate synthesis.
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P00374
     target: GO:0046654
     evidence:
@@ -55,7 +58,8 @@ links:
         supports: SUPPORT
         evidence_source: OTHER
         explanation: DHFR participates in tetrahydrofolate synthesis, confirming its positive regulatory role in that biosynthetic process.
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: GO:0046654
     target: GO:0071897
     evidence:
@@ -69,7 +73,8 @@ links:
         supports: SUPPORT
         evidence_source: HUMAN_CLINICAL
         explanation: Decreasing folate-dependent enzyme activities (including the tetrahydrofolate biosynthetic pathway) impairs DNA synthesis, confirming folate metabolism positively regulates the DNA biosynthetic process.
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: GO:0071897
     target: GO:0008283
     evidence:
diff --git a/tests/phase3_eval_outputs/P10.yaml b/tests/phase3_eval_outputs/P10.yaml
index 0828de7..6ce548d 100644
--- a/tests/phase3_eval_outputs/P10.yaml
+++ b/tests/phase3_eval_outputs/P10.yaml
@@ -21,7 +21,7 @@ nodes:
     name: Breast Neoplasms
     label: Disease
 links:
-  - key: molecularly interacts with
+  - key: directly physically interacts with
     source: MESH:D000068878
     target: UniProt:P04626
     evidence:
@@ -30,7 +30,9 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: Direct binding of trastuzumab to HER2 was demonstrated in CHO cells expressing human HER2, confirming that trastuzumab molecularly interacts with the ERBB2/HER2 receptor.
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:D000068878
     target: UniProt:P04626
     evidence:
@@ -44,7 +46,8 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: Trastuzumab reduces PI3K activity downstream of ERBB2, supporting that it decreases ERBB2-mediated signaling activity.
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P04626
     target: GO:0008283
     evidence:
diff --git a/tests/phase3_eval_outputs/P11.yaml b/tests/phase3_eval_outputs/P11.yaml
index 29cd5b5..02d5c89 100644
--- a/tests/phase3_eval_outputs/P11.yaml
+++ b/tests/phase3_eval_outputs/P11.yaml
@@ -24,7 +24,9 @@ nodes:
     name: Pulmonary tuberculosis
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:D012293
     target: UniProt:P9WGY9
     evidence:
@@ -38,7 +40,8 @@ links:
         supports: SUPPORT
         evidence_source: OTHER
         explanation: RIF acts on RpoB (RNA polymerase beta subunit); nearly all resistance mutations map to this subunit, confirming it is the direct target of rifampicin inhibition.
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P9WGY9
     target: GO:0006351
     evidence:
diff --git a/tests/phase3_eval_outputs/P12.yaml b/tests/phase3_eval_outputs/P12.yaml
index 3086301..0a9a362 100644
--- a/tests/phase3_eval_outputs/P12.yaml
+++ b/tests/phase3_eval_outputs/P12.yaml
@@ -24,7 +24,9 @@ nodes:
     name: Pulmonary Tuberculosis
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:D007538
     target: UniProt:P9WGR1
     evidence:
@@ -38,7 +40,8 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: InhA is directly identified as the primary enzymatic target of isoniazid in M. tuberculosis.
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P9WGR1
     target: GO:0071768
     evidence:
diff --git a/tests/phase3_eval_outputs/P13.yaml b/tests/phase3_eval_outputs/P13.yaml
index 67d0e2e..0948579 100644
--- a/tests/phase3_eval_outputs/P13.yaml
+++ b/tests/phase3_eval_outputs/P13.yaml
@@ -24,7 +24,7 @@ nodes:
     name: Methicillin-Resistant Staphylococcal Infections
     label: Disease
 links:
-  - key: molecularly interacts with
+  - key: directly physically interacts with
     source: MESH:D014640
     target: CHEBI:16576
     evidence:
diff --git a/tests/phase3_eval_outputs/P14.yaml b/tests/phase3_eval_outputs/P14.yaml
index cc733cc..263725f 100644
--- a/tests/phase3_eval_outputs/P14.yaml
+++ b/tests/phase3_eval_outputs/P14.yaml
@@ -41,7 +41,9 @@ links:
         supports: SUPPORT
         evidence_source: HUMAN_CLINICAL
         explanation: Confirms oseltamivir is a prodrug and its active metabolite is oseltamivir carboxylate, supporting the has metabolite relationship.
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: CHEBI:64337
     target: UniProt:P03472
     evidence:
@@ -55,7 +57,8 @@ links:
         supports: SUPPORT
         evidence_source: OTHER
         explanation: Establishes NA as the antiviral drug target; combined with the first evidence item, confirms oseltamivir carboxylate decreases NA activity.
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P03472
     target: GO:0019076
     evidence:
diff --git a/tests/phase3_eval_outputs/P15.yaml b/tests/phase3_eval_outputs/P15.yaml
index c94a44c..711e864 100644
--- a/tests/phase3_eval_outputs/P15.yaml
+++ b/tests/phase3_eval_outputs/P15.yaml
@@ -45,7 +45,9 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: "Thymidine kinase that phosphorylates acyclovir is encoded by herpes simplex virus, establishing the protein's taxon assignment."
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:D000212
     target: UniProt:P04293
     evidence:
@@ -63,7 +65,8 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: "The DNA polymerase catalytic subunit (Pol) targeted by acyclovir is encoded by herpes simplex virus."
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P04293
     target: GO:0039693
     evidence:
diff --git a/tests/phase3_eval_outputs/P16.yaml b/tests/phase3_eval_outputs/P16.yaml
index c5d0c5e..56a8e12 100644
--- a/tests/phase3_eval_outputs/P16.yaml
+++ b/tests/phase3_eval_outputs/P16.yaml
@@ -24,7 +24,7 @@ nodes:
     name: Parkinson's disease
     label: Disease
 links:
-  - key: molecularly interacts with
+  - key: directly physically interacts with
     source: MESH:D007980
     target: UniProt:P20711
     evidence:
@@ -47,7 +47,8 @@ links:
         supports: SUPPORT
         evidence_source: OTHER
         explanation: Review confirming that L-DOPA is converted into dopamine by the enzyme aromatic L-amino acid decarboxylase (AADC).
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: MESH:D004298
     target: GO:0001963
     evidence:
diff --git a/tests/phase3_eval_outputs/P17.yaml b/tests/phase3_eval_outputs/P17.yaml
index 9afdc2c..f11c62b 100644
--- a/tests/phase3_eval_outputs/P17.yaml
+++ b/tests/phase3_eval_outputs/P17.yaml
@@ -27,7 +27,9 @@ nodes:
     name: Major depressive disorder
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:D005473
     target: UniProt:P31645
     evidence:
@@ -41,7 +43,8 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: Fluoxetine binds the central substrate site of SERT, competitively blocking its serotonin uptake activity.
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P31645
     target: GO:0051610
     evidence:
@@ -55,7 +58,9 @@ links:
         supports: SUPPORT
         evidence_source: HUMAN_CLINICAL
         explanation: SERT is responsible for serotonin reuptake from the synaptic cleft — confirming it positively regulates the serotonin uptake process.
-  - key: decreases abundance of
+  - key: affects
+    object_aspect_qualifier: abundance
+    object_direction_qualifier: decreased
     source: GO:0051610
     target: MESH:D012701
     evidence:
diff --git a/tests/phase3_eval_outputs/P18.yaml b/tests/phase3_eval_outputs/P18.yaml
index ffbc90b..47125d2 100644
--- a/tests/phase3_eval_outputs/P18.yaml
+++ b/tests/phase3_eval_outputs/P18.yaml
@@ -21,7 +21,9 @@ nodes:
     name: Bipolar Disorder
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:D008094
     target: UniProt:P49841
     evidence:
@@ -39,7 +41,8 @@ links:
         explanation: >-
           Medicinal chemistry paper developing GSK-3beta inhibitors for bipolar
           disorder, confirming lithium's known direct inhibitory action on GSK-3beta.
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P49841
     target: GO:0006915
     evidence:
diff --git a/tests/phase3_eval_outputs/P19.yaml b/tests/phase3_eval_outputs/P19.yaml
index 82f0fd2..4cc9b92 100644
--- a/tests/phase3_eval_outputs/P19.yaml
+++ b/tests/phase3_eval_outputs/P19.yaml
@@ -24,7 +24,9 @@ nodes:
     name: Epilepsy
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:D000077306
     target: UniProt:P54289
     evidence:
@@ -38,7 +40,8 @@ links:
         supports: SUPPORT
         evidence_source: OTHER
         explanation: The α2δ-1 protein is both the high-affinity binding site and required mediator of gabapentin's mechanism, confirming gabapentin decreases its activity.
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P54289
     target: GO:0070588
     evidence:
@@ -52,7 +55,8 @@ links:
         supports: SUPPORT
         evidence_source: OTHER
         explanation: As a regulatory subunit of voltage-gated calcium channels, α2δ-1 positively regulates calcium ion flux across the neuronal membrane.
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: GO:0070588
     target: GO:0007269
     evidence:
diff --git a/tests/phase3_eval_outputs/P20.yaml b/tests/phase3_eval_outputs/P20.yaml
index 34e9aef..e25d7d8 100644
--- a/tests/phase3_eval_outputs/P20.yaml
+++ b/tests/phase3_eval_outputs/P20.yaml
@@ -24,7 +24,9 @@ nodes:
     name: Alzheimer's disease
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: DB:DB00843
     target: UniProt:P22303
     evidence:
@@ -38,7 +40,8 @@ links:
         supports: SUPPORT
         evidence_source: HUMAN_CLINICAL
         explanation: "Clinical review confirming donepezil is an acetylcholinesterase inhibitor with established efficacy in Alzheimer disease."
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P22303
     target: GO:0006581
     evidence:
@@ -52,7 +55,9 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: "AChE is the key enzyme that hydrolyzes acetylcholine, confirming its positive regulatory role in the acetylcholine catabolic process."
-  - key: decreases abundance of
+  - key: affects
+    object_aspect_qualifier: abundance
+    object_direction_qualifier: decreased
     source: GO:0006581
     target: MESH:D000109
     evidence:
diff --git a/tests/phase3_eval_outputs/P21.yaml b/tests/phase3_eval_outputs/P21.yaml
index 994a58a..5f1eeab 100644
--- a/tests/phase3_eval_outputs/P21.yaml
+++ b/tests/phase3_eval_outputs/P21.yaml
@@ -24,7 +24,9 @@ nodes:
     name: Rheumatoid Arthritis
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:D008727
     target: UniProt:P31939
     evidence:
@@ -33,7 +35,9 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: Methotrexate polyglutamates (the active intracellular form of MTX) directly inhibit ATIC activity, the enzyme encoded by the ATIC gene (UniProt:P31939), thereby decreasing its catalytic function.
-  - key: decreases abundance of
+  - key: affects
+    object_aspect_qualifier: abundance
+    object_direction_qualifier: decreased
     source: UniProt:P31939
     target: MESH:D000241
     evidence:
@@ -47,7 +51,8 @@ links:
         supports: SUPPORT
         evidence_source: HUMAN_CLINICAL
         explanation: Confirms that extracellular adenosine generation is the key downstream effector in MTX-treated RA patients; ATIC inhibition is the upstream step that releases this brake on adenosine abundance.
-  - key: negatively regulates
+  - key: regulates
+    object_direction_qualifier: decreased
     source: MESH:D000241
     target: GO:0006954
     evidence:
diff --git a/tests/phase3_eval_outputs/P22.yaml b/tests/phase3_eval_outputs/P22.yaml
index d5d2621..437f584 100644
--- a/tests/phase3_eval_outputs/P22.yaml
+++ b/tests/phase3_eval_outputs/P22.yaml
@@ -24,7 +24,7 @@ nodes:
     name: Crohn's disease
     label: Disease
 links:
-  - key: molecularly interacts with
+  - key: directly physically interacts with
     source: MESH:D000069285
     target: UniProt:P01375
     evidence:
@@ -33,7 +33,9 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: "Infliximab's MoA is defined by its physical binding to both soluble and membrane-bound TNF-α, establishing a direct molecular interaction between the drug and its target protein."
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:D000069285
     target: UniProt:P01375
     evidence:
@@ -42,7 +44,8 @@ links:
         supports: SUPPORT
         evidence_source: OTHER
         explanation: "Infliximab neutralizes TNF-α, preventing it from engaging its receptors. Neutralization is equivalent to decreasing TNF-α functional activity."
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P01375
     target: GO:0038061
     evidence:
@@ -51,7 +54,8 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: "TNF-α directly activates NF-κB signaling (GO:0038061 NIK/NF-κB signaling), as shown by IκB-α degradation and NF-κB p65 nuclear translocation upon TNF-α stimulation."
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: GO:0038061
     target: GO:0006954
     evidence:
diff --git a/tests/phase3_eval_outputs/P23.yaml b/tests/phase3_eval_outputs/P23.yaml
index 9c53ca5..ec4a910 100644
--- a/tests/phase3_eval_outputs/P23.yaml
+++ b/tests/phase3_eval_outputs/P23.yaml
@@ -21,7 +21,9 @@ nodes:
     name: Systemic Lupus Erythematosus
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:D006886
     target: UniProt:Q9NR96
     evidence:
@@ -40,7 +42,8 @@ links:
         supports: SUPPORT
         evidence_source: OTHER
         explanation: "Katz and Russell review confirm that antimalarials including hydroxychloroquine act by inhibiting endosomal/intracellular TLRs, particularly TLR9."
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:Q9NR96
     target: GO:0032606
     evidence:
diff --git a/tests/phase3_eval_outputs/P24.yaml b/tests/phase3_eval_outputs/P24.yaml
index 61b28d6..5c1db60 100644
--- a/tests/phase3_eval_outputs/P24.yaml
+++ b/tests/phase3_eval_outputs/P24.yaml
@@ -36,7 +36,9 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: Confirms MMF is a prodrug of MPA, hydrolyzed by esterases to release the active metabolite MPA.
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: CHEBI:168618
     target: UniProt:P12268
     evidence:
@@ -50,7 +52,8 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: In vitro demonstration of MPA dose-dependently inhibiting IMPDH activity, supporting decreases activity of edge.
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P12268
     target: GO:0006177
     evidence:
@@ -64,7 +67,8 @@ links:
         supports: SUPPORT
         evidence_source: OTHER
         explanation: Blocking IMPDH prevents guanosine nucleotide production, confirming IMPDH positively regulates GMP biosynthesis.
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: GO:0006177
     target: GO:0046651
     evidence:
diff --git a/tests/phase3_eval_outputs/P25.yaml b/tests/phase3_eval_outputs/P25.yaml
index 36fae90..ffc1083 100644
--- a/tests/phase3_eval_outputs/P25.yaml
+++ b/tests/phase3_eval_outputs/P25.yaml
@@ -24,7 +24,9 @@ nodes:
     name: Psoriasis
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:D000068879
     target: UniProt:P01375
     evidence:
@@ -38,7 +40,8 @@ links:
         supports: SUPPORT
         evidence_source: OTHER
         explanation: "Expert review confirming adalimumab is a fully human anti-TNF-alpha monoclonal antibody that neutralizes TNF-alpha activity."
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P01375
     target: GO:0038061
     evidence:
@@ -52,7 +55,8 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: "TNF induces NF-κBp65 phosphorylation in keratinocytes, demonstrating that TNF-alpha positively regulates NIK/NF-kappaB signaling in psoriasis-relevant cells."
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: GO:0038061
     target: GO:0006954
     evidence:
diff --git a/tests/phase3_eval_outputs/P26.yaml b/tests/phase3_eval_outputs/P26.yaml
index 7383631..f976b8c 100644
--- a/tests/phase3_eval_outputs/P26.yaml
+++ b/tests/phase3_eval_outputs/P26.yaml
@@ -24,7 +24,9 @@ nodes:
     name: Diabetes mellitus type 2
     label: Disease
 links:
-  - key: increases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: increased
     source: MESH:D008687
     target: UniProt:Q13131
     evidence:
@@ -38,7 +40,8 @@ links:
         supports: SUPPORT
         evidence_source: OTHER
         explanation: Comprehensive review confirming that metformin raises cytosolic AMP, which activates AMPK (including the PRKAA1-containing heterotrimeric complex).
-  - key: negatively regulates
+  - key: regulates
+    object_direction_qualifier: decreased
     source: UniProt:Q13131
     target: GO:0006094
     evidence:
diff --git a/tests/phase3_eval_outputs/P27.yaml b/tests/phase3_eval_outputs/P27.yaml
index 6be9f83..8afff3f 100644
--- a/tests/phase3_eval_outputs/P27.yaml
+++ b/tests/phase3_eval_outputs/P27.yaml
@@ -24,7 +24,7 @@ nodes:
     name: Diabetes mellitus type 1
     label: Disease
 links:
-  - key: molecularly interacts with
+  - key: directly physically interacts with
     source: MESH:D007328
     target: UniProt:P06213
     evidence:
@@ -33,7 +33,8 @@ links:
         supports: SUPPORT
         evidence_source: OTHER
         explanation: Insulin binds directly to the insulin receptor (INSR/UniProt:P06213) on cell surfaces; this molecular interaction is the initiating event of the insulin signalling cascade that lowers blood glucose.
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P06213
     target: GO:0046323
     evidence:
diff --git a/tests/phase3_eval_outputs/P28.yaml b/tests/phase3_eval_outputs/P28.yaml
index 63c2133..caf0d4d 100644
--- a/tests/phase3_eval_outputs/P28.yaml
+++ b/tests/phase3_eval_outputs/P28.yaml
@@ -38,7 +38,9 @@ links:
         supports: SUPPORT
         evidence_source: OTHER
         explanation: Deiodination of T4 to T3 is the key activation step; administered levothyroxine (T4) is therefore a prodrug whose active form is T3.
-  - key: increases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: increased
     source: MESH:D014284
     target: UniProt:P10828
     evidence:
@@ -52,7 +54,8 @@ links:
         supports: SUPPORT
         evidence_source: OTHER
         explanation: T3 acts via its nuclear receptors TRα and TRβ (UniProt:P10828); local T3 availability drives receptor activity.
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P10828
     target: GO:0002154
     evidence:
@@ -66,7 +69,8 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: TRs including THRB are T3-activated transcription factors that drive thyroid hormone-responsive gene expression, i.e. they positively regulate the thyroid hormone mediated signaling pathway.
-  - key: negatively regulates
+  - key: regulates
+    object_direction_qualifier: decreased
     source: GO:0002154
     target: MESH:D007037
     evidence:
diff --git a/tests/phase3_eval_outputs/P29.yaml b/tests/phase3_eval_outputs/P29.yaml
index 79f78df..752f2e5 100644
--- a/tests/phase3_eval_outputs/P29.yaml
+++ b/tests/phase3_eval_outputs/P29.yaml
@@ -24,7 +24,9 @@ nodes:
     name: Gout
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:D000493
     target: UniProt:P47989
     evidence:
@@ -38,7 +40,8 @@ links:
         supports: SUPPORT
         evidence_source: IN_VITRO
         explanation: In vitro study showing allopurinol (ALP) inhibits XDH/XOD activity and reduces uric acid (UA) levels in MSU-treated cells.
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P47989
     target: GO:0002103
     evidence:
@@ -52,7 +55,9 @@ links:
         supports: SUPPORT
         evidence_source: OTHER
         explanation: XO/XDH is identified as the rate-limiting enzyme in uric acid production, confirming it positively regulates the uric acid biosynthetic process.
-  - key: increases abundance of
+  - key: affects
+    object_aspect_qualifier: abundance
+    object_direction_qualifier: increased
     source: GO:0002103
     target: CHEBI:27226
     evidence:
diff --git a/tests/phase3_eval_outputs/P30.yaml b/tests/phase3_eval_outputs/P30.yaml
index c115519..9748fa4 100644
--- a/tests/phase3_eval_outputs/P30.yaml
+++ b/tests/phase3_eval_outputs/P30.yaml
@@ -24,7 +24,9 @@ nodes:
     name: Diabetes Mellitus, Type 2
     label: Disease
 links:
-  - key: decreases activity of
+  - key: affects
+    object_aspect_qualifier: activity
+    object_direction_qualifier: decreased
     source: MESH:C000591311
     target: UniProt:P31639
     evidence:
@@ -33,7 +35,8 @@ links:
         supports: SUPPORT
         evidence_source: OTHER
         explanation: "Pharmacological review confirming empagliflozin selectively inhibits SGLT2 activity, constraining its renal glucose reabsorption function."
-  - key: positively regulates
+  - key: regulates
+    object_direction_qualifier: increased
     source: UniProt:P31639
     target: GO:0035623
     evidence:
diff --git a/tests/test_canonicalize_predicates.py b/tests/test_canonicalize_predicates.py
index 0b2ab67..085f547 100644
--- a/tests/test_canonicalize_predicates.py
+++ b/tests/test_canonicalize_predicates.py
@@ -90,9 +90,37 @@ def test_unmapped_drift_stays_out_of_enum():
 
 # ─── loaders ─────────────────────────────────────────────────────────────────
 
-def test_load_enum_is_the_67_predicate_vocabulary():
-    assert len(ENUM) == 67
-    assert "decreases activity of" in ENUM
+def test_load_enum_covers_both_biolink_eras():
+    """The enum spans eras: current Biolink plus the legacy vocabulary kb/paths uses.
+
+    Its size is not asserted — it grows when we adopt a predicate from a new Biolink
+    release. The invariant is that every enum value has a status entry and vice versa,
+    since Layer 3 reads the two together.
+    """
+    import yaml
+    status = yaml.safe_load(
+        (REPO / "src" / "drugmechdb" / "schema" / "biolink_predicate_status.yaml").read_text()
+    )["predicates"]
+    assert set(status) == ENUM
+    assert "decreases activity of" in ENUM          # legacy-only, still accepted
+    assert "affects" in ENUM                        # current Biolink
+
+
+def test_every_replacement_points_at_a_current_predicate():
+    """A `replacement:` that isn't itself a current enum member would migrate a record
+    straight into a Layer 3 failure — the mapping has to be closed over the enum."""
+    import yaml
+    status = yaml.safe_load(
+        (REPO / "src" / "drugmechdb" / "schema" / "biolink_predicate_status.yaml").read_text()
+    )["predicates"]
+    for pred, entry in status.items():
+        replacement = entry.get("replacement") or {}
+        target = replacement.get("key")
+        if not target:
+            continue
+        assert target in ENUM, f"{pred!r} maps to {target!r}, which is not in the enum"
+        assert status[target]["status"] == "current", (
+            f"{pred!r} maps to {target!r}, which is not a current predicate")
 
 
 def test_load_aliases_returns_a_mapping():
diff --git a/tests/test_qc_layers.py b/tests/test_qc_layers.py
index 804c3a8..e40db2b 100644
--- a/tests/test_qc_layers.py
+++ b/tests/test_qc_layers.py
@@ -31,6 +31,14 @@
 import yaml
 
 REPO = Path(__file__).resolve().parent.parent
+
+
+def _enum_size() -> int:
+    """Size of the committed BiolinkPredicate enum — read, never hardcoded, because
+    the enum spans two Biolink eras and grows when we adopt a new release's predicate."""
+    import yaml
+    schema = REPO / "src" / "drugmechdb" / "schema" / "biolink_predicates.yaml"
+    return len(yaml.safe_load(schema.read_text())["enums"]["BiolinkPredicate"]["permissible_values"])
 SCRIPTS = REPO / "scripts"
 VENV_PY = REPO / ".venv-py310" / "bin" / "python"
 
@@ -152,7 +160,7 @@ def test_layer3_valid_clean_record_passes(tmp_path):
     code, data, _ = _run("validate_predicates.py", str(f))
     assert code == 0, data
     assert data["failure_count"] == 0
-    assert data["enum_size"] == 67
+    assert data["enum_size"] == _enum_size()   # not a literal: the enum grows with Biolink
 
 
 def test_layer3_rejects_non_enum_predicate(tmp_path):
diff --git a/tests/test_validation.py b/tests/test_validation.py
index 3c6a785..3e19c78 100644
--- a/tests/test_validation.py
+++ b/tests/test_validation.py
@@ -20,6 +20,14 @@
 import pytest
 
 REPO = Path(__file__).resolve().parent.parent
+
+
+def _enum_size() -> int:
+    """Size of the committed BiolinkPredicate enum — read, never hardcoded, because
+    the enum spans two Biolink eras and grows when we adopt a new release's predicate."""
+    import yaml
+    schema = REPO / "src" / "drugmechdb" / "schema" / "biolink_predicates.yaml"
+    return len(yaml.safe_load(schema.read_text())["enums"]["BiolinkPredicate"]["permissible_values"])
 FIXTURES = REPO / "tests" / "fixtures"
 VENV_PY = REPO / ".venv-py310" / "bin" / "python"
 
@@ -86,7 +94,7 @@ def test_layer3_legacy_corpus_passes_exit_criterion():
     exit_code, data = _run("scripts/validate_predicates.py")
     assert exit_code == 0
     assert data["failure_count"] == 0
-    assert data["enum_size"] == 67
+    assert data["enum_size"] == _enum_size()   # not a literal: the enum grows with Biolink
 
 
 def test_layer3_ai_curated_fixture_passes():
diff --git a/web-revamp-mockup/browse.html b/web-revamp-mockup/browse.html
index 990fb38..70b9940 100644
--- a/web-revamp-mockup/browse.html
+++ b/web-revamp-mockup/browse.html
@@ -7,7 +7,7 @@
 <link rel="stylesheet" href="styles.css?v=6">
 </head>
 <body>
-<div class="mock-banner">MOCKUP · DrugMechDB website revamp · sample data, not final — navigation is search-driven (no giant sidebar)</div>
+<div class="mock-banner">LIVE · 135 AI-curated records from 4 agentic curation runs (built by scripts/build_site_data.py) · site design still a mockup</div>
 
 <nav class="nav"><div class="container nav-inner">
   <a class="brand" href="index.html"><span class="mark">D</span>DrugMech<span class="tail">DB</span></a>
@@ -24,6 +24,10 @@
 
     <!-- FACETS -->
     <aside class="facets" data-reveal aria-label="Filters">
+      <div class="facet">
+        <h4>Curation run</h4>
+        <div id="f-run"></div>
+      </div>
       <div class="facet">
         <h4>Disease area</h4>
         <div id="f-area"></div>
@@ -81,11 +85,12 @@ <h4>Path length</h4>
    Wrapped in an async IIFE so live mode (fetch) works with no page changes. */
 (async () => {
 const IDX = await window.DMDB.getIndex();
-const sel = { area:new Set(), type:new Set(), len:new Set() };
+const sel = { run:new Set(), area:new Set(), type:new Set(), len:new Set() };
 
 function counts(key, val){ return IDX.filter(r => key==="type" ? r.types.includes(val) : key==="len" ? lenBucket(r.steps)===val : r[key]===val).length; }
 function lenBucket(s){ return s<=3?"3 or fewer":s<=5?"4–5":"6+"; }
 
+const runs  = [...new Set(IDX.map(r=>r.run))].sort();
 const areas = [...new Set(IDX.map(r=>r.area))].sort();
 const types = [...new Set(IDX.flatMap(r=>r.types))];
 const lens = ["3 or fewer","4–5","6+"];
@@ -94,6 +99,7 @@ <h4>Path length</h4>
   document.getElementById(elId).innerHTML = vals.map(v=>
     `<label><input type="checkbox" data-k="${key}" value="${v}"> ${v} <span class="fc">${counts(key,v)}</span></label>`).join("");
 }
+facet("f-run","run",runs);
 facet("f-area","area",areas);
 facet("f-type","type",types);
 facet("f-len","len",lens);
@@ -116,10 +122,10 @@ <h4>Path length</h4>
 });
 
 /* --- field-boosted, prefix-aware search (zero-dependency) --- */
-const FIELD_BOOST = { drug:10, disease:8, target:4, area:2, id:1 };
+const FIELD_BOOST = { drug:10, disease:8, target:4, area:2, run:2, id:1 };
 const norm = s => (s||"").toLowerCase();
 function termScore(term, r){
-  const fields = { drug:r.drug, disease:r.disease, target:r.target, area:r.area, id:r.id };
+  const fields = { drug:r.drug, disease:r.disease, target:r.target, area:r.area, run:r.run, id:r.record_id||r.id };
   let best = 0;
   for(const f in fields){
     const val = norm(fields[f]); if(!val) continue;
@@ -160,10 +166,11 @@ <h4>Path length</h4>
   const q = norm(document.getElementById("q").value).trim();
   const terms = q.split(/\s+/).filter(Boolean);
   const sortKey = document.getElementById("sort").value;
-  const anyFilter = q || sel.area.size || sel.type.size || sel.len.size || sortKey!=="relevance";
+  const anyFilter = q || sel.run.size || sel.area.size || sel.type.size || sel.len.size || sortKey!=="relevance";
   document.getElementById("clear").hidden = !anyFilter;
 
   let out = IDX.filter(r=>{
+    if(sel.run.size && !sel.run.has(r.run)) return false;
     if(sel.area.size && !sel.area.has(r.area)) return false;
     if(sel.type.size && ![...sel.type].every(t=>r.types.includes(t))) return false;
     if(sel.len.size && !sel.len.has(lenBucket(r.steps))) return false;
@@ -179,9 +186,11 @@ <h4>Path length</h4>
     const preview = r.types.map((t,i)=>
       `<span class="mini-node" style="background:${TYPE_COLOR[t]||'#6b7280'}">${t.replace(/([a-z])([A-Z])/g,'$1 $2')}</span>`+
       (i<r.types.length-1?'<span class="mini-ar">→</span>':'')).join("");
-    return `<a class="result" href="record.html">
+    const src = r.sourced!==undefined ? ` · ${r.sourced}/${r.edges} edges sourced` : "";
+    const flag = r.flagged ? ` · ⚑ ${r.flagged} flagged` : "";
+    return `<a class="result" href="record.html?id=${encodeURIComponent(r.id)}">
       <div class="r-title"><span class="drug">${hl(r.drug,terms)}</span> <span class="ar">↓</span> <span class="disease">${hl(r.disease,terms)}</span></div>
-      <div class="r-meta">${esc(r.area)} · target: ${hl(r.target||'',terms)} · ${r.steps} steps · <span class="mono">${esc(r.id)}</span></div>
+      <div class="r-meta">${esc(r.area)} · target: ${hl(r.target||'',terms)} · ${r.steps} steps${src}${flag} · <span class="mono">${esc(r.record_id||r.id)}</span> · ${esc(r.run||'')}</div>
       <div class="r-path">${preview}</div></a>`;
   }).join("") || `<div class="card" style="padding:40px;text-align:center;color:var(--muted)">No paths match these filters.</div>`;
 }
diff --git a/web-revamp-mockup/data/index.json b/web-revamp-mockup/data/index.json
new file mode 100644
index 0000000..f240bf1
--- /dev/null
+++ b/web-revamp-mockup/data/index.json
@@ -0,0 +1,2614 @@
+[
+  {
+    "id": "opus__P15",
+    "record_id": "P15_DB00787_MESH_D006561",
+    "run": "Opus (model eval)",
+    "drug": "Acyclovir",
+    "disease": "Herpes Simplex",
+    "area": "Infectious disease",
+    "target": "Herpes simplex virus type 1 thymidine kinase",
+    "types": [
+      "Drug",
+      "ChemicalSubstance",
+      "Protein",
+      "BiologicalProcess",
+      "OrganismTaxon",
+      "Disease"
+    ],
+    "steps": 5,
+    "edges": 6,
+    "sourced": 6,
+    "flagged": 0
+  },
+  {
+    "id": "phase3__P15",
+    "record_id": "P15_DB00787_MESH_D006561",
+    "run": "Phase-3 eval",
+    "drug": "Acyclovir",
+    "disease": "Herpes Simplex",
+    "area": "Infectious disease",
+    "target": "HSV-1 thymidine kinase",
+    "types": [
+      "Drug",
+      "Protein",
+      "BiologicalProcess",
+      "OrganismTaxon",
+      "Disease"
+    ],
+    "steps": 4,
+    "edges": 7,
+    "sourced": 7,
+    "flagged": 0
+  },
+  {
+    "id": "sonnet__P15",
+    "record_id": "P15_DB00787_MESH_D006561",
+    "run": "Sonnet (model eval)",
+    "drug": "Acyclovir",
+    "disease": "Herpes Simplex",
+    "area": "Infectious disease",
+    "target": "DNA polymerase (HSV-1 UL30)",
+    "types": [
+      "Drug",
+      "ChemicalSubstance",
+      "Protein",
+      "BiologicalProcess",
+      "Disease"
+    ],
+    "steps": 4,
+    "edges": 4,
+    "sourced": 4,
+    "flagged": 0
+  },
+  {
+    "id": "opus__P25",
+    "record_id": "P25_DB00051_MESH_D011565",
+    "run": "Opus (model eval)",
+    "drug": "Adalimumab",
+    "disease": "Psoriasis",
+    "area": "Immune",
+    "target": "Tumor necrosis factor",
+    "types": [
+      "Drug",
+      "Protein",
+      "BiologicalProcess",
+      "Disease"
+    ],
+    "steps": 3,
+    "edges": 3,
+    "sourced": 3,
+    "flagged": 0
+  },
+  {
+    "id": "phase3__P25",
+    "record_id": "P25_DB00051_MESH_D011565",
+    "run": "Phase-3 eval",
+    "drug": "Adalimumab",
+    "disease": "Psoriasis",
+    "area": "Immune",
+    "target": "Tumor necrosis factor",
+    "types": [
+      "Drug",
+      "Protein",
+      "BiologicalProcess",
+      "Disease"
+    ],
+    "steps": 4,
+    "edges": 4,
+    "sourced": 4,
+    "flagged": 0
+  },
+  {
+    "id": "sonnet__P25",
+    "record_id": "P25_DB00051_MESH_D011565",
+    "run": "Sonnet (model eval)",
+    "drug": "Adalimumab",
+    "disease": "Psoriasis",
+    "area": "Immune",
+    "target": "Tumor necrosis factor",
+    "types": [
+      "Drug",
+      "Protein",
+      "BiologicalProcess",
+      "Disease"
+    ],
+    "steps": 3,
+    "edges": 4,
+    "sourced": 4,
+    "flagged": 0
+  },
+  {
+    "id": "opus__P29",
+    "record_id": "P29_DB00437_MESH_D006073",
+    "run": "Opus (model eval)",
+    "drug": "Allopurinol",
+    "disease": "Gout",
+    "area": "Metabolic",
+    "target": "Xanthine dehydrogenase/oxidase",
+    "types": [
+      "Drug",
+      "Protein",
+      "ChemicalSubstance",
+      "Disease"
+    ],
+    "steps": 4,
+    "edges": 4,
+    "sourced": 4,
+    "flagged": 0
+  },
+  {
+    "id": "phase3__P29",
+    "record_id": "P29_DB00437_MESH_D006073",
+    "run": "Phase-3 eval",
+    "drug": "Allopurinol",
+    "disease": "Gout",
+    "area": "Metabolic",
+    "target": "Xanthine dehydrogenase/oxidase",
+    "types": [
+      "Drug",
+      "Protein",
+      "BiologicalProcess",
+      "ChemicalSubstance",
+      "Disease"
+    ],
+    "steps": 4,
+    "edges": 4,
+    "sourced": 4,
+    "flagged": 0
+  },
+  {
+    "id": "sonnet__P29",
+    "record_id": "P29_DB00437_MESH_D006073",
+    "run": "Sonnet (model eval)",
+    "drug": "Allopurinol",
+    "disease": "Gout",
+    "area": "Metabolic",
+    "target": "Xanthine oxidoreductase",
+    "types": [
+      "Drug",
+      "Protein",
+      "ChemicalSubstance",
+      "Disease"
+    ],
+    "steps": 3,
+    "edges": 3,
+    "sourced": 3,
+    "flagged": 0
+  },
+  {
+    "id": "pilot__DB00009_MESH_D011655_1",
+    "record_id": "DB00009_MESH_D011655_1",
+    "run": "Pilot run",
+    "drug": "alteplase",
+    "disease": "Pulmonary embolism",
+    "area": "Cardiovascular",
+    "target": "Plasminogen",
+    "types": [
+      "Drug",
+      "Protein",
+      "ChemicalSubstance",
+      "Disease"
+    ],
+    "steps": 3,
+    "edges": 3,
+    "sourced": 3,
+    "flagged": 0
+  },
+  {
+    "id": "pilot__DB00009_MESH_D011655_1__r2",
+    "record_id": "DB00009_MESH_D011655_1",
+    "run": "Pilot run",
+    "drug": "alteplase",
+    "disease": "Pulmonary embolism",
+    "area": "Cardiovascular",
+    "target": "Plasminogen",
+    "types": [
+      "Drug",
+      "Protein",
+      "BiologicalProcess",
+      "PhenotypicFeature",
+      "Disease"
+    ],
+    "steps": 4,
+    "edges": 4,
+    "sourced": 4,
+    "flagged": 0
+  },
+  {
+    "id": "pilot__DB00009_MESH_D011655_1__r3",
+    "record_id": "DB00009_MESH_D011655_1",
+    "run": "Pilot run",
+    "drug": "alteplase",
+    "disease": "Pulmonary embolism",
+    "area": "Cardiovascular",
+    "target": "Plasmin",
+    "types": [
+      "Drug",
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+    "edges": 4,
+    "sourced": 4,
+    "flagged": 0
+  },
+  {
+    "id": "opus__P13",
+    "record_id": "P13_DB00512_MESH_D055624",
+    "run": "Opus (model eval)",
+    "drug": "Vancomycin",
+    "disease": "Methicillin-Resistant Staphylococcus aureus Infection",
+    "area": "Infectious disease",
+    "target": "D-alanyl-D-alanine",
+    "types": [
+      "Drug",
+      "ChemicalSubstance",
+      "BiologicalProcess",
+      "OrganismTaxon",
+      "Disease"
+    ],
+    "steps": 4,
+    "edges": 5,
+    "sourced": 5,
+    "flagged": 0
+  },
+  {
+    "id": "sonnet__P13",
+    "record_id": "P13_DB00512_MESH_D055624",
+    "run": "Sonnet (model eval)",
+    "drug": "Vancomycin",
+    "disease": "MRSA Infection",
+    "area": "Infectious disease",
+    "target": "Lipid II",
+    "types": [
+      "Drug",
+      "ChemicalSubstance",
+      "BiologicalProcess",
+      "OrganismTaxon",
+      "Disease"
+    ],
+    "steps": 3,
+    "edges": 4,
+    "sourced": 4,
+    "flagged": 0
+  },
+  {
+    "id": "opus__P31",
+    "record_id": "P31_DB00067_MESH_D006467",
+    "run": "Opus (model eval)",
+    "drug": "Vasopressin",
+    "disease": "Hemophilia A",
+    "area": "Blood",
+    "target": "Vasopressin V2 receptor",
+    "types": [
+      "Drug",
+      "Protein",
+      "BiologicalProcess",
+      "Disease"
+    ],
+    "steps": 5,
+    "edges": 5,
+    "sourced": 5,
+    "flagged": 0
+  },
+  {
+    "id": "sonnet__P31",
+    "record_id": "P31_DB00067_MESH_D006467",
+    "run": "Sonnet (model eval)",
+    "drug": "Vasopressin",
+    "disease": "Hemophilia A",
+    "area": "Blood",
+    "target": "Vasopressin V2 receptor",
+    "types": [
+      "Drug",
+      "Protein",
+      "BiologicalProcess",
+      "Disease"
+    ],
+    "steps": 6,
+    "edges": 6,
+    "sourced": 6,
+    "flagged": 0
+  }
+]
diff --git a/web-revamp-mockup/data/records/opus__P01.json b/web-revamp-mockup/data/records/opus__P01.json
new file mode 100644
index 0000000..41ca050
--- /dev/null
+++ b/web-revamp-mockup/data/records/opus__P01.json
@@ -0,0 +1,219 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P01_DB00945_MESH_D009203",
+    "drug": "Aspirin",
+    "drug_mesh": "MESH:D001241",
+    "drugbank": "DB:DB00945",
+    "disease": "Myocardial infarction",
+    "disease_mesh": "MESH:D009203",
+    "summary": "Aspirin → Prostaglandin G/H synthase 1 (Cyclooxygenase-1, COX-1) → Thromboxane A2 → platelet aggregation → Myocardial infarction"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D001241",
+      "name": "Aspirin",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P23219",
+      "name": "Prostaglandin G/H synthase 1 (Cyclooxygenase-1, COX-1)",
+      "label": "Protein"
+    },
+    {
+      "id": "CHEBI:50124",
+      "name": "Thromboxane A2",
+      "label": "ChemicalSubstance"
+    },
+    {
+      "id": "GO:0070527",
+      "name": "platelet aggregation",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D009203",
+      "name": "Myocardial infarction",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D001241",
+      "target": "UniProt:P23219",
+      "evidence": [
+        {
+          "reference": "PMID:18612540",
+          "snippet": "Aspirin prevents thrombotic events by inhibiting platelet cyclooxygenase-1 (COX-1), thus reducing thromboxane A2 formation and platelet aggregation.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Aspirin irreversibly acetylates and inhibits platelet COX-1.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "The C50T polymorphism of the cyclooxygenase-1 gene and the risk of thrombotic events during low-dose therapy with acetyl salicylic acid.",
+            "authors": [
+              "Clappers N",
+              "van Oijen MG",
+              "Sundaresan S",
+              "Brouwer MA",
+              "Te Morsche RH",
+              "Keuper W",
+              "Peters WH",
+              "Drenth JP",
+              "Verheugt FW"
+            ],
+            "journal": "Thrombosis and haemostasis",
+            "year": "2008",
+            "doi": "10.1160/TH08-03-0172",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:24942808",
+          "snippet": "the acetylation of platelet cyclooxygenase (COX)-1 at serine-529 is the direct mechanism of action of low-dose aspirin",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Reappraisal of the clinical pharmacology of low-dose aspirin by comparing novel direct and traditional indirect biomarkers of drug action.",
+            "authors": [
+              "Patrignani P",
+              "Tacconelli S",
+              "Piazuelo E",
+              "Di Francesco L",
+              "Dovizio M",
+              "Sostres C",
+              "Marcantoni E",
+              "Guillem-Llobat P",
+              "Del Boccio P",
+              "Zucchelli M",
+              "Patrono C",
+              "Lanas A"
+            ],
+            "journal": "Journal of thrombosis and haemostasis : JTH",
+            "year": "2014",
+            "doi": "10.1111/jth.12637",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P23219",
+      "target": "CHEBI:50124",
+      "evidence": [
+        {
+          "reference": "PMID:18612540",
+          "snippet": "Aspirin prevents thrombotic events by inhibiting platelet cyclooxygenase-1 (COX-1), thus reducing thromboxane A2 formation and platelet aggregation.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "COX-1 activity drives thromboxane A2 formation; inhibiting COX-1 reduces thromboxane A2.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "The C50T polymorphism of the cyclooxygenase-1 gene and the risk of thrombotic events during low-dose therapy with acetyl salicylic acid.",
+            "authors": [
+              "Clappers N",
+              "van Oijen MG",
+              "Sundaresan S",
+              "Brouwer MA",
+              "Te Morsche RH",
+              "Keuper W",
+              "Peters WH",
+              "Drenth JP",
+              "Verheugt FW"
+            ],
+            "journal": "Thrombosis and haemostasis",
+            "year": "2008",
+            "doi": "10.1160/TH08-03-0172",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "CHEBI:50124",
+      "target": "GO:0070527",
+      "evidence": [
+        {
+          "reference": "PMID:17073586",
+          "snippet": "Various platelet agonists like adenosine diphosphate (ADP), thrombin and thromboxane A2 (TXA2) activate platelets by acting via their respective surface receptors",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Thromboxane A2 is a platelet agonist that activates platelets to form stable platelet aggregates.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "G-protein dependent platelet signaling--perspectives for therapy.",
+            "authors": [
+              "Shankar H",
+              "Kahner B",
+              "Kunapuli SP"
+            ],
+            "journal": "Current drug targets",
+            "year": "2006",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "contributes to",
+      "source": "GO:0070527",
+      "target": "MESH:D009203",
+      "evidence": [
+        {
+          "reference": "PMID:17073586",
+          "snippet": "Platelet activation and aggregation is an integral component of the pathophysiology that leads to thrombotic and ischemic diseases such as cerebral stroke, peripheral vascular disease and myocardial infarction.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Platelet aggregation drives coronary thrombosis and the pathophysiology leading to myocardial infarction.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "G-protein dependent platelet signaling--perspectives for therapy.",
+            "authors": [
+              "Shankar H",
+              "Kahner B",
+              "Kunapuli SP"
+            ],
+            "journal": "Current drug targets",
+            "year": "2006",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00945",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    }
+  ],
+  "site": {
+    "id": "opus__P01",
+    "record_id": "P01_DB00945_MESH_D009203",
+    "run": "opus",
+    "run_label": "Opus (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/opus/outputs/P01.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/opus__P02.json b/web-revamp-mockup/data/records/opus__P02.json
new file mode 100644
index 0000000..15389b8
--- /dev/null
+++ b/web-revamp-mockup/data/records/opus__P02.json
@@ -0,0 +1,215 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P02_DB01076_MESH_D006937",
+    "drug": "Atorvastatin",
+    "drug_mesh": "MESH:D000069059",
+    "drugbank": "DB:DB01076",
+    "disease": "Hypercholesterolemia",
+    "disease_mesh": "MESH:D006937",
+    "summary": "Atorvastatin → 3-hydroxy-3-methylglutaryl-coenzyme A reductase → Low-density lipoprotein receptor → Low-density lipoprotein cholesterol"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D000069059",
+      "name": "Atorvastatin",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P04035",
+      "name": "3-hydroxy-3-methylglutaryl-coenzyme A reductase",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0006695",
+      "name": "cholesterol biosynthetic process",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "UniProt:P01130",
+      "name": "Low-density lipoprotein receptor",
+      "label": "Protein"
+    },
+    {
+      "id": "MESH:D008078",
+      "name": "Low-density lipoprotein cholesterol",
+      "label": "ChemicalSubstance"
+    },
+    {
+      "id": "MESH:D006937",
+      "name": "Hypercholesterolemia",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D000069059",
+      "target": "UniProt:P04035",
+      "evidence": [
+        {
+          "reference": "PMID:9409231",
+          "snippet": "Inhibition of HMG-CoA reductase by atorvastatin decreases both VLDL and LDL apolipoprotein B production in miniature pigs.",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Inhibition of HMG-CoA reductase by atorvastatin decreases both VLDL and LDL apolipoprotein B production in miniature pigs.",
+            "authors": [
+              "Burnett JR",
+              "Wilcox LJ",
+              "Telford DE",
+              "Kleinstiver SJ",
+              "Barrett PH",
+              "Newton RS",
+              "Huff MW"
+            ],
+            "journal": "Arteriosclerosis, thrombosis, and vascular biology",
+            "year": "1997",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "participates in",
+      "source": "UniProt:P04035",
+      "target": "GO:0006695",
+      "evidence": [
+        {
+          "reference": "PMID:34207840",
+          "snippet": "their ability to inhibit HMG-CoA reductase, the rate-limiting enzyme of de novo cholesterol synthesis",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Comparison of Transcriptomic Profiles of MiaPaCa-2 Pancreatic Cancer Cells Treated with Different Statins.",
+            "authors": [
+              "Rimpelová S",
+              "Kolář M",
+              "Strnad H",
+              "Ruml T",
+              "Vítek L",
+              "Gbelcová H"
+            ],
+            "journal": "Molecules (Basel, Switzerland)",
+            "year": "2021",
+            "doi": "10.3390/molecules26123528",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "decreased",
+      "source": "UniProt:P04035",
+      "target": "UniProt:P01130",
+      "evidence": [
+        {
+          "reference": "PMID:16633945",
+          "snippet": "Through inhibition of HMG-CoA reductase, they restrict the rate-limiting step of cholesterol synthesis, which leads to upregulation of LDL receptors on the cell membrane and thus reduction of atherogenic LDLs.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Inhibiting HMG-CoA reductase leads to upregulation of LDL receptors, i.e. the enzyme's activity negatively regulates LDL receptor expression.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "The role of statins in clinical medicine--LDL--cholesterol lowering and beyond.",
+            "authors": [
+              "Rutishauser J"
+            ],
+            "journal": "Swiss medical weekly",
+            "year": "2006",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "UniProt:P01130",
+      "target": "MESH:D008078",
+      "evidence": [
+        {
+          "reference": "PMID:16633945",
+          "snippet": "which leads to upregulation of LDL receptors on the cell membrane and thus reduction of atherogenic LDLs",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Upregulated LDL receptors clear LDL from plasma, reducing atherogenic LDL cholesterol.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "The role of statins in clinical medicine--LDL--cholesterol lowering and beyond.",
+            "authors": [
+              "Rutishauser J"
+            ],
+            "journal": "Swiss medical weekly",
+            "year": "2006",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "treats",
+      "source": "MESH:D000069059",
+      "target": "MESH:D006937",
+      "evidence": [
+        {
+          "reference": "PMID:34207840",
+          "snippet": "Statins have been widely used for the treatment of hypercholesterolemia due to their ability to inhibit HMG-CoA reductase",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Comparison of Transcriptomic Profiles of MiaPaCa-2 Pancreatic Cancer Cells Treated with Different Statins.",
+            "authors": [
+              "Rimpelová S",
+              "Kolář M",
+              "Strnad H",
+              "Ruml T",
+              "Vítek L",
+              "Gbelcová H"
+            ],
+            "journal": "Molecules (Basel, Switzerland)",
+            "year": "2021",
+            "doi": "10.3390/molecules26123528",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB01076",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    }
+  ],
+  "site": {
+    "id": "opus__P02",
+    "record_id": "P02_DB01076_MESH_D006937",
+    "run": "opus",
+    "run_label": "Opus (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/opus/outputs/P02.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/opus__P03.json b/web-revamp-mockup/data/records/opus__P03.json
new file mode 100644
index 0000000..8237325
--- /dev/null
+++ b/web-revamp-mockup/data/records/opus__P03.json
@@ -0,0 +1,278 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P03_DB00722_MESH_D006973",
+    "drug": "Lisinopril",
+    "drug_mesh": "MESH:D017706",
+    "drugbank": "DB:DB00722",
+    "disease": "Hypertension",
+    "disease_mesh": "MESH:D006973",
+    "summary": "Lisinopril → Angiotensin-converting enzyme → Angiotensin II → Type-1 angiotensin II receptor → vasoconstriction → Hypertension"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D017706",
+      "name": "Lisinopril",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P12821",
+      "name": "Angiotensin-converting enzyme",
+      "label": "Protein"
+    },
+    {
+      "id": "MESH:D000804",
+      "name": "Angiotensin II",
+      "label": "ChemicalSubstance"
+    },
+    {
+      "id": "UniProt:P30556",
+      "name": "Type-1 angiotensin II receptor",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0042310",
+      "name": "vasoconstriction",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D006973",
+      "name": "Hypertension",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D017706",
+      "target": "UniProt:P12821",
+      "evidence": [
+        {
+          "reference": "PMID:33048477",
+          "snippet": "Lisinopril, a highly hydrophilic long-acting angiotensin-converting enzyme inhibitor, is frequently prescribed for the treatment of hypertension and congestive heart failure.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Lisinopril is identified as an angiotensin-converting enzyme inhibitor, i.e. it decreases ACE activity.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Impact of Green Tea Catechin Ingestion on the Pharmacokinetics of Lisinopril in Healthy Volunteers.",
+            "authors": [
+              "Misaka S",
+              "Ono Y",
+              "Uchida A",
+              "Ono T",
+              "Abe O",
+              "Ogata H",
+              "Sato H",
+              "Suzuki M",
+              "Onoue S",
+              "Shikama Y",
+              "Shimomura K"
+            ],
+            "journal": "Clinical and translational science",
+            "year": "2021",
+            "doi": "10.1111/cts.12905",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P12821",
+      "target": "MESH:D000804",
+      "evidence": [
+        {
+          "reference": "PMID:27992423",
+          "snippet": "The angiotensin-I converting enzyme (ACE) plays a central role in the renin-angiotensin system, acting by converting the hormone angiotensin-I to the active peptide angiotensin-II (Ang-II).",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "ACE converts angiotensin-I into angiotensin-II, increasing angiotensin II formation.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Angiotensin Converting Enzyme Regulates Cell Proliferation and Migration.",
+            "authors": [
+              "Alvarenga EC",
+              "Fonseca MC",
+              "Carvalho CC",
+              "Florentino RM",
+              "França A",
+              "Matias E",
+              "Guimarães PB",
+              "Batista C",
+              "Freire V",
+              "Carmona AK",
+              "Pesquero JB",
+              "de Paula AM",
+              "Foureaux G",
+              "Leite MF"
+            ],
+            "journal": "PloS one",
+            "year": "2016",
+            "doi": "10.1371/journal.pone.0165371",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "increased",
+      "source": "MESH:D000804",
+      "target": "UniProt:P30556",
+      "evidence": [
+        {
+          "reference": "PMID:29556787",
+          "snippet": "Ang II and AVP, acting on AT1R and V1aR, respectively, exert vasoconstriction, increase cardiac contractility, stimulate the sympathoadrenal system, and elevate blood pressure.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Angiotensin II acts on AT1 receptors (AT1R), activating the receptor.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Dysregulation of the Renin-Angiotensin System and the Vasopressinergic System Interactions in Cardiovascular Disorders.",
+            "authors": [
+              "Szczepanska-Sadowska E",
+              "Czarzasta K",
+              "Cudnoch-Jedrzejewska A"
+            ],
+            "journal": "Current hypertension reports",
+            "year": "2018",
+            "doi": "10.1007/s11906-018-0823-9",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P30556",
+      "target": "GO:0042310",
+      "evidence": [
+        {
+          "reference": "PMID:29556787",
+          "snippet": "Ang II and AVP, acting on AT1R and V1aR, respectively, exert vasoconstriction, increase cardiac contractility, stimulate the sympathoadrenal system, and elevate blood pressure.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Angiotensin II acting on AT1R exerts vasoconstriction.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Dysregulation of the Renin-Angiotensin System and the Vasopressinergic System Interactions in Cardiovascular Disorders.",
+            "authors": [
+              "Szczepanska-Sadowska E",
+              "Czarzasta K",
+              "Cudnoch-Jedrzejewska A"
+            ],
+            "journal": "Current hypertension reports",
+            "year": "2018",
+            "doi": "10.1007/s11906-018-0823-9",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "causes",
+      "source": "GO:0042310",
+      "target": "MESH:D006973",
+      "evidence": [
+        {
+          "reference": "PMID:33972750",
+          "snippet": "SNX1 impairment increases arterial AT1R expression, leading to increased vasoconstriction and blood pressure.",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "explanation": "Increased vasoconstriction leads to increased blood pressure, i.e. hypertension.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Increased AT1 receptor expression mediates vasoconstriction leading to hypertension in Snx1-/- mice.",
+            "authors": [
+              "Liu C",
+              "Li X",
+              "Fu J",
+              "Chen K",
+              "Liao Q",
+              "Wang J",
+              "Chen C",
+              "Luo H",
+              "Jose PA",
+              "Yang Y",
+              "Yang J",
+              "Zeng C"
+            ],
+            "journal": "Hypertension research : official journal of the Japanese Society of Hypertension",
+            "year": "2021",
+            "doi": "10.1038/s41440-021-00661-x",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "treats",
+      "source": "MESH:D017706",
+      "target": "MESH:D006973",
+      "evidence": [
+        {
+          "reference": "PMID:33048477",
+          "snippet": "Lisinopril, a highly hydrophilic long-acting angiotensin-converting enzyme inhibitor, is frequently prescribed for the treatment of hypertension and congestive heart failure.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Lisinopril is prescribed for the treatment of hypertension.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Impact of Green Tea Catechin Ingestion on the Pharmacokinetics of Lisinopril in Healthy Volunteers.",
+            "authors": [
+              "Misaka S",
+              "Ono Y",
+              "Uchida A",
+              "Ono T",
+              "Abe O",
+              "Ogata H",
+              "Sato H",
+              "Suzuki M",
+              "Onoue S",
+              "Shikama Y",
+              "Shimomura K"
+            ],
+            "journal": "Clinical and translational science",
+            "year": "2021",
+            "doi": "10.1111/cts.12905",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00722",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    }
+  ],
+  "site": {
+    "id": "opus__P03",
+    "record_id": "P03_DB00722_MESH_D006973",
+    "run": "opus",
+    "run_label": "Opus (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/opus/outputs/P03.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/opus__P04.json b/web-revamp-mockup/data/records/opus__P04.json
new file mode 100644
index 0000000..ba21ddd
--- /dev/null
+++ b/web-revamp-mockup/data/records/opus__P04.json
@@ -0,0 +1,179 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P04_DB00264_MESH_D006333",
+    "drug": "metoprolol",
+    "drug_mesh": "MESH:D008790",
+    "drugbank": "DB:DB00264",
+    "disease": "Heart failure",
+    "disease_mesh": "MESH:D006333",
+    "summary": "metoprolol → Beta-1 adrenergic receptor → cardiac muscle cell apoptotic process → Heart failure"
+  },
+  "nodes": [
+    {
+      "id": "DB:DB00264",
+      "name": "metoprolol",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P08588",
+      "name": "Beta-1 adrenergic receptor",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0010659",
+      "name": "cardiac muscle cell apoptotic process",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D006333",
+      "name": "Heart failure",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "DB:DB00264",
+      "target": "UniProt:P08588",
+      "evidence": [
+        {
+          "reference": "PMID:24667281",
+          "snippet": "We tested the efficiency of a combination of oral β1-adrenergic receptor blocker metoprolol and subcutaneous BNP infusion in decompensated heart failure.",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "explanation": "Metoprolol is described as a β1-adrenergic receptor blocker, i.e. it decreases the activity of the β1-adrenergic receptor.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Β-adrenergic blockade combined with subcutaneous B-type natriuretic peptide: a promising approach to reduce ventricular arrhythmia in heart failure?",
+            "authors": [
+              "Thireau J",
+              "Karam S",
+              "Roberge S",
+              "Roussel J",
+              "Aimond F",
+              "Cassan C",
+              "Gac A",
+              "Babuty D",
+              "Le Guennec JY",
+              "Lacampagne A",
+              "Fauconnier J",
+              "Richard S"
+            ],
+            "journal": "Heart (British Cardiac Society)",
+            "year": "2014",
+            "doi": "10.1136/heartjnl-2013-305167",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P08588",
+      "target": "GO:0010659",
+      "evidence": [
+        {
+          "reference": "PMID:21776383",
+          "snippet": "Specifically, β(1)-AR and β(2)-AR coupled to Gαs exert a proapoptotic action, while β(2)-AR coupled to Gi exerts an antiapoptotic action.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "β1-adrenergic receptor (β1-AR) signaling exerts a proapoptotic action on cardiac myocytes, positively regulating cardiac muscle cell apoptosis.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "β-Adrenergic Receptor-Stimulated Cardiac Myocyte Apoptosis: Role of β1 Integrins.",
+            "authors": [
+              "Amin P",
+              "Singh M",
+              "Singh K"
+            ],
+            "journal": "Journal of signal transduction",
+            "year": "2011",
+            "doi": "10.1155/2011/179057",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "contributes to",
+      "source": "GO:0010659",
+      "target": "MESH:D006333",
+      "evidence": [
+        {
+          "reference": "PMID:26746354",
+          "snippet": "Cardiomyocyte apoptosis contributes to ischemic cardiac injury and the development of heart failure.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Cardiomyocyte (cardiac muscle cell) apoptosis contributes to the development of heart failure.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Higenamine protects ischemia/reperfusion induced cardiac injury and myocyte apoptosis through activation of β2-AR/PI3K/AKT signaling pathway.",
+            "authors": [
+              "Wu MP",
+              "Zhang YS",
+              "Zhou QM",
+              "Xiong J",
+              "Dong YR",
+              "Yan C"
+            ],
+            "journal": "Pharmacological research",
+            "year": "2016",
+            "doi": "10.1016/j.phrs.2015.12.032",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "treats",
+      "source": "DB:DB00264",
+      "target": "MESH:D006333",
+      "evidence": [
+        {
+          "reference": "PMID:10376614",
+          "snippet": "Metoprolol CR/XL once daily in addition to optimum standard therapy improved survival.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "In the MERIT-HF randomised controlled trial in chronic heart failure patients, metoprolol CR/XL improved survival, treating heart failure.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Effect of metoprolol CR/XL in chronic heart failure: Metoprolol CR/XL Randomised Intervention Trial in Congestive Heart Failure (MERIT-HF).",
+            "authors": [],
+            "journal": "Lancet (London, England)",
+            "year": "1999",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00264",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    }
+  ],
+  "site": {
+    "id": "opus__P04",
+    "record_id": "P04_DB00264_MESH_D006333",
+    "run": "opus",
+    "run_label": "Opus (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/opus/outputs/P04.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/opus__P05.json b/web-revamp-mockup/data/records/opus__P05.json
new file mode 100644
index 0000000..c85d205
--- /dev/null
+++ b/web-revamp-mockup/data/records/opus__P05.json
@@ -0,0 +1,217 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P05_DB00758_MESH_D020521",
+    "drug": "Clopidogrel",
+    "drug_mesh": "MESH:D000077144",
+    "drugbank": "DB:DB00758",
+    "disease": "Stroke",
+    "disease_mesh": "MESH:D020521",
+    "summary": "Cytochrome P450 2C19 (CYP2C19) → Clopidogrel → P2Y purinoceptor 12 (P2Y12 receptor) → platelet aggregation → blood coagulation → Stroke"
+  },
+  "nodes": [
+    {
+      "id": "DB:DB00758",
+      "name": "Clopidogrel",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P33261",
+      "name": "Cytochrome P450 2C19 (CYP2C19)",
+      "label": "Protein"
+    },
+    {
+      "id": "UniProt:Q9H244",
+      "name": "P2Y purinoceptor 12 (P2Y12 receptor)",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0070527",
+      "name": "platelet aggregation",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "GO:0007596",
+      "name": "blood coagulation",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D020521",
+      "name": "Stroke",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P33261",
+      "target": "DB:DB00758",
+      "evidence": [
+        {
+          "reference": "PMID:41265989",
+          "snippet": "The CYP2C19 enzyme metabolizes clopidogrel, a prodrug, to its active form.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "CYP2C19 activates the clopidogrel prodrug to its active metabolite.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Genetic Determinants of Response to P2Y12 Inhibitors and Clinical Implications.",
+            "authors": [
+              "Cavallari LH",
+              "Coons JC"
+            ],
+            "journal": "Heart failure clinics",
+            "year": "2026",
+            "doi": "10.1016/j.hfc.2025.09.002",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "DB:DB00758",
+      "target": "UniProt:Q9H244",
+      "evidence": [
+        {
+          "reference": "PMID:22221409",
+          "snippet": "Clopidogrel is an antithrombotic prodrug, whose active metabolite inhibits platelet function by irreversibly binding to the platelet receptor for adenosine diphosphate, P2Y(12).",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "The active metabolite of clopidogrel irreversibly binds and inhibits the P2Y12 ADP receptor.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Response variability to clopidogrel: is tailored treatment, based on laboratory testing, the right solution?",
+            "authors": [
+              "Cattaneo M"
+            ],
+            "journal": "Journal of thrombosis and haemostasis : JTH",
+            "year": "2012",
+            "doi": "10.1111/j.1538-7836.2011.04602.x",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "participates in",
+      "source": "UniProt:Q9H244",
+      "target": "GO:0070527",
+      "evidence": [
+        {
+          "reference": "PMID:39940972",
+          "snippet": "A key component of thrombotic events is the activation and aggregation of platelets, of which the P2Y1 and P2Y12 receptors play a crucial role in this process.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "The P2Y12 receptor mediates platelet aggregation.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "P2Y1 and P2Y12 Receptors Mediate Aggregation of Dog and Cat Platelets: A Comparison to Human Platelets.",
+            "authors": [
+              "Sophocleous RA",
+              "Curtis SJ",
+              "Curtis BL",
+              "Ooi L",
+              "Sluyter R"
+            ],
+            "journal": "International journal of molecular sciences",
+            "year": "2025",
+            "doi": "10.3390/ijms26031206",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "GO:0070527",
+      "target": "GO:0007596",
+      "evidence": [
+        {
+          "reference": "PMID:37066902",
+          "snippet": "its surface membrane protein GPIIb/IIIa receptors activate platelets through fibrinogen to form platelet-platelet aggregates, and further activation of active substances such as ADP and TXA2 released by platelet alpha particles, which contribute to the formation of irreversible platelet aggregation.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Platelet aggregation drives thrombus formation and coagulation.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Effect of pathological high shear exposure time on platelet activation and aggregation.",
+            "authors": [
+              "Zhang T",
+              "Huang X",
+              "Gao X",
+              "Liu L",
+              "Chen D",
+              "Huan X",
+              "He C",
+              "Li Y"
+            ],
+            "journal": "Clinical hemorheology and microcirculation",
+            "year": "2023",
+            "doi": "10.3233/CH-221567",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "causes",
+      "source": "GO:0007596",
+      "target": "MESH:D020521",
+      "evidence": [
+        {
+          "reference": "PMID:33039767",
+          "snippet": "cerebellar ischemic lesions secondary to thrombus formation in dolichoectatic basilar artery.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Thrombus formation causes ischemic stroke lesions.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Bilateral Internal Carotid Artery Agenesis and Posterior Circulation Stroke: A Rare Association.",
+            "authors": [
+              "Giragani S",
+              "Kumar Rn K",
+              "Kasireddy AR",
+              "Alwala S"
+            ],
+            "journal": "Journal of stroke and cerebrovascular diseases : the official journal of National Stroke Association",
+            "year": "2020",
+            "doi": "10.1016/j.jstrokecerebrovasdis.2020.105342",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00758",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    }
+  ],
+  "site": {
+    "id": "opus__P05",
+    "record_id": "P05_DB00758_MESH_D020521",
+    "run": "opus",
+    "run_label": "Opus (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/opus/outputs/P05.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/opus__P06.json b/web-revamp-mockup/data/records/opus__P06.json
new file mode 100644
index 0000000..5cca693
--- /dev/null
+++ b/web-revamp-mockup/data/records/opus__P06.json
@@ -0,0 +1,205 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P06_DB00675_MESH_D001943",
+    "drug": "Tamoxifen",
+    "drug_mesh": "MESH:D013629",
+    "drugbank": "DB:DB00675",
+    "disease": "Breast Cancer",
+    "disease_mesh": "MESH:D001943",
+    "summary": "Tamoxifen → Endoxifen → Estrogen receptor alpha → cell population proliferation → Breast Cancer"
+  },
+  "nodes": [
+    {
+      "id": "DB:DB00675",
+      "name": "Tamoxifen",
+      "label": "Drug"
+    },
+    {
+      "id": "CHEBI:71176",
+      "name": "Endoxifen",
+      "label": "ChemicalSubstance"
+    },
+    {
+      "id": "UniProt:P03372",
+      "name": "Estrogen receptor alpha",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0008283",
+      "name": "cell population proliferation",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D001943",
+      "name": "Breast Cancer",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "has metabolite",
+      "source": "DB:DB00675",
+      "target": "CHEBI:71176",
+      "evidence": [
+        {
+          "reference": "PMID:22041137",
+          "snippet": "Tamoxifen requires metabolic activation by cytochrome P450 (CYP) enzymes for formation of active metabolites, 4-hydroxytamoxifen and endoxifen, which have 30- to 100-fold greater affinity to the estrogen receptor and the potency to suppress estrogen-dependent breast cancer cell proliferation.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Tamoxifen is metabolized by CYP enzymes to its active metabolite endoxifen.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Pharmacogenomics of tamoxifen: roles of drug metabolizing enzymes and transporters.",
+            "authors": [
+              "Kiyotani K",
+              "Mushiroda T",
+              "Nakamura Y",
+              "Zembutsu H"
+            ],
+            "journal": "Drug metabolism and pharmacokinetics",
+            "year": "2012",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "CHEBI:71176",
+      "target": "UniProt:P03372",
+      "evidence": [
+        {
+          "reference": "PMID:19244106",
+          "snippet": "endoxifen blocks ERalpha transcriptional activity and inhibits estrogen-induced breast cancer cell proliferation even in the presence of tamoxifen, N-desmethyl-tamoxifen, and 4-hydroxytamoxifen.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Endoxifen is a potent antiestrogen that blocks ERalpha transcriptional activity and targets it for degradation, after binding the receptor with high affinity.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "The tamoxifen metabolite, endoxifen, is a potent antiestrogen that targets estrogen receptor alpha for degradation in breast cancer cells.",
+            "authors": [
+              "Wu X",
+              "Hawse JR",
+              "Subramaniam M",
+              "Goetz MP",
+              "Ingle JN",
+              "Spelsberg TC"
+            ],
+            "journal": "Cancer research",
+            "year": "2009",
+            "doi": "10.1158/0008-5472.CAN-08-3933",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P03372",
+      "target": "GO:0008283",
+      "evidence": [
+        {
+          "reference": "PMID:32130619",
+          "snippet": "G1T48 is a potent and efficacious inhibitor of estrogen-mediated transcription and proliferation in ER-positive breast cancer cells, similar to the pure antiestrogen fulvestrant.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Estrogen receptor signaling mediates (drives) proliferation in ER-positive breast cancer cells; inhibiting ER inhibits proliferation.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "G1T48, an oral selective estrogen receptor degrader, and the CDK4/6 inhibitor lerociclib inhibit tumor growth in animal models of endocrine-resistant breast cancer.",
+            "authors": [
+              "Andreano KJ",
+              "Wardell SE",
+              "Baker JG",
+              "Desautels TK",
+              "Baldi R",
+              "Chao CA",
+              "Heetderks KA",
+              "Bae Y",
+              "Xiong R",
+              "Tonetti DA",
+              "Gutgesell LM",
+              "Zhao J",
+              "Sorrentino JA",
+              "Thompson DA",
+              "Bisi JE",
+              "Strum JC",
+              "Thatcher GRJ",
+              "Norris JD"
+            ],
+            "journal": "Breast cancer research and treatment",
+            "year": "2020",
+            "doi": "10.1007/s10549-020-05575-9",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "participates in",
+      "source": "GO:0008283",
+      "target": "MESH:D001943",
+      "evidence": [
+        {
+          "reference": "PMID:38901667",
+          "snippet": "Knockdown of FOXK2 significantly inhibited breast cancer cell proliferation, migration, anchorage-independent growth, and delayed tumor growth in a xenograft mouse model.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Breast cancer cell proliferation drives tumor growth in breast cancer.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "FOXK2 amplification promotes breast cancer development and chemoresistance.",
+            "authors": [
+              "Yu Y",
+              "Cao WM",
+              "Cheng F",
+              "Shi Z",
+              "Han L",
+              "Yi J",
+              "da Silva EM",
+              "Dopeso H",
+              "Chen H",
+              "Yang J",
+              "Wang X",
+              "Zhang C",
+              "Zhang H"
+            ],
+            "journal": "Cancer letters",
+            "year": "2024",
+            "doi": "10.1016/j.canlet.2024.217074",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00675",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    }
+  ],
+  "site": {
+    "id": "opus__P06",
+    "record_id": "P06_DB00675_MESH_D001943",
+    "run": "opus",
+    "run_label": "Opus (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/opus/outputs/P06.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/opus__P07.json b/web-revamp-mockup/data/records/opus__P07.json
new file mode 100644
index 0000000..5e8310e
--- /dev/null
+++ b/web-revamp-mockup/data/records/opus__P07.json
@@ -0,0 +1,153 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P07_DB00619_MESH_D015464",
+    "drug": "Imatinib",
+    "drug_mesh": "MESH:D000068877",
+    "drugbank": "DB:DB00619",
+    "disease": "Chronic Myeloid Leukemia",
+    "disease_mesh": "MESH:D015464",
+    "summary": "Imatinib → BCR-ABL tyrosine kinase (ABL1) → Chronic Myeloid Leukemia"
+  },
+  "nodes": [
+    {
+      "id": "DB:DB00619",
+      "name": "Imatinib",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P00519",
+      "name": "BCR-ABL tyrosine kinase (ABL1)",
+      "label": "Protein"
+    },
+    {
+      "id": "MESH:D015464",
+      "name": "Chronic Myeloid Leukemia",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "DB:DB00619",
+      "target": "UniProt:P00519",
+      "evidence": [
+        {
+          "reference": "PMID:11831067",
+          "snippet": "STI571 was shown to be a competitive inhibitor at the ATP-binding site of the Bcr-Abl tyrosine kinase",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Imatinib (STI571) is a competitive inhibitor at the ATP-binding site of the BCR-ABL tyrosine kinase, decreasing its activity.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "[Bcr-Abl inhibition as molecular therapy approach in chronic myeloid leukemia].",
+            "authors": [
+              "Buchdunger E"
+            ],
+            "journal": "Medizinische Klinik (Munich, Germany : 1983)",
+            "year": "2002",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:36882601",
+          "snippet": "CML can be effectively treated using tyrosine kinase inhibitors (TKIs) such as imatinib, which prevent phosphorylation of downstream targets by blockade of the BCR-ABL kinase",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Imatinib blocks the BCR-ABL kinase, preventing phosphorylation of downstream targets.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Molecular Mechanisms of Tyrosine Kinase Inhibitor Resistance in Chronic Myeloid Leukemia.",
+            "authors": [
+              "Kaehler M",
+              "Cascorbi I"
+            ],
+            "journal": "Handbook of experimental pharmacology",
+            "year": "2023",
+            "doi": "10.1007/164_2023_639",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "causes",
+      "source": "UniProt:P00519",
+      "target": "MESH:D015464",
+      "evidence": [
+        {
+          "reference": "PMID:36882601",
+          "snippet": "This fusion gene encodes a constitutively active tyrosine kinase, which results in malignant transformation of the cells",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "The constitutively active BCR-ABL tyrosine kinase results in malignant transformation underlying CML.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Molecular Mechanisms of Tyrosine Kinase Inhibitor Resistance in Chronic Myeloid Leukemia.",
+            "authors": [
+              "Kaehler M",
+              "Cascorbi I"
+            ],
+            "journal": "Handbook of experimental pharmacology",
+            "year": "2023",
+            "doi": "10.1007/164_2023_639",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "treats",
+      "source": "DB:DB00619",
+      "target": "MESH:D015464",
+      "evidence": [
+        {
+          "reference": "PMID:36882601",
+          "snippet": "Since 2001, CML can be effectively treated using tyrosine kinase inhibitors (TKIs) such as imatinib",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Imatinib effectively treats CML.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Molecular Mechanisms of Tyrosine Kinase Inhibitor Resistance in Chronic Myeloid Leukemia.",
+            "authors": [
+              "Kaehler M",
+              "Cascorbi I"
+            ],
+            "journal": "Handbook of experimental pharmacology",
+            "year": "2023",
+            "doi": "10.1007/164_2023_639",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00619",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    }
+  ],
+  "site": {
+    "id": "opus__P07",
+    "record_id": "P07_DB00619_MESH_D015464",
+    "run": "opus",
+    "run_label": "Opus (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/opus/outputs/P07.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/opus__P08.json b/web-revamp-mockup/data/records/opus__P08.json
new file mode 100644
index 0000000..d1b38c2
--- /dev/null
+++ b/web-revamp-mockup/data/records/opus__P08.json
@@ -0,0 +1,257 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P08_DB00002_MESH_D015179",
+    "drug": "Cetuximab",
+    "drug_mesh": "MESH:D000068818",
+    "drugbank": "DB:DB00002",
+    "disease": "Colorectal Cancer",
+    "disease_mesh": "MESH:D015179",
+    "summary": "Cetuximab → Epidermal growth factor receptor → MAPK cascade → cell population proliferation → Colorectal Cancer"
+  },
+  "nodes": [
+    {
+      "id": "DB:DB00002",
+      "name": "Cetuximab",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P00533",
+      "name": "Epidermal growth factor receptor",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0000165",
+      "name": "MAPK cascade",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "GO:0008283",
+      "name": "cell population proliferation",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D015179",
+      "name": "Colorectal Cancer",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "physically interacts with",
+      "source": "DB:DB00002",
+      "target": "UniProt:P00533",
+      "evidence": [
+        {
+          "reference": "PMID:19892771",
+          "snippet": "the blocking of EGFR ligand binding using antibodies directed against the extracellular domain of the receptor (e.g., cetuximab)",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Cetuximab is an antibody directed against the extracellular ligand-binding domain of EGFR.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "The role of EGFR inhibition in the treatment of non-small cell lung cancer.",
+            "authors": [
+              "Ray M",
+              "Salgia R",
+              "Vokes EE"
+            ],
+            "journal": "The oncologist",
+            "year": "2009",
+            "doi": "10.1634/theoncologist.2009-0054",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "DB:DB00002",
+      "target": "UniProt:P00533",
+      "evidence": [
+        {
+          "reference": "PMID:18813952",
+          "snippet": "the effect of epidermal growth factor receptor (EGFR) blockade on cell survival and on downstream signalling pathways using the monoclonal antibody cetuximab",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Cetuximab produces EGFR blockade affecting downstream signalling pathways in colon cancer cell lines.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Epidermal growth factor receptor status and persistent activation of Akt and p44/42 MAPK pathways correlate with the effect of cetuximab in head and neck and colon cancer cell lines.",
+            "authors": [
+              "Yamatodani T",
+              "Ekblad L",
+              "Kjellén E",
+              "Johnsson A",
+              "Mineta H",
+              "Wennerberg J"
+            ],
+            "journal": "Journal of cancer research and clinical oncology",
+            "year": "2009",
+            "doi": "10.1007/s00432-008-0475-2",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P00533",
+      "target": "GO:0000165",
+      "evidence": [
+        {
+          "reference": "PMID:33184860",
+          "snippet": "It activates the downstream signal pathway AKT-MTOR and RAS-MAPK, increases proliferation, migration, and invasion",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "EGFR activation drives the downstream RAS-MAPK signaling pathway in colorectal cancer cells.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Morphine promotes tumorigenesis and cetuximab resistance via EGFR signaling activation in human colorectal cancer.",
+            "authors": [
+              "Lu H",
+              "Zhang H",
+              "Weng ML",
+              "Zhang J",
+              "Jiang N",
+              "Cata JP",
+              "Ma D",
+              "Chen WK",
+              "Miao CH"
+            ],
+            "journal": "Journal of cellular physiology",
+            "year": "2021",
+            "doi": "10.1002/jcp.30161",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "GO:0000165",
+      "target": "GO:0008283",
+      "evidence": [
+        {
+          "reference": "PMID:32098826",
+          "snippet": "Reduced NF1 expression permitted sustained signaling through the MAPK pathway to promote cell proliferation in the presence of EGFR inhibition",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Signaling through the MAPK pathway promotes cell proliferation in colorectal cancer cells.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Inactivation of NF1 Promotes Resistance to EGFR Inhibition in KRAS/NRAS/BRAFV600 -Wild-Type Colorectal Cancer.",
+            "authors": [
+              "Georgiou A",
+              "Stewart A",
+              "Cunningham D",
+              "Banerji U",
+              "Whittaker SR"
+            ],
+            "journal": "Molecular cancer research : MCR",
+            "year": "2020",
+            "doi": "10.1158/1541-7786.MCR-19-1201",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "positively correlated with",
+      "source": "GO:0008283",
+      "target": "MESH:D015179",
+      "evidence": [
+        {
+          "reference": "PMID:33184860",
+          "snippet": "treatment with morphine could activate MOR and lead to the promotion of proliferation, migration, and invasion in HCT116 and DLD1 colorectal cancer (CRC) cells",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Proliferation drives the malignant phenotype of colorectal cancer cells.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Morphine promotes tumorigenesis and cetuximab resistance via EGFR signaling activation in human colorectal cancer.",
+            "authors": [
+              "Lu H",
+              "Zhang H",
+              "Weng ML",
+              "Zhang J",
+              "Jiang N",
+              "Cata JP",
+              "Ma D",
+              "Chen WK",
+              "Miao CH"
+            ],
+            "journal": "Journal of cellular physiology",
+            "year": "2021",
+            "doi": "10.1002/jcp.30161",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "treats",
+      "source": "DB:DB00002",
+      "target": "MESH:D015179",
+      "evidence": [
+        {
+          "reference": "PMID:26437179",
+          "snippet": "Anti-EGFR monoclonal antibodies such as cetuximab (CTX) have been approved for the treatment of various malignancies, including colorectal cancer (CRC) with wild-type KRAS",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Cetuximab is an approved anti-EGFR antibody for the treatment of colorectal cancer.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Combination therapy with zoledronic acid and cetuximab effectively suppresses growth of colorectal cancer cells regardless of KRAS status.",
+            "authors": [
+              "Kato J",
+              "Futamura M",
+              "Kanematsu M",
+              "Gaowa S",
+              "Mori R",
+              "Tanahashi T",
+              "Matsuhashi N",
+              "Yoshida K"
+            ],
+            "journal": "International journal of cancer",
+            "year": "2016",
+            "doi": "10.1002/ijc.29881",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00002",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    }
+  ],
+  "site": {
+    "id": "opus__P08",
+    "record_id": "P08_DB00002_MESH_D015179",
+    "run": "opus",
+    "run_label": "Opus (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/opus/outputs/P08.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/opus__P09.json b/web-revamp-mockup/data/records/opus__P09.json
new file mode 100644
index 0000000..cadbd0b
--- /dev/null
+++ b/web-revamp-mockup/data/records/opus__P09.json
@@ -0,0 +1,289 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P09_DB00563_MESH_D054198",
+    "drug": "methotrexate",
+    "drug_mesh": "MESH:D008727",
+    "drugbank": "DB:DB00563",
+    "disease": "Acute lymphoblastic leukemia",
+    "disease_mesh": "MESH:D054198",
+    "summary": "methotrexate → Dihydrofolate reductase → tetrahydrofolate biosynthetic process → purine nucleotide biosynthetic process → DNA biosynthetic process"
+  },
+  "nodes": [
+    {
+      "id": "DB:DB00563",
+      "name": "methotrexate",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P00374",
+      "name": "Dihydrofolate reductase",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0046654",
+      "name": "tetrahydrofolate biosynthetic process",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "GO:0006164",
+      "name": "purine nucleotide biosynthetic process",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "UniProt:P04818",
+      "name": "Thymidylate synthase",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0071897",
+      "name": "DNA biosynthetic process",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D054198",
+      "name": "Acute lymphoblastic leukemia",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "DB:DB00563",
+      "target": "UniProt:P00374",
+      "evidence": [
+        {
+          "reference": "PMID:25136372",
+          "snippet": "MTX competitively inhibits dihydrofolate reductase (DHFR), an enzyme that participates in the tetrahydrofolate synthesis so as to inhibit purine synthesis.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Review of MTX mechanism in childhood ALL treatment.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Treatment of acute lymphoblastic leukemia from traditional chinese medicine.",
+            "authors": [
+              "Hsiao YL",
+              "Chang PC",
+              "Huang HJ",
+              "Kuo CC",
+              "Chen CY"
+            ],
+            "journal": "Evidence-based complementary and alternative medicine : eCAM",
+            "year": "2014",
+            "doi": "10.1155/2014/601064",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "participates in",
+      "source": "UniProt:P00374",
+      "target": "GO:0046654",
+      "evidence": [
+        {
+          "reference": "PMID:25136372",
+          "snippet": "MTX competitively inhibits dihydrofolate reductase (DHFR), an enzyme that participates in the tetrahydrofolate synthesis so as to inhibit purine synthesis.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Treatment of acute lymphoblastic leukemia from traditional chinese medicine.",
+            "authors": [
+              "Hsiao YL",
+              "Chang PC",
+              "Huang HJ",
+              "Kuo CC",
+              "Chen CY"
+            ],
+            "journal": "Evidence-based complementary and alternative medicine : eCAM",
+            "year": "2014",
+            "doi": "10.1155/2014/601064",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "GO:0046654",
+      "target": "GO:0006164",
+      "evidence": [
+        {
+          "reference": "PMID:25136372",
+          "snippet": "MTX competitively inhibits dihydrofolate reductase (DHFR), an enzyme that participates in the tetrahydrofolate synthesis so as to inhibit purine synthesis.",
+          "supports": "SUPPORT",
+          "explanation": "Tetrahydrofolate synthesis is required for purine synthesis; inhibiting DHFR (and thus tetrahydrofolate synthesis) inhibits purine synthesis.",
+          "evidence_source": "OTHER",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Treatment of acute lymphoblastic leukemia from traditional chinese medicine.",
+            "authors": [
+              "Hsiao YL",
+              "Chang PC",
+              "Huang HJ",
+              "Kuo CC",
+              "Chen CY"
+            ],
+            "journal": "Evidence-based complementary and alternative medicine : eCAM",
+            "year": "2014",
+            "doi": "10.1155/2014/601064",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "GO:0006164",
+      "target": "GO:0071897",
+      "evidence": [
+        {
+          "reference": "PMID:25136372",
+          "snippet": "Therefore, MTX can inhibit the synthesis of DNA.",
+          "supports": "SUPPORT",
+          "explanation": "Purine synthesis supplies nucleotides for DNA synthesis; MTX-mediated inhibition of purine synthesis contributes to inhibition of DNA synthesis.",
+          "evidence_source": "OTHER",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Treatment of acute lymphoblastic leukemia from traditional chinese medicine.",
+            "authors": [
+              "Hsiao YL",
+              "Chang PC",
+              "Huang HJ",
+              "Kuo CC",
+              "Chen CY"
+            ],
+            "journal": "Evidence-based complementary and alternative medicine : eCAM",
+            "year": "2014",
+            "doi": "10.1155/2014/601064",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "DB:DB00563",
+      "target": "UniProt:P04818",
+      "evidence": [
+        {
+          "reference": "PMID:25136372",
+          "snippet": "its downstream metabolite methotrexate polyglutamates (MTX-PGs) inhibit the thymidylate synthase (TS).",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Treatment of acute lymphoblastic leukemia from traditional chinese medicine.",
+            "authors": [
+              "Hsiao YL",
+              "Chang PC",
+              "Huang HJ",
+              "Kuo CC",
+              "Chen CY"
+            ],
+            "journal": "Evidence-based complementary and alternative medicine : eCAM",
+            "year": "2014",
+            "doi": "10.1155/2014/601064",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P04818",
+      "target": "GO:0071897",
+      "evidence": [
+        {
+          "reference": "PMID:26273805",
+          "snippet": "These drugs inhibit DNA synthesis by targeting the enzymes dihydrofolate reductase (DHFR) and/or thymidylate synthase (TYMS).",
+          "supports": "SUPPORT",
+          "explanation": "Thymidylate synthase activity is required for DNA synthesis; antifolate inhibition of TYMS inhibits DNA synthesis.",
+          "evidence_source": "IN_VITRO",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Antithymidylate resistance enables transgene selection and cell survival for T cells in the presence of 5-fluorouracil and antifolates.",
+            "authors": [
+              "Rushworth D",
+              "Alpert A",
+              "Santana-Carrero R",
+              "Olivares S",
+              "Spencer D",
+              "Cooper LJ"
+            ],
+            "journal": "Gene therapy",
+            "year": "2016",
+            "doi": "10.1038/gt.2015.88",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "treats",
+      "source": "DB:DB00563",
+      "target": "MESH:D054198",
+      "evidence": [
+        {
+          "reference": "PMID:25136372",
+          "snippet": "In particular, for the treatment of childhood acute lymphoblastic leukemia, it had significant effect.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Treatment of acute lymphoblastic leukemia from traditional chinese medicine.",
+            "authors": [
+              "Hsiao YL",
+              "Chang PC",
+              "Huang HJ",
+              "Kuo CC",
+              "Chen CY"
+            ],
+            "journal": "Evidence-based complementary and alternative medicine : eCAM",
+            "year": "2014",
+            "doi": "10.1155/2014/601064",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00563",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    }
+  ],
+  "site": {
+    "id": "opus__P09",
+    "record_id": "P09_DB00563_MESH_D054198",
+    "run": "opus",
+    "run_label": "Opus (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/opus/outputs/P09.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/opus__P10.json b/web-revamp-mockup/data/records/opus__P10.json
new file mode 100644
index 0000000..1cb6747
--- /dev/null
+++ b/web-revamp-mockup/data/records/opus__P10.json
@@ -0,0 +1,253 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P10_DB00072_MESH_D001943",
+    "drug": "Trastuzumab",
+    "drug_mesh": "MESH:D000068878",
+    "drugbank": "DB:DB00072",
+    "disease": "HER2-positive Breast Cancer",
+    "disease_mesh": "MESH:D001943",
+    "summary": "Trastuzumab → Receptor tyrosine-protein kinase erbB-2 (HER2) → phosphatidylinositol 3-kinase/protein kinase B signal transduction → cell population proliferation"
+  },
+  "nodes": [
+    {
+      "id": "DB:DB00072",
+      "name": "Trastuzumab",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P04626",
+      "name": "Receptor tyrosine-protein kinase erbB-2 (HER2)",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0043491",
+      "name": "phosphatidylinositol 3-kinase/protein kinase B signal transduction",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "GO:0008283",
+      "name": "cell population proliferation",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D001943",
+      "name": "HER2-positive Breast Cancer",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "DB:DB00072",
+      "target": "UniProt:P04626",
+      "evidence": [
+        {
+          "reference": "PMID:14617784",
+          "snippet": "Exposure of the cells to trastuzumab down-regulated the levels of HER2 and reduced phosphorylation levels of Akt and MAPK in MCF7HER2 cells",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Trastuzumab, directed against the HER2 extracellular domain (PMID:24462377), down-regulates HER2 and reduces downstream phosphorylation.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Sensitization of breast cancer cells to radiation by trastuzumab.",
+            "authors": [
+              "Liang K",
+              "Lu Y",
+              "Jin W",
+              "Ang KK",
+              "Milas L",
+              "Fan Z"
+            ],
+            "journal": "Molecular cancer therapeutics",
+            "year": "2003",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P04626",
+      "target": "GO:0043491",
+      "evidence": [
+        {
+          "reference": "PMID:14617784",
+          "snippet": "MCF7HER2 cells showed increased phosphorylation of at least two important HER2 downstream molecules, protein kinase B/Akt and mitogen-activated protein kinase (MAPK)",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "High HER2 increases phosphorylation of downstream Akt, indicating HER2 positively regulates PI3K/Akt signaling.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Sensitization of breast cancer cells to radiation by trastuzumab.",
+            "authors": [
+              "Liang K",
+              "Lu Y",
+              "Jin W",
+              "Ang KK",
+              "Milas L",
+              "Fan Z"
+            ],
+            "journal": "Molecular cancer therapeutics",
+            "year": "2003",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "DB:DB00072",
+      "target": "GO:0043491",
+      "evidence": [
+        {
+          "reference": "PMID:14617784",
+          "snippet": "Exposure of the cells to trastuzumab down-regulated the levels of HER2 and reduced phosphorylation levels of Akt and MAPK in MCF7HER2 cells",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Trastuzumab reduces Akt phosphorylation, decreasing PI3K/Akt signal transduction.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Sensitization of breast cancer cells to radiation by trastuzumab.",
+            "authors": [
+              "Liang K",
+              "Lu Y",
+              "Jin W",
+              "Ang KK",
+              "Milas L",
+              "Fan Z"
+            ],
+            "journal": "Molecular cancer therapeutics",
+            "year": "2003",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "GO:0043491",
+      "target": "GO:0008283",
+      "evidence": [
+        {
+          "reference": "PMID:33795719",
+          "snippet": "enhancing DNA synthesis through the PI3K-AKT signaling in human breast cancer T47D cells",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "PI3K-AKT signaling promotes DNA synthesis and proliferation of breast cancer cells.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Nectin-4 and p95-ErbB2 cooperatively regulate Hippo signaling-dependent SOX2 gene expression, enhancing anchorage-independent T47D cell proliferation.",
+            "authors": [
+              "Kedashiro S",
+              "Kameyama T",
+              "Mizutani K",
+              "Takai Y"
+            ],
+            "journal": "Scientific reports",
+            "year": "2021",
+            "doi": "10.1038/s41598-021-86437-2",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "decreased",
+      "source": "DB:DB00072",
+      "target": "GO:0008283",
+      "evidence": [
+        {
+          "reference": "PMID:14617784",
+          "snippet": "trastuzumab (Herceptin), a humanized monoclonal antibody that may inhibit breast cancer cell proliferation",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Trastuzumab inhibits breast cancer cell proliferation.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Sensitization of breast cancer cells to radiation by trastuzumab.",
+            "authors": [
+              "Liang K",
+              "Lu Y",
+              "Jin W",
+              "Ang KK",
+              "Milas L",
+              "Fan Z"
+            ],
+            "journal": "Molecular cancer therapeutics",
+            "year": "2003",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "treats",
+      "source": "DB:DB00072",
+      "target": "MESH:D001943",
+      "evidence": [
+        {
+          "reference": "PMID:24462377",
+          "snippet": "Two compounds have been registered for HER-2-positive tumour treatment: trastuzumab, a humanised antibody directed against the HER-2 extracellular domain",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Trastuzumab is registered for treatment of HER2-positive tumours/breast cancer.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Resistance to human epidermal growth factor receptor type 2-targeted therapies.",
+            "authors": [
+              "Thery JC",
+              "Spano JP",
+              "Azria D",
+              "Raymond E",
+              "Penault Llorca F"
+            ],
+            "journal": "European journal of cancer (Oxford, England : 1990)",
+            "year": "2014",
+            "doi": "10.1016/j.ejca.2014.01.003",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00072",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    }
+  ],
+  "site": {
+    "id": "opus__P10",
+    "record_id": "P10_DB00072_MESH_D001943",
+    "run": "opus",
+    "run_label": "Opus (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/opus/outputs/P10.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/opus__P11.json b/web-revamp-mockup/data/records/opus__P11.json
new file mode 100644
index 0000000..4b91113
--- /dev/null
+++ b/web-revamp-mockup/data/records/opus__P11.json
@@ -0,0 +1,209 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P11_DB01045_MESH_D014397",
+    "drug": "Rifampicin",
+    "drug_mesh": "MESH:D012293",
+    "drugbank": "DB:DB01045",
+    "disease": "Pulmonary Tuberculosis",
+    "disease_mesh": "MESH:D014397",
+    "summary": "Rifampicin → DNA-templated transcription → Mycobacterium tuberculosis → Pulmonary Tuberculosis"
+  },
+  "nodes": [
+    {
+      "id": "DB:DB01045",
+      "name": "Rifampicin",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P9WGY9",
+      "name": "DNA-directed RNA polymerase subunit beta (RpoB)",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0006351",
+      "name": "DNA-templated transcription",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "NCBITaxon:1773",
+      "name": "Mycobacterium tuberculosis",
+      "label": "OrganismTaxon"
+    },
+    {
+      "id": "MESH:D014397",
+      "name": "Pulmonary Tuberculosis",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "DB:DB01045",
+      "target": "UniProt:P9WGY9",
+      "evidence": [
+        {
+          "reference": "PMID:25288092",
+          "snippet": "rifampin (RIF) binds to the beta subunit of the RNA polymerase (RpoB) of Mycobacterium tuberculosis",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Rifampin binds the RpoB beta subunit, inhibiting the RNA polymerase enzyme.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Rifampin induces hydroxyl radical formation in Mycobacterium tuberculosis.",
+            "authors": [
+              "Piccaro G",
+              "Pietraforte D",
+              "Giannoni F",
+              "Mustazzolu A",
+              "Fattorini L"
+            ],
+            "journal": "Antimicrobial agents and chemotherapy",
+            "year": "2014",
+            "doi": "10.1128/AAC.03169-14",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "DB:DB01045",
+      "target": "GO:0006351",
+      "evidence": [
+        {
+          "reference": "PMID:31269464",
+          "snippet": "The antimicrobial activity of RIF is attributed to its ability to inhibit transcription by binding to the β subunit of bacterial RNA polymerase (encoded by rpoB).",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Unveiling the molecular basis for pleiotropy in selected rif mutants of Escherichia coli: Possible role for Tyrosine in the Rif binding pocket and fast movement of RNA polymerase.",
+            "authors": [
+              "Karthik M",
+              "Meenakshi S",
+              "Munavar MH"
+            ],
+            "journal": "Gene",
+            "year": "2019",
+            "doi": "10.1016/j.gene.2019.143951",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "occurs in",
+      "source": "GO:0006351",
+      "target": "NCBITaxon:1773",
+      "evidence": [
+        {
+          "reference": "PMID:25288092",
+          "snippet": "rifampin (RIF) binds to the beta subunit of the RNA polymerase (RpoB) of Mycobacterium tuberculosis",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "RpoB-containing RNA polymerase performs DNA-templated transcription in M. tuberculosis.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Rifampin induces hydroxyl radical formation in Mycobacterium tuberculosis.",
+            "authors": [
+              "Piccaro G",
+              "Pietraforte D",
+              "Giannoni F",
+              "Mustazzolu A",
+              "Fattorini L"
+            ],
+            "journal": "Antimicrobial agents and chemotherapy",
+            "year": "2014",
+            "doi": "10.1128/AAC.03169-14",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "decreased",
+      "source": "DB:DB01045",
+      "target": "NCBITaxon:1773",
+      "evidence": [
+        {
+          "reference": "PMID:25288092",
+          "snippet": "M. tuberculosis killing by RIF stimulated an increase in the rate of formation of the CPH radical",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Rifampin induces hydroxyl radical formation in Mycobacterium tuberculosis.",
+            "authors": [
+              "Piccaro G",
+              "Pietraforte D",
+              "Giannoni F",
+              "Mustazzolu A",
+              "Fattorini L"
+            ],
+            "journal": "Antimicrobial agents and chemotherapy",
+            "year": "2014",
+            "doi": "10.1128/AAC.03169-14",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "causes",
+      "source": "NCBITaxon:1773",
+      "target": "MESH:D014397",
+      "evidence": [
+        {
+          "reference": "PMID:40916634",
+          "snippet": "Tuberculosis, caused by Mycobacterium tuberculosis, persists as a significant worldwide health issue",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Unveiling the molecular toxicity of Isoniazid and Rifampicin in tuberculosis therapy: emerging insights and therapeutic strategies.",
+            "authors": [
+              "Shivaji P",
+              "Prince SE"
+            ],
+            "journal": "Toxicology mechanisms and methods",
+            "year": "2025",
+            "doi": "10.1080/15376516.2025.2554918",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB01045",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    }
+  ],
+  "site": {
+    "id": "opus__P11",
+    "record_id": "P11_DB01045_MESH_D014397",
+    "run": "opus",
+    "run_label": "Opus (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/opus/outputs/P11.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/opus__P12.json b/web-revamp-mockup/data/records/opus__P12.json
new file mode 100644
index 0000000..13e3b86
--- /dev/null
+++ b/web-revamp-mockup/data/records/opus__P12.json
@@ -0,0 +1,207 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P12_DB00951_MESH_D014397",
+    "drug": "Isoniazid",
+    "drug_mesh": "MESH:D007538",
+    "drugbank": "DB:DB00951",
+    "disease": "Pulmonary Tuberculosis",
+    "disease_mesh": "MESH:D014397",
+    "summary": "Isoniazid → Enoyl-[acyl-carrier-protein] reductase [NADH] InhA → mycolic acid biosynthetic process"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D007538",
+      "name": "Isoniazid",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P9WIE5",
+      "name": "Catalase-peroxidase KatG",
+      "label": "Protein"
+    },
+    {
+      "id": "UniProt:P9WGR1",
+      "name": "Enoyl-[acyl-carrier-protein] reductase [NADH] InhA",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0071768",
+      "name": "mycolic acid biosynthetic process",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D014397",
+      "name": "Pulmonary Tuberculosis",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "increased",
+      "source": "MESH:D007538",
+      "target": "UniProt:P9WIE5",
+      "evidence": [
+        {
+          "reference": "PMID:26104204",
+          "snippet": "INH is activated by the catalase-peroxidase KatG, while ETH is activated by the monooxygenase EthA.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "KatG activates the isoniazid prodrug into its reactive species.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Resistance to Isoniazid and Ethionamide in Mycobacterium tuberculosis: Genes, Mutations, and Causalities.",
+            "authors": [
+              "Vilchèze C",
+              "Jacobs WR"
+            ],
+            "journal": "Microbiology spectrum",
+            "year": "2014",
+            "doi": "10.1128/microbiolspec.MGM2-0014-2013",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D007538",
+      "target": "UniProt:P9WGR1",
+      "evidence": [
+        {
+          "reference": "PMID:26104204",
+          "snippet": "The resulting active species reacts with NAD+ to form an INH-NAD or ETH-NAD adduct, which inhibits the enoyl ACP reductase InhA, leading to mycolic acid biosynthesis inhibition and mycobacterial cell death.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "The INH-NAD adduct inhibits InhA enoyl-ACP reductase.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Resistance to Isoniazid and Ethionamide in Mycobacterium tuberculosis: Genes, Mutations, and Causalities.",
+            "authors": [
+              "Vilchèze C",
+              "Jacobs WR"
+            ],
+            "journal": "Microbiology spectrum",
+            "year": "2014",
+            "doi": "10.1128/microbiolspec.MGM2-0014-2013",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "participates in",
+      "source": "UniProt:P9WGR1",
+      "target": "GO:0071768",
+      "evidence": [
+        {
+          "reference": "PMID:16842188",
+          "snippet": "InhA is a member of the mycobacterial Type II fatty acid biosynthesis system, which elongates acyl fatty acid precursors of mycolic acids.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "InhA participates in mycolic acid biosynthesis.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Slow-onset inhibition of 2-trans-enoyl-ACP (CoA) reductase from Mycobacterium tuberculosis by an inorganic complex.",
+            "authors": [
+              "Oliveira JS",
+              "de Sousa EH",
+              "de Souza ON",
+              "Moreira IS",
+              "Santos DS",
+              "Basso LA"
+            ],
+            "journal": "Current pharmaceutical design",
+            "year": "2006",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "disrupts",
+      "source": "MESH:D007538",
+      "target": "GO:0071768",
+      "evidence": [
+        {
+          "reference": "PMID:26104204",
+          "snippet": "which inhibits the enoyl ACP reductase InhA, leading to mycolic acid biosynthesis inhibition and mycobacterial cell death",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Inhibition of InhA by isoniazid disrupts mycolic acid biosynthesis.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Resistance to Isoniazid and Ethionamide in Mycobacterium tuberculosis: Genes, Mutations, and Causalities.",
+            "authors": [
+              "Vilchèze C",
+              "Jacobs WR"
+            ],
+            "journal": "Microbiology spectrum",
+            "year": "2014",
+            "doi": "10.1128/microbiolspec.MGM2-0014-2013",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "treats",
+      "source": "MESH:D007538",
+      "target": "MESH:D014397",
+      "evidence": [
+        {
+          "reference": "PMID:37476899",
+          "snippet": "isoniazid (H) is an important first-line agent in tuberculosis (TB) treatment",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Isoniazid is a first-line agent in the treatment of pulmonary tuberculosis.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Evaluation of treatment regimens and long-term clinical outcomes in patients with isoniazid-resistant pulmonary tuberculosis: a 5-year follow-up.",
+            "authors": [
+              "Aslan AF",
+              "Ortaköylü MG",
+              "Bağcı BA",
+              "Toprak S"
+            ],
+            "journal": "Turkish journal of medical sciences",
+            "year": "2023",
+            "doi": "10.55730/1300-0144.5639",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00951",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    }
+  ],
+  "site": {
+    "id": "opus__P12",
+    "record_id": "P12_DB00951_MESH_D014397",
+    "run": "opus",
+    "run_label": "Opus (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/opus/outputs/P12.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/opus__P13.json b/web-revamp-mockup/data/records/opus__P13.json
new file mode 100644
index 0000000..068dea2
--- /dev/null
+++ b/web-revamp-mockup/data/records/opus__P13.json
@@ -0,0 +1,212 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P13_DB00512_MESH_D055624",
+    "drug": "Vancomycin",
+    "drug_mesh": "MESH:D014640",
+    "drugbank": "DB:DB00512",
+    "disease": "Methicillin-Resistant Staphylococcus aureus Infection",
+    "disease_mesh": "MESH:D055624",
+    "summary": "Vancomycin → D-alanyl-D-alanine → peptidoglycan biosynthetic process → Staphylococcus aureus → Methicillin-Resistant Staphylococcus aureus Infection"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D014640",
+      "name": "Vancomycin",
+      "label": "Drug"
+    },
+    {
+      "id": "CHEBI:73835",
+      "name": "D-alanyl-D-alanine",
+      "label": "ChemicalSubstance"
+    },
+    {
+      "id": "GO:0009252",
+      "name": "peptidoglycan biosynthetic process",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "NCBITaxon:1280",
+      "name": "Staphylococcus aureus",
+      "label": "OrganismTaxon"
+    },
+    {
+      "id": "MESH:D055624",
+      "name": "Methicillin-Resistant Staphylococcus aureus Infection",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "physically interacts with",
+      "source": "MESH:D014640",
+      "target": "CHEBI:73835",
+      "evidence": [
+        {
+          "reference": "PMID:27663982",
+          "snippet": "This is achieved primarily through binding to the d-alanyl-d-alanine terminus of the lipid II bacterial cell-wall precursor, preventing cross-linking of the peptidoglycan layer.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Approved Glycopeptide Antibacterial Drugs: Mechanism of Action and Resistance.",
+            "authors": [
+              "Zeng D",
+              "Debabov D",
+              "Hartsell TL",
+              "Cano RJ",
+              "Adams S",
+              "Schuyler JA",
+              "McMillan R",
+              "Pace JL"
+            ],
+            "journal": "Cold Spring Harbor perspectives in medicine",
+            "year": "2016",
+            "doi": "10.1101/cshperspect.a026989",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "disrupts",
+      "source": "CHEBI:73835",
+      "target": "GO:0009252",
+      "evidence": [
+        {
+          "reference": "PMID:24685455",
+          "snippet": "bind to d-alanyl-d-alanine stem termini on the peptidoglycan precursors of the cell wall. This binding inhibits cross-linking between the peptides and subsequently prevents cell wall synthesis.",
+          "supports": "SUPPORT",
+          "evidence_source": "COMPUTATIONAL",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Molecular modeling of Gram-positive bacteria peptidoglycan layer, selected glycopeptide antibiotics and vancomycin derivatives modified with sugar moieties.",
+            "authors": [
+              "Ślusarz R",
+              "Szulc M",
+              "Madaj J"
+            ],
+            "journal": "Carbohydrate research",
+            "year": "2014",
+            "doi": "10.1016/j.carres.2014.02.002",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "occurs in",
+      "source": "GO:0009252",
+      "target": "NCBITaxon:1280",
+      "evidence": [
+        {
+          "reference": "PMID:17316058",
+          "snippet": "The clinically important vancomycin antibiotic inhibits the growth of pathogens such as Staphylococcus aureus by blocking cell wall synthesis through specific recognition of nascent peptidoglycan terminating in D-Ala-D-Ala.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Single-molecule force spectroscopy and imaging of the vancomycin/D-Ala-D-Ala interaction.",
+            "authors": [
+              "Gilbert Y",
+              "Deghorain M",
+              "Wang L",
+              "Xu B",
+              "Pollheimer PD",
+              "Gruber HJ",
+              "Errington J",
+              "Hallet B",
+              "Haulot X",
+              "Verbelen C",
+              "Hols P",
+              "Dufrêne YF"
+            ],
+            "journal": "Nano letters",
+            "year": "2007",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "causes",
+      "source": "NCBITaxon:1280",
+      "target": "MESH:D055624",
+      "evidence": [
+        {
+          "reference": "PMID:34508427",
+          "snippet": "Staphylococcus aureus is both a frequent commensal and a leading cause of endocarditis, bacteremia, osteomyelitis and skin and soft tissue infections and device-related infections.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Methicillin-resistant Staphylococcus aureus in Nepal.",
+            "authors": [
+              "Shrestha LB",
+              "Syangtan G",
+              "Basnet A",
+              "Acharya KP",
+              "Chand AB",
+              "Pokhrel K"
+            ],
+            "journal": "JNMA; journal of the Nepal Medical Association",
+            "year": "2021",
+            "doi": "10.31729/jnma.6251",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "treats",
+      "source": "MESH:D014640",
+      "target": "MESH:D055624",
+      "evidence": [
+        {
+          "reference": "PMID:17724497",
+          "snippet": "vancomycin, the gold standard in the treatment of MRSA",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Dalbavancin: a review.",
+            "authors": [
+              "Scheinfeld N"
+            ],
+            "journal": "Drugs of today (Barcelona, Spain : 1998)",
+            "year": "2007",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00512",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    }
+  ],
+  "site": {
+    "id": "opus__P13",
+    "record_id": "P13_DB00512_MESH_D055624",
+    "run": "opus",
+    "run_label": "Opus (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/opus/outputs/P13.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/opus__P14.json b/web-revamp-mockup/data/records/opus__P14.json
new file mode 100644
index 0000000..95d787c
--- /dev/null
+++ b/web-revamp-mockup/data/records/opus__P14.json
@@ -0,0 +1,188 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P14_DB00198_MESH_D007251",
+    "drug": "Oseltamivir",
+    "drug_mesh": "MESH:D053139",
+    "drugbank": "DB:DB00198",
+    "disease": "Influenza",
+    "disease_mesh": "MESH:D007251",
+    "summary": "Oseltamivir → Oseltamivir carboxylate → Neuraminidase → viral release from host cell → Influenza"
+  },
+  "nodes": [
+    {
+      "id": "DB:DB00198",
+      "name": "Oseltamivir",
+      "label": "Drug"
+    },
+    {
+      "id": "MESH:C111791",
+      "name": "Oseltamivir carboxylate",
+      "label": "ChemicalSubstance"
+    },
+    {
+      "id": "UniProt:P03468",
+      "name": "Neuraminidase",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0019076",
+      "name": "viral release from host cell",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D007251",
+      "name": "Influenza",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "has metabolite",
+      "source": "DB:DB00198",
+      "target": "MESH:C111791",
+      "evidence": [
+        {
+          "reference": "PMID:23436258",
+          "snippet": "Oseltamivir is a prodrug for the active carboxylate metabolite.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Pharmacokinetic properties of anti-influenza neuraminidase inhibitors.",
+            "authors": [
+              "Chairat K",
+              "Tarning J",
+              "White NJ",
+              "Lindegardh N"
+            ],
+            "journal": "Journal of clinical pharmacology",
+            "year": "2013",
+            "doi": "10.1177/0091270012440280",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:C111791",
+      "target": "UniProt:P03468",
+      "evidence": [
+        {
+          "reference": "PMID:39151273",
+          "snippet": "citrus-derived flavanones displayed comparable or even more potent in vitro inhibitory activity than oseltamivir carboxylate against NA",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Oseltamivir carboxylate is the reference neuraminidase (NA) inhibitor; the comparison establishes its inhibitory activity against NA.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Citrus-derived flavanones as neuraminidase inhibitors: In vitro and in silico study.",
+            "authors": [
+              "Chen P",
+              "Li C",
+              "Chen L",
+              "Li X",
+              "Zhu S"
+            ],
+            "journal": "European journal of medicinal chemistry",
+            "year": "2024",
+            "doi": "10.1016/j.ejmech.2024.116758",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "participates in",
+      "source": "UniProt:P03468",
+      "target": "GO:0019076",
+      "evidence": [
+        {
+          "reference": "PMID:36382275",
+          "snippet": "Neuraminidase, an exo-glycosidase displayed on the surface of influenza virions, is responsible for the release of the virions and their spread in the infected host.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Ultrasensitive chemiluminescent neuraminidase probe for rapid screening and identification of small-molecules with antiviral activity against influenza A virus in mammalian cells.",
+            "authors": [
+              "Shelef O",
+              "Gutkin S",
+              "Feder D",
+              "Ben-Bassat A",
+              "Mandelboim M",
+              "Haitin Y",
+              "Ben-Tal N",
+              "Bacharach E",
+              "Shabat D"
+            ],
+            "journal": "Chemical science",
+            "year": "2022",
+            "doi": "10.1039/d2sc03460c",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "contributes to",
+      "source": "GO:0019076",
+      "target": "MESH:D007251",
+      "evidence": [
+        {
+          "reference": "PMID:36382275",
+          "snippet": "Neuraminidase, an exo-glycosidase displayed on the surface of influenza virions, is responsible for the release of the virions and their spread in the infected host.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Release and spread of virions in the infected host drives propagation of influenza A virus infection.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Ultrasensitive chemiluminescent neuraminidase probe for rapid screening and identification of small-molecules with antiviral activity against influenza A virus in mammalian cells.",
+            "authors": [
+              "Shelef O",
+              "Gutkin S",
+              "Feder D",
+              "Ben-Bassat A",
+              "Mandelboim M",
+              "Haitin Y",
+              "Ben-Tal N",
+              "Bacharach E",
+              "Shabat D"
+            ],
+            "journal": "Chemical science",
+            "year": "2022",
+            "doi": "10.1039/d2sc03460c",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00198",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    }
+  ],
+  "site": {
+    "id": "opus__P14",
+    "record_id": "P14_DB00198_MESH_D007251",
+    "run": "opus",
+    "run_label": "Opus (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/opus/outputs/P14.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/opus__P15.json b/web-revamp-mockup/data/records/opus__P15.json
new file mode 100644
index 0000000..b33236d
--- /dev/null
+++ b/web-revamp-mockup/data/records/opus__P15.json
@@ -0,0 +1,238 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P15_DB00787_MESH_D006561",
+    "drug": "Acyclovir",
+    "drug_mesh": "MESH:D000212",
+    "drugbank": "DB:DB00787",
+    "disease": "Herpes Simplex",
+    "disease_mesh": "MESH:D006561",
+    "summary": "Acyclovir → Acyclovir triphosphate → Herpes simplex virus type 1 DNA polymerase → DNA replication → Human herpesvirus 1 → Herpes Simplex"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D000212",
+      "name": "Acyclovir",
+      "label": "Drug"
+    },
+    {
+      "id": "MESH:C025643",
+      "name": "Acyclovir triphosphate",
+      "label": "ChemicalSubstance"
+    },
+    {
+      "id": "UniProt:P03176",
+      "name": "Herpes simplex virus type 1 thymidine kinase",
+      "label": "Protein"
+    },
+    {
+      "id": "UniProt:P04293",
+      "name": "Herpes simplex virus type 1 DNA polymerase",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0006260",
+      "name": "DNA replication",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "NCBITaxon:10298",
+      "name": "Human herpesvirus 1",
+      "label": "OrganismTaxon"
+    },
+    {
+      "id": "MESH:D006561",
+      "name": "Herpes Simplex",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "has metabolite",
+      "source": "MESH:D000212",
+      "target": "MESH:C025643",
+      "evidence": [
+        {
+          "reference": "PMID:6313600",
+          "snippet": "Acyclovir monophosphate is subsequently converted to a triphosphate which is a more potent inhibitor of herpes virus DNA polymerases than of cellular DNA polymerases.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "The biochemistry and mechanism of action of acyclovir.",
+            "authors": [
+              "Elion GB"
+            ],
+            "journal": "The Journal of antimicrobial chemotherapy",
+            "year": "1983",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "participates in",
+      "source": "UniProt:P03176",
+      "target": "GO:0006260",
+      "evidence": [
+        {
+          "reference": "PMID:6313600",
+          "snippet": "This selectivity is due to the initial activation of the drug by phosphorylation by a herpes virus-specified thymidine kinase.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "The biochemistry and mechanism of action of acyclovir.",
+            "authors": [
+              "Elion GB"
+            ],
+            "journal": "The Journal of antimicrobial chemotherapy",
+            "year": "1983",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:C025643",
+      "target": "UniProt:P04293",
+      "evidence": [
+        {
+          "reference": "PMID:6291456",
+          "snippet": "HSV-1 DNA polymerase was the most sensitive to inhibition by acyclovir triphosphate (ACVTP).",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Mode of action of acyclovir triphosphate on herpesviral and cellular DNA polymerases.",
+            "authors": [
+              "Allaudeen HS",
+              "Descamps J",
+              "Sehgal RK"
+            ],
+            "journal": "Antiviral research",
+            "year": "1982",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "participates in",
+      "source": "UniProt:P04293",
+      "target": "GO:0006260",
+      "evidence": [
+        {
+          "reference": "PMID:6291456",
+          "snippet": "it appeared to act as a chain terminator in DNA replication catalyzed by either HSV-1 DNA polymerase or DNA polymerase alpha",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Mode of action of acyclovir triphosphate on herpesviral and cellular DNA polymerases.",
+            "authors": [
+              "Allaudeen HS",
+              "Descamps J",
+              "Sehgal RK"
+            ],
+            "journal": "Antiviral research",
+            "year": "1982",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "occurs in",
+      "source": "GO:0006260",
+      "target": "NCBITaxon:10298",
+      "evidence": [
+        {
+          "reference": "PMID:6291456",
+          "snippet": "it appeared to act as a chain terminator in DNA replication catalyzed by either HSV-1 DNA polymerase or DNA polymerase alpha",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Mode of action of acyclovir triphosphate on herpesviral and cellular DNA polymerases.",
+            "authors": [
+              "Allaudeen HS",
+              "Descamps J",
+              "Sehgal RK"
+            ],
+            "journal": "Antiviral research",
+            "year": "1982",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "causes",
+      "source": "NCBITaxon:10298",
+      "target": "MESH:D006561",
+      "evidence": [
+        {
+          "reference": "PMID:23389903",
+          "snippet": "Herpes simplex virus (HSV) is a significant human pathogen causing mucocutaneous lesions primarily in the oral or genital mucosa.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Peptide inhibitors against herpes simplex virus infections.",
+            "authors": [
+              "Galdiero S",
+              "Falanga A",
+              "Tarallo R",
+              "Russo L",
+              "Galdiero E",
+              "Cantisani M",
+              "Morelli G",
+              "Galdiero M"
+            ],
+            "journal": "Journal of peptide science : an official publication of the European Peptide Society",
+            "year": "2013",
+            "doi": "10.1002/psc.2489",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00787",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    }
+  ],
+  "site": {
+    "id": "opus__P15",
+    "record_id": "P15_DB00787_MESH_D006561",
+    "run": "opus",
+    "run_label": "Opus (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/opus/outputs/P15.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/opus__P16.json b/web-revamp-mockup/data/records/opus__P16.json
new file mode 100644
index 0000000..1ea9348
--- /dev/null
+++ b/web-revamp-mockup/data/records/opus__P16.json
@@ -0,0 +1,203 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P16_DB01235_MESH_D010300",
+    "drug": "Levodopa",
+    "drug_mesh": "MESH:D007980",
+    "drugbank": "DB:DB01235",
+    "disease": "Parkinson's Disease",
+    "disease_mesh": "MESH:D010300",
+    "summary": "Levodopa → Dopamine → Striatum"
+  },
+  "nodes": [
+    {
+      "id": "DB:DB01235",
+      "name": "Levodopa",
+      "label": "Drug"
+    },
+    {
+      "id": "MESH:D004298",
+      "name": "Dopamine",
+      "label": "ChemicalSubstance"
+    },
+    {
+      "id": "UBERON:0002435",
+      "name": "Striatum",
+      "label": "GrossAnatomicalStructure"
+    },
+    {
+      "id": "MESH:D010300",
+      "name": "Parkinson's Disease",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "has metabolite",
+      "source": "DB:DB01235",
+      "target": "MESH:D004298",
+      "evidence": [
+        {
+          "reference": "PMID:23020119",
+          "snippet": "L-Dopa is converted to DA",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Aromatic L-amino acid decarboxylase converts levodopa to dopamine after it crosses the blood-brain barrier.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Protective effects of L-dopa and carbidopa combined treatments on human catecholaminergic cells.",
+            "authors": [
+              "Colamartino M",
+              "Padua L",
+              "Meneghini C",
+              "Leone S",
+              "Cornetta T",
+              "Testa A",
+              "Cozzi R"
+            ],
+            "journal": "DNA and cell biology",
+            "year": "2012",
+            "doi": "10.1089/dna.2011.1546",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:11215754",
+          "snippet": "Aromatic L-amino acid decarboxylase (AAAD) converts L-DOPA to dopamine.",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "SCH 23390 enhances exogenous L-DOPA decarboxylation in nigrostriatal neurons.",
+            "authors": [
+              "Neff NH",
+              "Wemlinger TA",
+              "Hadjiconstantinou M"
+            ],
+            "journal": "Journal of neural transmission (Vienna, Austria : 1996)",
+            "year": "2000",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "located in",
+      "source": "MESH:D004298",
+      "target": "UBERON:0002435",
+      "evidence": [
+        {
+          "reference": "PMID:23020119",
+          "snippet": "decreased levels of the neurotransmitter dopamine (DA) in the striatum of the brain",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Dopamine acts in the striatum; PD reflects its deficiency there, which levodopa-derived dopamine replenishes.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Protective effects of L-dopa and carbidopa combined treatments on human catecholaminergic cells.",
+            "authors": [
+              "Colamartino M",
+              "Padua L",
+              "Meneghini C",
+              "Leone S",
+              "Cornetta T",
+              "Testa A",
+              "Cozzi R"
+            ],
+            "journal": "DNA and cell biology",
+            "year": "2012",
+            "doi": "10.1089/dna.2011.1546",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "located in",
+      "source": "MESH:D010300",
+      "target": "UBERON:0002435",
+      "evidence": [
+        {
+          "reference": "PMID:29971496",
+          "snippet": "Unilateral arm UPDRS bradykinesia scores were associated with DAT uptake in the contralateral putamen.",
+          "supports": "PARTIAL",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Parkinsonian motor deficits localize to nigrostriatal dopamine loss in the striatum (putamen).",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Impaired finger dexterity and nigrostriatal dopamine loss in Parkinson's disease.",
+            "authors": [
+              "Lee SH",
+              "Lee MJ",
+              "Lyoo CH",
+              "Cho H",
+              "Lee MS"
+            ],
+            "journal": "Journal of neural transmission (Vienna, Austria : 1996)",
+            "year": "2018",
+            "doi": "10.1007/s00702-018-1901-5",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "treats",
+      "source": "DB:DB01235",
+      "target": "MESH:D010300",
+      "evidence": [
+        {
+          "reference": "PMID:23020119",
+          "snippet": "Levodopa (L-Dopa) crosses the blood-brain barrier and its administration replenishes the loss of DA in dopaminergic neurons in PD patients.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "By replenishing striatal dopamine, levodopa is the cornerstone treatment for Parkinson's disease.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Protective effects of L-dopa and carbidopa combined treatments on human catecholaminergic cells.",
+            "authors": [
+              "Colamartino M",
+              "Padua L",
+              "Meneghini C",
+              "Leone S",
+              "Cornetta T",
+              "Testa A",
+              "Cozzi R"
+            ],
+            "journal": "DNA and cell biology",
+            "year": "2012",
+            "doi": "10.1089/dna.2011.1546",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB01235",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    }
+  ],
+  "site": {
+    "id": "opus__P16",
+    "record_id": "P16_DB01235_MESH_D010300",
+    "run": "opus",
+    "run_label": "Opus (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/opus/outputs/P16.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/opus__P17.json b/web-revamp-mockup/data/records/opus__P17.json
new file mode 100644
index 0000000..1375542
--- /dev/null
+++ b/web-revamp-mockup/data/records/opus__P17.json
@@ -0,0 +1,161 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P17_DB00472_MESH_D003865",
+    "drug": "fluoxetine",
+    "drug_mesh": "MESH:D005473",
+    "drugbank": "DB:DB00472",
+    "disease": "Major Depressive Disorder",
+    "disease_mesh": "MESH:D003865",
+    "summary": "Fluoxetine → Sodium-dependent serotonin transporter → Serotonin → Major Depressive Disorder"
+  },
+  "nodes": [
+    {
+      "id": "DB:DB00472",
+      "name": "Fluoxetine",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P31645",
+      "name": "Sodium-dependent serotonin transporter",
+      "label": "Protein"
+    },
+    {
+      "id": "MESH:D012701",
+      "name": "Serotonin",
+      "label": "ChemicalSubstance"
+    },
+    {
+      "id": "MESH:D003865",
+      "name": "Major Depressive Disorder",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "DB:DB00472",
+      "target": "UniProt:P31645",
+      "evidence": [
+        {
+          "reference": "PMID:20739712",
+          "snippet": "Fluoxetine acts primarily as an inhibitor of the serotonin reuptake transporter (SERT) to block the removal of serotonin from the synaptic cleft, thereby enhancing serotonin signals.",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "explanation": "Fluoxetine inhibits (decreases the activity of) the serotonin transporter SERT.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "A genetic survey of fluoxetine action on synaptic transmission in Caenorhabditis elegans.",
+            "authors": [
+              "Kullyev A",
+              "Dempsey CM",
+              "Miller S",
+              "Kuan CJ",
+              "Hapiak VM",
+              "Komuniecki RW",
+              "Griffin CT",
+              "Sze JY"
+            ],
+            "journal": "Genetics",
+            "year": "2010",
+            "doi": "10.1534/genetics.110.118877",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "decreased",
+      "source": "UniProt:P31645",
+      "target": "MESH:D012701",
+      "evidence": [
+        {
+          "reference": "PMID:20739712",
+          "snippet": "Fluoxetine acts primarily as an inhibitor of the serotonin reuptake transporter (SERT) to block the removal of serotonin from the synaptic cleft, thereby enhancing serotonin signals.",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "explanation": "SERT removes serotonin from the synaptic cleft, lowering extracellular serotonin; inhibiting it enhances serotonin signals.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "A genetic survey of fluoxetine action on synaptic transmission in Caenorhabditis elegans.",
+            "authors": [
+              "Kullyev A",
+              "Dempsey CM",
+              "Miller S",
+              "Kuan CJ",
+              "Hapiak VM",
+              "Komuniecki RW",
+              "Griffin CT",
+              "Sze JY"
+            ],
+            "journal": "Genetics",
+            "year": "2010",
+            "doi": "10.1534/genetics.110.118877",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "treats",
+      "source": "MESH:D012701",
+      "target": "MESH:D003865",
+      "evidence": [
+        {
+          "reference": "PMID:33845072",
+          "snippet": "Selective serotonin reuptake inhibitors (SSRIs) are designed to improve mood by raising extracellular serotonin levels through the blockade of the serotonin transporter.",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "explanation": "Raised extracellular serotonin levels mediate the mood-improving (antidepressant) effect of SSRIs in major depressive disorder.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "MicroRNA-34a regulates 5-HT2C expression in dorsal raphe and contributes to the anti-depressant-like effect of fluoxetine.",
+            "authors": [
+              "Lo Iacono L",
+              "Ielpo D",
+              "Parisi C",
+              "Napoli G",
+              "Accoto A",
+              "Di Segni M",
+              "Babicola L",
+              "D'Addario SL",
+              "Guzzo SM",
+              "Pascucci T",
+              "Ventura R",
+              "Andolina D"
+            ],
+            "journal": "Neuropharmacology",
+            "year": "2021",
+            "doi": "10.1016/j.neuropharm.2021.108559",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00472",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    }
+  ],
+  "site": {
+    "id": "opus__P17",
+    "record_id": "P17_DB00472_MESH_D003865",
+    "run": "opus",
+    "run_label": "Opus (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/opus/outputs/P17.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/opus__P18.json b/web-revamp-mockup/data/records/opus__P18.json
new file mode 100644
index 0000000..b472985
--- /dev/null
+++ b/web-revamp-mockup/data/records/opus__P18.json
@@ -0,0 +1,227 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P18_DB01356_MESH_D001714",
+    "drug": "Lithium",
+    "drug_mesh": "MESH:D008094",
+    "drugbank": "DB:DB01356",
+    "disease": "Bipolar Disorder",
+    "disease_mesh": "MESH:D001714",
+    "summary": "Lithium → Glycogen synthase kinase-3 beta → Catenin beta-1 → apoptotic process → Bipolar Disorder"
+  },
+  "nodes": [
+    {
+      "id": "DB:DB01356",
+      "name": "Lithium",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P49841",
+      "name": "Glycogen synthase kinase-3 beta",
+      "label": "Protein"
+    },
+    {
+      "id": "UniProt:P35222",
+      "name": "Catenin beta-1",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0006915",
+      "name": "apoptotic process",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D001714",
+      "name": "Bipolar Disorder",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "DB:DB01356",
+      "target": "UniProt:P49841",
+      "evidence": [
+        {
+          "reference": "PMID:8710892",
+          "snippet": "Lithium potently inhibits GSK-3 beta activity (Ki = 2 mM), but is not a general inhibitor of other protein kinases.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Lithium directly inhibits GSK-3 beta enzymatic activity.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "A molecular mechanism for the effect of lithium on development.",
+            "authors": [
+              "Klein PS",
+              "Melton DA"
+            ],
+            "journal": "Proceedings of the National Academy of Sciences of the United States of America",
+            "year": "1996",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:29232923",
+          "snippet": "the direct inhibition on glycogen synthase kinase 3β",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Review identifying direct GSK-3 beta inhibition as a mechanism of lithium in bipolar disorder.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "An Oldie but Goodie: Lithium in the Treatment of Bipolar Disorder through Neuroprotective and Neurotrophic Mechanisms.",
+            "authors": [
+              "Won E",
+              "Kim YK"
+            ],
+            "journal": "International journal of molecular sciences",
+            "year": "2017",
+            "doi": "10.3390/ijms18122679",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "decreased",
+      "source": "UniProt:P49841",
+      "target": "UniProt:P35222",
+      "evidence": [
+        {
+          "reference": "PMID:37011015",
+          "snippet": "Glycogen Synthase Kinase 3β (GSK3 β) phosphorylates and degrades catenin via the downstream Wnt signalling pathway",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "GSK-3 beta phosphorylates and degrades beta-catenin; its inhibition stabilizes beta-catenin.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Evaluation of wound healing active principles in the transdermal patch formulated with crude bio wastes and plant extracts against GSK-3 beta - an in silico study.",
+            "authors": [
+              "Subbukutti V",
+              "Sailatha E",
+              "Gunasekaran S",
+              "Manibalan S",
+              "Uma Devi KJ",
+              "Bhuvaneshwari K",
+              "Suvedha R"
+            ],
+            "journal": "Journal of biomolecular structure & dynamics",
+            "year": "2024",
+            "doi": "10.1080/07391102.2023.2194424",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:30336136",
+          "snippet": "lithium chloride inhibited glycogen synthase kinase-3β activation, which on one hand, suppressed downstream CRMP-2/NR2B, thus diminishing the excitotoxic index level; and on the other, stabilized β-catenin",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "explanation": "GSK-3 beta inhibition by lithium stabilizes beta-catenin.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "The neuroprotective effect of lithium chloride on cognitive impairment through glycogen synthase kinase-3β inhibition in intracerebral hemorrhage rats.",
+            "authors": [
+              "Liu Z",
+              "Li R",
+              "Jiang C",
+              "Zhao S",
+              "Li W",
+              "Tang X"
+            ],
+            "journal": "European journal of pharmacology",
+            "year": "2018",
+            "doi": "10.1016/j.ejphar.2018.10.019",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "decreased",
+      "source": "UniProt:P35222",
+      "target": "GO:0006915",
+      "evidence": [
+        {
+          "reference": "PMID:30336136",
+          "snippet": "stabilized β-catenin, thus modulating its downstream apoptosis-related factors such as NF-κB, Bcl-2 and Bax",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "explanation": "Stabilized beta-catenin modulates apoptosis-related factors and is paralleled by decreased neuronal death.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "The neuroprotective effect of lithium chloride on cognitive impairment through glycogen synthase kinase-3β inhibition in intracerebral hemorrhage rats.",
+            "authors": [
+              "Liu Z",
+              "Li R",
+              "Jiang C",
+              "Zhao S",
+              "Li W",
+              "Tang X"
+            ],
+            "journal": "European journal of pharmacology",
+            "year": "2018",
+            "doi": "10.1016/j.ejphar.2018.10.019",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "contributes to",
+      "source": "GO:0006915",
+      "target": "MESH:D001714",
+      "evidence": [
+        {
+          "reference": "PMID:34357564",
+          "snippet": "Li+'s neuroprotective properties are related to its modulation of nerve growth factors, inflammation, mitochondrial function, oxidative stress, and programmed cell death mechanisms such as autophagy and apoptosis.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Apoptotic (programmed cell death) mechanisms underlie the neuroprotective action of lithium relevant to bipolar disorder pathology.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Lithium as a Neuroprotective Agent for Bipolar Disorder: An Overview.",
+            "authors": [
+              "Ochoa ELM"
+            ],
+            "journal": "Cellular and molecular neurobiology",
+            "year": "2022",
+            "doi": "10.1007/s10571-021-01129-9",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB01356",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    }
+  ],
+  "site": {
+    "id": "opus__P18",
+    "record_id": "P18_DB01356_MESH_D001714",
+    "run": "opus",
+    "run_label": "Opus (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/opus/outputs/P18.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/opus__P19.json b/web-revamp-mockup/data/records/opus__P19.json
new file mode 100644
index 0000000..cf7b3fc
--- /dev/null
+++ b/web-revamp-mockup/data/records/opus__P19.json
@@ -0,0 +1,236 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P19_DB00996_MESH_D004827",
+    "drug": "Gabapentin",
+    "drug_mesh": "MESH:D000077306",
+    "drugbank": "DB:DB00996",
+    "disease": "Epilepsy",
+    "disease_mesh": "MESH:D004827",
+    "summary": "Gabapentin → Voltage-dependent calcium channel subunit alpha-2/delta-1 (CACNA2D1) → calcium ion import → neurotransmitter secretion → Epilepsy"
+  },
+  "nodes": [
+    {
+      "id": "DB:DB00996",
+      "name": "Gabapentin",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P54289",
+      "name": "Voltage-dependent calcium channel subunit alpha-2/delta-1 (CACNA2D1)",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0070509",
+      "name": "calcium ion import",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "GO:0007269",
+      "name": "neurotransmitter secretion",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D004827",
+      "name": "Epilepsy",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "DB:DB00996",
+      "target": "UniProt:P54289",
+      "evidence": [
+        {
+          "reference": "PMID:24668130",
+          "snippet": "its binding to neuronal alpha-2/delta subunits of voltage-gated calcium channels (VGCCs) is critical to its mechanism of action",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Gabapentin's anti-nausea and anti-emetic effects: a review.",
+            "authors": [
+              "Guttuso T"
+            ],
+            "journal": "Experimental brain research",
+            "year": "2014",
+            "doi": "10.1007/s00221-014-3905-1",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:17222465",
+          "snippet": "Binding of these ligands to the alpha2delta subunit is considered to explain their usefulness in treating several clinical disorders, including epilepsy",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Ca2+ channel alpha2delta ligands: novel modulators of neurotransmission.",
+            "authors": [
+              "Dooley DJ",
+              "Taylor CP",
+              "Donevan S",
+              "Feltner D"
+            ],
+            "journal": "Trends in pharmacological sciences",
+            "year": "2007",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "decreased",
+      "source": "UniProt:P54289",
+      "target": "GO:0070509",
+      "evidence": [
+        {
+          "reference": "PMID:32351366",
+          "snippet": "they exhibit a high affinity for the α2δ-1 and α2δ-2 subunits of voltage-activated calcium channels, wherein binding of gabapentinoids inhibits cellular calcium influx and attenuates neurotransmission",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Pregabalin as a Pain Therapeutic: Beyond Calcium Channels.",
+            "authors": [
+              "Alles SRA",
+              "Cain SM",
+              "Snutch TP"
+            ],
+            "journal": "Frontiers in cellular neuroscience",
+            "year": "2020",
+            "doi": "10.3389/fncel.2020.00083",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "GO:0070509",
+      "target": "GO:0007269",
+      "evidence": [
+        {
+          "reference": "PMID:32351366",
+          "snippet": "binding of gabapentinoids inhibits cellular calcium influx and attenuates neurotransmission",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Pregabalin as a Pain Therapeutic: Beyond Calcium Channels.",
+            "authors": [
+              "Alles SRA",
+              "Cain SM",
+              "Snutch TP"
+            ],
+            "journal": "Frontiers in cellular neuroscience",
+            "year": "2020",
+            "doi": "10.3389/fncel.2020.00083",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:17222465",
+          "snippet": "This modulation is characterized by a reduction of the excessive neurotransmitter release that is observed in certain neurological and psychiatric disorders",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Ca2+ channel alpha2delta ligands: novel modulators of neurotransmission.",
+            "authors": [
+              "Dooley DJ",
+              "Taylor CP",
+              "Donevan S",
+              "Feltner D"
+            ],
+            "journal": "Trends in pharmacological sciences",
+            "year": "2007",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "treats",
+      "source": "GO:0007269",
+      "target": "MESH:D004827",
+      "evidence": [
+        {
+          "reference": "PMID:32351366",
+          "snippet": "gabapentin and pregabalin are effective at suppressing seizures and subsequently approved as a new class of antiepileptic therapy for partial-onset epilepsy",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Pregabalin as a Pain Therapeutic: Beyond Calcium Channels.",
+            "authors": [
+              "Alles SRA",
+              "Cain SM",
+              "Snutch TP"
+            ],
+            "journal": "Frontiers in cellular neuroscience",
+            "year": "2020",
+            "doi": "10.3389/fncel.2020.00083",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:17126531",
+          "snippet": "possibly accounting for its actions in vivo to reduce neuronal excitability and seizures",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Pharmacology and mechanism of action of pregabalin: the calcium channel alpha2-delta (alpha2-delta) subunit as a target for antiepileptic drug discovery.",
+            "authors": [
+              "Taylor CP",
+              "Angelotti T",
+              "Fauman E"
+            ],
+            "journal": "Epilepsy research",
+            "year": "2007",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00996",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    }
+  ],
+  "site": {
+    "id": "opus__P19",
+    "record_id": "P19_DB00996_MESH_D004827",
+    "run": "opus",
+    "run_label": "Opus (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/opus/outputs/P19.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/opus__P20.json b/web-revamp-mockup/data/records/opus__P20.json
new file mode 100644
index 0000000..e174700
--- /dev/null
+++ b/web-revamp-mockup/data/records/opus__P20.json
@@ -0,0 +1,178 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P20_DB00843_MESH_D000544",
+    "drug": "donepezil",
+    "drug_mesh": "MESH:D000077856",
+    "drugbank": "DB:DB00843",
+    "disease": "Alzheimer's Disease",
+    "disease_mesh": "MESH:D000544",
+    "summary": "donepezil → Acetylcholinesterase → Acetylcholine → chemical synaptic transmission → Alzheimer's Disease"
+  },
+  "nodes": [
+    {
+      "id": "DB:DB00843",
+      "name": "donepezil",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P22303",
+      "name": "Acetylcholinesterase",
+      "label": "Protein"
+    },
+    {
+      "id": "MESH:D000109",
+      "name": "Acetylcholine",
+      "label": "ChemicalSubstance"
+    },
+    {
+      "id": "GO:0007268",
+      "name": "chemical synaptic transmission",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D000544",
+      "name": "Alzheimer's Disease",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "DB:DB00843",
+      "target": "UniProt:P22303",
+      "evidence": [
+        {
+          "reference": "PMID:23215841",
+          "snippet": "donepezil, a highly selective (IC(50) = 6.7 nM) centrally acting reversible acetylcholinesterase inhibitor that has been approved by FDA for treating cognitive deficit states such as in Alzheimer's disease",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Donepezil is a reversible acetylcholinesterase inhibitor, decreasing the enzyme's activity.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Assessing the prospect of donepezil in improving cognitive impairment in patients with schizophrenia.",
+            "authors": [
+              "Thakurathi N",
+              "Vincenzi B",
+              "Henderson DC"
+            ],
+            "journal": "Expert opinion on investigational drugs",
+            "year": "2013",
+            "doi": "10.1517/13543784.2013.750650",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "decreased",
+      "source": "UniProt:P22303",
+      "target": "MESH:D000109",
+      "evidence": [
+        {
+          "reference": "PMID:19877295",
+          "snippet": "Enzymatic hydrolysis of acetylcholine in the synaptic cleft is fast and quickly metabolizes to choline and acetate by acetylcholinesterase.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Acetylcholinesterase hydrolyzes acetylcholine; its inhibition by donepezil therefore raises acetylcholine levels.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Quantification of acetylcholine, an essential neurotransmitter, in brain microdialysis samples by liquid chromatography mass spectrometry.",
+            "authors": [
+              "Nirogi R",
+              "Mudigonda K",
+              "Kandikere V",
+              "Ponnamaneni R"
+            ],
+            "journal": "Biomedical chromatography : BMC",
+            "year": "2010",
+            "doi": "10.1002/bmc.1347",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "MESH:D000109",
+      "target": "GO:0007268",
+      "evidence": [
+        {
+          "reference": "PMID:28777299",
+          "snippet": "Acetylcholine (ACh), an ubiquitous mediator substance broadly expressed in nature, acts as neurotransmitter in cholinergic synapses, generating specific communications",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Acetylcholine acts as a neurotransmitter at cholinergic synapses, mediating synaptic transmission.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Ultrafast and Slow Cholinergic Transmission. Different Involvement of Acetylcholinesterase Molecular Forms.",
+            "authors": [
+              "Dunant Y",
+              "Gisiger V"
+            ],
+            "journal": "Molecules (Basel, Switzerland)",
+            "year": "2017",
+            "doi": "10.3390/molecules22081300",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "treats",
+      "source": "GO:0007268",
+      "target": "MESH:D000544",
+      "evidence": [
+        {
+          "reference": "PMID:40097131",
+          "snippet": "Cholinesterase inhibitors, such as donepezil and rivastigmine, increase acetylcholine (ACh) levels to enhance cognitive function in individuals with mild to moderate AD.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Restoring cholinergic synaptic transmission via increased acetylcholine enhances cognitive function in Alzheimer's disease.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Exploring Alzheimer's disease treatment: Established therapies and novel strategies for future care.",
+            "authors": [
+              "Soni U",
+              "Singh K",
+              "Jain D",
+              "Pujari R"
+            ],
+            "journal": "European journal of pharmacology",
+            "year": "2025",
+            "doi": "10.1016/j.ejphar.2025.177520",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00843",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    }
+  ],
+  "site": {
+    "id": "opus__P20",
+    "record_id": "P20_DB00843_MESH_D000544",
+    "run": "opus",
+    "run_label": "Opus (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/opus/outputs/P20.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/opus__P21.json b/web-revamp-mockup/data/records/opus__P21.json
new file mode 100644
index 0000000..4fa72ac
--- /dev/null
+++ b/web-revamp-mockup/data/records/opus__P21.json
@@ -0,0 +1,260 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P21_DB00563_MESH_D001172",
+    "drug": "Methotrexate",
+    "drug_mesh": "MESH:D008727",
+    "drugbank": "DB:DB00563",
+    "disease": "Rheumatoid Arthritis",
+    "disease_mesh": "MESH:D001172",
+    "summary": "Methotrexate → Bifunctional purine biosynthesis protein ATIC (AICAR transformylase) → Adenosine → Adenosine receptor A2a (ADORA2A) → Stromelysin-1 (MMP-3) → Rheumatoid Arthritis"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D008727",
+      "name": "Methotrexate",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P31939",
+      "name": "Bifunctional purine biosynthesis protein ATIC (AICAR transformylase)",
+      "label": "Protein"
+    },
+    {
+      "id": "CHEBI:16335",
+      "name": "Adenosine",
+      "label": "ChemicalSubstance"
+    },
+    {
+      "id": "UniProt:P29274",
+      "name": "Adenosine receptor A2a (ADORA2A)",
+      "label": "Protein"
+    },
+    {
+      "id": "UniProt:P08254",
+      "name": "Stromelysin-1 (MMP-3)",
+      "label": "Protein"
+    },
+    {
+      "id": "MESH:D001172",
+      "name": "Rheumatoid Arthritis",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D008727",
+      "target": "UniProt:P31939",
+      "evidence": [
+        {
+          "reference": "PMID:23464989",
+          "snippet": "intracellular MTX polyglutamates inhibit AICAR transformylase (ATIC) activity and thereby promote adenosine release",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Methotrexate (as polyglutamates) inhibits ATIC enzymatic activity.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Fibroblasts from methotrexate-sensitive mice accumulate methotrexate polyglutamates but those from methotrexate-resistant mice do not.",
+            "authors": [
+              "You X",
+              "Williams A",
+              "Dervieux T",
+              "He W",
+              "Cronstein BN"
+            ],
+            "journal": "Clinical and experimental rheumatology",
+            "year": "2013",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P31939",
+      "target": "CHEBI:16335",
+      "evidence": [
+        {
+          "reference": "PMID:23464989",
+          "snippet": "intracellular MTX polyglutamates inhibit AICAR transformylase (ATIC) activity and thereby promote adenosine release",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Inhibition of ATIC promotes release of adenosine; ATIC inhibition is the upstream driver of adenosine accumulation.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Fibroblasts from methotrexate-sensitive mice accumulate methotrexate polyglutamates but those from methotrexate-resistant mice do not.",
+            "authors": [
+              "You X",
+              "Williams A",
+              "Dervieux T",
+              "He W",
+              "Cronstein BN"
+            ],
+            "journal": "Clinical and experimental rheumatology",
+            "year": "2013",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "increased",
+      "source": "CHEBI:16335",
+      "target": "UniProt:P29274",
+      "evidence": [
+        {
+          "reference": "PMID:35410356",
+          "snippet": "adenosine signaling via A2A AdoRs, adenylyl cyclase, and cAMP reduces TNFα-induced MMP-3 production by interfering with p38 MAPK/ATF-2 activity",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Adenosine activates A2A adenosine receptor signaling in rheumatoid synoviocytes.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Adenosine inhibits TNFα-induced MMP-3 production in MH7A rheumatoid arthritis synoviocytes via A2A receptor signaling.",
+            "authors": [
+              "Konishi H",
+              "Kanou SE",
+              "Yukimatsu R",
+              "Inui M",
+              "Sato M",
+              "Yamamoto N",
+              "Nakano M",
+              "Koshiba M"
+            ],
+            "journal": "Scientific reports",
+            "year": "2022",
+            "doi": "10.1038/s41598-022-10012-6",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "UniProt:P29274",
+      "target": "UniProt:P08254",
+      "evidence": [
+        {
+          "reference": "PMID:35410356",
+          "snippet": "adenosine signaling via A2A AdoRs, adenylyl cyclase, and cAMP reduces TNFα-induced MMP-3 production by interfering with p38 MAPK/ATF-2 activity",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "A2A receptor activation reduces TNFα-induced MMP-3 production by rheumatoid synovial cells.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Adenosine inhibits TNFα-induced MMP-3 production in MH7A rheumatoid arthritis synoviocytes via A2A receptor signaling.",
+            "authors": [
+              "Konishi H",
+              "Kanou SE",
+              "Yukimatsu R",
+              "Inui M",
+              "Sato M",
+              "Yamamoto N",
+              "Nakano M",
+              "Koshiba M"
+            ],
+            "journal": "Scientific reports",
+            "year": "2022",
+            "doi": "10.1038/s41598-022-10012-6",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "contributes to",
+      "source": "UniProt:P08254",
+      "target": "MESH:D001172",
+      "evidence": [
+        {
+          "reference": "PMID:35410356",
+          "snippet": "matrix metalloproteinase 3 (MMP-3) is released by fibroblast-like synoviocytes in response to inflammatory signaling",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "MMP-3 released by rheumatoid synoviocytes mediates the inflammatory tissue destruction of rheumatoid arthritis; reducing it is the therapeutic endpoint.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Adenosine inhibits TNFα-induced MMP-3 production in MH7A rheumatoid arthritis synoviocytes via A2A receptor signaling.",
+            "authors": [
+              "Konishi H",
+              "Kanou SE",
+              "Yukimatsu R",
+              "Inui M",
+              "Sato M",
+              "Yamamoto N",
+              "Nakano M",
+              "Koshiba M"
+            ],
+            "journal": "Scientific reports",
+            "year": "2022",
+            "doi": "10.1038/s41598-022-10012-6",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "treats",
+      "source": "MESH:D008727",
+      "target": "MESH:D001172",
+      "evidence": [
+        {
+          "reference": "PMID:15914465",
+          "snippet": "Methotrexate administered weekly in low doses is a mainstay in the therapy of rheumatoid arthritis.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Low-dose methotrexate is a mainstay treatment of rheumatoid arthritis.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Low-dose methotrexate: a mainstay in the treatment of rheumatoid arthritis.",
+            "authors": [
+              "Cronstein BN"
+            ],
+            "journal": "Pharmacological reviews",
+            "year": "2005",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00563",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    }
+  ],
+  "site": {
+    "id": "opus__P21",
+    "record_id": "P21_DB00563_MESH_D001172",
+    "run": "opus",
+    "run_label": "Opus (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/opus/outputs/P21.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/opus__P22.json b/web-revamp-mockup/data/records/opus__P22.json
new file mode 100644
index 0000000..0605df8
--- /dev/null
+++ b/web-revamp-mockup/data/records/opus__P22.json
@@ -0,0 +1,183 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P22_DB00065_MESH_D003424",
+    "drug": "Infliximab",
+    "drug_mesh": "MESH:D000069285",
+    "drugbank": "DB:DB00065",
+    "disease": "Crohn's Disease",
+    "disease_mesh": "MESH:D003424",
+    "summary": "Infliximab → Tumor necrosis factor → inflammatory response → Crohn's Disease"
+  },
+  "nodes": [
+    {
+      "id": "DB:DB00065",
+      "name": "Infliximab",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P01375",
+      "name": "Tumor necrosis factor",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0006954",
+      "name": "inflammatory response",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D003424",
+      "name": "Crohn's Disease",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "DB:DB00065",
+      "target": "UniProt:P01375",
+      "evidence": [
+        {
+          "reference": "PMID:11563881",
+          "snippet": "Ifx bound to transmembrane TNF-alpha of activated T cells",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Infliximab binds transmembrane TNF-alpha; it is the TNF-alpha neutralizing antibody described in this study.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Infliximab downregulates interferon-gamma production in activated gut T-lymphocytes from patients with Crohn's disease.",
+            "authors": [
+              "Agnholt J",
+              "Kaltoft K"
+            ],
+            "journal": "Cytokine",
+            "year": "2001",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:29518978",
+          "snippet": "These drugs block TNFα from interacting with its receptors",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Infliximab is named among these anti-TNF drugs that block TNF from interacting with its receptors, i.e. neutralize its activity.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Structural Biology of the TNFα Antagonists Used in the Treatment of Rheumatoid Arthritis.",
+            "authors": [
+              "Lim H",
+              "Lee SH",
+              "Lee HT",
+              "Lee JU",
+              "Son JY",
+              "Shin W",
+              "Heo YS"
+            ],
+            "journal": "International journal of molecular sciences",
+            "year": "2018",
+            "doi": "10.3390/ijms19030768",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P01375",
+      "target": "GO:0006954",
+      "evidence": [
+        {
+          "reference": "PMID:29518978",
+          "snippet": "The binding of the tumor necrosis factor α (TNFα) to its cognate receptor initiates many immune and inflammatory processes.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Structural Biology of the TNFα Antagonists Used in the Treatment of Rheumatoid Arthritis.",
+            "authors": [
+              "Lim H",
+              "Lee SH",
+              "Lee HT",
+              "Lee JU",
+              "Son JY",
+              "Shin W",
+              "Heo YS"
+            ],
+            "journal": "International journal of molecular sciences",
+            "year": "2018",
+            "doi": "10.3390/ijms19030768",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "causes",
+      "source": "GO:0006954",
+      "target": "MESH:D003424",
+      "evidence": [
+        {
+          "reference": "PMID:41225190",
+          "snippet": "Crohn's disease (CD) is a chronic inflammatory bowel disorder characterized by transmural inflammation of the gastrointestinal tract.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Systematic Review of Bile Acids Metabolism in Crohn's Disease: Implications for Pathogenesis and Therapeutic Interventions.",
+            "authors": [
+              "Abubasheer TM",
+              "Saad K",
+              "Altaweel A",
+              "Alomari O",
+              "Kamal SK",
+              "Abdelfattah M",
+              "Abualkhair KA",
+              "Ezz MR",
+              "Elgendy MS",
+              "Omar A",
+              "Mubarak ES",
+              "Elhoufey A",
+              "Helmy AM",
+              "Hussein WM",
+              "Hussain SA",
+              "Hassan AM",
+              "Elgenidi A"
+            ],
+            "journal": "Digestive diseases and sciences",
+            "year": "2026",
+            "doi": "10.1007/s10620-025-09557-z",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00065",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    }
+  ],
+  "site": {
+    "id": "opus__P22",
+    "record_id": "P22_DB00065_MESH_D003424",
+    "run": "opus",
+    "run_label": "Opus (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/opus/outputs/P22.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/opus__P23.json b/web-revamp-mockup/data/records/opus__P23.json
new file mode 100644
index 0000000..93720b7
--- /dev/null
+++ b/web-revamp-mockup/data/records/opus__P23.json
@@ -0,0 +1,139 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P23_DB01611_MESH_D008180",
+    "drug": "Hydroxychloroquine",
+    "drug_mesh": "MESH:D006886",
+    "drugbank": "DB:DB01611",
+    "disease": "Systemic Lupus Erythematosus",
+    "disease_mesh": "MESH:D008180",
+    "summary": "Hydroxychloroquine → Toll-like receptor 7 → type I interferon production → Systemic Lupus Erythematosus"
+  },
+  "nodes": [
+    {
+      "id": "DB:DB01611",
+      "name": "Hydroxychloroquine",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:Q9NYK1",
+      "name": "Toll-like receptor 7",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0032606",
+      "name": "type I interferon production",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D008180",
+      "name": "Systemic Lupus Erythematosus",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "DB:DB01611",
+      "target": "UniProt:Q9NYK1",
+      "evidence": [
+        {
+          "reference": "PMID:34580855",
+          "snippet": "HCQ treatment of fresh PBMCs, CAL-1 leukemic, and primary human pDCs inhibits TLR7 cleavage and results in accumulation of full-length protein. As a consequence, we observe an inhibition of pDC activation in response to TLR7 stimulation",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Hydroxychloroquine inhibits the proteolytic maturation of TLR7 and thereby reduces TLR7-driven activation.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Hydroxychloroquine inhibits proteolytic processing of endogenous TLR7 protein in human primary plasmacytoid dendritic cells.",
+            "authors": [
+              "Cenac C",
+              "Ducatez MF",
+              "Guéry JC"
+            ],
+            "journal": "European journal of immunology",
+            "year": "2022",
+            "doi": "10.1002/eji.202149361",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:Q9NYK1",
+      "target": "GO:0032606",
+      "evidence": [
+        {
+          "reference": "PMID:34512664",
+          "snippet": "Plasmacytoid dendritic cells (pDCs) produce type I interferon (IFN-I) during HIV-1 infection in response to TLR7 stimulation.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "TLR7 stimulation drives type I interferon production by plasmacytoid dendritic cells.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Sex Differences in Primary HIV Infection: Revisiting the Role of TLR7-Driven Type 1 IFN Production by Plasmacytoid Dendritic Cells in Women.",
+            "authors": [
+              "Guéry JC"
+            ],
+            "journal": "Frontiers in immunology",
+            "year": "2021",
+            "doi": "10.3389/fimmu.2021.729233",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "contributes to",
+      "source": "GO:0032606",
+      "target": "MESH:D008180",
+      "evidence": [
+        {
+          "reference": "PMID:23445195",
+          "snippet": "interferon signaling is essential for the initiation and/or progression of lupus in several experimental models.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Type I interferon signaling drives the initiation and progression of lupus.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Fueling autoimmunity: type I interferon in autoimmune diseases.",
+            "authors": [
+              "Di Domizio J",
+              "Cao W"
+            ],
+            "journal": "Expert review of clinical immunology",
+            "year": "2013",
+            "doi": "10.1586/eci.12.106",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB01611",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    }
+  ],
+  "site": {
+    "id": "opus__P23",
+    "record_id": "P23_DB01611_MESH_D008180",
+    "run": "opus",
+    "run_label": "Opus (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/opus/outputs/P23.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/opus__P24.json b/web-revamp-mockup/data/records/opus__P24.json
new file mode 100644
index 0000000..58b7231
--- /dev/null
+++ b/web-revamp-mockup/data/records/opus__P24.json
@@ -0,0 +1,230 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P24_DB00688_MESH_D008181",
+    "drug": "Mycophenolate mofetil",
+    "drug_mesh": "MESH:D000077732",
+    "drugbank": "DB:DB00688",
+    "disease": "Lupus Nephritis",
+    "disease_mesh": "MESH:D008181",
+    "summary": "Mycophenolate mofetil → Mycophenolic acid → Inosine-5'-monophosphate dehydrogenase 2 → GMP biosynthetic process"
+  },
+  "nodes": [
+    {
+      "id": "DB:DB00688",
+      "name": "Mycophenolate mofetil",
+      "label": "Drug"
+    },
+    {
+      "id": "MESH:D015232",
+      "name": "Mycophenolic acid",
+      "label": "ChemicalSubstance"
+    },
+    {
+      "id": "UniProt:P12268",
+      "name": "Inosine-5'-monophosphate dehydrogenase 2",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0006177",
+      "name": "GMP biosynthetic process",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "GO:0046651",
+      "name": "lymphocyte proliferation",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D008181",
+      "name": "Lupus Nephritis",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "has metabolite",
+      "source": "DB:DB00688",
+      "target": "MESH:D015232",
+      "evidence": [
+        {
+          "reference": "PMID:10878285",
+          "snippet": "Mycophenolate mofetil (MMF, CellCept(R)) is a prodrug of mycophenolic acid (MPA), an inhibitor of inosine monophosphate dehydrogenase (IMPDH).",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "MMF is hydrolyzed to release the active metabolite mycophenolic acid.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Mycophenolate mofetil and its mechanisms of action.",
+            "authors": [
+              "Allison AC",
+              "Eugui EM"
+            ],
+            "journal": "Immunopharmacology",
+            "year": "2000",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D015232",
+      "target": "UniProt:P12268",
+      "evidence": [
+        {
+          "reference": "PMID:8680053",
+          "snippet": "release mycophenolic acid (MPA), a potent, selective, noncompetitive inhibitor of the type 2 isoform of inosine monophosphate dehydroxygenase (IMPDH) expressed in activated human T and B lymphocytes",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Purine metabolism and immunosuppressive effects of mycophenolate mofetil (MMF).",
+            "authors": [
+              "Allison AC",
+              "Eugui EM"
+            ],
+            "journal": "Clinical transplantation",
+            "year": "1996",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "participates in",
+      "source": "UniProt:P12268",
+      "target": "GO:0006177",
+      "evidence": [
+        {
+          "reference": "PMID:10878285",
+          "snippet": "an inhibitor of inosine monophosphate dehydrogenase (IMPDH). This is the rate-limiting enzyme in de novo synthesis of guanosine nucleotides.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Mycophenolate mofetil and its mechanisms of action.",
+            "authors": [
+              "Allison AC",
+              "Eugui EM"
+            ],
+            "journal": "Immunopharmacology",
+            "year": "2000",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D015232",
+      "target": "GO:0046651",
+      "evidence": [
+        {
+          "reference": "PMID:8680053",
+          "snippet": "By inhibiting IMPDH, MPA depletes the pool of dGTP required for DNA synthesis. MPA has a more potent cytostatic effect on lymphocytes than on other cell types",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Purine metabolism and immunosuppressive effects of mycophenolate mofetil (MMF).",
+            "authors": [
+              "Allison AC",
+              "Eugui EM"
+            ],
+            "journal": "Clinical transplantation",
+            "year": "1996",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:22571761",
+          "snippet": "MPA abrogated in vitro proliferation of purified B cells completely but had only moderate impact on B cell survival.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Mycophenolic acid counteracts B cell proliferation and plasmablast formation in patients with systemic lupus erythematosus.",
+            "authors": [
+              "Eickenberg S",
+              "Mickholz E",
+              "Jung E",
+              "Nofer JR",
+              "Pavenstadt HJ",
+              "Jacobi AM"
+            ],
+            "journal": "Arthritis research & therapy",
+            "year": "2012",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "causes",
+      "source": "GO:0046651",
+      "target": "MESH:D008181",
+      "evidence": [
+        {
+          "reference": "PMID:22571761",
+          "snippet": "The thorough inhibition of B cell activation and plasma cell formation by MMF might explain the favorable outcomes of previous clinical trials in patients with SLE, since enhanced B cell proliferation is a hallmark of this disease.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Enhanced lymphocyte (B cell) proliferation drives SLE/lupus nephritis pathology; MMF acts by suppressing it.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Mycophenolic acid counteracts B cell proliferation and plasmablast formation in patients with systemic lupus erythematosus.",
+            "authors": [
+              "Eickenberg S",
+              "Mickholz E",
+              "Jung E",
+              "Nofer JR",
+              "Pavenstadt HJ",
+              "Jacobi AM"
+            ],
+            "journal": "Arthritis research & therapy",
+            "year": "2012",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00688",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    }
+  ],
+  "site": {
+    "id": "opus__P24",
+    "record_id": "P24_DB00688_MESH_D008181",
+    "run": "opus",
+    "run_label": "Opus (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/opus/outputs/P24.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/opus__P25.json b/web-revamp-mockup/data/records/opus__P25.json
new file mode 100644
index 0000000..c946917
--- /dev/null
+++ b/web-revamp-mockup/data/records/opus__P25.json
@@ -0,0 +1,142 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P25_DB00051_MESH_D011565",
+    "drug": "Adalimumab",
+    "drug_mesh": "MESH:D000068879",
+    "drugbank": "DB:DB00051",
+    "disease": "Psoriasis",
+    "disease_mesh": "MESH:D011565",
+    "summary": "Adalimumab → Tumor necrosis factor → keratinocyte proliferation → Psoriasis"
+  },
+  "nodes": [
+    {
+      "id": "DB:DB00051",
+      "name": "Adalimumab",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P01375",
+      "name": "Tumor necrosis factor",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0043616",
+      "name": "keratinocyte proliferation",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D011565",
+      "name": "Psoriasis",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "DB:DB00051",
+      "target": "UniProt:P01375",
+      "evidence": [
+        {
+          "reference": "PMID:19799828",
+          "snippet": "Adalimumab, a fully human monoclonal antibody, binds to and neutralizes tumor necrosis factor.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Adalimumab in the treatment of psoriasis: pooled efficacy and safety results from three pivotal studies.",
+            "authors": [
+              "Papp K",
+              "Okun M",
+              "Vender R"
+            ],
+            "journal": "Journal of cutaneous medicine and surgery",
+            "year": "2009",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "contributes to",
+      "source": "UniProt:P01375",
+      "target": "GO:0043616",
+      "evidence": [
+        {
+          "reference": "PMID:17502868",
+          "snippet": "Overproduction of inflammatory mediators, such as tumor necrosis factor-alpha (TNF-alpha) and IFN-gamma, results in a self-sustaining inflammatory cascade, causing abnormal keratinocyte proliferation and differentiation.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Mechanisms of action of etanercept in psoriasis.",
+            "authors": [
+              "Tan JK",
+              "Aphale A",
+              "Malaviya R",
+              "Sun Y",
+              "Gottlieb AB"
+            ],
+            "journal": "The journal of investigative dermatology. Symposium proceedings",
+            "year": "2007",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "contributes to",
+      "source": "GO:0043616",
+      "target": "MESH:D011565",
+      "evidence": [
+        {
+          "reference": "PMID:15315008",
+          "snippet": "It follows that blockade of TNF-alpha should diminish inflammation and normalize keratinocyte proliferation in psoriasis.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "New development in the treatment of psoriasis--infliximab.",
+            "authors": [
+              "Pietrzak A",
+              "Chodorowska G",
+              "Jazienicka I",
+              "Junak-Bojarska A",
+              "Roliński J"
+            ],
+            "journal": "Annales Universitatis Mariae Curie-Sklodowska. Sectio D: Medicina",
+            "year": "2003",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00051",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    }
+  ],
+  "site": {
+    "id": "opus__P25",
+    "record_id": "P25_DB00051_MESH_D011565",
+    "run": "opus",
+    "run_label": "Opus (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/opus/outputs/P25.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/opus__P26.json b/web-revamp-mockup/data/records/opus__P26.json
new file mode 100644
index 0000000..247f55a
--- /dev/null
+++ b/web-revamp-mockup/data/records/opus__P26.json
@@ -0,0 +1,256 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P26_DB00331_MESH_D003924",
+    "drug": "Metformin",
+    "drug_mesh": "MESH:D008687",
+    "drugbank": "DB:DB00331",
+    "disease": "Type 2 Diabetes Mellitus",
+    "disease_mesh": "MESH:D003924",
+    "summary": "Metformin → 5'-AMP-activated protein kinase catalytic subunit alpha-1 (PRKAA1) → gluconeogenesis → Type 2 Diabetes Mellitus"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D008687",
+      "name": "Metformin",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:Q15831",
+      "name": "Serine/threonine-protein kinase STK11 (LKB1)",
+      "label": "Protein"
+    },
+    {
+      "id": "UniProt:Q13131",
+      "name": "5'-AMP-activated protein kinase catalytic subunit alpha-1 (PRKAA1)",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0006094",
+      "name": "gluconeogenesis",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D003924",
+      "name": "Type 2 Diabetes Mellitus",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "increased",
+      "source": "MESH:D008687",
+      "target": "UniProt:Q13131",
+      "evidence": [
+        {
+          "reference": "PMID:11602624",
+          "snippet": "Here we report that metformin activates AMPK in hepatocytes",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Metformin directly activates AMP-activated protein kinase in hepatocytes.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Role of AMP-activated protein kinase in mechanism of metformin action.",
+            "authors": [
+              "Zhou G",
+              "Myers R",
+              "Li Y",
+              "Chen Y",
+              "Shen X",
+              "Fenyk-Melody J",
+              "Wu M",
+              "Ventre J",
+              "Doebber T",
+              "Fujii N",
+              "Musi N",
+              "Hirshman MF",
+              "Goodyear LJ",
+              "Moller DE"
+            ],
+            "journal": "The Journal of clinical investigation",
+            "year": "2001",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:Q15831",
+      "target": "UniProt:Q13131",
+      "evidence": [
+        {
+          "reference": "PMID:16308421",
+          "snippet": "LKB1, which phosphorylates and activates AMPK",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "explanation": "LKB1 is the upstream kinase that phosphorylates and activates AMPK in the liver, mediating the therapeutic effect of metformin.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "The kinase LKB1 mediates glucose homeostasis in liver and therapeutic effects of metformin.",
+            "authors": [
+              "Shaw RJ",
+              "Lamia KA",
+              "Vasquez D",
+              "Koo SH",
+              "Bardeesy N",
+              "Depinho RA",
+              "Montminy M",
+              "Cantley LC"
+            ],
+            "journal": "Science (New York, N.Y.)",
+            "year": "2005",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "decreased",
+      "source": "UniProt:Q13131",
+      "target": "GO:0006094",
+      "evidence": [
+        {
+          "reference": "PMID:11602624",
+          "snippet": "we find that AMPK activation is required for metformin's inhibitory effect on glucose production by hepatocytes",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "AMPK activation mediates suppression of hepatic glucose production (gluconeogenesis).",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Role of AMP-activated protein kinase in mechanism of metformin action.",
+            "authors": [
+              "Zhou G",
+              "Myers R",
+              "Li Y",
+              "Chen Y",
+              "Shen X",
+              "Fenyk-Melody J",
+              "Wu M",
+              "Ventre J",
+              "Doebber T",
+              "Fujii N",
+              "Musi N",
+              "Hirshman MF",
+              "Goodyear LJ",
+              "Moller DE"
+            ],
+            "journal": "The Journal of clinical investigation",
+            "year": "2001",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "causes",
+      "source": "GO:0006094",
+      "target": "MESH:D003924",
+      "evidence": [
+        {
+          "reference": "PMID:11602624",
+          "snippet": "Its glucose-lowering effect results from decreased hepatic glucose production and increased glucose utilization",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Elevated hepatic glucose production via gluconeogenesis drives the hyperglycemia of type 2 diabetes; metformin lowers glucose by decreasing it.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Role of AMP-activated protein kinase in mechanism of metformin action.",
+            "authors": [
+              "Zhou G",
+              "Myers R",
+              "Li Y",
+              "Chen Y",
+              "Shen X",
+              "Fenyk-Melody J",
+              "Wu M",
+              "Ventre J",
+              "Doebber T",
+              "Fujii N",
+              "Musi N",
+              "Hirshman MF",
+              "Goodyear LJ",
+              "Moller DE"
+            ],
+            "journal": "The Journal of clinical investigation",
+            "year": "2001",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "treats",
+      "source": "MESH:D008687",
+      "target": "MESH:D003924",
+      "evidence": [
+        {
+          "reference": "PMID:11602624",
+          "snippet": "Metformin is a widely used drug for treatment of type 2 diabetes",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Metformin is a first-line therapeutic for type 2 diabetes mellitus.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Role of AMP-activated protein kinase in mechanism of metformin action.",
+            "authors": [
+              "Zhou G",
+              "Myers R",
+              "Li Y",
+              "Chen Y",
+              "Shen X",
+              "Fenyk-Melody J",
+              "Wu M",
+              "Ventre J",
+              "Doebber T",
+              "Fujii N",
+              "Musi N",
+              "Hirshman MF",
+              "Goodyear LJ",
+              "Moller DE"
+            ],
+            "journal": "The Journal of clinical investigation",
+            "year": "2001",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00331",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    }
+  ],
+  "site": {
+    "id": "opus__P26",
+    "record_id": "P26_DB00331_MESH_D003924",
+    "run": "opus",
+    "run_label": "Opus (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/opus/outputs/P26.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/opus__P27.json b/web-revamp-mockup/data/records/opus__P27.json
new file mode 100644
index 0000000..99c3388
--- /dev/null
+++ b/web-revamp-mockup/data/records/opus__P27.json
@@ -0,0 +1,213 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P27_DB00030_MESH_D003922",
+    "drug": "Insulin",
+    "drug_mesh": "MESH:D007328",
+    "drugbank": "DB:DB00030",
+    "disease": "Type 1 Diabetes Mellitus",
+    "disease_mesh": "MESH:D003922",
+    "summary": "Insulin → Insulin receptor → Solute carrier family 2, facilitated glucose transporter member 4 (GLUT4) → glucose import → Hyperglycemia → Type 1 Diabetes Mellitus"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D007328",
+      "name": "Insulin",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P06213",
+      "name": "Insulin receptor",
+      "label": "Protein"
+    },
+    {
+      "id": "UniProt:P14672",
+      "name": "Solute carrier family 2, facilitated glucose transporter member 4 (GLUT4)",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0046323",
+      "name": "glucose import",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "HP:0003074",
+      "name": "Hyperglycemia",
+      "label": "PhenotypicFeature"
+    },
+    {
+      "id": "MESH:D003922",
+      "name": "Type 1 Diabetes Mellitus",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "increased",
+      "source": "MESH:D007328",
+      "target": "UniProt:P06213",
+      "evidence": [
+        {
+          "reference": "PMID:37779149",
+          "snippet": "The binding of insulin to the insulin receptor (IR) triggers a cascade of receptor conformational changes and autophosphorylation, leading to the activation of metabolic and mitogenic pathways.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Insulin binds the insulin receptor and triggers its autophosphorylation/activation.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "A stepwise activation model for the insulin receptor.",
+            "authors": [
+              "Yunn NO",
+              "Kim J",
+              "Ryu SH",
+              "Cho Y"
+            ],
+            "journal": "Experimental & molecular medicine",
+            "year": "2023",
+            "doi": "10.1038/s12276-023-01101-1",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P06213",
+      "target": "UniProt:P14672",
+      "evidence": [
+        {
+          "reference": "PMID:16702775",
+          "snippet": "This insulin-induced redistribution of GLUT4 protein is achieved through a series of highly organized membrane trafficking events, orchestrated by insulin receptor signals.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Insulin receptor signals drive GLUT4 redistribution (translocation) to the plasma membrane.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Insulin receptor signals regulating GLUT4 translocation and actin dynamics.",
+            "authors": [
+              "Kanzaki M"
+            ],
+            "journal": "Endocrine journal",
+            "year": "2006",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "participates in",
+      "source": "UniProt:P14672",
+      "target": "GO:0046323",
+      "evidence": [
+        {
+          "reference": "PMID:16702775",
+          "snippet": "insulin-stimulated glucose uptake is dependent upon translocation of the insulin-responsive glucose transporter GLUT4 from intracellular storage compartments to the plasma membrane",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "GLUT4 at the plasma membrane mediates insulin-stimulated glucose uptake/import.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Insulin receptor signals regulating GLUT4 translocation and actin dynamics.",
+            "authors": [
+              "Kanzaki M"
+            ],
+            "journal": "Endocrine journal",
+            "year": "2006",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "decreased",
+      "source": "GO:0046323",
+      "target": "HP:0003074",
+      "evidence": [
+        {
+          "reference": "PMID:27521155",
+          "snippet": "The enhanced disposal of glucose by the peripheral tissue is an important mechanism to regulate hyperglycemia.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Enhanced glucose uptake/disposal by peripheral tissues reduces hyperglycemia.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Glucose uptake stimulatory potential and antidiabetic activity of the Arnebin-1 from Arnabia nobelis.",
+            "authors": [
+              "Pandeti S",
+              "Arha D",
+              "Mishra A",
+              "Reddy SS",
+              "Srivastava AK",
+              "Narender T",
+              "Tamrakar AK"
+            ],
+            "journal": "European journal of pharmacology",
+            "year": "2016",
+            "doi": "10.1016/j.ejphar.2016.08.010",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "manifestation of",
+      "source": "HP:0003074",
+      "target": "MESH:D003922",
+      "evidence": [
+        {
+          "reference": "PMID:40163169",
+          "snippet": "This well-characterized T1D model develops insulin deficiency with chronic hyperglycemia",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "explanation": "Chronic hyperglycemia is a defining feature of type 1 diabetes.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "In vivo Detection and Correlation of Cerebral Ketone Bodies with Neurotransmitters in Streptozotocin-Induced Type 1 Diabetic Rats.",
+            "authors": [
+              "Choi IY",
+              "Wang WT",
+              "Smirnova IV",
+              "Lee P"
+            ],
+            "journal": "Neurochemical research",
+            "year": "2025",
+            "doi": "10.1007/s11064-025-04385-z",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00030",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    }
+  ],
+  "site": {
+    "id": "opus__P27",
+    "record_id": "P27_DB00030_MESH_D003922",
+    "run": "opus",
+    "run_label": "Opus (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/opus/outputs/P27.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/opus__P28.json b/web-revamp-mockup/data/records/opus__P28.json
new file mode 100644
index 0000000..36a0dd5
--- /dev/null
+++ b/web-revamp-mockup/data/records/opus__P28.json
@@ -0,0 +1,193 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P28_DB00451_MESH_D007037",
+    "drug": "Levothyroxine",
+    "drug_mesh": "MESH:D013974",
+    "drugbank": "DB:DB00451",
+    "disease": "Hypothyroidism",
+    "disease_mesh": "MESH:D007037",
+    "summary": "Levothyroxine → Triiodothyronine → Thyroid hormone receptor beta → regulation of DNA-templated transcription → Hypothyroidism"
+  },
+  "nodes": [
+    {
+      "id": "DB:DB00451",
+      "name": "Levothyroxine",
+      "label": "Drug"
+    },
+    {
+      "id": "MESH:D014284",
+      "name": "Triiodothyronine",
+      "label": "ChemicalSubstance"
+    },
+    {
+      "id": "UniProt:P10828",
+      "name": "Thyroid hormone receptor beta",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0006355",
+      "name": "regulation of DNA-templated transcription",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D007037",
+      "name": "Hypothyroidism",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "has metabolite",
+      "source": "DB:DB00451",
+      "target": "MESH:D014284",
+      "evidence": [
+        {
+          "reference": "PMID:40077932",
+          "snippet": "The standard treatment involves synthetic levothyroxine (LT4) monotherapy, which alleviates symptoms by converting to the active hormone, T3.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Levothyroxine (LT4) is converted to the active hormone triiodothyronine (T3).",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Shared Decisionmaking in the Treatment of Hypothyroidism.",
+            "authors": [
+              "Bianco AC"
+            ],
+            "journal": "Clinical endocrinology",
+            "year": "2025",
+            "doi": "10.1111/cen.15228",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "increased",
+      "source": "MESH:D014284",
+      "target": "UniProt:P10828",
+      "evidence": [
+        {
+          "reference": "PMID:23307792",
+          "snippet": "a T(3)-bound TRβ1/RXRα heterodimer inhibits SRE-binding protein-1c-induced transcriptional activity",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "T3 binds and forms the active liganded thyroid hormone receptor beta 1 (TRβ1)/RXRα heterodimer.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Thyroid hormones decrease plasma 1α,25-dihydroxyvitamin D levels through transcriptional repression of the renal 25-hydroxyvitamin D3 1α-hydroxylase gene (CYP27B1).",
+            "authors": [
+              "Kozai M",
+              "Yamamoto H",
+              "Ishiguro M",
+              "Harada N",
+              "Masuda M",
+              "Kagawa T",
+              "Takei Y",
+              "Otani A",
+              "Nakahashi O",
+              "Ikeda S",
+              "Taketani Y",
+              "Takeyama K",
+              "Kato S",
+              "Takeda E"
+            ],
+            "journal": "Endocrinology",
+            "year": "2013",
+            "doi": "10.1210/en.2012-1647",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "participates in",
+      "source": "UniProt:P10828",
+      "target": "GO:0006355",
+      "evidence": [
+        {
+          "reference": "PMID:23307792",
+          "snippet": "Promoter analysis revealed that T(3) decreases the basal transcriptional activity of the CYP27B1 gene through thyroid hormone receptors (TRα and TRβ1) and the retinoid X receptor α (RXRα) in renal proximal tubular cells.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Liganded thyroid hormone receptor beta regulates transcriptional activity of target genes.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Thyroid hormones decrease plasma 1α,25-dihydroxyvitamin D levels through transcriptional repression of the renal 25-hydroxyvitamin D3 1α-hydroxylase gene (CYP27B1).",
+            "authors": [
+              "Kozai M",
+              "Yamamoto H",
+              "Ishiguro M",
+              "Harada N",
+              "Masuda M",
+              "Kagawa T",
+              "Takei Y",
+              "Otani A",
+              "Nakahashi O",
+              "Ikeda S",
+              "Taketani Y",
+              "Takeyama K",
+              "Kato S",
+              "Takeda E"
+            ],
+            "journal": "Endocrinology",
+            "year": "2013",
+            "doi": "10.1210/en.2012-1647",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "treats",
+      "source": "GO:0006355",
+      "target": "MESH:D007037",
+      "evidence": [
+        {
+          "reference": "PMID:40077932",
+          "snippet": "The standard treatment involves synthetic levothyroxine (LT4) monotherapy, which alleviates symptoms by converting to the active hormone, T3.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Restoration of thyroid hormone-dependent gene transcription alleviates hypothyroidism symptoms.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Shared Decisionmaking in the Treatment of Hypothyroidism.",
+            "authors": [
+              "Bianco AC"
+            ],
+            "journal": "Clinical endocrinology",
+            "year": "2025",
+            "doi": "10.1111/cen.15228",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00451",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    }
+  ],
+  "site": {
+    "id": "opus__P28",
+    "record_id": "P28_DB00451_MESH_D007037",
+    "run": "opus",
+    "run_label": "Opus (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/opus/outputs/P28.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/opus__P29.json b/web-revamp-mockup/data/records/opus__P29.json
new file mode 100644
index 0000000..2ca51df
--- /dev/null
+++ b/web-revamp-mockup/data/records/opus__P29.json
@@ -0,0 +1,184 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P29_DB00437_MESH_D006073",
+    "drug": "Allopurinol",
+    "drug_mesh": "MESH:D000493",
+    "drugbank": "DB:DB00437",
+    "disease": "Gout",
+    "disease_mesh": "MESH:D006073",
+    "summary": "Allopurinol → Xanthine dehydrogenase/oxidase → Uric acid → NLRP3 → Gout"
+  },
+  "nodes": [
+    {
+      "id": "DB:DB00437",
+      "name": "Allopurinol",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P47989",
+      "name": "Xanthine dehydrogenase/oxidase",
+      "label": "Protein"
+    },
+    {
+      "id": "MESH:D014527",
+      "name": "Uric acid",
+      "label": "ChemicalSubstance"
+    },
+    {
+      "id": "UniProt:Q96P20",
+      "name": "NLRP3",
+      "label": "Protein"
+    },
+    {
+      "id": "MESH:D006073",
+      "name": "Gout",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "DB:DB00437",
+      "target": "UniProt:P47989",
+      "evidence": [
+        {
+          "reference": "PMID:37625592",
+          "snippet": "Allopurinol, an analog of hypoxanthine, is widely used as an antigout drug, as xanthine oxidoreductase-mediated metabolism of allopurinol to oxypurinol leads to oxypurinol rotation in the enzyme active site and reduction of the molybdenum Mo(VI) active center to Mo(IV), inhibiting subsequent urate production.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Allopurinol is metabolized by xanthine oxidoreductase to oxypurinol, which inhibits the enzyme's active center.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Allopurinol and oxypurinol differ in their strength and mechanisms of inhibition of xanthine oxidoreductase.",
+            "authors": [
+              "Sekine M",
+              "Okamoto K",
+              "Pai EF",
+              "Nagata K",
+              "Ichida K",
+              "Hille R",
+              "Nishino T"
+            ],
+            "journal": "The Journal of biological chemistry",
+            "year": "2023",
+            "doi": "10.1016/j.jbc.2023.105189",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P47989",
+      "target": "MESH:D014527",
+      "evidence": [
+        {
+          "reference": "PMID:37625592",
+          "snippet": "Xanthine oxidoreductase is a metalloenzyme that catalyzes the final steps in purine metabolism by converting hypoxanthine to xanthine and then uric acid.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Xanthine oxidoreductase produces uric acid as the final step of purine metabolism.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Allopurinol and oxypurinol differ in their strength and mechanisms of inhibition of xanthine oxidoreductase.",
+            "authors": [
+              "Sekine M",
+              "Okamoto K",
+              "Pai EF",
+              "Nagata K",
+              "Ichida K",
+              "Hille R",
+              "Nishino T"
+            ],
+            "journal": "The Journal of biological chemistry",
+            "year": "2023",
+            "doi": "10.1016/j.jbc.2023.105189",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "increased",
+      "source": "MESH:D014527",
+      "target": "UniProt:Q96P20",
+      "evidence": [
+        {
+          "reference": "PMID:41863697",
+          "snippet": "Both the soluble and crystalline forms of UA act as inflammatory triggers, leading to the formation and activation of the NLRP3 inflammasome further promoting caspase 1-dependent release of the pro-inflammatory cytokines interleukin (IL)-1β and IL-18, as well as to gasdermin D-mediated pyroptotic cell death.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Uric acid, in soluble and crystalline forms, triggers formation and activation of the NLRP3 inflammasome.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Is Gout an Autoinflammatory Disease?",
+            "authors": [
+              "Schlesinger N",
+              "Kaufmann D"
+            ],
+            "journal": "Current rheumatology reports",
+            "year": "2026",
+            "doi": "10.1007/s11926-026-01216-0",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "causes",
+      "source": "UniProt:Q96P20",
+      "target": "MESH:D006073",
+      "evidence": [
+        {
+          "reference": "PMID:41863697",
+          "snippet": "the NLRP3 inflammasome complex, an innate immune sentinel and nonspecific sensor of cellular perturbation, is the initiator and key participant in gouty inflammation",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "The NLRP3 inflammasome is the initiator and key participant in gouty inflammation.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Is Gout an Autoinflammatory Disease?",
+            "authors": [
+              "Schlesinger N",
+              "Kaufmann D"
+            ],
+            "journal": "Current rheumatology reports",
+            "year": "2026",
+            "doi": "10.1007/s11926-026-01216-0",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00437",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    }
+  ],
+  "site": {
+    "id": "opus__P29",
+    "record_id": "P29_DB00437_MESH_D006073",
+    "run": "opus",
+    "run_label": "Opus (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/opus/outputs/P29.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/opus__P30.json b/web-revamp-mockup/data/records/opus__P30.json
new file mode 100644
index 0000000..964fa1e
--- /dev/null
+++ b/web-revamp-mockup/data/records/opus__P30.json
@@ -0,0 +1,224 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P30_DB09038_MESH_D003924",
+    "drug": "empagliflozin",
+    "drug_mesh": "MESH:C000591311",
+    "drugbank": "DB:DB09038",
+    "disease": "Type 2 Diabetes Mellitus",
+    "disease_mesh": "MESH:D003924",
+    "summary": "empagliflozin → Sodium/glucose cotransporter 2 → renal glucose absorption → Glycosuria → Blood Glucose → Type 2 Diabetes Mellitus"
+  },
+  "nodes": [
+    {
+      "id": "DB:DB09038",
+      "name": "empagliflozin",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P31639",
+      "name": "Sodium/glucose cotransporter 2",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0035623",
+      "name": "renal glucose absorption",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "HP:0003076",
+      "name": "Glycosuria",
+      "label": "PhenotypicFeature"
+    },
+    {
+      "id": "MESH:D001786",
+      "name": "Blood Glucose",
+      "label": "ChemicalSubstance"
+    },
+    {
+      "id": "MESH:D003924",
+      "name": "Type 2 Diabetes Mellitus",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "DB:DB09038",
+      "target": "UniProt:P31639",
+      "evidence": [
+        {
+          "reference": "PMID:35070111",
+          "snippet": "block the SGLT2 protein within the kidneys, inhibiting glucose reabsorption, and causing an associated osmotic diuresis",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "SGLT2 inhibitors (-flozin drugs, including empagliflozin) block the SGLT2 protein in the kidneys.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Cardiovascular benefits from SGLT2 inhibition in type 2 diabetes mellitus patients is not impaired with phosphate flux related to pharmacotherapy.",
+            "authors": [
+              "Nashawi M",
+              "Ahmed MS",
+              "Amin T",
+              "Abualfoul M",
+              "Chilton R"
+            ],
+            "journal": "World journal of cardiology",
+            "year": "2021",
+            "doi": "10.4330/wjc.v13.i12.676",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "participates in",
+      "source": "UniProt:P31639",
+      "target": "GO:0035623",
+      "evidence": [
+        {
+          "reference": "PMID:38363006",
+          "snippet": "the compensatory effect of SGLT1 in renal glucose reabsorption (RGR) when SGLT2 is inhibited",
+          "supports": "SUPPORT",
+          "evidence_source": "COMPUTATIONAL",
+          "explanation": "SGLT2 mediates renal glucose reabsorption; inhibiting SGLT2 reduces this process.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Mechanistic Modeling of Empagliflozin: Predicting Pharmacokinetics, Urinary Glucose Excretion, and Investigating Compensatory Role of SGLT1 in Renal Glucose Reabsorption.",
+            "authors": [
+              "Ping X",
+              "Wang G",
+              "Gao D"
+            ],
+            "journal": "Journal of clinical pharmacology",
+            "year": "2024",
+            "doi": "10.1002/jcph.2413",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "decreased",
+      "source": "GO:0035623",
+      "target": "HP:0003076",
+      "evidence": [
+        {
+          "reference": "PMID:34865099",
+          "snippet": "empagliflozin lowers blood glucose via reduced tubular reabsorption of filtered glucose",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "explanation": "Reduced tubular reabsorption of filtered glucose causes filtered glucose to be excreted in the urine (glycosuria) instead of reabsorbed.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Regression of diabetic nephropathy by treatment with empagliflozin in BTBR ob/ob mice.",
+            "authors": [
+              "Hudkins KL",
+              "Li X",
+              "Holland AL",
+              "Swaminathan S",
+              "Alpers CE"
+            ],
+            "journal": "Nephrology, dialysis, transplantation : official publication of the European Dialysis and Transplant Association - European Renal Association",
+            "year": "2022",
+            "doi": "10.1093/ndt/gfab330",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "negatively correlated with",
+      "source": "HP:0003076",
+      "target": "MESH:D001786",
+      "evidence": [
+        {
+          "reference": "PMID:36794422",
+          "snippet": "and glucose (from median, 0.03 [IQR, 0.02; 0.04] to 34.8 [IQR, 31.6; 40.2] %, P < .0001), and sodium fractional excretion rates (from median, 0.48 [IQR, 0.34; 0.65] to 0.71 [IQR, 0.55; 0.85] %, P = .0001), whereas plasma glucose and insulin concentrations decreased",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "As urinary glucose excretion increased after empagliflozin, plasma glucose concentrations decreased.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Empagliflozin and Renal Sodium-Hydrogen Exchange in Healthy Subjects.",
+            "authors": [
+              "Biancalana E",
+              "Rossi C",
+              "Raggi F",
+              "Distaso M",
+              "Tricò D",
+              "Baldi S",
+              "Ferrannini E",
+              "Solini A"
+            ],
+            "journal": "The Journal of clinical endocrinology and metabolism",
+            "year": "2023",
+            "doi": "10.1210/clinem/dgad088",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "manifestation of",
+      "source": "MESH:D001786",
+      "target": "MESH:D003924",
+      "evidence": [
+        {
+          "reference": "PMID:40830335",
+          "snippet": "Diabetes mellitus (DM) is a chronic metabolic disorder characterized by elevated blood glucose levels due to insulin deficiency or resistance",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Elevated blood glucose is the defining feature of type 2 diabetes mellitus; empagliflozin exerts its therapeutic effect by lowering blood glucose.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Kefir-derived exopolysaccharide ameliorates hyperglycemic control and beta cell integrity in a rat model of type 2 diabetes mellitus.",
+            "authors": [
+              "Yen CC",
+              "Tsai CL",
+              "Chang GR",
+              "Ko CH",
+              "Tu MY",
+              "Lan YW",
+              "Chen HL",
+              "Chen CM"
+            ],
+            "journal": "Nutrition & diabetes",
+            "year": "2025",
+            "doi": "10.1038/s41387-025-00388-5",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB09038",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    }
+  ],
+  "site": {
+    "id": "opus__P30",
+    "record_id": "P30_DB09038_MESH_D003924",
+    "run": "opus",
+    "run_label": "Opus (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/opus/outputs/P30.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/opus__P31.json b/web-revamp-mockup/data/records/opus__P31.json
new file mode 100644
index 0000000..2b3f3ee
--- /dev/null
+++ b/web-revamp-mockup/data/records/opus__P31.json
@@ -0,0 +1,277 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P31_DB00067_MESH_D006467",
+    "drug": "Vasopressin",
+    "drug_mesh": "MESH:C016671",
+    "drugbank": "DB:DB00067",
+    "disease": "Hemophilia A",
+    "disease_mesh": "MESH:D006467",
+    "summary": "Vasopressin → Vasopressin V2 receptor → von Willebrand factor secretion → von Willebrand factor → Coagulation factor VIII → Hemophilia A"
+  },
+  "nodes": [
+    {
+      "id": "DB:DB00067",
+      "name": "Vasopressin",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P30518",
+      "name": "Vasopressin V2 receptor",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0061156",
+      "name": "von Willebrand factor secretion",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "UniProt:P04275",
+      "name": "von Willebrand factor",
+      "label": "Protein"
+    },
+    {
+      "id": "UniProt:P00451",
+      "name": "Coagulation factor VIII",
+      "label": "Protein"
+    },
+    {
+      "id": "MESH:D006467",
+      "name": "Hemophilia A",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "increased",
+      "source": "DB:DB00067",
+      "target": "UniProt:P30518",
+      "evidence": [
+        {
+          "reference": "PMID:10880054",
+          "snippet": "We tested the hypothesis that DDAVP induces vWF secretion by binding to V2R and activating cAMP-mediated signaling in endothelial cells.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "DDAVP (desmopressin), a vasopressin analogue, acts as a specific agonist at the vasopressin V2 receptor.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Vasopressin-induced von Willebrand factor secretion from endothelial cells involves V2 receptors and cAMP.",
+            "authors": [
+              "Kaufmann JE",
+              "Oksche A",
+              "Wollheim CB",
+              "Günther G",
+              "Rosenthal W",
+              "Vischer UM"
+            ],
+            "journal": "The Journal of clinical investigation",
+            "year": "2000",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P30518",
+      "target": "GO:0061156",
+      "evidence": [
+        {
+          "reference": "PMID:10880054",
+          "snippet": "These results indicate that vasopressin induces cAMP-mediated vWF secretion by a direct effect on endothelial cells.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "V2 receptor activation drives cAMP-mediated von Willebrand factor secretion from endothelial cells.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Vasopressin-induced von Willebrand factor secretion from endothelial cells involves V2 receptors and cAMP.",
+            "authors": [
+              "Kaufmann JE",
+              "Oksche A",
+              "Wollheim CB",
+              "Günther G",
+              "Rosenthal W",
+              "Vischer UM"
+            ],
+            "journal": "The Journal of clinical investigation",
+            "year": "2000",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "GO:0061156",
+      "target": "UniProt:P04275",
+      "evidence": [
+        {
+          "reference": "PMID:10880054",
+          "snippet": "Vasopressin and its analogue 1-deamino-8-D-arginine vasopressin (DDAVP) are known to raise plasma von Willebrand factor (vWF) levels.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Secretion of von Willebrand factor from endothelial stores raises circulating plasma vWF levels.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Vasopressin-induced von Willebrand factor secretion from endothelial cells involves V2 receptors and cAMP.",
+            "authors": [
+              "Kaufmann JE",
+              "Oksche A",
+              "Wollheim CB",
+              "Günther G",
+              "Rosenthal W",
+              "Vischer UM"
+            ],
+            "journal": "The Journal of clinical investigation",
+            "year": "2000",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P04275",
+      "target": "UniProt:P00451",
+      "evidence": [
+        {
+          "reference": "PMID:12826528",
+          "snippet": "recent biochemical investigations have confirmed that VWF is a key partner for FVIII, playing significant roles in FVIII function, its production and its stabilization",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "von Willebrand factor binds and stabilizes coagulation factor VIII in plasma, sustaining functional FVIII levels.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "The factor VIII/von Willebrand factor complex: basic and clinical issues.",
+            "authors": [
+              "Federici AB"
+            ],
+            "journal": "Haematologica",
+            "year": "2003",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:28581694",
+          "snippet": "VWF serving as the carrier for FVIII. VWF indirectly influences secondary hemostasis by stabilizing FVIII and transporting it to the site of primary hemostasis.",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "explanation": "By stabilizing and carrying factor VIII, von Willebrand factor sustains functional plasma FVIII levels.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Abnormal von Willebrand factor secretion, factor VIII stabilization and thrombus dynamics in type 2N von Willebrand disease mice.",
+            "authors": [
+              "Swystun LL",
+              "Georgescu I",
+              "Mewburn J",
+              "Deforest M",
+              "Nesbitt K",
+              "Hebert K",
+              "Dwyer C",
+              "Brown C",
+              "Notley C",
+              "Lillicrap D"
+            ],
+            "journal": "Journal of thrombosis and haemostasis : JTH",
+            "year": "2017",
+            "doi": "10.1111/jth.13749",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "treats",
+      "source": "UniProt:P00451",
+      "target": "MESH:D006467",
+      "evidence": [
+        {
+          "reference": "PMID:23265678",
+          "snippet": "Desmopressin is a synthetic vasopressin analog that increases the plasma levels of coagulation factor VIII, von Willebrand factor, and tissue plasminogen activator.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Raising plasma coagulation factor VIII corrects the FVIII deficiency underlying hemophilia A.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Desmopressin-related myocardial infarction in a patient with Wegener's granulomatosis: a case report and review of the literature.",
+            "authors": [
+              "Pape E",
+              "Béné J",
+              "Buchdahl AL",
+              "Gautier S",
+              "Hatron PY",
+              "Lambert M"
+            ],
+            "journal": "Journal des maladies vasculaires",
+            "year": "2013",
+            "doi": "10.1016/j.jmv.2012.11.001",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:23265678",
+          "snippet": "has been approved for use in the prevention and treatment of hemorrhagic events during surgery in patients with hemophilia A",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Vasopressin analogue desmopressin is approved to treat bleeding in hemophilia A via increased factor VIII.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Desmopressin-related myocardial infarction in a patient with Wegener's granulomatosis: a case report and review of the literature.",
+            "authors": [
+              "Pape E",
+              "Béné J",
+              "Buchdahl AL",
+              "Gautier S",
+              "Hatron PY",
+              "Lambert M"
+            ],
+            "journal": "Journal des maladies vasculaires",
+            "year": "2013",
+            "doi": "10.1016/j.jmv.2012.11.001",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00067",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    }
+  ],
+  "site": {
+    "id": "opus__P31",
+    "record_id": "P31_DB00067_MESH_D006467",
+    "run": "opus",
+    "run_label": "Opus (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/opus/outputs/P31.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/opus__P32.json b/web-revamp-mockup/data/records/opus__P32.json
new file mode 100644
index 0000000..3ab66b7
--- /dev/null
+++ b/web-revamp-mockup/data/records/opus__P32.json
@@ -0,0 +1,176 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P32_DB00126_MESH_D001206",
+    "drug": "Ascorbic acid",
+    "drug_mesh": "MESH:D001205",
+    "drugbank": "DB:DB00126",
+    "disease": "Ascorbic acid deficiency",
+    "disease_mesh": "MESH:D001206",
+    "summary": "Ascorbic acid → Prolyl 4-hydroxylase subunit alpha-1 → collagen biosynthetic process → Ascorbic acid deficiency"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D001205",
+      "name": "Ascorbic acid",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P13674",
+      "name": "Prolyl 4-hydroxylase subunit alpha-1",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0032964",
+      "name": "collagen biosynthetic process",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D001206",
+      "name": "Ascorbic acid deficiency",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "MESH:D001205",
+      "target": "UniProt:P13674",
+      "evidence": [
+        {
+          "reference": "PMID:23228664",
+          "snippet": "Ascorbic acid (AA) is essential for collagen biosynthesis as a cofactor for prolyl and lysyl hydroxylase",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Ascorbic acid acts as a cofactor for prolyl hydroxylase, enabling its enzymatic activity.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Ascorbic acid enhances the expression of type 1 and type 4 collagen and SVCT2 in cultured human skin fibroblasts.",
+            "authors": [
+              "Kishimoto Y",
+              "Saito N",
+              "Kurita K",
+              "Shimokado K",
+              "Maruyama N",
+              "Ishigami A"
+            ],
+            "journal": "Biochemical and biophysical research communications",
+            "year": "2013",
+            "doi": "10.1016/j.bbrc.2012.11.110",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "participates in",
+      "source": "UniProt:P13674",
+      "target": "GO:0032964",
+      "evidence": [
+        {
+          "reference": "PMID:21346252",
+          "snippet": "Prolyl-4-hydroxylation is necessary for proper structural assembly of collagens",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Prolyl 4-hydroxylase catalyzes proline hydroxylation required for collagen assembly/biosynthesis.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Vitamin C is dispensable for oxygen sensing in vivo.",
+            "authors": [
+              "Nytko KJ",
+              "Maeda N",
+              "Schläfli P",
+              "Spielmann P",
+              "Wenger RH",
+              "Stiehl DP"
+            ],
+            "journal": "Blood",
+            "year": "2011",
+            "doi": "10.1182/blood-2010-09-307637",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "manifestation of",
+      "source": "GO:0032964",
+      "target": "MESH:D001206",
+      "evidence": [
+        {
+          "reference": "PMID:21346252",
+          "snippet": "vitamin C deficiency is known to cause the collagen-disassembly disease scurvy",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "explanation": "Ascorbic acid deficiency (scurvy) is a collagen-disassembly disease, i.e. impaired collagen biosynthesis is a manifestation of the deficiency.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Vitamin C is dispensable for oxygen sensing in vivo.",
+            "authors": [
+              "Nytko KJ",
+              "Maeda N",
+              "Schläfli P",
+              "Spielmann P",
+              "Wenger RH",
+              "Stiehl DP"
+            ],
+            "journal": "Blood",
+            "year": "2011",
+            "doi": "10.1182/blood-2010-09-307637",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "treats",
+      "source": "MESH:D001205",
+      "target": "MESH:D001206",
+      "evidence": [
+        {
+          "reference": "PMID:32238982",
+          "snippet": "Deficiency in vitamin C results in the potentially fatal disease scurvy, which can be cured only by administering vitamin C.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Administration of ascorbic acid cures the deficiency disease.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Vitamin C and Its Role in Periodontal Diseases - The Past and the Present: A Narrative Review.",
+            "authors": [
+              "Van der Velden U"
+            ],
+            "journal": "Oral health & preventive dentistry",
+            "year": "2020",
+            "doi": "10.3290/j.ohpd.a44306",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00126",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    }
+  ],
+  "site": {
+    "id": "opus__P32",
+    "record_id": "P32_DB00126_MESH_D001206",
+    "run": "opus",
+    "run_label": "Opus (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/opus/outputs/P32.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/opus__P33.json b/web-revamp-mockup/data/records/opus__P33.json
new file mode 100644
index 0000000..262b81e
--- /dev/null
+++ b/web-revamp-mockup/data/records/opus__P33.json
@@ -0,0 +1,252 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P33_DB00068_MESH_D020529",
+    "drug": "Interferon beta-1b",
+    "drug_mesh": "MESH:D000068576",
+    "drugbank": "DB:DB00068",
+    "disease": "Relapsing-remitting multiple sclerosis",
+    "disease_mesh": "MESH:D020529",
+    "summary": "Interferon beta-1b → Interleukin-27 subunit alpha → T-helper 17 cell → Relapsing-remitting multiple sclerosis"
+  },
+  "nodes": [
+    {
+      "id": "DB:DB00068",
+      "name": "Interferon beta-1b",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P17181",
+      "name": "Interferon alpha/beta receptor 1",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0007259",
+      "name": "cell surface receptor signaling pathway via JAK-STAT",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "UniProt:Q8NEV9",
+      "name": "Interleukin-27 subunit alpha",
+      "label": "Protein"
+    },
+    {
+      "id": "CL:0000899",
+      "name": "T-helper 17 cell",
+      "label": "Cell"
+    },
+    {
+      "id": "MESH:D020529",
+      "name": "Relapsing-remitting multiple sclerosis",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "increased",
+      "source": "DB:DB00068",
+      "target": "UniProt:P17181",
+      "evidence": [
+        {
+          "reference": "PMID:26008745",
+          "snippet": "Quantitative single-molecule imaging of receptor assembly in the plasma membrane of living cells clearly identified IFN-induced dimerization of IFNAR1 and IFNAR2.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "IFN-beta engages and dimerizes the type I interferon receptor chains IFNAR1 and IFNAR2, activating the receptor; IFN-beta has ~100-fold higher binding affinity to efficiently recruit IFNAR1.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Receptor dimerization dynamics as a regulatory valve for plasticity of type I interferon signaling.",
+            "authors": [
+              "Wilmes S",
+              "Beutel O",
+              "Li Z",
+              "Francois-Newton V",
+              "Richter CP",
+              "Janning D",
+              "Kroll C",
+              "Hanhart P",
+              "Hötte K",
+              "You C",
+              "Uzé G",
+              "Pellegrini S",
+              "Piehler J"
+            ],
+            "journal": "The Journal of cell biology",
+            "year": "2015",
+            "doi": "10.1083/jcb.201412049",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "participates in",
+      "source": "UniProt:P17181",
+      "target": "GO:0007259",
+      "evidence": [
+        {
+          "reference": "PMID:21106255",
+          "snippet": "IFNß exerts its activity through the interaction with IFNAR, through activation of the JAK/STAT pathway.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Gene expression in IFNß signalling pathway differs between monocytes, CD4 and CD8 T cells from MS patients.",
+            "authors": [
+              "Oliver-Martos B",
+              "Órpez T",
+              "Pinto-Medel MJ",
+              "Mayorga C",
+              "García-León JA",
+              "Maldonado-Sanchez R",
+              "Suardíaz M",
+              "Guerrero M",
+              "Luque G",
+              "Leyva L",
+              "Fernández O"
+            ],
+            "journal": "Journal of neuroimmunology",
+            "year": "2011",
+            "doi": "10.1016/j.jneuroim.2010.10.033",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "DB:DB00068",
+      "target": "UniProt:Q8NEV9",
+      "evidence": [
+        {
+          "reference": "PMID:21420486",
+          "snippet": "IFN-β induced IL-27 expression by DC, and neutralisation of IL-27 abrogated the suppressive effects of IFN-β on zymosan-induced IL-1 and IL-23 production and the generation of Th17 cells in vitro.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "IL-27 mediates the response to IFN-β therapy in multiple sclerosis patients by inhibiting Th17 cells.",
+            "authors": [
+              "Sweeney CM",
+              "Lonergan R",
+              "Basdeo SA",
+              "Kinsella K",
+              "Dungan LS",
+              "Higgins SC",
+              "Kelly PJ",
+              "Costelloe L",
+              "Tubridy N",
+              "Mills KH",
+              "Fletcher JM"
+            ],
+            "journal": "Brain, behavior, and immunity",
+            "year": "2011",
+            "doi": "10.1016/j.bbi.2011.03.007",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "decreased",
+      "source": "UniProt:Q8NEV9",
+      "target": "CL:0000899",
+      "evidence": [
+        {
+          "reference": "PMID:21420486",
+          "snippet": "IFN-β induced IL-27 expression by DC, and neutralisation of IL-27 abrogated the suppressive effects of IFN-β on zymosan-induced IL-1 and IL-23 production and the generation of Th17 cells in vitro.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "IL-27 mediates the IFN-beta-driven suppression of Th17 cell generation; neutralising IL-27 abrogates this suppression.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "IL-27 mediates the response to IFN-β therapy in multiple sclerosis patients by inhibiting Th17 cells.",
+            "authors": [
+              "Sweeney CM",
+              "Lonergan R",
+              "Basdeo SA",
+              "Kinsella K",
+              "Dungan LS",
+              "Higgins SC",
+              "Kelly PJ",
+              "Costelloe L",
+              "Tubridy N",
+              "Mills KH",
+              "Fletcher JM"
+            ],
+            "journal": "Brain, behavior, and immunity",
+            "year": "2011",
+            "doi": "10.1016/j.bbi.2011.03.007",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "contributes to",
+      "source": "CL:0000899",
+      "target": "MESH:D020529",
+      "evidence": [
+        {
+          "reference": "PMID:26095162",
+          "snippet": "These findings suggest that the p38 signalling pathway, by modulating the Th17 differentiation and response, is involved in the pathogenesis of MS",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Th17 differentiation and response are involved in the pathogenesis of multiple sclerosis, studied here in relapsing-remitting MS patients.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "The p38 mitogen-activated protein kinase cascade modulates T helper type 17 differentiation and functionality in multiple sclerosis.",
+            "authors": [
+              "Di Mitri D",
+              "Sambucci M",
+              "Loiarro M",
+              "De Bardi M",
+              "Volpe E",
+              "Cencioni MT",
+              "Gasperini C",
+              "Centonze D",
+              "Sette C",
+              "Akbar AN",
+              "Borsellino G",
+              "Battistini L"
+            ],
+            "journal": "Immunology",
+            "year": "2015",
+            "doi": "10.1111/imm.12497",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00068",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    }
+  ],
+  "site": {
+    "id": "opus__P33",
+    "record_id": "P33_DB00068_MESH_D020529",
+    "run": "opus",
+    "run_label": "Opus (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/opus/outputs/P33.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/opus__P34.json b/web-revamp-mockup/data/records/opus__P34.json
new file mode 100644
index 0000000..b56d70e
--- /dev/null
+++ b/web-revamp-mockup/data/records/opus__P34.json
@@ -0,0 +1,215 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P34_DB00004_MESH_D016410",
+    "drug": "Denileukin diftitox",
+    "drug_mesh": "MESH:C078456",
+    "drugbank": "DB:DB00004",
+    "disease": "Primary cutaneous T-cell lymphoma",
+    "disease_mesh": "MESH:D016410",
+    "summary": "Denileukin diftitox → translation → apoptotic process → T cell"
+  },
+  "nodes": [
+    {
+      "id": "DB:DB00004",
+      "name": "Denileukin diftitox",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P01589",
+      "name": "Interleukin-2 receptor subunit alpha",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0006412",
+      "name": "translation",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "GO:0006915",
+      "name": "apoptotic process",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "CL:0000084",
+      "name": "T cell",
+      "label": "Cell"
+    },
+    {
+      "id": "MESH:D016410",
+      "name": "Primary cutaneous T-cell lymphoma",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "DB:DB00004",
+      "target": "UniProt:P01589",
+      "evidence": [
+        {
+          "reference": "PMID:24462799",
+          "snippet": "both monovalent and bivalent human IL-2 fusion toxins are capable of blocking the binding of biotinylated human IL-2 to human CD25 by flow cytometry",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Denileukin diftitox (the monovalent human IL-2 fusion toxin, Ontak) binds CD25 (IL-2R alpha) and blocks IL-2 binding to the receptor.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Diphtheria toxin-based bivalent human IL-2 fusion toxin with improved efficacy for targeting human CD25(+) cells.",
+            "authors": [
+              "Peraino JS",
+              "Zhang H",
+              "Rajasekera PV",
+              "Wei M",
+              "Madsen JC",
+              "Sachs DH",
+              "Huang CA",
+              "Wang Z"
+            ],
+            "journal": "Journal of immunological methods",
+            "year": "2014",
+            "doi": "10.1016/j.jim.2014.01.008",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "decreased",
+      "source": "DB:DB00004",
+      "target": "GO:0006412",
+      "evidence": [
+        {
+          "reference": "PMID:11707818",
+          "snippet": "The ADP-ribosyltransferase activity of diphtheria toxin is cleaved in the endosome and is translocated into the cytosol where it inhibits protein synthesis, leading to apoptosis.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "DAB(389)IL-2 (ONTAK): a novel fusion toxin therapy for lymphoma.",
+            "authors": [
+              "Foss FM"
+            ],
+            "journal": "Clinical lymphoma",
+            "year": "2000",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "GO:0006412",
+      "target": "GO:0006915",
+      "evidence": [
+        {
+          "reference": "PMID:11707818",
+          "snippet": "where it inhibits protein synthesis, leading to apoptosis",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "DAB(389)IL-2 (ONTAK): a novel fusion toxin therapy for lymphoma.",
+            "authors": [
+              "Foss FM"
+            ],
+            "journal": "Clinical lymphoma",
+            "year": "2000",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "occurs in",
+      "source": "GO:0006915",
+      "target": "CL:0000084",
+      "evidence": [
+        {
+          "reference": "PMID:36047157",
+          "snippet": "DD binds to IL-2 receptor (IL-2R) expressed on tumor cells and is taken up into the cells. Subsequently, DT fragments with adenosine diphosphate ribosylation enzyme inhibit protein synthesis, then ultimately trigger cell death.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Protein synthesis inhibition triggers death of the IL-2R-bearing malignant T cells.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "[Preclinical and clinical researches of Denileukin Diftitox (Genetical Recombination) (Remitoro®), a novel agent for T-cell lymphoma].",
+            "authors": [
+              "Shiiba H",
+              "Takechi A",
+              "Asakura S",
+              "Kawaguchi T",
+              "Sato M"
+            ],
+            "journal": "Nihon yakurigaku zasshi. Folia pharmacologica Japonica",
+            "year": "2022",
+            "doi": "10.1254/fpj.22032",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "treats",
+      "source": "DB:DB00004",
+      "target": "MESH:D016410",
+      "evidence": [
+        {
+          "reference": "PMID:16410787",
+          "snippet": "Denileukin diftitox was approved for the treatment of cutaneous T-cell lymphomas (CTCLs) with CD25+ expression.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "CD25 expression is correlated with histological grade and response to denileukin diftitox in cutaneous T-cell lymphoma.",
+            "authors": [
+              "Talpur R",
+              "Jones DM",
+              "Alencar AJ",
+              "Apisarnthanarax N",
+              "Herne KL",
+              "Yang Y",
+              "Duvic M"
+            ],
+            "journal": "The Journal of investigative dermatology",
+            "year": "2006",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00004",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    }
+  ],
+  "site": {
+    "id": "opus__P34",
+    "record_id": "P34_DB00004_MESH_D016410",
+    "run": "opus",
+    "run_label": "Opus (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/opus/outputs/P34.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/opus__P35.json b/web-revamp-mockup/data/records/opus__P35.json
new file mode 100644
index 0000000..f49a6d7
--- /dev/null
+++ b/web-revamp-mockup/data/records/opus__P35.json
@@ -0,0 +1,288 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P35_DB00008_MESH_D019698",
+    "drug": "Peginterferon alfa-2a",
+    "drug_mesh": "MESH:C100416",
+    "drugbank": "DB:DB00008",
+    "disease": "Chronic hepatitis C",
+    "disease_mesh": "MESH:D019698",
+    "summary": "Peginterferon alfa-2a → Interferon alpha/beta receptor 2 → Non-receptor tyrosine-protein kinase TYK2 → Signal transducer and activator of transcription 1-alpha/beta → defense response to virus → Hepacivirus C → Chronic hepatitis C"
+  },
+  "nodes": [
+    {
+      "id": "DB:DB00008",
+      "name": "Peginterferon alfa-2a",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P48551",
+      "name": "Interferon alpha/beta receptor 2",
+      "label": "Protein"
+    },
+    {
+      "id": "UniProt:P29597",
+      "name": "Non-receptor tyrosine-protein kinase TYK2",
+      "label": "Protein"
+    },
+    {
+      "id": "UniProt:P42224",
+      "name": "Signal transducer and activator of transcription 1-alpha/beta",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0051607",
+      "name": "defense response to virus",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "NCBITaxon:11103",
+      "name": "Hepacivirus C",
+      "label": "OrganismTaxon"
+    },
+    {
+      "id": "MESH:D019698",
+      "name": "Chronic hepatitis C",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "increased",
+      "source": "DB:DB00008",
+      "target": "UniProt:P48551",
+      "evidence": [
+        {
+          "reference": "PMID:16324217",
+          "snippet": "When IFN-alpha binds its receptor, two receptor associated tyrosine kinases, Tyk2 and Jak1 become activated by phosphorylation",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Peginterferon alfa-2a is a pegylated interferon alpha-2 that binds and activates the type I interferon receptor (IFNAR).",
+          "source_tier": "FULL_TEXT",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Effect of ethanol on innate antiviral pathways and HCV replication in human liver cells.",
+            "authors": [
+              "Plumlee CR",
+              "Lazaro CA",
+              "Fausto N",
+              "Polyak SJ"
+            ],
+            "journal": "Virology journal",
+            "year": "2005",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          }
+        }
+      ]
+    },
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P48551",
+      "target": "UniProt:P29597",
+      "evidence": [
+        {
+          "reference": "PMID:16324217",
+          "snippet": "When IFN-alpha binds its receptor, two receptor associated tyrosine kinases, Tyk2 and Jak1 become activated by phosphorylation",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "source_tier": "FULL_TEXT",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Effect of ethanol on innate antiviral pathways and HCV replication in human liver cells.",
+            "authors": [
+              "Plumlee CR",
+              "Lazaro CA",
+              "Fausto N",
+              "Polyak SJ"
+            ],
+            "journal": "Virology journal",
+            "year": "2005",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          }
+        }
+      ]
+    },
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P29597",
+      "target": "UniProt:P42224",
+      "evidence": [
+        {
+          "reference": "PMID:16324217",
+          "snippet": "Tyk2 and Jak1 become activated by phosphorylation, and phosphorylate Stat1 and Stat2 on conserved tyrosine residues",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "source_tier": "FULL_TEXT",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Effect of ethanol on innate antiviral pathways and HCV replication in human liver cells.",
+            "authors": [
+              "Plumlee CR",
+              "Lazaro CA",
+              "Fausto N",
+              "Polyak SJ"
+            ],
+            "journal": "Virology journal",
+            "year": "2005",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          }
+        }
+      ]
+    },
+    {
+      "key": "contributes to",
+      "source": "UniProt:P42224",
+      "target": "GO:0051607",
+      "evidence": [
+        {
+          "reference": "PMID:16324217",
+          "snippet": "Stat1 and Stat2 combine with the IRF-9 protein to form the transcription factor interferon stimulated gene factor 3 (ISGF-3), which binds to the interferon stimulated response element (ISRE), and induces transcription of IFN-alpha-induced genes (ISG). The ISGs mediate the antiviral effects of IFN",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "source_tier": "FULL_TEXT",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Effect of ethanol on innate antiviral pathways and HCV replication in human liver cells.",
+            "authors": [
+              "Plumlee CR",
+              "Lazaro CA",
+              "Fausto N",
+              "Polyak SJ"
+            ],
+            "journal": "Virology journal",
+            "year": "2005",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          }
+        }
+      ]
+    },
+    {
+      "key": "disrupts",
+      "source": "GO:0051607",
+      "target": "NCBITaxon:11103",
+      "evidence": [
+        {
+          "reference": "PMID:16324217",
+          "snippet": "IFN induced a significant 66-fold inhibition of HCV RNA at this time point",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "The interferon-induced antiviral state inhibits hepatitis C virus replication.",
+          "source_tier": "FULL_TEXT",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Effect of ethanol on innate antiviral pathways and HCV replication in human liver cells.",
+            "authors": [
+              "Plumlee CR",
+              "Lazaro CA",
+              "Fausto N",
+              "Polyak SJ"
+            ],
+            "journal": "Virology journal",
+            "year": "2005",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          }
+        }
+      ]
+    },
+    {
+      "key": "causes",
+      "source": "NCBITaxon:11103",
+      "target": "MESH:D019698",
+      "evidence": [
+        {
+          "reference": "PMID:16324217",
+          "snippet": "With a propensity to progress to chronic infection, approximately 70% of patients with chronic viremia develop histological evidence of chronic liver diseases including chronic hepatitis, cirrhosis, and hepatocellular carcinoma",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "source_tier": "FULL_TEXT",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Effect of ethanol on innate antiviral pathways and HCV replication in human liver cells.",
+            "authors": [
+              "Plumlee CR",
+              "Lazaro CA",
+              "Fausto N",
+              "Polyak SJ"
+            ],
+            "journal": "Virology journal",
+            "year": "2005",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          }
+        }
+      ]
+    },
+    {
+      "key": "treats",
+      "source": "DB:DB00008",
+      "target": "MESH:D019698",
+      "evidence": [
+        {
+          "reference": "PMID:12324553",
+          "snippet": "In patients with chronic hepatitis C, once-weekly peginterferon alfa-2a plus ribavirin was tolerated as well as interferon alfa-2b plus ribavirin and produced significant improvements in the rate of sustained virologic response",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Peginterferon alfa-2a plus ribavirin for chronic hepatitis C virus infection.",
+            "authors": [
+              "Fried MW",
+              "Shiffman ML",
+              "Reddy KR",
+              "Smith C",
+              "Marinos G",
+              "Gonçales FL",
+              "Häussinger D",
+              "Diago M",
+              "Carosi G",
+              "Dhumeaux D",
+              "Craxi A",
+              "Lin A",
+              "Hoffman J",
+              "Yu J"
+            ],
+            "journal": "The New England journal of medicine",
+            "year": "2002",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00008",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    }
+  ],
+  "site": {
+    "id": "opus__P35",
+    "record_id": "P35_DB00008_MESH_D019698",
+    "run": "opus",
+    "run_label": "Opus (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/opus/outputs/P35.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/opus__P36.json b/web-revamp-mockup/data/records/opus__P36.json
new file mode 100644
index 0000000..f3245f9
--- /dev/null
+++ b/web-revamp-mockup/data/records/opus__P36.json
@@ -0,0 +1,180 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P36_DB00027_MESH_D003234",
+    "drug": "gramicidin",
+    "drug_mesh": "MESH:D006096",
+    "drugbank": "DB:DB00027",
+    "disease": "Bacterial conjunctivitis",
+    "disease_mesh": "MESH:D003234",
+    "summary": "Gramicidin → monoatomic cation transmembrane transport → membrane depolarization"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D006096",
+      "name": "Gramicidin",
+      "label": "Drug"
+    },
+    {
+      "id": "GO:0005886",
+      "name": "plasma membrane",
+      "label": "CellularComponent"
+    },
+    {
+      "id": "GO:0098655",
+      "name": "monoatomic cation transmembrane transport",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "GO:0051899",
+      "name": "membrane depolarization",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D003234",
+      "name": "Bacterial conjunctivitis",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "located in",
+      "source": "MESH:D006096",
+      "target": "GO:0005886",
+      "evidence": [
+        {
+          "reference": "PMID:27496896",
+          "snippet": "Gramicidin, a channel-forming peptide causing membrane permeability to monovalent cations",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Gramicidin is a channel-forming peptide that inserts into the membrane.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Staphylococcus aureus α-toxin-mediated cation entry depolarizes membrane potential and activates p38 MAP kinase in airway epithelial cells.",
+            "authors": [
+              "Eiffler I",
+              "Behnke J",
+              "Ziesemer S",
+              "Müller C",
+              "Hildebrandt JP"
+            ],
+            "journal": "American journal of physiology. Lung cellular and molecular physiology",
+            "year": "2016",
+            "doi": "10.1152/ajplung.00090.2016",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "increased",
+      "source": "MESH:D006096",
+      "target": "GO:0098655",
+      "evidence": [
+        {
+          "reference": "PMID:27496896",
+          "snippet": "Gramicidin, a channel-forming peptide causing membrane permeability to monovalent cations",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Gramicidin forms channels permeable to monovalent cations, increasing cation transmembrane transport.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Staphylococcus aureus α-toxin-mediated cation entry depolarizes membrane potential and activates p38 MAP kinase in airway epithelial cells.",
+            "authors": [
+              "Eiffler I",
+              "Behnke J",
+              "Ziesemer S",
+              "Müller C",
+              "Hildebrandt JP"
+            ],
+            "journal": "American journal of physiology. Lung cellular and molecular physiology",
+            "year": "2016",
+            "doi": "10.1152/ajplung.00090.2016",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "causes",
+      "source": "GO:0098655",
+      "target": "GO:0051899",
+      "evidence": [
+        {
+          "reference": "PMID:9765307",
+          "snippet": "Gramicidin, which generates pores that are permeable to monovalent cations, and concurrently eliminates the membrane potential",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Gramicidin cation pores collapse/eliminate the membrane potential, i.e. cause depolarization.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Regulation of adenylyl cyclase by membrane potential.",
+            "authors": [
+              "Cooper DM",
+              "Schell MJ",
+              "Thorn P",
+              "Irvine RF"
+            ],
+            "journal": "The Journal of biological chemistry",
+            "year": "1998",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "treats",
+      "source": "MESH:D006096",
+      "target": "MESH:D003234",
+      "evidence": [
+        {
+          "reference": "PMID:6204534",
+          "snippet": "polymyxin B-neomycin-gramicidin (Neosporin, the control) eliminated bacteria from the eyes of patients with conjunctivitis",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Gramicidin-containing ophthalmic solution eliminated bacteria in patients with bacterial conjunctivitis.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Clinical evaluation of trimethoprim-containing ophthalmic solutions in humans.",
+            "authors": [
+              "Lamberts DW",
+              "Buka T",
+              "Knowlton GM"
+            ],
+            "journal": "American journal of ophthalmology",
+            "year": "1984",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00027",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    }
+  ],
+  "site": {
+    "id": "opus__P36",
+    "record_id": "P36_DB00027_MESH_D003234",
+    "run": "opus",
+    "run_label": "Opus (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/opus/outputs/P36.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/opus__P37.json b/web-revamp-mockup/data/records/opus__P37.json
new file mode 100644
index 0000000..9afe1d4
--- /dev/null
+++ b/web-revamp-mockup/data/records/opus__P37.json
@@ -0,0 +1,182 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P37_DB00186_MESH_D001007",
+    "drug": "Lorazepam",
+    "drug_mesh": "MESH:D008140",
+    "drugbank": "DB:DB00186",
+    "disease": "Anxiety",
+    "disease_mesh": "MESH:D001007",
+    "summary": "Lorazepam → Gamma-aminobutyric acid receptor subunit alpha-1 → chloride transmembrane transport → inhibitory postsynaptic potential"
+  },
+  "nodes": [
+    {
+      "id": "DB:DB00186",
+      "name": "Lorazepam",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P14867",
+      "name": "Gamma-aminobutyric acid receptor subunit alpha-1",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:1902476",
+      "name": "chloride transmembrane transport",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "GO:0060080",
+      "name": "inhibitory postsynaptic potential",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D001007",
+      "name": "Anxiety",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "increased",
+      "source": "DB:DB00186",
+      "target": "UniProt:P14867",
+      "evidence": [
+        {
+          "reference": "PMID:30192388",
+          "snippet": "long-latency afferent inhibition (LAI) is reduced by the GABAA positive allosteric modulator lorazepam",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Lorazepam is a GABAA positive allosteric modulator, increasing GABAA receptor activity.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Effects of lorazepam and baclofen on short- and long-latency afferent inhibition.",
+            "authors": [
+              "Turco CV",
+              "El-Sayes J",
+              "Locke MB",
+              "Chen R",
+              "Baker S",
+              "Nelson AJ"
+            ],
+            "journal": "The Journal of physiology",
+            "year": "2018",
+            "doi": "10.1113/JP276710",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P14867",
+      "target": "GO:1902476",
+      "evidence": [
+        {
+          "reference": "PMID:22677032",
+          "snippet": "pre-ictal GABA(A) receptor-mediated chloride influx",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "explanation": "GABAA receptor activation mediates chloride influx across the neuronal membrane.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Pyramidal cells accumulate chloride at seizure onset.",
+            "authors": [
+              "Lillis KP",
+              "Kramer MA",
+              "Mertz J",
+              "Staley KJ",
+              "White JA"
+            ],
+            "journal": "Neurobiology of disease",
+            "year": "2012",
+            "doi": "10.1016/j.nbd.2012.05.016",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "causes",
+      "source": "GO:1902476",
+      "target": "GO:0060080",
+      "evidence": [
+        {
+          "reference": "PMID:32105770",
+          "snippet": "GABA) generally induces hyperpolarization and inhibition in the adult brain",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Chloride influx through GABAA receptors hyperpolarizes and inhibits neurons.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Chloride homeodynamics underlying modal shifts in cellular and network oscillations.",
+            "authors": [
+              "Fukuda A"
+            ],
+            "journal": "Neuroscience research",
+            "year": "2020",
+            "doi": "10.1016/j.neures.2020.02.010",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "treats",
+      "source": "DB:DB00186",
+      "target": "MESH:D001007",
+      "evidence": [
+        {
+          "reference": "PMID:39410894",
+          "snippet": "Lorazepam (LZP), a classical anti-anxiety medicine",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "explanation": "Lorazepam is an established anti-anxiety medication.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Resveratrol Neuroprotective Action Against Cognitive Impairments Induced by Lorazepam in Male Rats.",
+            "authors": [
+              "Chakraborty AK",
+              "Tiwari P",
+              "Khobragade DS",
+              "Kadiri SK",
+              "Sheikh IA",
+              "Thakur J"
+            ],
+            "journal": "Current drug safety",
+            "year": "2025",
+            "doi": "10.2174/0115748863312358240919103439",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00186",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    }
+  ],
+  "site": {
+    "id": "opus__P37",
+    "record_id": "P37_DB00186_MESH_D001007",
+    "run": "opus",
+    "run_label": "Opus (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/opus/outputs/P37.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/opus__P38.json b/web-revamp-mockup/data/records/opus__P38.json
new file mode 100644
index 0000000..40f16d6
--- /dev/null
+++ b/web-revamp-mockup/data/records/opus__P38.json
@@ -0,0 +1,249 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P38_DB00175_MESH_D006937",
+    "drug": "pravastatin",
+    "drug_mesh": "MESH:D017035",
+    "drugbank": "DB:DB00175",
+    "disease": "Hypercholesterolemia",
+    "disease_mesh": "MESH:D006937",
+    "summary": "pravastatin → 3-hydroxy-3-methylglutaryl-coenzyme A reductase → cholesterol biosynthetic process → Sterol regulatory element-binding protein 2 → Low-density lipoprotein receptor → lipoprotein metabolic process"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D017035",
+      "name": "pravastatin",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P04035",
+      "name": "3-hydroxy-3-methylglutaryl-coenzyme A reductase",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0006695",
+      "name": "cholesterol biosynthetic process",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "UniProt:Q12772",
+      "name": "Sterol regulatory element-binding protein 2",
+      "label": "Protein"
+    },
+    {
+      "id": "UniProt:P01130",
+      "name": "Low-density lipoprotein receptor",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0042157",
+      "name": "lipoprotein metabolic process",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D006937",
+      "name": "Hypercholesterolemia",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D017035",
+      "target": "UniProt:P04035",
+      "evidence": [
+        {
+          "reference": "PMID:19787197",
+          "snippet": "A dozen of the synthetic compounds mimic the inhibition of purified HMG-CoA reductase activity caused by pravastatin, fluvastatin and sodium salts of lovastatin, mevastatin and simvastatin in this cell-free assay, suggesting direct interaction with the rate-limiting enzyme of cholesterol biosynthesis.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Novel synthetic inhibitors of 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase activity that inhibit tumor cell proliferation and are structurally unrelated to existing statins.",
+            "authors": [
+              "Perchellet JP",
+              "Perchellet EM",
+              "Crow KR",
+              "Buszek KR",
+              "Brown N",
+              "Ellappan S",
+              "Gao G",
+              "Luo D",
+              "Minatoya M",
+              "Lushington GH"
+            ],
+            "journal": "International journal of molecular medicine",
+            "year": "2009",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "participates in",
+      "source": "UniProt:P04035",
+      "target": "GO:0006695",
+      "evidence": [
+        {
+          "reference": "PMID:34207840",
+          "snippet": "Statins have been widely used for the treatment of hypercholesterolemia due to their ability to inhibit HMG-CoA reductase, the rate-limiting enzyme of de novo cholesterol synthesis, via the so-called mevalonate pathway.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Comparison of Transcriptomic Profiles of MiaPaCa-2 Pancreatic Cancer Cells Treated with Different Statins.",
+            "authors": [
+              "Rimpelová S",
+              "Kolář M",
+              "Strnad H",
+              "Ruml T",
+              "Vítek L",
+              "Gbelcová H"
+            ],
+            "journal": "Molecules (Basel, Switzerland)",
+            "year": "2021",
+            "doi": "10.3390/molecules26123528",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "decreased",
+      "source": "GO:0006695",
+      "target": "UniProt:Q12772",
+      "evidence": [
+        {
+          "reference": "PMID:27888906",
+          "snippet": "The decrease of the hepatic intracellular cholesterol pool produced by these drugs upregulates the activity of the SREBP2 transcription factor, which subsequently stimulates the expression of the LDL receptor gene, an effect that is followed by an increase in the serum concentration of PCSK9.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "[Lipid-lowering drugs and PCSK9].",
+            "authors": [
+              "Millán Núñez-Cortés J",
+              "Mostaza Prieto JM"
+            ],
+            "journal": "Clinica e investigacion en arteriosclerosis : publicacion oficial de la Sociedad Espanola de Arteriosclerosis",
+            "year": "2016",
+            "doi": "10.1016/S0214-9168(16)30165-6",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:Q12772",
+      "target": "UniProt:P01130",
+      "evidence": [
+        {
+          "reference": "PMID:27888906",
+          "snippet": "The decrease of the hepatic intracellular cholesterol pool produced by these drugs upregulates the activity of the SREBP2 transcription factor, which subsequently stimulates the expression of the LDL receptor gene, an effect that is followed by an increase in the serum concentration of PCSK9.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "[Lipid-lowering drugs and PCSK9].",
+            "authors": [
+              "Millán Núñez-Cortés J",
+              "Mostaza Prieto JM"
+            ],
+            "journal": "Clinica e investigacion en arteriosclerosis : publicacion oficial de la Sociedad Espanola de Arteriosclerosis",
+            "year": "2016",
+            "doi": "10.1016/S0214-9168(16)30165-6",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "participates in",
+      "source": "UniProt:P01130",
+      "target": "GO:0042157",
+      "evidence": [
+        {
+          "reference": "PMID:1412144",
+          "snippet": "Inhibition of cholesterol synthesis leads to upregulation of LDL-receptors in the liver and subsequent increased LDL clearance.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "[Extended worldwide experience. HMG-CoA reductase inhibitors: lovastatin and simvastatin].",
+            "authors": [
+              "Mantell G"
+            ],
+            "journal": "Therapie",
+            "year": "1992",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "treats",
+      "source": "MESH:D017035",
+      "target": "MESH:D006937",
+      "evidence": [
+        {
+          "reference": "PMID:15293079",
+          "snippet": "Fluvastatin and pravastatin are efficient in lowering total and LDL cholesterol levels in HIV-positive patients receiving HAART.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Lipid lowering therapy with fluvastatin and pravastatin in patients with HIV infection and antiretroviral therapy: comparison of efficacy and interaction with indinavir.",
+            "authors": [
+              "Benesic A",
+              "Zilly M",
+              "Kluge F",
+              "Weissbrich B",
+              "Winzer R",
+              "Klinker H",
+              "Langmann P"
+            ],
+            "journal": "Infection",
+            "year": "2004",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00175",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    }
+  ],
+  "site": {
+    "id": "opus__P38",
+    "record_id": "P38_DB00175_MESH_D006937",
+    "run": "opus",
+    "run_label": "Opus (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/opus/outputs/P38.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/opus__P39.json b/web-revamp-mockup/data/records/opus__P39.json
new file mode 100644
index 0000000..45291ec
--- /dev/null
+++ b/web-revamp-mockup/data/records/opus__P39.json
@@ -0,0 +1,223 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P39_DB00046_MESH_D003922",
+    "drug": "Insulin lispro",
+    "drug_mesh": "MESH:D061268",
+    "drugbank": "DB:DB00046",
+    "disease": "Type 1 Diabetes Mellitus",
+    "disease_mesh": "MESH:D003922",
+    "summary": "Insulin lispro → Insulin receptor → glucose import → Hyperglycemia → Type 1 Diabetes Mellitus"
+  },
+  "nodes": [
+    {
+      "id": "DB:DB00046",
+      "name": "Insulin lispro",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P06213",
+      "name": "Insulin receptor",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0046323",
+      "name": "glucose import",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "HP:0003074",
+      "name": "Hyperglycemia",
+      "label": "PhenotypicFeature"
+    },
+    {
+      "id": "MESH:D003922",
+      "name": "Type 1 Diabetes Mellitus",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "increased",
+      "source": "DB:DB00046",
+      "target": "UniProt:P06213",
+      "evidence": [
+        {
+          "reference": "PMID:9410552",
+          "snippet": "The affinity in vitro was identical to that of insulin for its receptor.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Insulin lispro (created by inverting lysine and proline at B28/B29) binds the insulin receptor with affinity identical to native insulin, acting as a full receptor agonist.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "[From the concept of fast acting analogs to the properties of the insulin Lispro].",
+            "authors": [
+              "Selam JL"
+            ],
+            "journal": "Diabetes & metabolism",
+            "year": "1997",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:11712394",
+          "snippet": "the binding causes conformational changes in the receptor molecule",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Ligand binding to the insulin receptor alpha subunits triggers conformational changes that stimulate autophosphorylation and promote the receptor's kinase activity.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "[Chemical structure, active sites and receptor binding of insulin molecule and its signal transduction].",
+            "authors": [
+              "Ishida H",
+              "Nagamatsu S"
+            ],
+            "journal": "Nihon rinsho. Japanese journal of clinical medicine",
+            "year": "2001",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P06213",
+      "target": "GO:0046323",
+      "evidence": [
+        {
+          "reference": "PMID:25325535",
+          "snippet": "insulin promotes membrane trafficking of the glucose transporter GLUT4 from GLUT4 storage vesicles to the plasma membrane, thereby facilitating the uptake of glucose from the circulation",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Activation of the insulin receptor by insulin drives GLUT4 translocation to the plasma membrane, promoting glucose import into muscle and adipose tissue.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Molecular mechanisms for the regulation of insulin-stimulated glucose uptake by small guanosine triphosphatases in skeletal muscle and adipocytes.",
+            "authors": [
+              "Satoh T"
+            ],
+            "journal": "International journal of molecular sciences",
+            "year": "2014",
+            "doi": "10.3390/ijms151018677",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:33274014",
+          "snippet": "insulin-induced GLUT4 translocation from intracellular compartments to the cell membrane, which increases the overall rate of glucose flux into a cell",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Insulin receptor signaling increases glucose flux into cells via GLUT4 translocation.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Current understanding of glucose transporter 4 expression and functional mechanisms.",
+            "authors": [
+              "Wang T",
+              "Wang J",
+              "Hu X",
+              "Huang XJ",
+              "Chen GX"
+            ],
+            "journal": "World journal of biological chemistry",
+            "year": "2020",
+            "doi": "10.4331/wjbc.v11.i3.76",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "decreased",
+      "source": "GO:0046323",
+      "target": "HP:0003074",
+      "evidence": [
+        {
+          "reference": "PMID:34240660",
+          "snippet": "glucose uptake into skeletal muscle and lower blood glucose levels",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "explanation": "Increased glucose uptake into tissues lowers blood glucose levels, opposing hyperglycemia.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "14-Deoxy-11,12-Didehydroandrographolide Ameliorates Glucose Intolerance Enhancing the LKB1/AMPK[Formula: see text]/TBC1D1/GLUT4 Signaling Pathway and Inducing GLUT4 Expression in Myotubes and Skeletal Muscle of Obese Mice.",
+            "authors": [
+              "Chen CC",
+              "Lii CK",
+              "Lo CW",
+              "Lin YH",
+              "Yang YC",
+              "Huang CS",
+              "Chen HW"
+            ],
+            "journal": "The American journal of Chinese medicine",
+            "year": "2021",
+            "doi": "10.1142/S0192415X21500695",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "manifestation of",
+      "source": "HP:0003074",
+      "target": "MESH:D003922",
+      "evidence": [
+        {
+          "reference": "PMID:40969771",
+          "snippet": "Type 1 diabetes (T1D) is an organ-specific autoimmune disease characterized by the immune-mediated destruction of pancreatic β cells, leading to absolute insulin deficiency and chronic hyperglycemia.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Chronic hyperglycemia is a defining manifestation of Type 1 Diabetes Mellitus resulting from insulin deficiency; insulin lispro replaces the deficient insulin to correct it.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Sensing danger in the islet: the roles of pattern recognition receptors in β cells and type 1 diabetes.",
+            "authors": [
+              "Tong L",
+              "Tu Y",
+              "Huang S",
+              "Zheng P"
+            ],
+            "journal": "Frontiers in immunology",
+            "year": "2025",
+            "doi": "10.3389/fimmu.2025.1677177",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00046",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    }
+  ],
+  "site": {
+    "id": "opus__P39",
+    "record_id": "P39_DB00046_MESH_D003922",
+    "run": "opus",
+    "run_label": "Opus (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/opus/outputs/P39.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/opus__P40.json b/web-revamp-mockup/data/records/opus__P40.json
new file mode 100644
index 0000000..7a18ebb
--- /dev/null
+++ b/web-revamp-mockup/data/records/opus__P40.json
@@ -0,0 +1,253 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P40_DB00043_MESH_D001249",
+    "drug": "omalizumab",
+    "drug_mesh": "MESH:D000069444",
+    "drugbank": "DB:DB00043",
+    "disease": "Asthma",
+    "disease_mesh": "MESH:D001249",
+    "summary": "Omalizumab → Immunoglobulin heavy constant epsilon (IgE) → High affinity immunoglobulin epsilon receptor subunit alpha (FcepsilonRI) → Mast cell degranulation → Asthma"
+  },
+  "nodes": [
+    {
+      "id": "DB:DB00043",
+      "name": "Omalizumab",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P01854",
+      "name": "Immunoglobulin heavy constant epsilon (IgE)",
+      "label": "Protein"
+    },
+    {
+      "id": "UniProt:P12319",
+      "name": "High affinity immunoglobulin epsilon receptor subunit alpha (FcepsilonRI)",
+      "label": "Protein"
+    },
+    {
+      "id": "CL:0000097",
+      "name": "Mast cell",
+      "label": "Cell"
+    },
+    {
+      "id": "GO:0043303",
+      "name": "Mast cell degranulation",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D001249",
+      "name": "Asthma",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "DB:DB00043",
+      "target": "UniProt:P01854",
+      "evidence": [
+        {
+          "reference": "PMID:12110823",
+          "snippet": "Omalizumab (Xolair; formerly rhuMAb-E25) binds to circulating IgE, thus preventing induction of the allergic process.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Omalizumab binds and sequesters free IgE, neutralizing its function.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "The effect of omalizumab on nasal allergic inflammation.",
+            "authors": [
+              "Plewako H",
+              "Arvidsson M",
+              "Petruson K",
+              "Oancea I",
+              "Holmberg K",
+              "Adelroth E",
+              "Gustafsson H",
+              "Sandström T",
+              "Rak S"
+            ],
+            "journal": "The Journal of allergy and clinical immunology",
+            "year": "2002",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "UniProt:P01854",
+      "target": "UniProt:P12319",
+      "evidence": [
+        {
+          "reference": "PMID:16318424",
+          "snippet": "The humanised monoclonal IgE antibody Xolair (omalizumab) complexes with free circulating IgE, thereby preventing binding of IgE to FcepsilonRI receptors on immune cells.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "By sequestering free IgE, omalizumab prevents IgE from engaging and activating FcepsilonRI.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Omalizumab: a future innovation for treatment of severe ocular allergy?",
+            "authors": [
+              "Williams PB",
+              "Sheppard JD"
+            ],
+            "journal": "Expert opinion on biological therapy",
+            "year": "2005",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "located in",
+      "source": "UniProt:P12319",
+      "target": "CL:0000097",
+      "evidence": [
+        {
+          "reference": "PMID:16750976",
+          "snippet": "can block IgE's binding to high-affinity IgE Fc receptors (FcepsilonRI) on mast cells and basophils",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Anti-IgE as a mast cell-stabilizing therapeutic agent.",
+            "authors": [
+              "Chang TW",
+              "Shiung YY"
+            ],
+            "journal": "The Journal of allergy and clinical immunology",
+            "year": "2006",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "decreased",
+      "source": "UniProt:P12319",
+      "target": "GO:0043303",
+      "evidence": [
+        {
+          "reference": "PMID:26509363",
+          "snippet": "We found that OmAb dissociates pre-bound IgE from mast cells and basophils, resulting in a reduction of proximal phosphorylation-mediated signalling events (Syk, PLCγ, and LAT) and in a decrease in degranulation and leukotriene synthesis.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Loss of IgE-FcepsilonRI signalling reduces mast cell degranulation.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Comparable actions of omalizumab on mast cells and basophils.",
+            "authors": [
+              "Serrano-Candelas E",
+              "Martinez-Aranguren R",
+              "Valero A",
+              "Bartra J",
+              "Gastaminza G",
+              "Goikoetxea MJ",
+              "Martín M",
+              "Ferrer M"
+            ],
+            "journal": "Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology",
+            "year": "2016",
+            "doi": "10.1111/cea.12668",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "causes",
+      "source": "GO:0043303",
+      "target": "MESH:D001249",
+      "evidence": [
+        {
+          "reference": "PMID:12110823",
+          "snippet": "coupling between IgE and FcepsilonRI receptors on mast cells leads to release of proinflammatory mediators and a subsequent influx of inflammatory cells to the affected organ",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Mast cell mediator release drives the allergic inflammation underlying asthma.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "The effect of omalizumab on nasal allergic inflammation.",
+            "authors": [
+              "Plewako H",
+              "Arvidsson M",
+              "Petruson K",
+              "Oancea I",
+              "Holmberg K",
+              "Adelroth E",
+              "Gustafsson H",
+              "Sandström T",
+              "Rak S"
+            ],
+            "journal": "The Journal of allergy and clinical immunology",
+            "year": "2002",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "treats",
+      "source": "DB:DB00043",
+      "target": "MESH:D001249",
+      "evidence": [
+        {
+          "reference": "PMID:16318424",
+          "snippet": "Omalizumab effectively alleviates the signs and symptoms of asthma.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Omalizumab: a future innovation for treatment of severe ocular allergy?",
+            "authors": [
+              "Williams PB",
+              "Sheppard JD"
+            ],
+            "journal": "Expert opinion on biological therapy",
+            "year": "2005",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00043",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    }
+  ],
+  "site": {
+    "id": "opus__P40",
+    "record_id": "P40_DB00043_MESH_D001249",
+    "run": "opus",
+    "run_label": "Opus (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/opus/outputs/P40.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/phase3__P01.json b/web-revamp-mockup/data/records/phase3__P01.json
new file mode 100644
index 0000000..2a35baa
--- /dev/null
+++ b/web-revamp-mockup/data/records/phase3__P01.json
@@ -0,0 +1,322 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P01_DB00945_MESH_D009203",
+    "drug": "Aspirin",
+    "drug_mesh": "MESH:D001241",
+    "drugbank": "DB:DB00945",
+    "disease": "Myocardial Infarction",
+    "disease_mesh": "MESH:D009203",
+    "summary": "Aspirin → Prostaglandin G/H synthase 1 → prostaglandin biosynthetic process → Thromboxane A2 → platelet aggregation → Myocardial Infarction"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D001241",
+      "name": "Aspirin",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P23219",
+      "name": "Prostaglandin G/H synthase 1",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0001516",
+      "name": "prostaglandin biosynthetic process",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D013928",
+      "name": "Thromboxane A2",
+      "label": "ChemicalSubstance"
+    },
+    {
+      "id": "GO:0070527",
+      "name": "platelet aggregation",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D009203",
+      "name": "Myocardial Infarction",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D001241",
+      "target": "UniProt:P23219",
+      "evidence": [
+        {
+          "reference": "PMID:23422285",
+          "snippet": "It acetylates Ser529 residue in cyclooxygenase-1 (COX-1) and prevents thromboxane A2 (TXA2) formation from arachidonic acid (AA) in platelets.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Aspirin covalently acetylates Ser529 of platelet COX-1, irreversibly inhibiting its catalytic activity (study in 108 aspirin-treated volunteers).",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "New direct and indirect methods for the detection of cyclooxygenase 1 acetylation by aspirin; the lack of aspirin resistance among healthy individuals.",
+            "authors": [
+              "Kovács EG",
+              "Katona E",
+              "Bereczky Z",
+              "Homoródi N",
+              "Balogh L",
+              "Tóth E",
+              "Péterfy H",
+              "Kiss RG",
+              "Edes I",
+              "Muszbek L"
+            ],
+            "journal": "Thrombosis research",
+            "year": "2013",
+            "doi": "10.1016/j.thromres.2013.01.033",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:32535107",
+          "snippet": "The most recognized mechanism of aspirin (acetylsalicylic acid, ASA) action, at therapeutic dosing, is the inhibition of prostanoid biosynthesis through the acetylation of cyclooxygenase (COX)-isozymes (COX-1 at serine-529 and COX-2 at serine-516).",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Quantitative proteomic confirmation that aspirin acetylates COX-1 at Ser529, the canonical mechanistic step.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Characterization of cyclooxygenase-2 acetylation and prostanoid inhibition by aspirin in cellular systems.",
+            "authors": [
+              "Tacconelli S",
+              "Contursi A",
+              "Falcone L",
+              "Mucci M",
+              "D'Agostino I",
+              "Fullone R",
+              "Sacco A",
+              "Zucchelli M",
+              "Bruno A",
+              "Ballerini P",
+              "Dovizio M",
+              "Patrignani P"
+            ],
+            "journal": "Biochemical pharmacology",
+            "year": "2020",
+            "doi": "10.1016/j.bcp.2020.114094",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P23219",
+      "target": "GO:0001516",
+      "evidence": [
+        {
+          "reference": "PMID:32535107",
+          "snippet": "The most recognized mechanism of aspirin (acetylsalicylic acid, ASA) action, at therapeutic dosing, is the inhibition of prostanoid biosynthesis through the acetylation of cyclooxygenase (COX)-isozymes (COX-1 at serine-529 and COX-2 at serine-516).",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Catalytically active COX-1 is required for prostanoid biosynthesis; acetylating COX-1 inhibits the prostaglandin biosynthetic process, confirming COX-1 positively regulates it.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Characterization of cyclooxygenase-2 acetylation and prostanoid inhibition by aspirin in cellular systems.",
+            "authors": [
+              "Tacconelli S",
+              "Contursi A",
+              "Falcone L",
+              "Mucci M",
+              "D'Agostino I",
+              "Fullone R",
+              "Sacco A",
+              "Zucchelli M",
+              "Bruno A",
+              "Ballerini P",
+              "Dovizio M",
+              "Patrignani P"
+            ],
+            "journal": "Biochemical pharmacology",
+            "year": "2020",
+            "doi": "10.1016/j.bcp.2020.114094",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "has output",
+      "source": "GO:0001516",
+      "target": "MESH:D013928",
+      "evidence": [
+        {
+          "reference": "PMID:23422285",
+          "snippet": "It acetylates Ser529 residue in cyclooxygenase-1 (COX-1) and prevents thromboxane A2 (TXA2) formation from arachidonic acid (AA) in platelets.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "TXA2 is the platelet-specific prostanoid generated from arachidonic acid via COX-1 — i.e. it is an output of the prostaglandin biosynthetic process in platelets.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "New direct and indirect methods for the detection of cyclooxygenase 1 acetylation by aspirin; the lack of aspirin resistance among healthy individuals.",
+            "authors": [
+              "Kovács EG",
+              "Katona E",
+              "Bereczky Z",
+              "Homoródi N",
+              "Balogh L",
+              "Tóth E",
+              "Péterfy H",
+              "Kiss RG",
+              "Edes I",
+              "Muszbek L"
+            ],
+            "journal": "Thrombosis research",
+            "year": "2013",
+            "doi": "10.1016/j.thromres.2013.01.033",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "MESH:D013928",
+      "target": "GO:0070527",
+      "evidence": [
+        {
+          "reference": "PMID:18752570",
+          "snippet": "These studies demonstrate a linear relationship between inhibition of platelet TXA(2) generation and TXA(2)-mediated aggregation.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "TXA2 generation tracks linearly with TXA2-mediated platelet aggregation; reducing TXA2 reduces aggregation, indicating positive regulation.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Aspirin and the in vitro linear relationship between thromboxane A2-mediated platelet aggregation and platelet production of thromboxane A2.",
+            "authors": [
+              "Armstrong PC",
+              "Truss NJ",
+              "Ali FY",
+              "Dhanji AA",
+              "Vojnovic I",
+              "Zain ZN",
+              "Bishop-Bailey D",
+              "Paul-Clark MJ",
+              "Tucker AT",
+              "Mitchell JA",
+              "Warner TD"
+            ],
+            "journal": "Journal of thrombosis and haemostasis : JTH",
+            "year": "2008",
+            "doi": "10.1111/j.1538-7836.2008.03133.x",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:16359516",
+          "snippet": "Collagen-induced TxA2 production of the entire cohort was 128.7 +/- 21.6 pg 10(-8) cells, and was significantly correlated with platelet aggregation (Spearman's correlation coefficient = 0.44; P < 0.0001).",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "In aspirin-treated patients, residual platelet TXA2 production correlates significantly with platelet aggregation, confirming TXA2 positively regulates aggregation in vivo.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Persistent production of platelet thromboxane A2 in patients chronically treated with aspirin.",
+            "authors": [
+              "Pulcinelli FM",
+              "Riondino S",
+              "Celestini A",
+              "Pignatelli P",
+              "Trifirò E",
+              "Di Renzo L",
+              "Violi F"
+            ],
+            "journal": "Journal of thrombosis and haemostasis : JTH",
+            "year": "2005",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "contributes to",
+      "source": "GO:0070527",
+      "target": "MESH:D009203",
+      "evidence": [
+        {
+          "reference": "PMID:2899772",
+          "snippet": "Aspirin significantly reduced non-fatal reinfarction (1.0% vs 2.0%) and non-fatal stroke (0.3% vs 0.6%), and was not associated with any significant increase in cerebral haemorrhage or in bleeds requiring transfusion.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "ISIS-2 landmark trial (n=17,187): aspirin — whose principal action is inhibition of platelet aggregation — halved non-fatal MI reinfarction, demonstrating that platelet aggregation contributes to MI.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Randomised trial of intravenous streptokinase, oral aspirin, both, or neither among 17,187 cases of suspected acute myocardial infarction: ISIS-2. ISIS-2 (Second International Study of Infarct Survival) Collaborative Group.",
+            "authors": [],
+            "journal": "Lancet (London, England)",
+            "year": "1988",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:2500270",
+          "snippet": "These finding suggest that platelet aggregation limits the response to coronary thrombolysis and that platelet activation in this setting is partly TXA2-dependent.",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "explanation": "Canine coronary thrombosis model showing platelet aggregation drives coronary thrombosis — the proximate pathophysiologic cause of myocardial infarction.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Increased thromboxane biosynthesis during coronary thrombolysis. Evidence that platelet activation and thromboxane A2 modulate the response to tissue-type plasminogen activator in vivo.",
+            "authors": [
+              "Fitzgerald DJ",
+              "Wright F",
+              "FitzGerald GA"
+            ],
+            "journal": "Circulation research",
+            "year": "1989",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00945#mechanism-of-action",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    },
+    {
+      "url": "https://www.uniprot.org/uniprot/P23219#function",
+      "type": "other",
+      "label": "uniprot.org — record source"
+    }
+  ],
+  "site": {
+    "id": "phase3__P01",
+    "record_id": "P01_DB00945_MESH_D009203",
+    "run": "phase3",
+    "run_label": "Phase-3 eval",
+    "source_file": "tests/phase3_eval_outputs/P01.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/phase3__P01_no_provider.json b/web-revamp-mockup/data/records/phase3__P01_no_provider.json
new file mode 100644
index 0000000..8ac572d
--- /dev/null
+++ b/web-revamp-mockup/data/records/phase3__P01_no_provider.json
@@ -0,0 +1,319 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P01_DB00945_MESH_D009203",
+    "drug": "Aspirin",
+    "drug_mesh": "MESH:D001241",
+    "drugbank": "DB:DB00945",
+    "disease": "Myocardial Infarction",
+    "disease_mesh": "MESH:D009203",
+    "summary": "Aspirin → Prostaglandin G/H synthase 1 → prostaglandin biosynthetic process → Thromboxane A2 → platelet aggregation → Myocardial Infarction"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D001241",
+      "name": "Aspirin",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P23219",
+      "name": "Prostaglandin G/H synthase 1",
+      "label": "Protein"
+    },
+    {
+      "id": "UniProt:P35354",
+      "name": "Prostaglandin G/H synthase 2",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0001516",
+      "name": "prostaglandin biosynthetic process",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D013928",
+      "name": "Thromboxane A2",
+      "label": "ChemicalSubstance"
+    },
+    {
+      "id": "GO:0070527",
+      "name": "platelet aggregation",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D009203",
+      "name": "Myocardial Infarction",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D001241",
+      "target": "UniProt:P23219",
+      "evidence": [
+        {
+          "reference": "PMID:23422285",
+          "snippet": "It acetylates Ser529 residue in cyclooxygenase-1 (COX-1) and prevents thromboxane A2 (TXA2) formation from arachidonic acid (AA) in platelets.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Aspirin covalently acetylates Ser529 of platelet COX-1, irreversibly inhibiting its catalytic activity.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "New direct and indirect methods for the detection of cyclooxygenase 1 acetylation by aspirin; the lack of aspirin resistance among healthy individuals.",
+            "authors": [
+              "Kovács EG",
+              "Katona E",
+              "Bereczky Z",
+              "Homoródi N",
+              "Balogh L",
+              "Tóth E",
+              "Péterfy H",
+              "Kiss RG",
+              "Edes I",
+              "Muszbek L"
+            ],
+            "journal": "Thrombosis research",
+            "year": "2013",
+            "doi": "10.1016/j.thromres.2013.01.033",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D001241",
+      "target": "UniProt:P35354",
+      "evidence": [
+        {
+          "reference": "PMID:36588714",
+          "snippet": "In cancer cells, ASA and IP1867B acted by inhibiting PGE2 and TXB2 generation via the acetylation of COX-2.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Aspirin (ASA) acetylates COX-2 at Serine 516, inhibiting its prostanoid-generating activity.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Characterization of the acetylation of cyclooxygenase-isozymes and targeted lipidomics of eicosanoids in serum and colon cancer cells by the new aspirin formulation IP1867B versus aspirin in vitro.",
+            "authors": [
+              "Hofling U",
+              "Tacconelli S",
+              "Contursi A",
+              "Bruno A",
+              "Mucci M",
+              "Ballerini P",
+              "Cohen S",
+              "Patrignani P"
+            ],
+            "journal": "Frontiers in pharmacology",
+            "year": "2022",
+            "doi": "10.3389/fphar.2022.1070277",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P23219",
+      "target": "GO:0001516",
+      "evidence": [
+        {
+          "reference": "PMID:38495101",
+          "snippet": "All aspirin doses caused comparable % acetylation of platelet COX-1 at Serine 529 associated with similar profound inhibition of platelet-dependent thromboxane (TX)A2 generation ex vivo (serum TXB2) and in vivo (urinary TXM).",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Catalytically intact COX-1 drives platelet prostanoid biosynthesis; its acetylation by aspirin suppresses thromboxane A2 (a prostaglandin-class product) generation.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Optimizing aspirin dose for colorectal cancer patients through deep phenotyping using novel biomarkers of drug action.",
+            "authors": [
+              "Patrignani P",
+              "Tacconelli S",
+              "Contursi A",
+              "Piazuelo E",
+              "Bruno A",
+              "Nobili S",
+              "Mazzei M",
+              "Milillo C",
+              "Hofling U",
+              "Hijos-Mallada G",
+              "Sostres C",
+              "Lanas A"
+            ],
+            "journal": "Frontiers in pharmacology",
+            "year": "2024",
+            "doi": "10.3389/fphar.2024.1362217",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P35354",
+      "target": "GO:0001516",
+      "evidence": [
+        {
+          "reference": "PMID:36588714",
+          "snippet": "In cancer cells, ASA and IP1867B acted by inhibiting PGE2 and TXB2 generation via the acetylation of COX-2.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "COX-2 activity is required for PGE2 and TXB2 (prostaglandin biosynthetic) generation; acetylation of COX-2 by aspirin reduces it.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Characterization of the acetylation of cyclooxygenase-isozymes and targeted lipidomics of eicosanoids in serum and colon cancer cells by the new aspirin formulation IP1867B versus aspirin in vitro.",
+            "authors": [
+              "Hofling U",
+              "Tacconelli S",
+              "Contursi A",
+              "Bruno A",
+              "Mucci M",
+              "Ballerini P",
+              "Cohen S",
+              "Patrignani P"
+            ],
+            "journal": "Frontiers in pharmacology",
+            "year": "2022",
+            "doi": "10.3389/fphar.2022.1070277",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "has output",
+      "source": "GO:0001516",
+      "target": "MESH:D013928",
+      "evidence": [
+        {
+          "reference": "PMID:23422285",
+          "snippet": "It acetylates Ser529 residue in cyclooxygenase-1 (COX-1) and prevents thromboxane A2 (TXA2) formation from arachidonic acid (AA) in platelets.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "TXA2 is the platelet-specific prostanoid output of COX-1-mediated arachidonic acid metabolism (the prostaglandin biosynthetic process).",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "New direct and indirect methods for the detection of cyclooxygenase 1 acetylation by aspirin; the lack of aspirin resistance among healthy individuals.",
+            "authors": [
+              "Kovács EG",
+              "Katona E",
+              "Bereczky Z",
+              "Homoródi N",
+              "Balogh L",
+              "Tóth E",
+              "Péterfy H",
+              "Kiss RG",
+              "Edes I",
+              "Muszbek L"
+            ],
+            "journal": "Thrombosis research",
+            "year": "2013",
+            "doi": "10.1016/j.thromres.2013.01.033",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "MESH:D013928",
+      "target": "GO:0070527",
+      "evidence": [
+        {
+          "reference": "PMID:21844189",
+          "snippet": "Exposing aspirin to erythrocytes blocked its ability to inhibit thromboxane A(2) synthesis and platelet aggregation.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Loss of inhibition of TXA2 synthesis tracks with loss of inhibition of platelet aggregation, consistent with TXA2 driving aggregation.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Intracellular erythrocyte platelet-activating factor acetylhydrolase I inactivates aspirin in blood.",
+            "authors": [
+              "Zhou G",
+              "Marathe GK",
+              "Willard B",
+              "McIntyre TM"
+            ],
+            "journal": "The Journal of biological chemistry",
+            "year": "2011",
+            "doi": "10.1074/jbc.M111.267161",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "contributes to",
+      "source": "GO:0070527",
+      "target": "MESH:D009203",
+      "evidence": [
+        {
+          "reference": "PMID:17323609",
+          "snippet": "aspirin significantly reduced the risk of both, fatal and non-fatal myocardial infarction",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Aspirin's inhibition of platelet aggregation translates to a reduction in MI risk, indicating platelet aggregation contributes to MI.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "[Milestones of cardivascular pharmacotherapy: salicylates and aspirin].",
+            "authors": [
+              "Jerie P"
+            ],
+            "journal": "Casopis lekaru ceskych",
+            "year": "2006",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00945#mechanism-of-action",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    },
+    {
+      "url": "https://www.uniprot.org/uniprot/P23219#function",
+      "type": "other",
+      "label": "uniprot.org — record source"
+    },
+    {
+      "url": "https://www.uniprot.org/uniprot/P35354#function",
+      "type": "other",
+      "label": "uniprot.org — record source"
+    }
+  ],
+  "site": {
+    "id": "phase3__P01_no_provider",
+    "record_id": "P01_DB00945_MESH_D009203",
+    "run": "phase3",
+    "run_label": "Phase-3 eval",
+    "source_file": "tests/phase3_eval_outputs/P01_no_provider.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/phase3__P02.json b/web-revamp-mockup/data/records/phase3__P02.json
new file mode 100644
index 0000000..364ce3e
--- /dev/null
+++ b/web-revamp-mockup/data/records/phase3__P02.json
@@ -0,0 +1,264 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P02_DB01076_MESH_D006937",
+    "drug": "Atorvastatin",
+    "drug_mesh": "MESH:D000069059",
+    "drugbank": "DB:DB01076",
+    "disease": "Hypercholesterolemia",
+    "disease_mesh": "MESH:D006937",
+    "summary": "Atorvastatin → 3-hydroxy-3-methylglutaryl-coenzyme A reductase → cholesterol biosynthetic process → Cholesterol → Hypercholesterolemia"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D000069059",
+      "name": "Atorvastatin",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P04035",
+      "name": "3-hydroxy-3-methylglutaryl-coenzyme A reductase",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0006695",
+      "name": "cholesterol biosynthetic process",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D002784",
+      "name": "Cholesterol",
+      "label": "ChemicalSubstance"
+    },
+    {
+      "id": "MESH:D006937",
+      "name": "Hypercholesterolemia",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D000069059",
+      "target": "UniProt:P04035",
+      "evidence": [
+        {
+          "reference": "PMID:21182938",
+          "snippet": "Atorvastatin is a selective HMG-CoA reductase competitive inhibitor, used for the treatment of hyperlipidaemia.",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "explanation": "Atorvastatin is a selective competitive inhibitor of HMG-CoA reductase, decreasing the enzyme's catalytic activity (stated in a rat pharmacokinetic study).",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Influence of atorvastatin on the pharmacokinetics and pharmacodynamics of glyburide in normal and diabetic rats.",
+            "authors": [
+              "Neerati P",
+              "Gade J"
+            ],
+            "journal": "European journal of pharmaceutical sciences : official journal of the European Federation for Pharmaceutical Sciences",
+            "year": "2011",
+            "doi": "10.1016/j.ejps.2010.12.006",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:9825877",
+          "snippet": "Atorvastatin calcium, a synthetic stereoisomer of a pentasubstituted pyrrole, prevents the conversion of HMG-CoA by competitive and selective inhibition of HMG-CoA reductase.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Pharmacology review confirming atorvastatin acts by competitive and selective inhibition of HMG-CoA reductase, blocking conversion of its HMG-CoA substrate.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Atorvastatin: a hydroxymethylglutaryl-coenzyme A reductase inhibitor.",
+            "authors": [
+              "Malinowski JM"
+            ],
+            "journal": "American journal of health-system pharmacy : AJHP : official journal of the American Society of Health-System Pharmacists",
+            "year": "1998",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P04035",
+      "target": "GO:0006695",
+      "evidence": [
+        {
+          "reference": "PMID:42015365",
+          "snippet": "Functional assays revealed that atorvastatin-mediated HMG-CoA reductase inhibition, the rate limiting enzyme in cholesterol biosynthesis, prevents cholesterol buildup and lipid droplet formation in macrophages.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "HMG-CoA reductase is identified as the rate-limiting enzyme of cholesterol biosynthesis; its catalytic activity drives (positively regulates) the cholesterol biosynthetic process.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "An environmentally relevant mixture of organophosphate esters induces cholesterol biosynthesis in THP-1 macrophages.",
+            "authors": [
+              "Giles BH",
+              "Robaire B",
+              "Mann KK"
+            ],
+            "journal": "Toxicological sciences : an official journal of the Society of Toxicology",
+            "year": "2026",
+            "doi": "10.1093/toxsci/kfag048",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:42112329",
+          "snippet": "Atorvastatin, a widely used statin, primarily functions by inhibiting 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase, the rate-limiting enzyme in the mevalonate pathway, thereby lowering cholesterol.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "HMG-CoA reductase is the rate-limiting enzyme of the mevalonate pathway (cholesterol biosynthesis); inhibiting it lowers cholesterol, confirming the enzyme positively regulates the biosynthetic process.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Atorvastatin as a pleiotropic anticancer agent: mechanisms, evidence, and therapeutic repurposing potential.",
+            "authors": [
+              "Su J",
+              "Ji C",
+              "Niu X",
+              "Wu Z",
+              "Shi L",
+              "Kang L",
+              "Li D",
+              "Ma Y",
+              "Pang G",
+              "Ma X",
+              "Zhou CM",
+              "Jiang X",
+              "Pang B"
+            ],
+            "journal": "Frontiers in immunology",
+            "year": "2026",
+            "doi": "10.3389/fimmu.2026.1808729",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "abundance",
+      "object_direction_qualifier": "increased",
+      "source": "GO:0006695",
+      "target": "MESH:D002784",
+      "evidence": [
+        {
+          "reference": "PMID:42015365",
+          "snippet": "Functional assays revealed that atorvastatin-mediated HMG-CoA reductase inhibition, the rate limiting enzyme in cholesterol biosynthesis, prevents cholesterol buildup and lipid droplet formation in macrophages.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Blocking the cholesterol biosynthetic process (via HMG-CoA reductase inhibition) prevents cholesterol buildup — i.e. the biosynthetic process increases cellular cholesterol abundance.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "An environmentally relevant mixture of organophosphate esters induces cholesterol biosynthesis in THP-1 macrophages.",
+            "authors": [
+              "Giles BH",
+              "Robaire B",
+              "Mann KK"
+            ],
+            "journal": "Toxicological sciences : an official journal of the Society of Toxicology",
+            "year": "2026",
+            "doi": "10.1093/toxsci/kfag048",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:42112329",
+          "snippet": "Atorvastatin, a widely used statin, primarily functions by inhibiting 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase, the rate-limiting enzyme in the mevalonate pathway, thereby lowering cholesterol.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Inhibiting the rate-limiting step of the cholesterol biosynthetic (mevalonate) pathway lowers cholesterol, confirming the pathway's output is cholesterol.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Atorvastatin as a pleiotropic anticancer agent: mechanisms, evidence, and therapeutic repurposing potential.",
+            "authors": [
+              "Su J",
+              "Ji C",
+              "Niu X",
+              "Wu Z",
+              "Shi L",
+              "Kang L",
+              "Li D",
+              "Ma Y",
+              "Pang G",
+              "Ma X",
+              "Zhou CM",
+              "Jiang X",
+              "Pang B"
+            ],
+            "journal": "Frontiers in immunology",
+            "year": "2026",
+            "doi": "10.3389/fimmu.2026.1808729",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "contributes to",
+      "source": "MESH:D002784",
+      "target": "MESH:D006937",
+      "evidence": [
+        {
+          "reference": "PMID:9825877",
+          "snippet": "Like other statins, atorvastatin reduces low-density-lipoprotein cholesterol (LDL-C) and total cholesterol in patients with hypercholesterolemia.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Elevated total/LDL cholesterol is the defining feature of hypercholesterolemia; reducing cholesterol in patients with hypercholesterolemia treats the disease, confirming cholesterol contributes to the disease state.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Atorvastatin: a hydroxymethylglutaryl-coenzyme A reductase inhibitor.",
+            "authors": [
+              "Malinowski JM"
+            ],
+            "journal": "American journal of health-system pharmacy : AJHP : official journal of the American Society of Health-System Pharmacists",
+            "year": "1998",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB01076#mechanism-of-action",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    },
+    {
+      "url": "https://www.uniprot.org/uniprot/P04035#function",
+      "type": "other",
+      "label": "uniprot.org — record source"
+    }
+  ],
+  "site": {
+    "id": "phase3__P02",
+    "record_id": "P02_DB01076_MESH_D006937",
+    "run": "phase3",
+    "run_label": "Phase-3 eval",
+    "source_file": "tests/phase3_eval_outputs/P02.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/phase3__P03.json b/web-revamp-mockup/data/records/phase3__P03.json
new file mode 100644
index 0000000..51b36b6
--- /dev/null
+++ b/web-revamp-mockup/data/records/phase3__P03.json
@@ -0,0 +1,203 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P03_DB00722_MESH_D006973",
+    "drug": "Lisinopril",
+    "drug_mesh": "MESH:D017706",
+    "drugbank": "DB:DB00722",
+    "disease": "Hypertension",
+    "disease_mesh": "MESH:D006973",
+    "summary": "Lisinopril → Angiotensin-converting enzyme → Angiotensin II → Hypertension"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D017706",
+      "name": "Lisinopril",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P12821",
+      "name": "Angiotensin-converting enzyme",
+      "label": "Protein"
+    },
+    {
+      "id": "MESH:D000804",
+      "name": "Angiotensin II",
+      "label": "ChemicalSubstance"
+    },
+    {
+      "id": "MESH:D006973",
+      "name": "Hypertension",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D017706",
+      "target": "UniProt:P12821",
+      "evidence": [
+        {
+          "reference": "PMID:41534066",
+          "snippet": "we treated flies with the angiotensin-converting enzyme (ACE) inhibitor lisinopril.",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "explanation": "Lisinopril is identified as an angiotensin-converting enzyme (ACE) inhibitor, i.e. it decreases the catalytic activity of ACE.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Selection for Postponed Senescence in Drosophila melanogaster Reveals Distinct Metabolic Aging Trajectories Modifiable by the Angiotensin-Converting Enzyme Inhibitor Lisinopril.",
+            "authors": [
+              "Vecchié D",
+              "Anholt RRH",
+              "Mackay TFC",
+              "De Luca M"
+            ],
+            "journal": "Aging cell",
+            "year": "2026",
+            "doi": "10.1111/acel.70375",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:41532628",
+          "snippet": "lisinopril suppressed Ang II",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "explanation": "In spontaneously hypertensive rats, lisinopril suppressed angiotensin II, the functional readout of decreased ACE activity (ACE is the enzyme that produces Ang II).",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Combined RAS Modulation: The Effect on Plasma and Tissue Angiotensin Peptide Levels.",
+            "authors": [
+              "Paulis L",
+              "Rajkovicova R",
+              "Repova K",
+              "Gubo G",
+              "Barta A",
+              "Poglitsch M",
+              "Domenig O",
+              "Andelova N",
+              "Ferko M",
+              "Pechanova O",
+              "Simko F"
+            ],
+            "journal": "Physiological research",
+            "year": "2025",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "produces",
+      "source": "UniProt:P12821",
+      "target": "MESH:D000804",
+      "evidence": [
+        {
+          "reference": "PMID:41154607",
+          "snippet": "controls blood pressure through Angiotensin II, an octapeptide hormone generated from Angiotensin I by Angiotensin-Converting Enzyme (ACE)",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Angiotensin-Converting Enzyme generates the octapeptide hormone Angiotensin II from Angiotensin I, i.e. ACE produces angiotensin II.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Angiotensin-Converting Enzyme Inhibitors and Metabolic Aging: A Drosophila Perspective.",
+            "authors": [
+              "Vecchie' D",
+              "Faber VG",
+              "Jumbo-Lucioni P",
+              "Anholt RRH",
+              "Mackay TFC",
+              "De Luca M"
+            ],
+            "journal": "Biomolecules",
+            "year": "2025",
+            "doi": "10.3390/biom15101378",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:42244833",
+          "snippet": "ATII is converted from angiotensin I by the action of the angiotensin-converting enzyme (ACE).",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Angiotensin II (ATII) is produced from angiotensin I by the action of ACE, confirming ACE produces angiotensin II.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Successful treatment of refractory anaphylactic shock with angiotensin II: A case report.",
+            "authors": [
+              "Bajec KB",
+              "Möller Petrun A"
+            ],
+            "journal": "European journal of anaesthesiology and intensive care",
+            "year": "2026",
+            "doi": "10.1097/EA9.0000000000000104",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "causes",
+      "source": "MESH:D000804",
+      "target": "MESH:D006973",
+      "evidence": [
+        {
+          "reference": "PMID:41185995",
+          "snippet": "Ang II (angiotensin II) causes hypertension and vascular inflammation both directly and indirectly via cytokines",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "explanation": "Angiotensin II causes hypertension, the terminal disease node; reducing Ang II (via lisinopril's ACE inhibition) therefore lowers blood pressure.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Smooth Muscle LRRC8A Knockout Preserves Vascular Function in Ang II Hypertension.",
+            "authors": [
+              "Choi H",
+              "Panja S",
+              "Nguyen HN",
+              "Stark RJ",
+              "Lamb FS"
+            ],
+            "journal": "Hypertension (Dallas, Tex. : 1979)",
+            "year": "2026",
+            "doi": "10.1161/HYPERTENSIONAHA.125.25222",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00722#mechanism-of-action",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    },
+    {
+      "url": "https://www.uniprot.org/uniprot/P12821#function",
+      "type": "other",
+      "label": "uniprot.org — record source"
+    }
+  ],
+  "site": {
+    "id": "phase3__P03",
+    "record_id": "P03_DB00722_MESH_D006973",
+    "run": "phase3",
+    "run_label": "Phase-3 eval",
+    "source_file": "tests/phase3_eval_outputs/P03.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/phase3__P04.json b/web-revamp-mockup/data/records/phase3__P04.json
new file mode 100644
index 0000000..56f0fa3
--- /dev/null
+++ b/web-revamp-mockup/data/records/phase3__P04.json
@@ -0,0 +1,252 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P04_DB00264_MESH_D006333",
+    "drug": "Metoprolol",
+    "drug_mesh": "MESH:D008790",
+    "drugbank": "DB:DB00264",
+    "disease": "Heart failure",
+    "disease_mesh": "MESH:D006333",
+    "summary": "Metoprolol → Beta-1 adrenergic receptor → cardiac muscle hypertrophy → Heart failure"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D008790",
+      "name": "Metoprolol",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P08588",
+      "name": "Beta-1 adrenergic receptor",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0003300",
+      "name": "cardiac muscle hypertrophy",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D006333",
+      "name": "Heart failure",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D008790",
+      "target": "UniProt:P08588",
+      "evidence": [
+        {
+          "reference": "PMID:22617407",
+          "snippet": "Most of these effects were reduced in BNP-Sham and PMI mice by the selective β1-adrenergic blocker metoprolol.",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "explanation": "Identifies metoprolol as a selective β1-adrenergic blocker, i.e. it decreases the activity of the beta-1 adrenergic receptor.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Functional evidence for an active role of B-type natriuretic peptide in cardiac remodelling and pro-arrhythmogenicity.",
+            "authors": [
+              "Thireau J",
+              "Karam S",
+              "Fauconnier J",
+              "Roberge S",
+              "Cassan C",
+              "Cazorla O",
+              "Aimond F",
+              "Lacampagne A",
+              "Babuty D",
+              "Richard S"
+            ],
+            "journal": "Cardiovascular research",
+            "year": "2012",
+            "doi": "10.1093/cvr/cvs167",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:41920890",
+          "snippet": "Metoprolol tartrate, a β1-receptor blocker with a short half-life and low oral bioavailability, was selected as the model drug.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Confirms metoprolol's mechanism class as a β1-receptor blocker (antagonist), decreasing beta-1 adrenergic receptor activity.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Design and evaluation of a novel expandable gastroretentive film for sustained Metoprolol release.",
+            "authors": [
+              "Khalaf MM",
+              "Sajad O",
+              "Sammour RMF",
+              "Abdul Rasool BK"
+            ],
+            "journal": "PloS one",
+            "year": "2026",
+            "doi": "10.1371/journal.pone.0345598",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P08588",
+      "target": "GO:0003300",
+      "evidence": [
+        {
+          "reference": "PMID:35053304",
+          "snippet": "The present study tested the hypothesis that sympathetic-mediated hypertrophy of neonatal rat ventricular cardiomyocytes (NRVMs) translated to an increase in calcium influx secondary to the upregulation of CaV1.2 channel subunits.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Sympathetic (catecholamine/β1-adrenergic) stimulation of ventricular cardiomyocytes drives a hypertrophic response, i.e. β1-adrenergic receptor signaling positively regulates cardiac muscle hypertrophy.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Sympathetic Stimulation Upregulates the Ca2+ Channel Subunit, CaVα2δ1, via the β1 and ERK 1/2 Pathway in Neonatal Ventricular Cardiomyocytes.",
+            "authors": [
+              "Al Katat A",
+              "Zhao J",
+              "Calderone A",
+              "Parent L"
+            ],
+            "journal": "Cells",
+            "year": "2022",
+            "doi": "10.3390/cells11020188",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:35053304",
+          "snippet": "Confocal imaging of norepinephrine (NE)-treated NRVMs revealed a hypertrophic response compared to untreated NRVMs.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Norepinephrine acting through the β1-adrenergic receptor produces a hypertrophic response in ventricular cardiomyocytes, evidencing positive regulation of cardiac muscle hypertrophy by β1-AR signaling.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Sympathetic Stimulation Upregulates the Ca2+ Channel Subunit, CaVα2δ1, via the β1 and ERK 1/2 Pathway in Neonatal Ventricular Cardiomyocytes.",
+            "authors": [
+              "Al Katat A",
+              "Zhao J",
+              "Calderone A",
+              "Parent L"
+            ],
+            "journal": "Cells",
+            "year": "2022",
+            "doi": "10.3390/cells11020188",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:27001422",
+          "snippet": "Overstimulation of the orthosympathetic system leads to cardiovascular cell and tissue damage through prolonged activation of β-1-2 adrenergic receptors (BARs).",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Prolonged activation of β1 adrenergic receptors drives maladaptive cardiac tissue changes (including hypertrophy), supporting that β1-AR signaling positively regulates pathological cardiac muscle hypertrophy.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Cardiac salvage by tweaking with beta-3-adrenergic receptors.",
+            "authors": [
+              "Balligand JL"
+            ],
+            "journal": "Cardiovascular research",
+            "year": "2016",
+            "doi": "10.1093/cvr/cvw056",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "contributes to",
+      "source": "GO:0003300",
+      "target": "MESH:D006333",
+      "evidence": [
+        {
+          "reference": "PMID:26631854",
+          "snippet": "Chronic activation of the sympathetic nervous system (SNS) contributes to cardiac remodeling and the transition to heart failure (HF).",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "explanation": "Pathological cardiac muscle hypertrophy is the central maladaptive component of cardiac remodeling; chronic sympathetic-driven remodeling contributes to the transition to heart failure.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Renal denervation mitigates cardiac remodeling and renal damage in Dahl rats: a comparison with β-receptor blockade.",
+            "authors": [
+              "Watanabe H",
+              "Iwanaga Y",
+              "Miyaji Y",
+              "Yamamoto H",
+              "Miyazaki S"
+            ],
+            "journal": "Hypertension research : official journal of the Japanese Society of Hypertension",
+            "year": "2016",
+            "doi": "10.1038/hr.2015.133",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:22617407",
+          "snippet": "Elevated BNP levels, by inducing sympathetic overdrive and altering Ca(2+) handling, promote adverse cardiac remodelling and VAs, which could account in part for the progression of HF after MI.",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "explanation": "Adverse cardiac remodelling (of which pathological muscle hypertrophy is the core process) contributes to the progression of heart failure.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Functional evidence for an active role of B-type natriuretic peptide in cardiac remodelling and pro-arrhythmogenicity.",
+            "authors": [
+              "Thireau J",
+              "Karam S",
+              "Fauconnier J",
+              "Roberge S",
+              "Cassan C",
+              "Cazorla O",
+              "Aimond F",
+              "Lacampagne A",
+              "Babuty D",
+              "Richard S"
+            ],
+            "journal": "Cardiovascular research",
+            "year": "2012",
+            "doi": "10.1093/cvr/cvs167",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00264#mechanism-of-action",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    },
+    {
+      "url": "https://www.uniprot.org/uniprot/P08588#function",
+      "type": "other",
+      "label": "uniprot.org — record source"
+    }
+  ],
+  "site": {
+    "id": "phase3__P04",
+    "record_id": "P04_DB00264_MESH_D006333",
+    "run": "phase3",
+    "run_label": "Phase-3 eval",
+    "source_file": "tests/phase3_eval_outputs/P04.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/phase3__P05.json b/web-revamp-mockup/data/records/phase3__P05.json
new file mode 100644
index 0000000..a2414a6
--- /dev/null
+++ b/web-revamp-mockup/data/records/phase3__P05.json
@@ -0,0 +1,225 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P05_DB00758_MESH_D020521",
+    "drug": "Clopidogrel",
+    "drug_mesh": "MESH:D000077144",
+    "drugbank": "DB:DB00758",
+    "disease": "Stroke",
+    "disease_mesh": "MESH:D020521",
+    "summary": "Clopidogrel → P2Y purinoceptor 12 → platelet aggregation → Stroke"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D000077144",
+      "name": "Clopidogrel",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:Q9H244",
+      "name": "P2Y purinoceptor 12",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0070527",
+      "name": "platelet aggregation",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D020521",
+      "name": "Stroke",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D000077144",
+      "target": "UniProt:Q9H244",
+      "evidence": [
+        {
+          "reference": "PMID:27386066",
+          "snippet": "Clopidogrel is a prodrug that converts in the liver to an active thiol metabolite, which irreversibly inhibits the platelet P2Y12 adenosine diphosphate receptor.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Clopidogrel is a prodrug whose active thiol metabolite irreversibly inhibits the platelet P2Y12 ADP receptor, decreasing the receptor's activity.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "\"Influence of methadone on clopidogrel in addicts on methadone maintenance therapy\" Drug interaction between methadone and clopidogrel.",
+            "authors": [
+              "Fallah F",
+              "Hamidikenari A",
+              "Sajadi SN",
+              "Sajadi SR",
+              "Shiran M"
+            ],
+            "journal": "Caspian journal of internal medicine",
+            "year": "2016",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:40195768",
+          "snippet": "The pharmacological activity of clopidogrel and prasugrel is mediated by sulfhydryl-containing active metabolites, which form disulfide bonds with P2Y12 receptors on the surface of platelets to inhibit their aggregation.",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "explanation": "Clopidogrel's active metabolite forms disulfide bonds with platelet P2Y12 receptors, irreversibly inhibiting the receptor and thereby its downstream aggregation function.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Mesoporous Silica Nanotraps for Mitigating Bleeding Risk From 'Irreversible' Antiplatelet Drugs.",
+            "authors": [
+              "Liu Y",
+              "Wang C",
+              "Wei P",
+              "Yang C",
+              "Cheng X",
+              "Zhang Y",
+              "Nie G"
+            ],
+            "journal": "Advanced materials (Deerfield Beach, Fla.)",
+            "year": "2025",
+            "doi": "10.1002/adma.202501576",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:Q9H244",
+      "target": "GO:0070527",
+      "evidence": [
+        {
+          "reference": "PMID:15955565",
+          "snippet": "The ATP-gated channel P2X1 and the 2 G protein-coupled P2Y1 and P2Y12 ADP receptors selectively contribute to platelet aggregation.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "The P2Y12 ADP receptor selectively contributes to (positively regulates) platelet aggregation, per a pharmacology review of platelet P2 receptors.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "The platelet P2 receptors as molecular targets for old and new antiplatelet drugs.",
+            "authors": [
+              "Gachet C"
+            ],
+            "journal": "Pharmacology & therapeutics",
+            "year": "2005",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:15955565",
+          "snippet": "the P2Y12 receptor is responsible for the completion and amplification of the response to ADP and to all platelet agonists, including thromboxane A2 (TXA2), thrombin, and collagen.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "P2Y12 drives the completion and amplification of platelet activation to ADP and all platelet agonists, establishing it as a positive regulator of platelet aggregation.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "The platelet P2 receptors as molecular targets for old and new antiplatelet drugs.",
+            "authors": [
+              "Gachet C"
+            ],
+            "journal": "Pharmacology & therapeutics",
+            "year": "2005",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "contributes to",
+      "source": "GO:0070527",
+      "target": "MESH:D020521",
+      "evidence": [
+        {
+          "reference": "PMID:41896895",
+          "snippet": "Platelets bind to collagen, leading to platelet activation, aggregation, and thrombus formation.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Platelet aggregation leads to thrombus formation, the proximate cause of ischemic stroke; the review frames atherosclerosis-driven platelet aggregation as a cause of ischemic stroke.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Research advances on platelet glycoprotein VI in ischemic stroke.",
+            "authors": [
+              "Xiang H",
+              "Ding K",
+              "Meng F",
+              "Huo M",
+              "Yao W",
+              "Wang H"
+            ],
+            "journal": "Thrombosis journal",
+            "year": "2026",
+            "doi": "10.1186/s12959-026-00859-4",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:29157825",
+          "snippet": "Platelet activation and subsequent accumulation at sites of vascular injury perform a central role in thrombus formation, which is believed to be the trigger of several cardiovascular diseases, such as atherosclerosis, myocardial infarction and strokes.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Platelet activation/aggregation drives thrombus formation, identified as the trigger of strokes, so platelet aggregation contributes to stroke.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "1, 6-di-O-caffeoyl-β-D-glucopyranoside, a natural compound from Callicarpa nudiflora Hook impairs P2Y12 and thromboxane A2 receptor-mediated amplification of platelet activation and aggregation.",
+            "authors": [
+              "Fu J",
+              "Zhu X",
+              "Wang W",
+              "Lu H",
+              "Zhang Z",
+              "Liu T",
+              "Xu H",
+              "Fu H",
+              "Ma S",
+              "Luo Y"
+            ],
+            "journal": "Phytomedicine : international journal of phytotherapy and phytopharmacology",
+            "year": "2017",
+            "doi": "10.1016/j.phymed.2017.10.012",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00758#mechanism-of-action",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    },
+    {
+      "url": "https://www.uniprot.org/uniprot/Q9H244#function",
+      "type": "other",
+      "label": "uniprot.org — record source"
+    }
+  ],
+  "site": {
+    "id": "phase3__P05",
+    "record_id": "P05_DB00758_MESH_D020521",
+    "run": "phase3",
+    "run_label": "Phase-3 eval",
+    "source_file": "tests/phase3_eval_outputs/P05.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/phase3__P06.json b/web-revamp-mockup/data/records/phase3__P06.json
new file mode 100644
index 0000000..4404c6f
--- /dev/null
+++ b/web-revamp-mockup/data/records/phase3__P06.json
@@ -0,0 +1,261 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P06_DB00675_MESH_D001943",
+    "drug": "Tamoxifen",
+    "drug_mesh": "MESH:D013629",
+    "drugbank": "DB:DB00675",
+    "disease": "Breast Neoplasms",
+    "disease_mesh": "MESH:D001943",
+    "summary": "Tamoxifen → Estrogen receptor → cell population proliferation → Breast Neoplasms"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D013629",
+      "name": "Tamoxifen",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P03372",
+      "name": "Estrogen receptor",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0008283",
+      "name": "cell population proliferation",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D001943",
+      "name": "Breast Neoplasms",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D013629",
+      "target": "UniProt:P03372",
+      "evidence": [
+        {
+          "reference": "PMID:41173946",
+          "snippet": "Endoxifen is a potent antiestrogen that binds and blocks estrogen receptor alpha (ERα) and estrogen receptor beta (ERβ).",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Endoxifen is the active metabolite of tamoxifen; as a potent antiestrogen it binds and blocks the estrogen receptor, decreasing its transcriptional activity — the established mechanism by which tamoxifen acts on the estrogen receptor.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Evaluation of (Z)-endoxifen as a potential therapy for glioblastoma multiforme through computational and experimental analyses.",
+            "authors": [
+              "Shneyderman A",
+              "Hammer SS",
+              "Remmel HL",
+              "Veviorskiy A",
+              "Alawi KM",
+              "Ustiugova A",
+              "Korzinkin M",
+              "Zhavoronkov A",
+              "Quay SC"
+            ],
+            "journal": "Scientific reports",
+            "year": "2025",
+            "doi": "10.1038/s41598-025-22034-x",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:42249585",
+          "snippet": "Estrogen receptor-positive (ER+) tumors are treated with endocrine therapies such as tamoxifen or aromatase inhibitors (AI), aimed at disrupting estrogen signaling.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Tamoxifen is an endocrine therapy that acts by disrupting estrogen signaling through the estrogen receptor, i.e. decreasing receptor activity.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "PAK1 activation drives divergent resistance mechanisms to aromatase inhibition and tamoxifen in a luminal: A breast cancer model.",
+            "authors": [
+              "Schwarzmüller L",
+              "Müller J",
+              "Vlachavas EI",
+              "Beumers L",
+              "Fleischhacker L",
+              "Burmester S",
+              "Wörner A",
+              "Karolus S",
+              "Helm D",
+              "Körner C",
+              "Wiemann S"
+            ],
+            "journal": "Molecular oncology",
+            "year": "2026",
+            "doi": "10.1002/1878-0261.70286",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P03372",
+      "target": "GO:0008283",
+      "evidence": [
+        {
+          "reference": "PMID:42210419",
+          "snippet": "Estrogen receptor alpha (ERα) plays a crucial role in the proliferation and survival of ER-positive breast cancer cells, and tamoxifen (TAM) remains the mainstay of endocrine therapy.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Estrogen receptor alpha signaling drives (positively regulates) the proliferation of ER-positive breast cancer cells; blocking it with tamoxifen removes this proliferative drive.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Cannabidiol enhances tamoxifen efficacy via CREB-mediated suppression of ERα signaling in ER-positive breast cancer cells.",
+            "authors": [
+              "Kim BG",
+              "Kim O",
+              "Lee DY",
+              "Kim BR",
+              "Kim DY",
+              "Namgung Y",
+              "Bong JW",
+              "Kang S",
+              "Lee SI",
+              "Oh SC"
+            ],
+            "journal": "Cell & bioscience",
+            "year": "2026",
+            "doi": "10.1186/s13578-026-01588-x",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "positively correlated with",
+      "source": "GO:0008283",
+      "target": "MESH:D001943",
+      "evidence": [
+        {
+          "reference": "PMID:42210419",
+          "snippet": "Estrogen receptor alpha (ERα) plays a crucial role in the proliferation and survival of ER-positive breast cancer cells, and tamoxifen (TAM) remains the mainstay of endocrine therapy.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Sustained cell proliferation of ER-positive breast cancer cells is the hallmark driving the breast neoplasm; proliferation is positively correlated with the malignant disease state.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Cannabidiol enhances tamoxifen efficacy via CREB-mediated suppression of ERα signaling in ER-positive breast cancer cells.",
+            "authors": [
+              "Kim BG",
+              "Kim O",
+              "Lee DY",
+              "Kim BR",
+              "Kim DY",
+              "Namgung Y",
+              "Bong JW",
+              "Kang S",
+              "Lee SI",
+              "Oh SC"
+            ],
+            "journal": "Cell & bioscience",
+            "year": "2026",
+            "doi": "10.1186/s13578-026-01588-x",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "treats",
+      "source": "MESH:D013629",
+      "target": "MESH:D001943",
+      "evidence": [
+        {
+          "reference": "PMID:42249585",
+          "snippet": "Estrogen receptor-positive (ER+) tumors are treated with endocrine therapies such as tamoxifen or aromatase inhibitors (AI), aimed at disrupting estrogen signaling.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Tamoxifen is the mainstay endocrine therapy used to treat estrogen receptor-positive breast tumors by disrupting estrogen signaling that drives tumor proliferation.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "PAK1 activation drives divergent resistance mechanisms to aromatase inhibition and tamoxifen in a luminal: A breast cancer model.",
+            "authors": [
+              "Schwarzmüller L",
+              "Müller J",
+              "Vlachavas EI",
+              "Beumers L",
+              "Fleischhacker L",
+              "Burmester S",
+              "Wörner A",
+              "Karolus S",
+              "Helm D",
+              "Körner C",
+              "Wiemann S"
+            ],
+            "journal": "Molecular oncology",
+            "year": "2026",
+            "doi": "10.1002/1878-0261.70286",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:42049437",
+          "snippet": "primary endocrine therapy with tamoxifen was initiated. The patient demonstrated clinical regression within three months and tolerated therapy well.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Clinical case of ER-positive breast cancer in which tamoxifen monotherapy produced clinical regression, demonstrating tamoxifen treats the disease.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Breast Cancer Recurrence After 46 Years of Remission: A Case Report and Clinical Implications.",
+            "authors": [
+              "Parkash H",
+              "Bandealy A",
+              "Rashid S",
+              "Kakuturu A",
+              "Parekh Y",
+              "Muzammil Z",
+              "Ali M",
+              "Rasool H"
+            ],
+            "journal": "In vivo (Athens, Greece)",
+            "year": "2026",
+            "doi": "10.21873/invivo.14331",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00675#mechanism-of-action",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    },
+    {
+      "url": "https://www.uniprot.org/uniprot/P03372#function",
+      "type": "other",
+      "label": "uniprot.org — record source"
+    }
+  ],
+  "site": {
+    "id": "phase3__P06",
+    "record_id": "P06_DB00675_MESH_D001943",
+    "run": "phase3",
+    "run_label": "Phase-3 eval",
+    "source_file": "tests/phase3_eval_outputs/P06.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/phase3__P07.json b/web-revamp-mockup/data/records/phase3__P07.json
new file mode 100644
index 0000000..f55ca09
--- /dev/null
+++ b/web-revamp-mockup/data/records/phase3__P07.json
@@ -0,0 +1,233 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P07_DB00619_MESH_D015464",
+    "drug": "Imatinib",
+    "drug_mesh": "MESH:D000068877",
+    "drugbank": "DB:DB00619",
+    "disease": "Chronic Myeloid Leukemia",
+    "disease_mesh": "MESH:D015464",
+    "summary": "Imatinib → Tyrosine-protein kinase ABL1 → leukocyte proliferation → Chronic Myeloid Leukemia"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D000068877",
+      "name": "Imatinib",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P00519",
+      "name": "Tyrosine-protein kinase ABL1",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0070661",
+      "name": "leukocyte proliferation",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D015464",
+      "name": "Chronic Myeloid Leukemia",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D000068877",
+      "target": "UniProt:P00519",
+      "evidence": [
+        {
+          "reference": "PMID:39182842",
+          "snippet": "inhibiting oncogenic protein BCR::ABL1 in a targeted manner with imatinib, a tyrosine kinase inhibitor.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Imatinib is a tyrosine kinase inhibitor that targets and inhibits the oncogenic BCR::ABL1 kinase (whose catalytic domain is ABL1, UniProt:P00519), decreasing its activity in CML patients.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Imatinib therapy of chronic myeloid leukemia significantly reduces carnitine cell intake, resulting in adverse events.",
+            "authors": [
+              "Burda P",
+              "Hlavackova A",
+              "Polivkova V",
+              "Curik N",
+              "Laznicka A",
+              "Krizkova J",
+              "Suttnar J",
+              "Klener P",
+              "Polakova KM"
+            ],
+            "journal": "Molecular metabolism",
+            "year": "2024",
+            "doi": "10.1016/j.molmet.2024.102016",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:36959211",
+          "snippet": "the inhibition of BCR-ABL1 kinase with Imatinib prevented Smad4 tyrosine phosphorylation and re-sensitized CML cells to TGF-β-induced antiproliferative and pro-apoptotic responses.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Imatinib inhibits BCR-ABL1 kinase activity, abolishing its downstream tyrosine-phosphorylation activity in CML cells — direct support for the decreases-activity-of edge.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Imatinib blocks tyrosine phosphorylation of Smad4 and restores TGF-β growth-suppressive signaling in BCR-ABL1-positive leukemia.",
+            "authors": [
+              "Wang L",
+              "Gu S",
+              "Chen F",
+              "Yu Y",
+              "Cao J",
+              "Li X",
+              "Gao C",
+              "Chen Y",
+              "Yuan S",
+              "Liu X",
+              "Qin J",
+              "Zhao B",
+              "Xu P",
+              "Liang T",
+              "Tong H",
+              "Lin X",
+              "Feng XH"
+            ],
+            "journal": "Signal transduction and targeted therapy",
+            "year": "2023",
+            "doi": "10.1038/s41392-023-01327-5",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P00519",
+      "target": "GO:0070661",
+      "evidence": [
+        {
+          "reference": "PMID:42011924",
+          "snippet": "generates the constitutively active BCR::ABL1 tyrosine kinase, driving uncontrolled myeloid proliferation.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "The constitutively active BCR::ABL1 tyrosine kinase (ABL1 catalytic moiety, UniProt:P00519) drives uncontrolled myeloid (leukocyte) proliferation — i.e. it positively regulates the proliferation process.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Importance of five membered heterocyclic compounds in treatment of chronic myeloid leukemia by targeting various pathways.",
+            "authors": [
+              "Ninave R",
+              "Mourya A",
+              "Prajapati N"
+            ],
+            "journal": "Future medicinal chemistry",
+            "year": "2026",
+            "doi": "10.1080/17568919.2026.2658831",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:35257901",
+          "snippet": "the dysregulated BCR-Abl fusion oncoprotein is formed and it produces the abnormal proliferation of white blood cells.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "The BCR-Abl fusion kinase produces (positively regulates) the abnormal proliferation of white blood cells (leukocytes).",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Targeting BCR-Abl in the treatment of Philadelphia-chromosome positive chronic myelogenous leukemia.",
+            "authors": [
+              "Roskoski R"
+            ],
+            "journal": "Pharmacological research",
+            "year": "2022",
+            "doi": "10.1016/j.phrs.2022.106156",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "causes",
+      "source": "GO:0070661",
+      "target": "MESH:D015464",
+      "evidence": [
+        {
+          "reference": "PMID:42011924",
+          "snippet": "Chronic myeloid leukemia (CML) is a clonal hematopoietic malignancy characterized by the presence of the Philadelphia chromosome, which generates the constitutively active BCR::ABL1 tyrosine kinase, driving uncontrolled myeloid proliferation.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "CML is defined as a malignancy characterized by uncontrolled myeloid (leukocyte) proliferation — the proliferative process is the defining cause/manifestation of the disease.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Importance of five membered heterocyclic compounds in treatment of chronic myeloid leukemia by targeting various pathways.",
+            "authors": [
+              "Ninave R",
+              "Mourya A",
+              "Prajapati N"
+            ],
+            "journal": "Future medicinal chemistry",
+            "year": "2026",
+            "doi": "10.1080/17568919.2026.2658831",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:42074261",
+          "snippet": "Chronic myeloid leukaemia (CML) is driven by the t(9;22) forming the BCR::ABL1 fusion gene, leading to the development of hyper-myeloid proliferation.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "CML development is characterized by hyper-myeloid proliferation, linking the leukocyte-proliferation process to the chronic myeloid leukemia disease state.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Allosteric and ATP-Pocket BCR::ABL1 Inhibition In Vitro, and Characterising Ex Vivo Thrombo-Inflammatory Biomarkers and Thrombin Generation in Asciminib-Treated CML Patients.",
+            "authors": [
+              "Omar MMA",
+              "Alanazi MA",
+              "Yeung DT",
+              "Hughes TP",
+              "Jackson DE"
+            ],
+            "journal": "International journal of molecular sciences",
+            "year": "2026",
+            "doi": "10.3390/ijms27083623",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00619#mechanism-of-action",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    },
+    {
+      "url": "https://www.uniprot.org/uniprot/P00519#function",
+      "type": "other",
+      "label": "uniprot.org — record source"
+    }
+  ],
+  "site": {
+    "id": "phase3__P07",
+    "record_id": "P07_DB00619_MESH_D015464",
+    "run": "phase3",
+    "run_label": "Phase-3 eval",
+    "source_file": "tests/phase3_eval_outputs/P07.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/phase3__P08.json b/web-revamp-mockup/data/records/phase3__P08.json
new file mode 100644
index 0000000..2ea18aa
--- /dev/null
+++ b/web-revamp-mockup/data/records/phase3__P08.json
@@ -0,0 +1,190 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P08_DB00002_MESH_D015179",
+    "drug": "Cetuximab",
+    "drug_mesh": "MESH:D000068818",
+    "drugbank": "DB:DB00002",
+    "disease": "Colorectal Neoplasms",
+    "disease_mesh": "MESH:D015179",
+    "summary": "Cetuximab → Epidermal growth factor receptor → MAPK cascade → cell population proliferation → Colorectal Neoplasms"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D000068818",
+      "name": "Cetuximab",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P00533",
+      "name": "Epidermal growth factor receptor",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0000165",
+      "name": "MAPK cascade",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "GO:0008283",
+      "name": "cell population proliferation",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D015179",
+      "name": "Colorectal Neoplasms",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D000068818",
+      "target": "UniProt:P00533",
+      "evidence": [
+        {
+          "reference": "PMID:16736979",
+          "snippet": "Monoclonal antibodies bind to the extracellular domain of EGFR, preventing ligand binding and interrupting the signaling cascade.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Cetuximab is a monoclonal antibody that binds the EGFR extracellular domain, blocking ligand-induced receptor activation and thereby decreasing EGFR signaling activity.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Anti-EGFR therapies: clinical experience in colorectal, lung, and head and neck cancers.",
+            "authors": [
+              "Vokes EE",
+              "Chu E"
+            ],
+            "journal": "Oncology (Williston Park, N.Y.)",
+            "year": "2006",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P00533",
+      "target": "GO:0000165",
+      "evidence": [
+        {
+          "reference": "PMID:33184860",
+          "snippet": "EGFR transactivation resulted in the activation of ERK1/2 and AKT.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Activated EGFR drives phosphorylation of ERK1/2 (the terminal kinases of the MAPK cascade), demonstrating that EGFR positively regulates the MAPK cascade in colorectal cancer cells.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Morphine promotes tumorigenesis and cetuximab resistance via EGFR signaling activation in human colorectal cancer.",
+            "authors": [
+              "Lu H",
+              "Zhang H",
+              "Weng ML",
+              "Zhang J",
+              "Jiang N",
+              "Cata JP",
+              "Ma D",
+              "Chen WK",
+              "Miao CH"
+            ],
+            "journal": "Journal of cellular physiology",
+            "year": "2021",
+            "doi": "10.1002/jcp.30161",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "GO:0000165",
+      "target": "GO:0008283",
+      "evidence": [
+        {
+          "reference": "PMID:30273442",
+          "snippet": "The Ras/mitogen-activated protein kinase (MAPK) pathway controls fundamental cellular processes such as proliferation, differentiation, and apoptosis.",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "explanation": "MAPK pathway activity drives epithelial cell proliferation; loss of ERK1/2 negative regulation (DUSP6 KO) increases proliferation, confirming MAPK positively regulates cell population proliferation.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Dual-specificity phosphatase 6 deletion protects the colonic epithelium against inflammation and promotes both proliferation and tumorigenesis.",
+            "authors": [
+              "Beaudry K",
+              "Langlois MJ",
+              "Montagne A",
+              "Cagnol S",
+              "Carrier JC",
+              "Rivard N"
+            ],
+            "journal": "Journal of cellular physiology",
+            "year": "2019",
+            "doi": "10.1002/jcp.27420",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "contributes to",
+      "source": "GO:0008283",
+      "target": "MESH:D015179",
+      "evidence": [
+        {
+          "reference": "PMID:41361128",
+          "snippet": "These mechanisms not only promote uncontrolled proliferation but also reinforce therapeutic resistance by dynamically modifying the tumor microenvironment (TME).",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Dysregulated signaling pathways in GI/colorectal cancers promote uncontrolled cell proliferation, which is a hallmark mechanism contributing to colorectal cancer progression.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Gastrointestinal cancer: molecular pathogenesis and targeted therapy.",
+            "authors": [
+              "Jin Y",
+              "He X",
+              "Wu Y"
+            ],
+            "journal": "Molecular biomedicine",
+            "year": "2025",
+            "doi": "10.1186/s43556-025-00361-9",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00002#mechanism-of-action",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    },
+    {
+      "url": "https://www.uniprot.org/uniprot/P00533#function",
+      "type": "other",
+      "label": "uniprot.org — record source"
+    }
+  ],
+  "site": {
+    "id": "phase3__P08",
+    "record_id": "P08_DB00002_MESH_D015179",
+    "run": "phase3",
+    "run_label": "Phase-3 eval",
+    "source_file": "tests/phase3_eval_outputs/P08.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/phase3__P09.json b/web-revamp-mockup/data/records/phase3__P09.json
new file mode 100644
index 0000000..934d38b
--- /dev/null
+++ b/web-revamp-mockup/data/records/phase3__P09.json
@@ -0,0 +1,375 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P09_DB00563_MESH_D054198",
+    "drug": "methotrexate",
+    "drug_mesh": "MESH:D008727",
+    "drugbank": "DB:DB00563",
+    "disease": "Acute Lymphoblastic Leukemia",
+    "disease_mesh": "MESH:D054198",
+    "summary": "methotrexate → Dihydrofolate reductase → tetrahydrofolate biosynthetic process → DNA biosynthetic process → cell population proliferation → Acute Lymphoblastic Leukemia"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D008727",
+      "name": "methotrexate",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P00374",
+      "name": "Dihydrofolate reductase",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0046654",
+      "name": "tetrahydrofolate biosynthetic process",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "GO:0071897",
+      "name": "DNA biosynthetic process",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "GO:0008283",
+      "name": "cell population proliferation",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D054198",
+      "name": "Acute Lymphoblastic Leukemia",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D008727",
+      "target": "UniProt:P00374",
+      "evidence": [
+        {
+          "reference": "PMID:40088855",
+          "snippet": "MTX acts as a folate antagonist by inhibiting dihydrofolate reductase (DHFR), an enzyme essential for the synthesis of tetrahydrofolate.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Review paper confirms methotrexate's primary mechanism is inhibition of DHFR, thereby decreasing its catalytic activity.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Methotrexate resistance and its regulatory mechanisms in pediatric tumors and beyond.",
+            "authors": [
+              "Nie J",
+              "Huang L",
+              "Shen Y",
+              "Pan H",
+              "Wang S",
+              "Zhao H",
+              "Gao P",
+              "Yang J",
+              "Huang X",
+              "Zeng S",
+              "Miao J"
+            ],
+            "journal": "Drug resistance updates : reviews and commentaries in antimicrobial and anticancer chemotherapy",
+            "year": "2025",
+            "doi": "10.1016/j.drup.2025.101225",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:25136372",
+          "snippet": "MTX competitively inhibits dihydrofolate reductase (DHFR), an enzyme that participates in the tetrahydrofolate synthesis so as to inhibit purine synthesis.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Confirms competitive inhibition of DHFR by MTX, reducing the enzyme's activity in tetrahydrofolate synthesis.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Treatment of acute lymphoblastic leukemia from traditional chinese medicine.",
+            "authors": [
+              "Hsiao YL",
+              "Chang PC",
+              "Huang HJ",
+              "Kuo CC",
+              "Chen CY"
+            ],
+            "journal": "Evidence-based complementary and alternative medicine : eCAM",
+            "year": "2014",
+            "doi": "10.1155/2014/601064",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P00374",
+      "target": "GO:0046654",
+      "evidence": [
+        {
+          "reference": "PMID:40088855",
+          "snippet": "MTX acts as a folate antagonist by inhibiting dihydrofolate reductase (DHFR), an enzyme essential for the synthesis of tetrahydrofolate.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "DHFR is identified as essential for the tetrahydrofolate biosynthetic process; inhibiting DHFR blocks this process, confirming DHFR positively regulates it.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Methotrexate resistance and its regulatory mechanisms in pediatric tumors and beyond.",
+            "authors": [
+              "Nie J",
+              "Huang L",
+              "Shen Y",
+              "Pan H",
+              "Wang S",
+              "Zhao H",
+              "Gao P",
+              "Yang J",
+              "Huang X",
+              "Zeng S",
+              "Miao J"
+            ],
+            "journal": "Drug resistance updates : reviews and commentaries in antimicrobial and anticancer chemotherapy",
+            "year": "2025",
+            "doi": "10.1016/j.drup.2025.101225",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:25136372",
+          "snippet": "MTX competitively inhibits dihydrofolate reductase (DHFR), an enzyme that participates in the tetrahydrofolate synthesis so as to inhibit purine synthesis.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "DHFR participates in tetrahydrofolate synthesis, confirming its positive regulatory role in that biosynthetic process.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Treatment of acute lymphoblastic leukemia from traditional chinese medicine.",
+            "authors": [
+              "Hsiao YL",
+              "Chang PC",
+              "Huang HJ",
+              "Kuo CC",
+              "Chen CY"
+            ],
+            "journal": "Evidence-based complementary and alternative medicine : eCAM",
+            "year": "2014",
+            "doi": "10.1155/2014/601064",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "GO:0046654",
+      "target": "GO:0071897",
+      "evidence": [
+        {
+          "reference": "PMID:17333344",
+          "snippet": "Folates play a key role in one-carbon metabolism essential for the biosynthesis of purines, thymidylate and hence DNA replication.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Tetrahydrofolate (reduced folate) drives one-carbon metabolism required for thymidylate and purine synthesis, which are needed for DNA replication (DNA biosynthetic process).",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Molecular basis of antifolate resistance.",
+            "authors": [
+              "Assaraf YG"
+            ],
+            "journal": "Cancer metastasis reviews",
+            "year": "2007",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:36532750",
+          "snippet": "the mechanism of action is to inhibit DNA synthesis, repair and cell proliferation by decreasing the activities of several folate-dependent enzymes.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Decreasing folate-dependent enzyme activities (including the tetrahydrofolate biosynthetic pathway) impairs DNA synthesis, confirming folate metabolism positively regulates the DNA biosynthetic process.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Association between high-dose methotrexate-induced toxicity and polymorphisms within methotrexate pathway genes in acute lymphoblastic leukemia.",
+            "authors": [
+              "Xu M",
+              "Wu S",
+              "Wang Y",
+              "Zhao Y",
+              "Wang X",
+              "Wei C",
+              "Liu X",
+              "Hao F",
+              "Hu C"
+            ],
+            "journal": "Frontiers in pharmacology",
+            "year": "2022",
+            "doi": "10.3389/fphar.2022.1003812",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "GO:0071897",
+      "target": "GO:0008283",
+      "evidence": [
+        {
+          "reference": "PMID:40088855",
+          "snippet": "This disruption impairs DNA synthesis, repair, and cellular replication, particularly affecting rapidly dividing cells.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "DNA synthesis is required for cellular replication (cell population proliferation); disrupting DNA synthesis halts proliferation, confirming that the DNA biosynthetic process positively regulates cell population proliferation.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Methotrexate resistance and its regulatory mechanisms in pediatric tumors and beyond.",
+            "authors": [
+              "Nie J",
+              "Huang L",
+              "Shen Y",
+              "Pan H",
+              "Wang S",
+              "Zhao H",
+              "Gao P",
+              "Yang J",
+              "Huang X",
+              "Zeng S",
+              "Miao J"
+            ],
+            "journal": "Drug resistance updates : reviews and commentaries in antimicrobial and anticancer chemotherapy",
+            "year": "2025",
+            "doi": "10.1016/j.drup.2025.101225",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:36532750",
+          "snippet": "the mechanism of action is to inhibit DNA synthesis, repair and cell proliferation by decreasing the activities of several folate-dependent enzymes.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "DNA synthesis inhibition leads directly to inhibition of cell proliferation, confirming the positive regulatory relationship between DNA biosynthetic process and cell population proliferation.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Association between high-dose methotrexate-induced toxicity and polymorphisms within methotrexate pathway genes in acute lymphoblastic leukemia.",
+            "authors": [
+              "Xu M",
+              "Wu S",
+              "Wang Y",
+              "Zhao Y",
+              "Wang X",
+              "Wei C",
+              "Liu X",
+              "Hao F",
+              "Hu C"
+            ],
+            "journal": "Frontiers in pharmacology",
+            "year": "2022",
+            "doi": "10.3389/fphar.2022.1003812",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "contributes to",
+      "source": "GO:0008283",
+      "target": "MESH:D054198",
+      "evidence": [
+        {
+          "reference": "PMID:25136372",
+          "snippet": "Acute lymphoblastic leukemia (ALL) is a cancer that immature white blood cells continuously overproduce in the bone marrow.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "ALL is characterized by uncontrolled proliferation (overproduction) of immature white blood cells, confirming that cell population proliferation contributes to the disease state.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Treatment of acute lymphoblastic leukemia from traditional chinese medicine.",
+            "authors": [
+              "Hsiao YL",
+              "Chang PC",
+              "Huang HJ",
+              "Kuo CC",
+              "Chen CY"
+            ],
+            "journal": "Evidence-based complementary and alternative medicine : eCAM",
+            "year": "2014",
+            "doi": "10.1155/2014/601064",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:40088855",
+          "snippet": "Methotrexate (MTX) is a critical antimetabolite drug in treating various pediatric diseases, including acute lymphoblastic leukemia (ALL), non-Hodgkin lymphoma (NHL), brain tumors, osteosarcoma, inflammatory myofibroblastic tumor (IMT), juvenile scleroderma (JS), and juvenile idiopathic arthritis (JIA).",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "MTX's efficacy against ALL as an antimetabolite (which blocks cell proliferation) supports that cell population proliferation is a key contributor to ALL.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Methotrexate resistance and its regulatory mechanisms in pediatric tumors and beyond.",
+            "authors": [
+              "Nie J",
+              "Huang L",
+              "Shen Y",
+              "Pan H",
+              "Wang S",
+              "Zhao H",
+              "Gao P",
+              "Yang J",
+              "Huang X",
+              "Zeng S",
+              "Miao J"
+            ],
+            "journal": "Drug resistance updates : reviews and commentaries in antimicrobial and anticancer chemotherapy",
+            "year": "2025",
+            "doi": "10.1016/j.drup.2025.101225",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00563#mechanism-of-action",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    },
+    {
+      "url": "https://www.uniprot.org/uniprot/P00374#function",
+      "type": "other",
+      "label": "uniprot.org — record source"
+    }
+  ],
+  "site": {
+    "id": "phase3__P09",
+    "record_id": "P09_DB00563_MESH_D054198",
+    "run": "phase3",
+    "run_label": "Phase-3 eval",
+    "source_file": "tests/phase3_eval_outputs/P09.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/phase3__P10.json b/web-revamp-mockup/data/records/phase3__P10.json
new file mode 100644
index 0000000..c45db7c
--- /dev/null
+++ b/web-revamp-mockup/data/records/phase3__P10.json
@@ -0,0 +1,260 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P10_DB00072_MESH_D001943",
+    "drug": "Trastuzumab",
+    "drug_mesh": "MESH:D000068878",
+    "drugbank": "DB:DB00072",
+    "disease": "Breast Neoplasms",
+    "disease_mesh": "MESH:D001943",
+    "summary": "Trastuzumab → Receptor tyrosine-protein kinase erbB-2 → cell population proliferation → Breast Neoplasms"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D000068878",
+      "name": "Trastuzumab",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P04626",
+      "name": "Receptor tyrosine-protein kinase erbB-2",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0008283",
+      "name": "cell population proliferation",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D001943",
+      "name": "Breast Neoplasms",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "directly physically interacts with",
+      "source": "MESH:D000068878",
+      "target": "UniProt:P04626",
+      "evidence": [
+        {
+          "reference": "PMID:29490608",
+          "snippet": "Trastuzumab bound to HER2 specifically and with high affinity.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Direct binding of trastuzumab to HER2 was demonstrated in CHO cells expressing human HER2, confirming that trastuzumab molecularly interacts with the ERBB2/HER2 receptor.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "The effects of trastuzumab on HER2-mediated cell signaling in CHO cells expressing human HER2.",
+            "authors": [
+              "Maadi H",
+              "Nami B",
+              "Tong J",
+              "Li G",
+              "Wang Z"
+            ],
+            "journal": "BMC cancer",
+            "year": "2018",
+            "doi": "10.1186/s12885-018-4143-x",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D000068878",
+      "target": "UniProt:P04626",
+      "evidence": [
+        {
+          "reference": "PMID:24835103",
+          "snippet": "Overexpression of CHK mimics trastuzumab treatment to mediate ErbB2-Y1248 phosphorylation, Akt downregulation, and growth inhibition of trastuzumab-sensitive breast cancer cells.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Trastuzumab binding to ERBB2 leads to downstream Akt downregulation and growth inhibition, indicating that trastuzumab decreases the effective oncogenic activity of the ERBB2 receptor in HER2-positive breast cancer cells.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Trastuzumab-induced recruitment of Csk-homologous kinase (CHK) to ErbB2 receptor is associated with ErbB2-Y1248 phosphorylation and ErbB2 degradation to mediate cell growth inhibition.",
+            "authors": [
+              "Dokmanovic M",
+              "Wu Y",
+              "Shen Y",
+              "Chen J",
+              "Hirsch DS",
+              "Wu WJ"
+            ],
+            "journal": "Cancer biology & therapy",
+            "year": "2014",
+            "doi": "10.4161/cbt.29171",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:19934303",
+          "snippet": "Trastuzumab partially decreased PI3K but not mTOR activity.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Trastuzumab reduces PI3K activity downstream of ERBB2, supporting that it decreases ERBB2-mediated signaling activity.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Inhibition of mammalian target of rapamycin is required for optimal antitumor effect of HER2 inhibitors against HER2-overexpressing cancer cells.",
+            "authors": [
+              "Miller TW",
+              "Forbes JT",
+              "Shah C",
+              "Wyatt SK",
+              "Manning HC",
+              "Olivares MG",
+              "Sanchez V",
+              "Dugger TC",
+              "de Matos Granja N",
+              "Narasanna A",
+              "Cook RS",
+              "Kennedy JP",
+              "Lindsley CW",
+              "Arteaga CL"
+            ],
+            "journal": "Clinical cancer research : an official journal of the American Association for Cancer Research",
+            "year": "2009",
+            "doi": "10.1158/1078-0432.CCR-09-1665",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P04626",
+      "target": "GO:0008283",
+      "evidence": [
+        {
+          "reference": "PMID:31656036",
+          "snippet": "HER2 is a receptor tyrosine kinase that activates downstream signalling pathways involved in cellular survival, growth and proliferation.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "ERBB2/HER2 is described as directly activating downstream signaling that drives cell growth and proliferation, establishing ERBB2 as a positive regulator of cell population proliferation.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "The role of autophagy in HER2-targeted therapy.",
+            "authors": [
+              "Janser FA",
+              "Tschan MP",
+              "Langer R"
+            ],
+            "journal": "Swiss medical weekly",
+            "year": "2019",
+            "doi": "10.4414/smw.2019.20138",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:23982598",
+          "snippet": "Inhibition of HER2 signalling results in a reduction of tumour cell proliferation, invasiveness and survival.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "The inverse relationship is stated directly — blocking HER2 signaling reduces tumour cell proliferation — confirming that HER2 signalling positively regulates tumour cell proliferation.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Pertuzumab: a review of its use for first-line combination treatment of HER2-positive metastatic breast cancer.",
+            "authors": [
+              "McCormack PL"
+            ],
+            "journal": "Drugs",
+            "year": "2013",
+            "doi": "10.1007/s40265-013-0109-0",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "contributes to",
+      "source": "GO:0008283",
+      "target": "MESH:D001943",
+      "evidence": [
+        {
+          "reference": "PMID:41310794",
+          "snippet": "HER2 overexpression reverses the proliferation inhibition caused by CAND1 loss both in vitro and in vivo.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "HER2-driven cell proliferation restores tumor growth in HER2-positive breast cancer models both in vitro and in vivo, demonstrating that cell population proliferation is a key contributor to HER2-positive breast cancer progression.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "CAND1 mediates CUL7-dependent HER2 protein stability to drive breast cancer progression.",
+            "authors": [
+              "Xia X",
+              "He X",
+              "Tang M",
+              "Chen Y",
+              "Liao Y",
+              "Zhang J",
+              "Huang H"
+            ],
+            "journal": "Breast cancer research : BCR",
+            "year": "2025",
+            "doi": "10.1186/s13058-025-02158-8",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:31656036",
+          "snippet": "Amplification of the gene and subsequent overexpression of the HER2 protein lead to increased activation of downstream signalling and are implicated in several cancer types.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "HER2 amplification leads to increased downstream signaling including cell proliferation, which is implicated in breast cancer (among other cancer types), supporting that cell proliferation contributes to HER2-positive breast cancer.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "The role of autophagy in HER2-targeted therapy.",
+            "authors": [
+              "Janser FA",
+              "Tschan MP",
+              "Langer R"
+            ],
+            "journal": "Swiss medical weekly",
+            "year": "2019",
+            "doi": "10.4414/smw.2019.20138",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00072#mechanism-of-action",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    },
+    {
+      "url": "https://www.uniprot.org/uniprot/P04626#function",
+      "type": "other",
+      "label": "uniprot.org — record source"
+    }
+  ],
+  "site": {
+    "id": "phase3__P10",
+    "record_id": "P10_DB00072_MESH_D001943",
+    "run": "phase3",
+    "run_label": "Phase-3 eval",
+    "source_file": "tests/phase3_eval_outputs/P10.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/phase3__P11.json b/web-revamp-mockup/data/records/phase3__P11.json
new file mode 100644
index 0000000..e71b7cd
--- /dev/null
+++ b/web-revamp-mockup/data/records/phase3__P11.json
@@ -0,0 +1,263 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P11_DB01045_MESH_D014397",
+    "drug": "Rifampicin",
+    "drug_mesh": "MESH:D012293",
+    "drugbank": "DB:DB01045",
+    "disease": "Pulmonary tuberculosis",
+    "disease_mesh": "MESH:D014397",
+    "summary": "Rifampicin → DNA-directed RNA polymerase subunit beta → transcription, DNA-templated → Mycobacterium tuberculosis → Pulmonary tuberculosis"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D012293",
+      "name": "Rifampicin",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P9WGY9",
+      "name": "DNA-directed RNA polymerase subunit beta",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0006351",
+      "name": "transcription, DNA-templated",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "NCBITaxon:1773",
+      "name": "Mycobacterium tuberculosis",
+      "label": "OrganismTaxon"
+    },
+    {
+      "id": "MESH:D014397",
+      "name": "Pulmonary tuberculosis",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D012293",
+      "target": "UniProt:P9WGY9",
+      "evidence": [
+        {
+          "reference": "PMID:31269464",
+          "snippet": "The antimicrobial activity of RIF is attributed to its ability to inhibit transcription by binding to the β subunit of bacterial RNA polymerase (encoded by rpoB).",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Rifampicin inhibits bacterial transcription by binding directly to the beta subunit (RpoB) of the RNA polymerase, thereby decreasing RpoB activity.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Unveiling the molecular basis for pleiotropy in selected rif mutants of Escherichia coli: Possible role for Tyrosine in the Rif binding pocket and fast movement of RNA polymerase.",
+            "authors": [
+              "Karthik M",
+              "Meenakshi S",
+              "Munavar MH"
+            ],
+            "journal": "Gene",
+            "year": "2019",
+            "doi": "10.1016/j.gene.2019.143951",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:29706316",
+          "snippet": "Because the action of RIF is on rpoB gene encoding RNA polymerase β subunit, 95% of RIF resistant mutations are present in rpoB gene.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "RIF acts on RpoB (RNA polymerase beta subunit); nearly all resistance mutations map to this subunit, confirming it is the direct target of rifampicin inhibition.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Mutations inside rifampicin-resistance determining region of rpoB gene associated with rifampicin-resistance in Mycobacterium tuberculosis.",
+            "authors": [
+              "Zaw MT",
+              "Emran NA",
+              "Lin Z"
+            ],
+            "journal": "Journal of infection and public health",
+            "year": "2018",
+            "doi": "10.1016/j.jiph.2018.04.005",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P9WGY9",
+      "target": "GO:0006351",
+      "evidence": [
+        {
+          "reference": "PMID:31269464",
+          "snippet": "The antimicrobial activity of RIF is attributed to its ability to inhibit transcription by binding to the β subunit of bacterial RNA polymerase (encoded by rpoB).",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Rifampicin inhibits transcription by binding RpoB; this confirms that RpoB (the beta subunit) is required for and positively regulates DNA-templated transcription in bacteria.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Unveiling the molecular basis for pleiotropy in selected rif mutants of Escherichia coli: Possible role for Tyrosine in the Rif binding pocket and fast movement of RNA polymerase.",
+            "authors": [
+              "Karthik M",
+              "Meenakshi S",
+              "Munavar MH"
+            ],
+            "journal": "Gene",
+            "year": "2019",
+            "doi": "10.1016/j.gene.2019.143951",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:20150242",
+          "snippet": "While the RNA polymerases from the parent or a mutant strain (harbouring a frequently occurring mutation, H442Y, in RpoB) were susceptible to Rif-mediated inhibition of transcription from calf thymus DNA, those from the insertion and deletion mutants were essentially refractory to such inhibition.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Wild-type RpoB is necessary for rifampicin to inhibit transcription, confirming that RpoB actively supports (positively regulates) the transcription process.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Novel insertion and deletion mutants of RpoB that render Mycobacterium smegmatis RNA polymerase resistant to rifampicin-mediated inhibition of transcription.",
+            "authors": [
+              "Malshetty V",
+              "Kurthkoti K",
+              "China A",
+              "Mallick B",
+              "Yamunadevi S",
+              "Sang PB",
+              "Srinivasan N",
+              "Nagaraja V",
+              "Varshney U"
+            ],
+            "journal": "Microbiology (Reading, England)",
+            "year": "2010",
+            "doi": "10.1099/mic.0.036970-0",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "in taxon",
+      "source": "GO:0006351",
+      "target": "NCBITaxon:1773",
+      "evidence": [
+        {
+          "reference": "PMID:29706316",
+          "snippet": "Rifampicin (RIF) plays a pivotal role in the treatment of tuberculosis due to its bactericidal effects. Because the action of RIF is on rpoB gene encoding RNA polymerase β subunit, 95% of RIF resistant mutations are present in rpoB gene.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "The paper discusses rpoB-encoded RNA polymerase transcription in the context of Mycobacterium tuberculosis, placing this DNA-templated transcription process in the M. tuberculosis taxon.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Mutations inside rifampicin-resistance determining region of rpoB gene associated with rifampicin-resistance in Mycobacterium tuberculosis.",
+            "authors": [
+              "Zaw MT",
+              "Emran NA",
+              "Lin Z"
+            ],
+            "journal": "Journal of infection and public health",
+            "year": "2018",
+            "doi": "10.1016/j.jiph.2018.04.005",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:41421076",
+          "snippet": "RNA polymerase encoded by rpoB is the primary target of the first-front antibiotics of rifampicin.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "The paper describes rpoB-encoded RNA polymerase in M. tuberculosis as the primary target of rifampicin, confirming the transcription process occurs in the M. tuberculosis taxon.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Clinically present mycobacterium tuberculosis RNA polymerase subunit RpoB K446 mutation confers broad-spectrum antibiotics resistance via pupylation.",
+            "authors": [
+              "Shen Q",
+              "Huang Y",
+              "Huo F",
+              "Xu H",
+              "Li M",
+              "Huang L",
+              "Xu Y",
+              "Li P",
+              "Huang H",
+              "Xie J"
+            ],
+            "journal": "Bioorganic chemistry",
+            "year": "2026",
+            "doi": "10.1016/j.bioorg.2025.109388",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "causes",
+      "source": "NCBITaxon:1773",
+      "target": "MESH:D014397",
+      "evidence": [
+        {
+          "reference": "PMID:40201850",
+          "snippet": "Mycobacterium tuberculosis (Mtb), a pathogen that belongs to the M. tuberculosis complex, causes tuberculosis (TB), an infectious bacterial disease. Although it usually affects the lungs and results in pulmonary TB, it can also lead to extra-pulmonary TB by affecting other regions of the body.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Mtb is the direct causative agent of pulmonary tuberculosis, primarily affecting the lungs.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "In silico evaluation of snake venom proteins against multidrug-resistant Mycobacterium tuberculosis: A molecular dynamics study and simulation dynamic.",
+            "authors": [
+              "Fouda M",
+              "Mantargi MJS",
+              "Germoush MO",
+              "Sarhan M",
+              "Husein MF",
+              "Abdel-Daim MM"
+            ],
+            "journal": "Open veterinary journal",
+            "year": "2025",
+            "doi": "10.5455/OVJ.2025.v15.i2.26",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB01045#mechanism-of-action",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    },
+    {
+      "url": "https://www.uniprot.org/uniprot/P9WGY9",
+      "type": "other",
+      "label": "uniprot.org — record source"
+    }
+  ],
+  "site": {
+    "id": "phase3__P11",
+    "record_id": "P11_DB01045_MESH_D014397",
+    "run": "phase3",
+    "run_label": "Phase-3 eval",
+    "source_file": "tests/phase3_eval_outputs/P11.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/phase3__P12.json b/web-revamp-mockup/data/records/phase3__P12.json
new file mode 100644
index 0000000..6301d16
--- /dev/null
+++ b/web-revamp-mockup/data/records/phase3__P12.json
@@ -0,0 +1,256 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P12_DB00951_MESH_D014397",
+    "drug": "Isoniazid",
+    "drug_mesh": "MESH:D007538",
+    "drugbank": "DB:DB00951",
+    "disease": "Pulmonary Tuberculosis",
+    "disease_mesh": "MESH:D014397",
+    "summary": "Isoniazid → Enoyl-[acyl-carrier-protein] reductase [NADH] InhA → mycolic acid biosynthetic process → Mycobacterium tuberculosis → Pulmonary Tuberculosis"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D007538",
+      "name": "Isoniazid",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P9WGR1",
+      "name": "Enoyl-[acyl-carrier-protein] reductase [NADH] InhA",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0071768",
+      "name": "mycolic acid biosynthetic process",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "NCBITaxon:1773",
+      "name": "Mycobacterium tuberculosis",
+      "label": "OrganismTaxon"
+    },
+    {
+      "id": "MESH:D014397",
+      "name": "Pulmonary Tuberculosis",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D007538",
+      "target": "UniProt:P9WGR1",
+      "evidence": [
+        {
+          "reference": "PMID:38460337",
+          "snippet": "Isoniazid (INH), a treatment for tuberculosis (TB), targets the enzyme InhA (mycobacterium enoyl acyl carrier protein reductase)",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Isoniazid targets and inhibits InhA, the enoyl-ACP reductase of M. tuberculosis, reducing its catalytic activity.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Unlocking InhA: Novel approaches to inhibit Mycobacterium tuberculosis.",
+            "authors": [
+              "Wahan SK",
+              "Bhargava G",
+              "Chawla V",
+              "Chawla PA"
+            ],
+            "journal": "Bioorganic chemistry",
+            "year": "2024",
+            "doi": "10.1016/j.bioorg.2024.107250",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:37482022",
+          "snippet": "InhA is the primary target of isoniazid (INH), one of the most effective compounds to treat TB.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "InhA is directly identified as the primary enzymatic target of isoniazid in M. tuberculosis.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Discovery of new diaryl ether inhibitors against Mycobacterium tuberculosis targeting the minor portal of InhA.",
+            "authors": [
+              "Chebaiki M",
+              "Delfourne E",
+              "Tamhaev R",
+              "Danoun S",
+              "Rodriguez F",
+              "Hoffmann P",
+              "Grosjean E",
+              "Goncalves F",
+              "Azéma-Despeyroux J",
+              "Pál A",
+              "Korduláková J",
+              "Preuilh N",
+              "Britton S",
+              "Constant P",
+              "Marrakchi H",
+              "Maveyraud L",
+              "Mourey L",
+              "Lherbet C"
+            ],
+            "journal": "European journal of medicinal chemistry",
+            "year": "2023",
+            "doi": "10.1016/j.ejmech.2023.115646",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P9WGR1",
+      "target": "GO:0071768",
+      "evidence": [
+        {
+          "reference": "PMID:10336454",
+          "snippet": "InhA, is a member of an unusual FAS-II system that prefers longer chain fatty acyl substrates for the purpose of synthesizing mycolic acids, a major component of mycobacterial cell walls.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "InhA (enoyl-ACP reductase) is part of the FAS-II system responsible for mycolic acid biosynthesis, confirming it positively regulates this process.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Crystal structure of the Mycobacterium tuberculosis enoyl-ACP reductase, InhA, in complex with NAD+ and a C16 fatty acyl substrate.",
+            "authors": [
+              "Rozwarski DA",
+              "Vilchèze C",
+              "Sugantino M",
+              "Bittman R",
+              "Sacchettini JC"
+            ],
+            "journal": "The Journal of biological chemistry",
+            "year": "1999",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "occurs in",
+      "source": "GO:0071768",
+      "target": "NCBITaxon:1773",
+      "evidence": [
+        {
+          "reference": "PMID:41432360",
+          "snippet": "Upon activation, INH inhibits InhA, thereby disrupting mycolic acid biosynthesis, a crucial process for maintaining Mtb's distinctive, lipid-rich cell wall.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Mycolic acid biosynthesis is explicitly described as a process occurring in and essential for M. tuberculosis (Mtb).",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Uncovering the structural impact of KatG Ser315 mutations in Mycobacterium tuberculosis via cryo-EM.",
+            "authors": [
+              "Allport T",
+              "Chaplin AK"
+            ],
+            "journal": "Protein science : a publication of the Protein Society",
+            "year": "2026",
+            "doi": "10.1002/pro.70409",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:37482022",
+          "snippet": "Enzymes belonging to the type II fatty acid synthase system (FAS-II) are involved in the biosynthesis of mycolic acids, cell envelope components essential for mycobacterial survival.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Mycolic acid biosynthesis by the FAS-II system occurs in mycobacteria; loss of this process is lethal to the organism.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Discovery of new diaryl ether inhibitors against Mycobacterium tuberculosis targeting the minor portal of InhA.",
+            "authors": [
+              "Chebaiki M",
+              "Delfourne E",
+              "Tamhaev R",
+              "Danoun S",
+              "Rodriguez F",
+              "Hoffmann P",
+              "Grosjean E",
+              "Goncalves F",
+              "Azéma-Despeyroux J",
+              "Pál A",
+              "Korduláková J",
+              "Preuilh N",
+              "Britton S",
+              "Constant P",
+              "Marrakchi H",
+              "Maveyraud L",
+              "Mourey L",
+              "Lherbet C"
+            ],
+            "journal": "European journal of medicinal chemistry",
+            "year": "2023",
+            "doi": "10.1016/j.ejmech.2023.115646",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "causes",
+      "source": "NCBITaxon:1773",
+      "target": "MESH:D014397",
+      "evidence": [
+        {
+          "reference": "PMID:41432360",
+          "snippet": "Mycobacterium tuberculosis (Mtb), the causative agent of tuberculosis (TB), is responsible for a global health burden affecting over a quarter of the world's population.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "M. tuberculosis is the established causative agent of tuberculosis, including pulmonary tuberculosis.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Uncovering the structural impact of KatG Ser315 mutations in Mycobacterium tuberculosis via cryo-EM.",
+            "authors": [
+              "Allport T",
+              "Chaplin AK"
+            ],
+            "journal": "Protein science : a publication of the Protein Society",
+            "year": "2026",
+            "doi": "10.1002/pro.70409",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00951#mechanism-of-action",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    },
+    {
+      "url": "https://www.uniprot.org/uniprot/P9WGR1",
+      "type": "other",
+      "label": "uniprot.org — record source"
+    }
+  ],
+  "site": {
+    "id": "phase3__P12",
+    "record_id": "P12_DB00951_MESH_D014397",
+    "run": "phase3",
+    "run_label": "Phase-3 eval",
+    "source_file": "tests/phase3_eval_outputs/P12.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/phase3__P13.json b/web-revamp-mockup/data/records/phase3__P13.json
new file mode 100644
index 0000000..74f2a2c
--- /dev/null
+++ b/web-revamp-mockup/data/records/phase3__P13.json
@@ -0,0 +1,290 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P13_DB00512_MESH_D055624",
+    "drug": "Vancomycin",
+    "drug_mesh": "MESH:D014640",
+    "drugbank": "DB:DB00512",
+    "disease": "Methicillin-Resistant Staphylococcal Infections",
+    "disease_mesh": "MESH:D055624",
+    "summary": "Vancomycin → D-alanyl-D-alanine → peptidoglycan biosynthetic process → Staphylococcus aureus → Methicillin-Resistant Staphylococcal Infections"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D014640",
+      "name": "Vancomycin",
+      "label": "Drug"
+    },
+    {
+      "id": "CHEBI:16576",
+      "name": "D-alanyl-D-alanine",
+      "label": "ChemicalSubstance"
+    },
+    {
+      "id": "GO:0009252",
+      "name": "peptidoglycan biosynthetic process",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "NCBITaxon:1280",
+      "name": "Staphylococcus aureus",
+      "label": "OrganismTaxon"
+    },
+    {
+      "id": "MESH:D055624",
+      "name": "Methicillin-Resistant Staphylococcal Infections",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "directly physically interacts with",
+      "source": "MESH:D014640",
+      "target": "CHEBI:16576",
+      "evidence": [
+        {
+          "reference": "PMID:39656010",
+          "snippet": "Vancomycin binds to the D-ala-D-ala terminus of the nascent peptidoglycan precursor lipid II, preventing cell wall biosynthesis.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Vancomycin directly binds the D-alanyl-D-alanine (D-ala-D-ala) terminus of peptidoglycan precursor lipid II, which is the molecular basis of its antibacterial mechanism.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Palmitoleic acid sensitizes vancomycin-resistant Staphylococcus aureus to vancomycin by outpacing the expression of resistance genes.",
+            "authors": [
+              "Tabashsum Z",
+              "Angeles-Solano M",
+              "Sidders AE",
+              "Parsons JB",
+              "Rowe SE"
+            ],
+            "journal": "Microbiology spectrum",
+            "year": "2025",
+            "doi": "10.1128/spectrum.01996-24",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:24805824",
+          "snippet": "They inhibit bacterial cell wall biosynthesis by binding to the D-Ala-D-Ala C-terminus of peptidoglycan precursors.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Glycopeptide antibiotics including vancomycin inhibit cell wall biosynthesis by binding to the D-Ala-D-Ala C-terminus of peptidoglycan precursors, directly confirming the binding relationship.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "New insights into glycopeptide antibiotic binding to cell wall precursors using SPR and NMR spectroscopy.",
+            "authors": [
+              "Treviño J",
+              "Bayón C",
+              "Ardá A",
+              "Marinelli F",
+              "Gandolfi R",
+              "Molinari F",
+              "Jimenez-Barbero J",
+              "Hernáiz MJ"
+            ],
+            "journal": "Chemistry (Weinheim an der Bergstrasse, Germany)",
+            "year": "2014",
+            "doi": "10.1002/chem.201303310",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "participates in",
+      "source": "CHEBI:16576",
+      "target": "GO:0009252",
+      "evidence": [
+        {
+          "reference": "PMID:41563485",
+          "snippet": "Vancomycin is a critical glycopeptide antibiotic for treating severe infections caused by Gram-positive bacteria, particularly MRSA and Clostridioides difficile, by inhibiting cell wall synthesis through binding to D-Ala-D-Ala termini of peptidoglycan precursors.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "D-Ala-D-Ala termini of peptidoglycan precursors are the substrates whose accessibility is required for peptidoglycan biosynthesis; vancomycin's binding to them disrupts the process, confirming that D-alanyl-D-alanine participates in peptidoglycan biosynthetic process.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Vancomycin resistance in gram-positive infections: evolutionary strategies of survival.",
+            "authors": [
+              "Hu T",
+              "Wang L"
+            ],
+            "journal": "Archives of microbiology",
+            "year": "2026",
+            "doi": "10.1007/s00203-025-04698-1",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:24805824",
+          "snippet": "They inhibit bacterial cell wall biosynthesis by binding to the D-Ala-D-Ala C-terminus of peptidoglycan precursors.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "The D-Ala-D-Ala C-terminus of peptidoglycan precursors is essential for cell wall (peptidoglycan) biosynthesis; blocking it inhibits the biosynthetic process, confirming D-alanyl-D-alanine participates in this process.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "New insights into glycopeptide antibiotic binding to cell wall precursors using SPR and NMR spectroscopy.",
+            "authors": [
+              "Treviño J",
+              "Bayón C",
+              "Ardá A",
+              "Marinelli F",
+              "Gandolfi R",
+              "Molinari F",
+              "Jimenez-Barbero J",
+              "Hernáiz MJ"
+            ],
+            "journal": "Chemistry (Weinheim an der Bergstrasse, Germany)",
+            "year": "2014",
+            "doi": "10.1002/chem.201303310",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "in taxon",
+      "source": "GO:0009252",
+      "target": "NCBITaxon:1280",
+      "evidence": [
+        {
+          "reference": "PMID:39656010",
+          "snippet": "The use of vancomycin, a frontline antibiotic used to treat hospitalized patients with methicillin-resistant Staphylococcus aureus (MRSA) infections, is complicated by high rates of treatment failure.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "The paper discusses vancomycin's mechanism of preventing cell wall biosynthesis specifically in the context of MRSA (methicillin-resistant Staphylococcus aureus), placing the peptidoglycan biosynthetic process in the S. aureus taxon.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Palmitoleic acid sensitizes vancomycin-resistant Staphylococcus aureus to vancomycin by outpacing the expression of resistance genes.",
+            "authors": [
+              "Tabashsum Z",
+              "Angeles-Solano M",
+              "Sidders AE",
+              "Parsons JB",
+              "Rowe SE"
+            ],
+            "journal": "Microbiology spectrum",
+            "year": "2025",
+            "doi": "10.1128/spectrum.01996-24",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:41563485",
+          "snippet": "Vancomycin is a critical glycopeptide antibiotic for treating severe infections caused by Gram-positive bacteria, particularly MRSA and Clostridioides difficile, by inhibiting cell wall synthesis through binding to D-Ala-D-Ala termini of peptidoglycan precursors.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "The paper describes vancomycin inhibiting cell wall synthesis (peptidoglycan biosynthesis) specifically in the context of MRSA (methicillin-resistant S. aureus), confirming the biosynthetic process occurs in the S. aureus taxon.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Vancomycin resistance in gram-positive infections: evolutionary strategies of survival.",
+            "authors": [
+              "Hu T",
+              "Wang L"
+            ],
+            "journal": "Archives of microbiology",
+            "year": "2026",
+            "doi": "10.1007/s00203-025-04698-1",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "causes",
+      "source": "NCBITaxon:1280",
+      "target": "MESH:D055624",
+      "evidence": [
+        {
+          "reference": "PMID:42248931",
+          "snippet": "methicillin-resistant Staphylococcus aureus (MRSA) represents one of the most widespread MDR bacterium responsible for severe nosocomial infections.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Methicillin-resistant Staphylococcus aureus (MRSA), a strain of S. aureus (NCBITaxon:1280), is the causative agent of MRSA infections; this paper confirms MRSA is responsible for severe nosocomial infections, supporting the causes relationship.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "A Korean native halophyte extract attenuates the virulence of methicillin-resistant Staphylococcus aureus by inhibiting biofilm formation.",
+            "authors": [
+              "Kim HS",
+              "Kim GY",
+              "Park JW",
+              "Lee JH",
+              "Yerke AM",
+              "Yun B",
+              "Hwang S",
+              "Moon KH"
+            ],
+            "journal": "Scientific reports",
+            "year": "2026",
+            "doi": "10.1038/s41598-026-53460-0",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:39656010",
+          "snippet": "The use of vancomycin, a frontline antibiotic used to treat hospitalized patients with methicillin-resistant Staphylococcus aureus (MRSA) infections, is complicated by high rates of treatment failure.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Methicillin-resistant Staphylococcus aureus (a strain of S. aureus, NCBITaxon:1280) causes MRSA infections in hospitalized patients, as established in this clinical context.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Palmitoleic acid sensitizes vancomycin-resistant Staphylococcus aureus to vancomycin by outpacing the expression of resistance genes.",
+            "authors": [
+              "Tabashsum Z",
+              "Angeles-Solano M",
+              "Sidders AE",
+              "Parsons JB",
+              "Rowe SE"
+            ],
+            "journal": "Microbiology spectrum",
+            "year": "2025",
+            "doi": "10.1128/spectrum.01996-24",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00512#mechanism-of-action",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    },
+    {
+      "url": "https://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:16576",
+      "type": "other",
+      "label": "ebi.ac.uk — record source"
+    },
+    {
+      "url": "https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?id=1280",
+      "type": "other",
+      "label": "ncbi.nlm.nih.gov — record source"
+    }
+  ],
+  "site": {
+    "id": "phase3__P13",
+    "record_id": "P13_DB00512_MESH_D055624",
+    "run": "phase3",
+    "run_label": "Phase-3 eval",
+    "source_file": "tests/phase3_eval_outputs/P13.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/phase3__P14.json b/web-revamp-mockup/data/records/phase3__P14.json
new file mode 100644
index 0000000..1bceb0e
--- /dev/null
+++ b/web-revamp-mockup/data/records/phase3__P14.json
@@ -0,0 +1,350 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P14_DB00198_MESH_D007251",
+    "drug": "Oseltamivir",
+    "drug_mesh": "MESH:D053139",
+    "drugbank": "DB:DB00198",
+    "disease": "Influenza",
+    "disease_mesh": "MESH:D007251",
+    "summary": "Oseltamivir → Oseltamivir carboxylate → Neuraminidase → viral release from host cell → Influenza A virus → Influenza"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D053139",
+      "name": "Oseltamivir",
+      "label": "Drug"
+    },
+    {
+      "id": "CHEBI:64337",
+      "name": "Oseltamivir carboxylate",
+      "label": "ChemicalSubstance"
+    },
+    {
+      "id": "UniProt:P03472",
+      "name": "Neuraminidase",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0019076",
+      "name": "viral release from host cell",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "NCBITaxon:11520",
+      "name": "Influenza A virus",
+      "label": "OrganismTaxon"
+    },
+    {
+      "id": "MESH:D007251",
+      "name": "Influenza",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "has metabolite",
+      "source": "MESH:D053139",
+      "target": "CHEBI:64337",
+      "evidence": [
+        {
+          "reference": "PMID:16966469",
+          "snippet": "This anti-influenza viral agent is an ester prodrug, and the antiviral activity is achieved by its hydrolytic metabolite: oseltamivir carboxylate.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Oseltamivir is an ester prodrug; its active metabolite oseltamivir carboxylate is the entity responsible for antiviral activity.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Anti-influenza prodrug oseltamivir is activated by carboxylesterase human carboxylesterase 1, and the activation is inhibited by antiplatelet agent clopidogrel.",
+            "authors": [
+              "Shi D",
+              "Yang J",
+              "Yang D",
+              "LeCluyse EL",
+              "Black C",
+              "You L",
+              "Akhlaghi F",
+              "Yan B"
+            ],
+            "journal": "The Journal of pharmacology and experimental therapeutics",
+            "year": "2006",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:27228223",
+          "snippet": "Oseltamivir, an inactive anti-influenza virus prodrug, is activated (hydrolysed) in vivo by carboxylesterase 1 (CES1) to its active metabolite oseltamivir carboxylate.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Confirms oseltamivir is a prodrug and its active metabolite is oseltamivir carboxylate, supporting the has metabolite relationship.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Association of Oseltamivir Activation with Gender and Carboxylesterase 1 Genetic Polymorphisms.",
+            "authors": [
+              "Shi J",
+              "Wang X",
+              "Eyler RF",
+              "Liang Y",
+              "Liu L",
+              "Mueller BA",
+              "Zhu HJ"
+            ],
+            "journal": "Basic & clinical pharmacology & toxicology",
+            "year": "2016",
+            "doi": "10.1111/bcpt.12625",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "CHEBI:64337",
+      "target": "UniProt:P03472",
+      "evidence": [
+        {
+          "reference": "PMID:39577572",
+          "snippet": "oseltamivir carboxylate or zanamivir, a competitive inhibitor of receptor-destroying neuraminidases (NAs)",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Oseltamivir carboxylate is described as a competitive inhibitor of neuraminidases (NAs), directly supporting that it decreases NA activity.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Edible bird's nest: N- and O-glycan analysis and synergistic anti-avian influenza virus activity with neuraminidase inhibitors.",
+            "authors": [
+              "Sriwilaijaroen N",
+              "Hanamatsu H",
+              "Yokota I",
+              "Nishikaze T",
+              "Ijichi T",
+              "Takahashi T",
+              "Sakoda Y",
+              "Furukawa JI",
+              "Suzuki Y"
+            ],
+            "journal": "Antiviral research",
+            "year": "2024",
+            "doi": "10.1016/j.antiviral.2024.106040",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:41917408",
+          "snippet": "The neuraminidase (NA) glycoprotein of influenza virus plays a critical role in the release of progeny viruses and their spread, making it an important target for antiviral drugs.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Establishes NA as the antiviral drug target; combined with the first evidence item, confirms oseltamivir carboxylate decreases NA activity.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Influenza Virus Neuraminidase Glycoprotein, Its Inhibitors, and Their Resistance.",
+            "authors": [
+              "Takashita E"
+            ],
+            "journal": "Advances in experimental medicine and biology",
+            "year": "2026",
+            "doi": "10.1007/978-3-032-04153-1_24",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P03472",
+      "target": "GO:0019076",
+      "evidence": [
+        {
+          "reference": "PMID:23349854",
+          "snippet": "HA attaches to sialic acid on host cell surface receptors to initiate virus infection while NA removes these sialic acids to facilitate release of progeny virions.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "NA facilitates (positively regulates) the release of progeny virions from infected cells by removing sialic acid receptor binding.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "NA proteins of influenza A viruses H1N1/2009, H5N1, and H9N2 show differential effects on infection initiation, virus release, and cell-cell fusion.",
+            "authors": [
+              "Chen Q",
+              "Huang S",
+              "Chen J",
+              "Zhang S",
+              "Chen Z"
+            ],
+            "journal": "PloS one",
+            "year": "2013",
+            "doi": "10.1371/journal.pone.0054334",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:23028967",
+          "snippet": "influenza virus neuraminidase (NA) cleaves terminal sialic acid residues on oligosaccharide chains that are receptors for virus binding, thus playing an important role in the release of virions from infected cells to promote the spread of cell-to-cell infection.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "NA activity directly enables virion release from infected cells, confirming NA positively regulates the viral release from host cell process.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Bacterial neuraminidase rescues influenza virus replication from inhibition by a neuraminidase inhibitor.",
+            "authors": [
+              "Nishikawa T",
+              "Shimizu K",
+              "Tanaka T",
+              "Kuroda K",
+              "Takayama T",
+              "Yamamoto T",
+              "Hanada N",
+              "Hamada Y"
+            ],
+            "journal": "PloS one",
+            "year": "2012",
+            "doi": "10.1371/journal.pone.0045371",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "in taxon",
+      "source": "GO:0019076",
+      "target": "NCBITaxon:11520",
+      "evidence": [
+        {
+          "reference": "PMID:41917408",
+          "snippet": "The neuraminidase (NA) glycoprotein of influenza virus plays a critical role in the release of progeny viruses and their spread, making it an important target for antiviral drugs.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Establishes that viral release is a process specific to influenza virus, supporting the in taxon relationship between the viral release process and Influenza A virus.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Influenza Virus Neuraminidase Glycoprotein, Its Inhibitors, and Their Resistance.",
+            "authors": [
+              "Takashita E"
+            ],
+            "journal": "Advances in experimental medicine and biology",
+            "year": "2026",
+            "doi": "10.1007/978-3-032-04153-1_24",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:23028967",
+          "snippet": "influenza virus neuraminidase (NA) cleaves terminal sialic acid residues on oligosaccharide chains that are receptors for virus binding, thus playing an important role in the release of virions from infected cells to promote the spread of cell-to-cell infection.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "The viral release process described is occurring in the context of influenza virus, supporting this process being in the Influenza A virus taxon.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Bacterial neuraminidase rescues influenza virus replication from inhibition by a neuraminidase inhibitor.",
+            "authors": [
+              "Nishikawa T",
+              "Shimizu K",
+              "Tanaka T",
+              "Kuroda K",
+              "Takayama T",
+              "Yamamoto T",
+              "Hanada N",
+              "Hamada Y"
+            ],
+            "journal": "PloS one",
+            "year": "2012",
+            "doi": "10.1371/journal.pone.0045371",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "causes",
+      "source": "NCBITaxon:11520",
+      "target": "MESH:D007251",
+      "evidence": [
+        {
+          "reference": "PMID:42212418",
+          "snippet": "Type A viruses caused over two-thirds of cases, with variability across WHO Regions and seasons.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Influenza A (Type A) viruses are identified as the predominant causal agents of influenza cases in global surveillance, supporting the causes relationship.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Global influenza epidemiology after 2020: patterns of circulation, epidemic timing and duration, and implications for vaccination strategies.",
+            "authors": [
+              "Del Riccio M",
+              "Caini S"
+            ],
+            "journal": "Euro surveillance : bulletin Europeen sur les maladies transmissibles = European communicable disease bulletin",
+            "year": "2026",
+            "doi": "10.2807/1560-7917.ES.2026.31.21.2500743",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:42057722",
+          "snippet": "NAIs, including oseltamivir, zanamivir, peramivir and laninamivir, block viral release, while polymerase inhibitors such as baloxavir disrupt viral RNA replication.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Reviews influenza A and B viral infections as the clinical context requiring antiviral therapy, implicitly confirming influenza A virus as causative of influenza disease.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Antiviral treatment for influenza.",
+            "authors": [
+              "Hui DS"
+            ],
+            "journal": "Philosophical transactions of the Royal Society of London. Series B, Biological sciences",
+            "year": "2026",
+            "doi": "10.1098/rstb.2024.0344",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00198#mechanism-of-action",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    },
+    {
+      "url": "https://www.uniprot.org/uniprot/P03472",
+      "type": "other",
+      "label": "uniprot.org — record source"
+    },
+    {
+      "url": "https://www.ncbi.nlm.nih.gov/taxonomy/11520",
+      "type": "other",
+      "label": "ncbi.nlm.nih.gov — record source"
+    }
+  ],
+  "site": {
+    "id": "phase3__P14",
+    "record_id": "P14_DB00198_MESH_D007251",
+    "run": "phase3",
+    "run_label": "Phase-3 eval",
+    "source_file": "tests/phase3_eval_outputs/P14.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/phase3__P15.json b/web-revamp-mockup/data/records/phase3__P15.json
new file mode 100644
index 0000000..54c328e
--- /dev/null
+++ b/web-revamp-mockup/data/records/phase3__P15.json
@@ -0,0 +1,314 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P15_DB00787_MESH_D006561",
+    "drug": "Acyclovir",
+    "drug_mesh": "MESH:D000212",
+    "drugbank": "DB:DB00787",
+    "disease": "Herpes Simplex",
+    "disease_mesh": "MESH:D006561",
+    "summary": "Acyclovir → HSV-1 DNA polymerase catalytic subunit → viral DNA genome replication → Human alphaherpesvirus 1 → Herpes Simplex"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D000212",
+      "name": "Acyclovir",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P03176",
+      "name": "HSV-1 thymidine kinase",
+      "label": "Protein"
+    },
+    {
+      "id": "UniProt:P04293",
+      "name": "HSV-1 DNA polymerase catalytic subunit",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0039693",
+      "name": "viral DNA genome replication",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "NCBITaxon:10298",
+      "name": "Human alphaherpesvirus 1",
+      "label": "OrganismTaxon"
+    },
+    {
+      "id": "MESH:D006561",
+      "name": "Herpes Simplex",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affected by",
+      "source": "MESH:D000212",
+      "target": "UniProt:P03176",
+      "evidence": [
+        {
+          "reference": "PMID:28027917",
+          "snippet": "The antiherpetic drugs acyclovir (ACV, valaciclovir) and penciclovir (famciclovir) are phosphorylated by viral thymidine kinase and terminate DNA synthesis.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Acyclovir is selectively phosphorylated to acyclovir monophosphate by HSV-encoded thymidine kinase, the first activation step in the antiviral pathway.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Profile of anti-herpetic action of ASP2151 (amenamevir) as a helicase-primase inhibitor.",
+            "authors": [
+              "Yajima M",
+              "Yamada H",
+              "Takemoto M",
+              "Daikoku T",
+              "Yoshida Y",
+              "Long T",
+              "Okuda T",
+              "Shiraki K"
+            ],
+            "journal": "Antiviral research",
+            "year": "2017",
+            "doi": "10.1016/j.antiviral.2016.12.008",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "in taxon",
+      "source": "UniProt:P03176",
+      "target": "NCBITaxon:10298",
+      "evidence": [
+        {
+          "reference": "PMID:25857706",
+          "snippet": "The inhibition of herpes simplex virus (HSV) by these compounds is not dependent on the viral thymidine kinase (TK), which is known to phosphorylate acyclovir (ACV), a standard treatment for HSV infections.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Thymidine kinase that phosphorylates acyclovir is encoded by herpes simplex virus, establishing the protein's taxon assignment.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "TAOK3 phosphorylates the methylenecyclopropane nucleoside MBX 2168 to its monophosphate.",
+            "authors": [
+              "Komazin-Meredith G",
+              "Cardinale SC",
+              "Comeau K",
+              "Magalhaes KJ",
+              "Hartline CB",
+              "Williams JD",
+              "Opperman TJ",
+              "Prichard MN",
+              "Bowlin TL"
+            ],
+            "journal": "Antiviral research",
+            "year": "2015",
+            "doi": "10.1016/j.antiviral.2015.04.001",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D000212",
+      "target": "UniProt:P04293",
+      "evidence": [
+        {
+          "reference": "PMID:8755822",
+          "snippet": "Acyclovir triphosphate, the active intracellular metabolite of acyclovir, exerts its antiviral effect by inhibiting herpesviral DNA polymerases through premature chain termination.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Once converted to acyclovir triphosphate by cellular kinases, the drug inhibits viral DNA polymerase via premature chain termination after incorporation into nascent viral DNA.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Acyclovir triphosphate inhibits the diagnostic polymerase chain reaction for cytomegalovirus.",
+            "authors": [
+              "Yedidag EN",
+              "Koffron AJ",
+              "Mueller KH",
+              "Kaplan B",
+              "Kaufman DB",
+              "Fryer JP",
+              "Stuart FP",
+              "Abecassis M"
+            ],
+            "journal": "Transplantation",
+            "year": "1996",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "in taxon",
+      "source": "UniProt:P04293",
+      "target": "NCBITaxon:10298",
+      "evidence": [
+        {
+          "reference": "PMID:39197451",
+          "snippet": "We determined cryoelectron microscopy (cryo-EM) structures of DNA-bound herpes simplex virus polymerase holoenzyme in multiple conformations and interacting with antivirals in clinical use.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "The DNA polymerase catalytic subunit (Pol) targeted by acyclovir is encoded by herpes simplex virus.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Viral DNA polymerase structures reveal mechanisms of antiviral drug resistance.",
+            "authors": [
+              "Shankar S",
+              "Pan J",
+              "Yang P",
+              "Bian Y",
+              "Oroszlán G",
+              "Yu Z",
+              "Mukherjee P",
+              "Filman DJ",
+              "Hogle JM",
+              "Shekhar M",
+              "Coen DM",
+              "Abraham J"
+            ],
+            "journal": "Cell",
+            "year": "2024",
+            "doi": "10.1016/j.cell.2024.07.048",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P04293",
+      "target": "GO:0039693",
+      "evidence": [
+        {
+          "reference": "PMID:39197451",
+          "snippet": "These structures reveal how the catalytic subunit Pol and the processivity factor UL42 bind DNA to promote processive DNA synthesis.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "The HSV Pol catalytic subunit drives processive viral DNA synthesis, i.e. viral DNA genome replication.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Viral DNA polymerase structures reveal mechanisms of antiviral drug resistance.",
+            "authors": [
+              "Shankar S",
+              "Pan J",
+              "Yang P",
+              "Bian Y",
+              "Oroszlán G",
+              "Yu Z",
+              "Mukherjee P",
+              "Filman DJ",
+              "Hogle JM",
+              "Shekhar M",
+              "Coen DM",
+              "Abraham J"
+            ],
+            "journal": "Cell",
+            "year": "2024",
+            "doi": "10.1016/j.cell.2024.07.048",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "in taxon",
+      "source": "GO:0039693",
+      "target": "NCBITaxon:10298",
+      "evidence": [
+        {
+          "reference": "PMID:39078136",
+          "snippet": "The conventional clinical management of HSK primarily relies on anti-virals to suppress HSV-1 replication, anti-inflammatory drugs (such as corticosteroids) to provide symptomatic relief from pain and inflammation, and surgical interventions in more severe cases to replace damaged cornea.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "HSV-1 replication (viral DNA genome replication) is the process targeted by antivirals such as acyclovir; the process is taxon-bound to HSV-1.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "The immunobiology of corneal HSV-1 infection and herpetic stromal keratitis.",
+            "authors": [
+              "Antony F",
+              "Kinha D",
+              "Nowińska A",
+              "Rouse BT",
+              "Suryawanshi A"
+            ],
+            "journal": "Clinical microbiology reviews",
+            "year": "2024",
+            "doi": "10.1128/cmr.00006-24",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "causes",
+      "source": "NCBITaxon:10298",
+      "target": "MESH:D006561",
+      "evidence": [
+        {
+          "reference": "PMID:36309081",
+          "snippet": "Herpes simplex viruses (HSV), the causative agents of recurrent orofacial and anogenital infections, can cause significant morbidity and mortality in both immunocompetent and immunocompromised individuals.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "HSV-1 is the etiologic agent of herpes simplex disease.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Acyclovir resistance in herpes simplex viruses: Prevalence and therapeutic alternatives.",
+            "authors": [
+              "Schalkwijk HH",
+              "Snoeck R",
+              "Andrei G"
+            ],
+            "journal": "Biochemical pharmacology",
+            "year": "2022",
+            "doi": "10.1016/j.bcp.2022.115322",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00787",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    },
+    {
+      "url": "https://www.uniprot.org/uniprot/P03176",
+      "type": "other",
+      "label": "uniprot.org — record source"
+    },
+    {
+      "url": "https://www.uniprot.org/uniprot/P04293",
+      "type": "other",
+      "label": "uniprot.org — record source"
+    }
+  ],
+  "site": {
+    "id": "phase3__P15",
+    "record_id": "P15_DB00787_MESH_D006561",
+    "run": "phase3",
+    "run_label": "Phase-3 eval",
+    "source_file": "tests/phase3_eval_outputs/P15.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/phase3__P16.json b/web-revamp-mockup/data/records/phase3__P16.json
new file mode 100644
index 0000000..dd4cad6
--- /dev/null
+++ b/web-revamp-mockup/data/records/phase3__P16.json
@@ -0,0 +1,252 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P16_DB01235_MESH_D010300",
+    "drug": "levodopa",
+    "drug_mesh": "MESH:D007980",
+    "drugbank": "DB:DB01235",
+    "disease": "Parkinson's disease",
+    "disease_mesh": "MESH:D010300",
+    "summary": "levodopa → aromatic-L-amino-acid decarboxylase → Dopamine → synaptic transmission, dopaminergic → Parkinson's disease"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D007980",
+      "name": "levodopa",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P20711",
+      "name": "aromatic-L-amino-acid decarboxylase",
+      "label": "Protein"
+    },
+    {
+      "id": "MESH:D004298",
+      "name": "Dopamine",
+      "label": "ChemicalSubstance"
+    },
+    {
+      "id": "GO:0001963",
+      "name": "synaptic transmission, dopaminergic",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D010300",
+      "name": "Parkinson's disease",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "directly physically interacts with",
+      "source": "MESH:D007980",
+      "target": "UniProt:P20711",
+      "evidence": [
+        {
+          "reference": "PMID:14634798",
+          "snippet": "l-DOPA with the tag bonded at position 5 served as the best substrate for AADC.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Levodopa (L-DOPA) is the substrate that directly interacts with aromatic amino acid decarboxylase (AADC) at its active site; this biochemical interaction is the first step in the conversion of levodopa to dopamine.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Enzymatic assay for perfluoro-tagged metabolites of l-DOPA using crude lysate from E. coli transformed with pKKAADCII.",
+            "authors": [
+              "Dingman S",
+              "Snyder-Leiby T",
+              "Mack DJ",
+              "Thomas R",
+              "Guo C"
+            ],
+            "journal": "Applied microbiology and biotechnology",
+            "year": "2004",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "produces",
+      "source": "UniProt:P20711",
+      "target": "MESH:D004298",
+      "evidence": [
+        {
+          "reference": "PMID:22061622",
+          "snippet": "recombinant human AADC, which actively catalyzes dopamine production from DOPA",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "AADC catalyzes the decarboxylation of L-DOPA (DOPA) to produce dopamine; this is the direct enzymatic product of AADC activity.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Does the aromatic L-amino acid decarboxylase contribute to thyronamine biosynthesis?",
+            "authors": [
+              "Hoefig CS",
+              "Renko K",
+              "Piehl S",
+              "Scanlan TS",
+              "Bertoldi M",
+              "Opladen T",
+              "Hoffmann GF",
+              "Klein J",
+              "Blankenstein O",
+              "Schweizer U",
+              "Köhrle J"
+            ],
+            "journal": "Molecular and cellular endocrinology",
+            "year": "2012",
+            "doi": "10.1016/j.mce.2011.10.024",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:40488810",
+          "snippet": "subsequently converted into dopamine via aromatic L-amino acid decarboxylase",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Review confirming that L-DOPA is converted into dopamine by the enzyme aromatic L-amino acid decarboxylase (AADC).",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "The role of L-DOPA in neurological and neurodegenerative complications: a review.",
+            "authors": [
+              "Kulkarni SR",
+              "Thokchom B",
+              "Abbigeri MB",
+              "Bhavi SM",
+              "Singh SR",
+              "Metri N",
+              "Yarajarla RB"
+            ],
+            "journal": "Molecular and cellular biochemistry",
+            "year": "2025",
+            "doi": "10.1007/s11010-025-05324-w",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "MESH:D004298",
+      "target": "GO:0001963",
+      "evidence": [
+        {
+          "reference": "PMID:38537648",
+          "snippet": "Dopamine's role as the principal neurotransmitter in motor functions has long been accepted.",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "explanation": "Dopamine is the neurotransmitter that mediates dopaminergic synaptic transmission; its presence positively regulates this biological process.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Ophthalmate is a new regulator of motor functions via CaSR: implications for movement disorders.",
+            "authors": [
+              "Alhassen S",
+              "Hogenkamp D",
+              "Nguyen HA",
+              "Al Masri S",
+              "Abbott GW",
+              "Civelli O",
+              "Alachkar A"
+            ],
+            "journal": "Brain : a journal of neurology",
+            "year": "2024",
+            "doi": "10.1093/brain/awae097",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "negatively correlated with",
+      "source": "GO:0001963",
+      "target": "MESH:D010300",
+      "evidence": [
+        {
+          "reference": "PMID:40966690",
+          "snippet": "reduced striatal dopaminergic transmission is a transdiagnostic substrate for psychomotor retardation underlying the motor features of conditions such as Parkinson's disease",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Reduced dopaminergic synaptic transmission is the defining pathophysiological feature of Parkinson's disease motor symptoms; dopaminergic transmission is therefore negatively correlated with Parkinson's disease.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Reduced striatal dopamine transmission as a transdiagnostic substrate of psychomotor retardation.",
+            "authors": [
+              "Leong IL",
+              "Ng TH",
+              "Sen K",
+              "Burchill E",
+              "Costello H",
+              "Badenoch JB",
+              "Coebergh J",
+              "McCutcheon RA",
+              "Nair A",
+              "Browning M",
+              "Huys QJM",
+              "Lewis G",
+              "Lees A",
+              "David AS",
+              "Rogers JP"
+            ],
+            "journal": "Brain : a journal of neurology",
+            "year": "2026",
+            "doi": "10.1093/brain/awaf335",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:35331828",
+          "snippet": "Parkinson's Disease (PD) occurs due to extensive damage of dopamine-producing neurons; this causes dopamine deficits in the midbrain",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Review confirming that dopamine deficiency (from neuronal loss) is the pathogenic basis of PD, establishing the negative correlation between dopaminergic neurotransmission and disease.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Restoration and targeting of aberrant neurotransmitters in Parkinson's disease therapeutics.",
+            "authors": [
+              "Yadav D",
+              "Kumar P"
+            ],
+            "journal": "Neurochemistry international",
+            "year": "2022",
+            "doi": "10.1016/j.neuint.2022.105327",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB01235#mechanism-of-action",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    },
+    {
+      "url": "https://www.uniprot.org/uniprot/P20711",
+      "type": "other",
+      "label": "uniprot.org — record source"
+    }
+  ],
+  "site": {
+    "id": "phase3__P16",
+    "record_id": "P16_DB01235_MESH_D010300",
+    "run": "phase3",
+    "run_label": "Phase-3 eval",
+    "source_file": "tests/phase3_eval_outputs/P16.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/phase3__P17.json b/web-revamp-mockup/data/records/phase3__P17.json
new file mode 100644
index 0000000..81207fe
--- /dev/null
+++ b/web-revamp-mockup/data/records/phase3__P17.json
@@ -0,0 +1,361 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P17_DB00472_MESH_D003865",
+    "drug": "Fluoxetine",
+    "drug_mesh": "MESH:D005473",
+    "drugbank": "DB:DB00472",
+    "disease": "Major depressive disorder",
+    "disease_mesh": "MESH:D003865",
+    "summary": "Fluoxetine → Sodium-dependent serotonin transporter → Serotonin uptake → Serotonin → Serotonin secretion, neurotransmission → Major depressive disorder"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D005473",
+      "name": "Fluoxetine",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P31645",
+      "name": "Sodium-dependent serotonin transporter",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0051610",
+      "name": "Serotonin uptake",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D012701",
+      "name": "Serotonin",
+      "label": "ChemicalSubstance"
+    },
+    {
+      "id": "GO:0060096",
+      "name": "Serotonin secretion, neurotransmission",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D003865",
+      "name": "Major depressive disorder",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D005473",
+      "target": "UniProt:P31645",
+      "evidence": [
+        {
+          "reference": "PMID:31480244",
+          "snippet": "Their primary mechanism of action is considered to be the increased synaptic concentration of serotonin through blockade of the serotonin transporter (SERT).",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Fluoxetine, as an SSRI, blocks SERT — decreasing the transporter's activity of removing serotonin from the synapse.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Fluoxetine Suppresses Glutamate- and GABA-Mediated Neurotransmission by Altering SNARE Complex.",
+            "authors": [
+              "Lazarevic V",
+              "Mantas I",
+              "Flais I",
+              "Svenningsson P"
+            ],
+            "journal": "International journal of molecular sciences",
+            "year": "2019",
+            "doi": "10.3390/ijms20174247",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:24516100",
+          "snippet": "We show that fluoxetine binds within the central substrate site of human SERT",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Fluoxetine binds the central substrate site of SERT, competitively blocking its serotonin uptake activity.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Molecular basis for selective serotonin reuptake inhibition by the antidepressant agent fluoxetine (Prozac).",
+            "authors": [
+              "Andersen J",
+              "Stuhr-Hansen N",
+              "Zachariassen LG",
+              "Koldsø H",
+              "Schiøtt B",
+              "Strømgaard K",
+              "Kristensen AS"
+            ],
+            "journal": "Molecular pharmacology",
+            "year": "2014",
+            "doi": "10.1124/mol.113.091249",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P31645",
+      "target": "GO:0051610",
+      "evidence": [
+        {
+          "reference": "PMID:26019340",
+          "snippet": "Serotonergic neurotransmission is terminated by reuptake of extracellular serotonin (5-HT) by the high-affinity serotonin transporter (SERT).",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "SERT is the primary transporter that mediates serotonin reuptake; its activity drives the serotonin uptake process.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Amphetamine action at the cocaine- and antidepressant-sensitive serotonin transporter is modulated by αCaMKII.",
+            "authors": [
+              "Steinkellner T",
+              "Montgomery TR",
+              "Hofmaier T",
+              "Kudlacek O",
+              "Yang JW",
+              "Rickhag M",
+              "Jung G",
+              "Lubec G",
+              "Gether U",
+              "Freissmuth M",
+              "Sitte HH"
+            ],
+            "journal": "The Journal of neuroscience : the official journal of the Society for Neuroscience",
+            "year": "2015",
+            "doi": "10.1523/JNEUROSCI.4034-14.2015",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:25652393",
+          "snippet": "The serotonin transporter (SERT), which is responsible for the reuptake of serotonin from the synaptic cleft into the neuron",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "SERT is responsible for serotonin reuptake from the synaptic cleft — confirming it positively regulates the serotonin uptake process.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Interaction between 5-HTTLPR and 5-HT1B genotype status enhances cerebral 5-HT1A receptor binding.",
+            "authors": [
+              "Baldinger P",
+              "Kraus C",
+              "Rami-Mark C",
+              "Gryglewski G",
+              "Kranz GS",
+              "Haeusler D",
+              "Hahn A",
+              "Spies M",
+              "Wadsak W",
+              "Mitterhauser M",
+              "Rujescu D",
+              "Kasper S",
+              "Lanzenberger R"
+            ],
+            "journal": "NeuroImage",
+            "year": "2015",
+            "doi": "10.1016/j.neuroimage.2015.01.049",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "abundance",
+      "object_direction_qualifier": "decreased",
+      "source": "GO:0051610",
+      "target": "MESH:D012701",
+      "evidence": [
+        {
+          "reference": "PMID:23796482",
+          "snippet": "SSRIs act specifically on synaptic serotonin concentrations by blocking its reuptake in the presynapse and increasing levels in the presynaptic membrane.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "By blocking serotonin reuptake, SSRIs increase synaptic serotonin — confirming that the reuptake process (GO:0051610) normally decreases synaptic serotonin abundance.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Selective serotonin reuptake inhibitor exposure.",
+            "authors": [
+              "Fitzgerald KT",
+              "Bronstein AC"
+            ],
+            "journal": "Topics in companion animal medicine",
+            "year": "2013",
+            "doi": "10.1053/j.tcam.2013.03.003",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:31480244",
+          "snippet": "by virtue of its inhibition at SERT, fluoxetine increases extracellular serotonin levels",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Blocking the serotonin uptake process raises extracellular serotonin, confirming that serotonin uptake normally decreases serotonin abundance.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Fluoxetine Suppresses Glutamate- and GABA-Mediated Neurotransmission by Altering SNARE Complex.",
+            "authors": [
+              "Lazarevic V",
+              "Mantas I",
+              "Flais I",
+              "Svenningsson P"
+            ],
+            "journal": "International journal of molecular sciences",
+            "year": "2019",
+            "doi": "10.3390/ijms20174247",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "positively correlated with",
+      "source": "MESH:D012701",
+      "target": "GO:0060096",
+      "evidence": [
+        {
+          "reference": "PMID:26019340",
+          "snippet": "Serotonergic neurotransmission is terminated by reuptake of extracellular serotonin (5-HT) by the high-affinity serotonin transporter (SERT).",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Extracellular serotonin drives serotonergic neurotransmission; its removal terminates signaling, confirming serotonin abundance is positively correlated with serotonergic neurotransmission.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Amphetamine action at the cocaine- and antidepressant-sensitive serotonin transporter is modulated by αCaMKII.",
+            "authors": [
+              "Steinkellner T",
+              "Montgomery TR",
+              "Hofmaier T",
+              "Kudlacek O",
+              "Yang JW",
+              "Rickhag M",
+              "Jung G",
+              "Lubec G",
+              "Gether U",
+              "Freissmuth M",
+              "Sitte HH"
+            ],
+            "journal": "The Journal of neuroscience : the official journal of the Society for Neuroscience",
+            "year": "2015",
+            "doi": "10.1523/JNEUROSCI.4034-14.2015",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:35090949",
+          "snippet": "swimming behavior has been associated with an increase in serotonergic neurotransmission",
+          "supports": "PARTIAL",
+          "evidence_source": "MODEL_ORGANISM",
+          "explanation": "Increased serotonin availability (via FLX-mediated reuptake block) is associated with increased serotonergic neurotransmission in animal models.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Preventive treatment with fish oil facilitates the antidepressant-like effect of antidepressant drugs in type-1 diabetes mellitus rats: Implication of serotonergic system.",
+            "authors": [
+              "Paula Farias Waltrick A",
+              "Henrique Bernardo de Lima Silva A",
+              "Cristina de Carvalho M",
+              "Aparecida Comotti de Oliveira B",
+              "Naliwaiko K",
+              "Maria da Cunha J",
+              "Menezes Zanoveli J"
+            ],
+            "journal": "Neuroscience letters",
+            "year": "2022",
+            "doi": "10.1016/j.neulet.2022.136477",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "treats",
+      "source": "GO:0060096",
+      "target": "MESH:D003865",
+      "evidence": [
+        {
+          "reference": "PMID:34658805",
+          "snippet": "synaptic deficiencies of monoaminergic neurotransmitters play a causative role in this neuropsychiatric disorder, and that boosting monoamines with drugs such as SSRIs, SNRIs, TCAs, and MAOIs has antidepressant effects",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Deficient serotonergic (monoaminergic) neurotransmission underlies MDD; boosting it via SSRIs treats the disorder.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Are Noradrenergic Transmission Reducing Drugs Antidepressants?",
+            "authors": [
+              "Fitzgerald PJ"
+            ],
+            "journal": "Frontiers in behavioral neuroscience",
+            "year": "2021",
+            "doi": "10.3389/fnbeh.2021.673634",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:31480244",
+          "snippet": "Major depressive disorder is one of the most common neuropsychiatric disorders worldwide. The treatment of choice that shows good efficacy in mood stabilization is based on selective serotonin reuptake inhibitors (SSRIs).",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "SSRIs, which work by increasing serotonergic neurotransmission, are the established treatment for MDD.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Fluoxetine Suppresses Glutamate- and GABA-Mediated Neurotransmission by Altering SNARE Complex.",
+            "authors": [
+              "Lazarevic V",
+              "Mantas I",
+              "Flais I",
+              "Svenningsson P"
+            ],
+            "journal": "International journal of molecular sciences",
+            "year": "2019",
+            "doi": "10.3390/ijms20174247",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00472#mechanism-of-action",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    },
+    {
+      "url": "https://www.uniprot.org/uniprot/P31645",
+      "type": "other",
+      "label": "uniprot.org — record source"
+    }
+  ],
+  "site": {
+    "id": "phase3__P17",
+    "record_id": "P17_DB00472_MESH_D003865",
+    "run": "phase3",
+    "run_label": "Phase-3 eval",
+    "source_file": "tests/phase3_eval_outputs/P17.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/phase3__P18.json b/web-revamp-mockup/data/records/phase3__P18.json
new file mode 100644
index 0000000..d6e5a54
--- /dev/null
+++ b/web-revamp-mockup/data/records/phase3__P18.json
@@ -0,0 +1,199 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P18_DB01356_MESH_D001714",
+    "drug": "Lithium",
+    "drug_mesh": "MESH:D008094",
+    "drugbank": "DB:DB01356",
+    "disease": "Bipolar Disorder",
+    "disease_mesh": "MESH:D001714",
+    "summary": "Lithium → Glycogen synthase kinase-3 beta → apoptotic process → Bipolar Disorder"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D008094",
+      "name": "Lithium",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P49841",
+      "name": "Glycogen synthase kinase-3 beta",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0006915",
+      "name": "apoptotic process",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D001714",
+      "name": "Bipolar Disorder",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D008094",
+      "target": "UniProt:P49841",
+      "evidence": [
+        {
+          "reference": "PMID:12071511",
+          "snippet": "lithium has been identified as a selective and direct inhibitor of GSK-3beta",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Seminal paper in Bipolar Disorders journal establishing lithium as a selective and direct inhibitor of GSK-3beta activity.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Glycogen synthase kinase-3beta, mood stabilizers, and neuroprotection.",
+            "authors": [
+              "Li X",
+              "Bijur GN",
+              "Jope RS"
+            ],
+            "journal": "Bipolar disorders",
+            "year": "2002",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:21732538",
+          "snippet": "lithium is known to be a direct inhibitor of GSK-3beta",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "explanation": "Medicinal chemistry paper developing GSK-3beta inhibitors for bipolar disorder, confirming lithium's known direct inhibitory action on GSK-3beta.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Identification of a glycogen synthase kinase-3β inhibitor that attenuates hyperactivity in CLOCK mutant mice.",
+            "authors": [
+              "Kozikowski AP",
+              "Gunosewoyo H",
+              "Guo S",
+              "Gaisina IN",
+              "Walter RL",
+              "Ketcherside A",
+              "McClung CA",
+              "Mesecar AD",
+              "Caldarone B"
+            ],
+            "journal": "ChemMedChem",
+            "year": "2011",
+            "doi": "10.1002/cmdc.201100188",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P49841",
+      "target": "GO:0006915",
+      "evidence": [
+        {
+          "reference": "PMID:12071511",
+          "snippet": "GSK-3beta is a pro-apoptotic enzyme",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "The paper explicitly identifies GSK-3beta as a pro-apoptotic enzyme, meaning it positively regulates the apoptotic process.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Glycogen synthase kinase-3beta, mood stabilizers, and neuroprotection.",
+            "authors": [
+              "Li X",
+              "Bijur GN",
+              "Jope RS"
+            ],
+            "journal": "Bipolar disorders",
+            "year": "2002",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "contributes to",
+      "source": "GO:0006915",
+      "target": "MESH:D001714",
+      "evidence": [
+        {
+          "reference": "PMID:12071511",
+          "snippet": "several drugs therapeutic for bipolar disorder can provide neuroprotection by inhibiting the pro-apoptotic effects of GSK-3beta, providing new evidence that dysregulation of GSK-3beta may contribute to the pathophysiology of bipolar disorder",
+          "supports": "PARTIAL",
+          "evidence_source": "IN_VITRO",
+          "explanation": "The efficacy of bipolar drugs is attributed to inhibiting GSK-3beta's pro-apoptotic effects, implying that apoptotic process driven by GSK-3beta contributes to bipolar disorder pathophysiology. Support is PARTIAL because \"may contribute\" is hedged language.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Glycogen synthase kinase-3beta, mood stabilizers, and neuroprotection.",
+            "authors": [
+              "Li X",
+              "Bijur GN",
+              "Jope RS"
+            ],
+            "journal": "Bipolar disorders",
+            "year": "2002",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:36440772",
+          "snippet": "inhibition of glycogen synthase kinase 3 beta and inositol monophosphatase, resulting in induction of brain-derived neurotrophic factor, antiapoptotic proteins, deprivation of calcium-induced apoptosis",
+          "supports": "PARTIAL",
+          "evidence_source": "OTHER",
+          "explanation": "Lithium treats bipolar disorder by inducing antiapoptotic proteins and depriving calcium-induced apoptosis, supporting that apoptotic process is a pathological contributor to bipolar disorder.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "[A systematic analysis of neurobiological roles of lithium].",
+            "authors": [
+              "Gogoleva IV",
+              "Gromova OA",
+              "Torshin IY",
+              "Grishina TR",
+              "Pronin AV"
+            ],
+            "journal": "Zhurnal nevrologii i psikhiatrii imeni S.S. Korsakova",
+            "year": "2022",
+            "doi": "10.17116/jnevro202212211117",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB01356#mechanism-of-action",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    },
+    {
+      "url": "https://www.uniprot.org/uniprot/P49841#function",
+      "type": "other",
+      "label": "uniprot.org — record source"
+    }
+  ],
+  "site": {
+    "id": "phase3__P18",
+    "record_id": "P18_DB01356_MESH_D001714",
+    "run": "phase3",
+    "run_label": "Phase-3 eval",
+    "source_file": "tests/phase3_eval_outputs/P18.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/phase3__P19.json b/web-revamp-mockup/data/records/phase3__P19.json
new file mode 100644
index 0000000..0c5a136
--- /dev/null
+++ b/web-revamp-mockup/data/records/phase3__P19.json
@@ -0,0 +1,275 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P19_DB00996_MESH_D004827",
+    "drug": "Gabapentin",
+    "drug_mesh": "MESH:D000077306",
+    "drugbank": "DB:DB00996",
+    "disease": "Epilepsy",
+    "disease_mesh": "MESH:D004827",
+    "summary": "Gabapentin → Voltage-dependent calcium channel subunit alpha-2/delta-1 → calcium ion transmembrane transport → neurotransmitter secretion → Epilepsy"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D000077306",
+      "name": "Gabapentin",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P54289",
+      "name": "Voltage-dependent calcium channel subunit alpha-2/delta-1",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0070588",
+      "name": "calcium ion transmembrane transport",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "GO:0007269",
+      "name": "neurotransmitter secretion",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D004827",
+      "name": "Epilepsy",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D000077306",
+      "target": "UniProt:P54289",
+      "evidence": [
+        {
+          "reference": "PMID:32607809",
+          "snippet": "α2δ proteins are the targets of the widely prescribed anti-epileptic and anti-allodynic drugs gabapentin and pregabalin",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Gabapentin binds to the α2δ-1 (CACNA2D1) auxiliary subunit of voltage-gated calcium channels, acting as a high-affinity ligand that reduces its functional activity.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Neuronal α2δ proteins and brain disorders.",
+            "authors": [
+              "Ablinger C",
+              "Geisler SM",
+              "Stanika RI",
+              "Klein CT",
+              "Obermair GJ"
+            ],
+            "journal": "Pflugers Archiv : European journal of physiology",
+            "year": "2020",
+            "doi": "10.1007/s00424-020-02420-2",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:32321743",
+          "snippet": "The α 2 δ-1 protein is required for the ability of gabapentin and pregabalin to reduce neurotransmitter release in neuronal tissue, consistent with a therapeutic mechanism of action via voltage-gated calcium channels.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "The α2δ-1 protein is both the high-affinity binding site and required mediator of gabapentin's mechanism, confirming gabapentin decreases its activity.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Analgesia with Gabapentin and Pregabalin May Involve N-Methyl-d-Aspartate Receptors, Neurexins, and Thrombospondins.",
+            "authors": [
+              "Taylor CP",
+              "Harris EW"
+            ],
+            "journal": "The Journal of pharmacology and experimental therapeutics",
+            "year": "2020",
+            "doi": "10.1124/jpet.120.266056",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P54289",
+      "target": "GO:0070588",
+      "evidence": [
+        {
+          "reference": "PMID:17403543",
+          "snippet": "All alpha2delta subunits increase the density at the plasma membrane of Ca(2+) channels activated by high voltage",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "The α2δ-1 subunit promotes trafficking of voltage-gated calcium channels to the plasma membrane, thereby positively regulating calcium ion transmembrane transport.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Functional biology of the alpha(2)delta subunits of voltage-gated calcium channels.",
+            "authors": [
+              "Davies A",
+              "Hendrich J",
+              "Van Minh AT",
+              "Wratten J",
+              "Douglas L",
+              "Dolphin AC"
+            ],
+            "journal": "Trends in pharmacological sciences",
+            "year": "2007",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:32607809",
+          "snippet": "They serve as regulatory subunits of voltage-gated calcium channels",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "As a regulatory subunit of voltage-gated calcium channels, α2δ-1 positively regulates calcium ion flux across the neuronal membrane.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Neuronal α2δ proteins and brain disorders.",
+            "authors": [
+              "Ablinger C",
+              "Geisler SM",
+              "Stanika RI",
+              "Klein CT",
+              "Obermair GJ"
+            ],
+            "journal": "Pflugers Archiv : European journal of physiology",
+            "year": "2020",
+            "doi": "10.1007/s00424-020-02420-2",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "GO:0070588",
+      "target": "GO:0007269",
+      "evidence": [
+        {
+          "reference": "PMID:29793598",
+          "snippet": "They inhibit calcium mediated neurotransmitter release through effects on α2δ-1 subunits",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Calcium-mediated neurotransmitter release is explicitly invoked — calcium ion transmembrane transport drives (positively regulates) neurotransmitter secretion at presynaptic terminals.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Analgesic mechanisms of gabapentinoids and effects in experimental pain models: a narrative review.",
+            "authors": [
+              "Chincholkar M"
+            ],
+            "journal": "British journal of anaesthesia",
+            "year": "2018",
+            "doi": "10.1016/j.bja.2018.02.066",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:21150315",
+          "snippet": "GBPs reduced release of various neurotransmitters from synapses in several neuronal tissues",
+          "supports": "PARTIAL",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Gabapentinoids reduce neurotransmitter release by modulating presynaptic Ca2+ currents, consistent with calcium influx positively driving neurotransmitter secretion.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Acute modulation of calcium currents and synaptic transmission by gabapentinoids.",
+            "authors": [
+              "Uchitel OD",
+              "Di Guilmi MN",
+              "Urbano FJ",
+              "Gonzalez-Inchauspe C"
+            ],
+            "journal": "Channels (Austin, Tex.)",
+            "year": "2010",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "contributes to",
+      "source": "GO:0007269",
+      "target": "MESH:D004827",
+      "evidence": [
+        {
+          "reference": "PMID:17126531",
+          "snippet": "Pregabalin subtly reduces the synaptic release of several neurotransmitters, apparently by binding to alpha2-delta subunits, and possibly accounting for its actions in vivo to reduce neuronal excitability and seizures",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "explanation": "Reducing neurotransmitter secretion reduces neuronal excitability and seizures; conversely, excess neurotransmitter secretion contributes to the seizure activity that defines epilepsy.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Pharmacology and mechanism of action of pregabalin: the calcium channel alpha2-delta (alpha2-delta) subunit as a target for antiepileptic drug discovery.",
+            "authors": [
+              "Taylor CP",
+              "Angelotti T",
+              "Fauman E"
+            ],
+            "journal": "Epilepsy research",
+            "year": "2007",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:17126531",
+          "snippet": "reduction of abnormal neuronal excitability through reduced neurotransmitter release",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "explanation": "Abnormal neurotransmitter release drives neuronal hyperexcitability and epileptic seizures; reducing secretion is the therapeutic rationale, confirming secretion contributes to epilepsy.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Pharmacology and mechanism of action of pregabalin: the calcium channel alpha2-delta (alpha2-delta) subunit as a target for antiepileptic drug discovery.",
+            "authors": [
+              "Taylor CP",
+              "Angelotti T",
+              "Fauman E"
+            ],
+            "journal": "Epilepsy research",
+            "year": "2007",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00996#mechanism-of-action",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    },
+    {
+      "url": "https://www.uniprot.org/uniprot/P54289",
+      "type": "other",
+      "label": "uniprot.org — record source"
+    }
+  ],
+  "site": {
+    "id": "phase3__P19",
+    "record_id": "P19_DB00996_MESH_D004827",
+    "run": "phase3",
+    "run_label": "Phase-3 eval",
+    "source_file": "tests/phase3_eval_outputs/P19.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/phase3__P20.json b/web-revamp-mockup/data/records/phase3__P20.json
new file mode 100644
index 0000000..05b84a9
--- /dev/null
+++ b/web-revamp-mockup/data/records/phase3__P20.json
@@ -0,0 +1,284 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P20_DB00843_MESH_D000544",
+    "drug": "Donepezil",
+    "drug_mesh": "MESH:D000077856",
+    "drugbank": "DB:DB00843",
+    "disease": "Alzheimer's disease",
+    "disease_mesh": "MESH:D000544",
+    "summary": "Donepezil → acetylcholinesterase → acetylcholine catabolic process → Acetylcholine → Alzheimer's disease"
+  },
+  "nodes": [
+    {
+      "id": "DB:DB00843",
+      "name": "Donepezil",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P22303",
+      "name": "acetylcholinesterase",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0006581",
+      "name": "acetylcholine catabolic process",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D000109",
+      "name": "Acetylcholine",
+      "label": "ChemicalSubstance"
+    },
+    {
+      "id": "MESH:D000544",
+      "name": "Alzheimer's disease",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "DB:DB00843",
+      "target": "UniProt:P22303",
+      "evidence": [
+        {
+          "reference": "PMID:36028305",
+          "snippet": "Donepezil inhibited muscle AChE with an approximate IC50 of 30 nM.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Direct measurement of donepezil inhibiting AChE enzymatic activity in isolated muscle preparations.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Donepezil inhibits neuromuscular junctional acetylcholinesterase and enhances synaptic transmission and function in isolated skeletal muscle.",
+            "authors": [
+              "Redman RR",
+              "Mackenzie H",
+              "Dissanayake KN",
+              "Eddleston M",
+              "Ribchester RR"
+            ],
+            "journal": "British journal of pharmacology",
+            "year": "2022",
+            "doi": "10.1111/bph.15940",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:41839797",
+          "snippet": "Donepezil is an acetylcholinesterase inhibitor that has shown efficacy in Alzheimer disease",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Clinical review confirming donepezil is an acetylcholinesterase inhibitor with established efficacy in Alzheimer disease.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Donepezil for Korsakoff Syndrome.",
+            "authors": [
+              "Fallone M",
+              "Sivananthan M",
+              "Joseph M"
+            ],
+            "journal": "American journal of therapeutics",
+            "year": "2026",
+            "doi": "10.1097/MJT.0000000000002102",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P22303",
+      "target": "GO:0006581",
+      "evidence": [
+        {
+          "reference": "PMID:38333993",
+          "snippet": "The enzyme acetylcholinesterase (AChE) hydrolyzes the neurotransmitter acetylcholine (ACh) at cholinergic synapses of the peripheral and central nervous system.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "AChE catalyzes hydrolysis of ACh — it drives (positively regulates) the acetylcholine catabolic process.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Acetylcholinesterase: A Versatile Template to Coin Potent Modulators of Multiple Therapeutic Targets.",
+            "authors": [
+              "Luque FJ",
+              "Muñoz-Torrero D"
+            ],
+            "journal": "Accounts of chemical research",
+            "year": "2024",
+            "doi": "10.1021/acs.accounts.3c00617",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:41373466",
+          "snippet": "Acetylcholinesterase (AChE) is a key enzyme responsible for terminating cholinergic neurotransmission by hydrolyzing acetylcholine.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "AChE is the key enzyme that hydrolyzes acetylcholine, confirming its positive regulatory role in the acetylcholine catabolic process.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Creatine and Taurine as Novel Competitive Inhibitors of Acetylcholinesterase: A Biochemical Basis for Nutritional Modulation of Brain Function.",
+            "authors": [
+              "Adamski P",
+              "Szeleszczuk Ł",
+              "Gackowski M",
+              "Grodner B"
+            ],
+            "journal": "International journal of molecular sciences",
+            "year": "2025",
+            "doi": "10.3390/ijms262311309",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "abundance",
+      "object_direction_qualifier": "decreased",
+      "source": "GO:0006581",
+      "target": "MESH:D000109",
+      "evidence": [
+        {
+          "reference": "PMID:41357417",
+          "snippet": "Cholinergic dysfunction due to the depletion of acetylcholine (ACh) levels in the synapse caused by increased acetylcholinesterase (AChE) activity is one of the major factors that drives AD progression.",
+          "supports": "SUPPORT",
+          "evidence_source": "COMPUTATIONAL",
+          "explanation": "Increased AChE activity (which drives acetylcholine catabolism) depletes ACh levels in the synapse, confirming the catabolic process decreases acetylcholine abundance.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "In silico decoding strategic pathways inhibition by coptisine for halting Alzheimer's pathology: a mechanistic insight.",
+            "authors": [
+              "Roy A",
+              "Kumar D",
+              "Bhattacharya P",
+              "Borah A"
+            ],
+            "journal": "In silico pharmacology",
+            "year": "2025",
+            "doi": "10.1007/s40203-025-00473-8",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:27039041",
+          "snippet": "Donepezil (1.3 mg/kg s.c.) increased extracellular ACh levels in the hippocampus",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "explanation": "Donepezil (an AChE inhibitor that blocks ACh catabolism) increases extracellular ACh levels, confirming that ACh catabolism normally decreases ACh abundance.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "The 5-HT6 receptor antagonist idalopirdine potentiates the effects of acetylcholinesterase inhibition on neuronal network oscillations and extracellular acetylcholine levels in the rat dorsal hippocampus.",
+            "authors": [
+              "Herrik KF",
+              "Mørk A",
+              "Richard N",
+              "Bundgaard C",
+              "Bastlund JF",
+              "de Jong IEM"
+            ],
+            "journal": "Neuropharmacology",
+            "year": "2016",
+            "doi": "10.1016/j.neuropharm.2016.03.043",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "negatively correlated with",
+      "source": "MESH:D000109",
+      "target": "MESH:D000544",
+      "evidence": [
+        {
+          "reference": "PMID:28714400",
+          "snippet": "deficit of acetylcholine has been evidenced in patients of Alzheimer's disease (AD), cholinesterase inhibitors are currently the most prescribed drugs for the treatment of AD.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Acetylcholine deficit is documented in Alzheimer's disease patients, establishing a negative correlation between acetylcholine levels and the disease.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Cholinesterase Inhibitory Activity of Some semi-Rigid Spiro Heterocycles: POM Analyses and Crystalline Structure of Pharmacophore Site.",
+            "authors": [
+              "Hadda TB",
+              "Talhi O",
+              "Silva ASM",
+              "Senol FS",
+              "Orhan IE",
+              "Rauf A",
+              "Mabkhot YN",
+              "Bachari K",
+              "Warad I",
+              "Farghaly TA",
+              "Althagafi II",
+              "Mubarak MS"
+            ],
+            "journal": "Mini reviews in medicinal chemistry",
+            "year": "2018",
+            "doi": "10.2174/1389557517666170713114039",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:40340068",
+          "snippet": "a series of influential publications revealed a loss of cholinergic markers in the cerebral cortex of postmortem Alzheimer disease brain samples.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Loss of cholinergic markers (including acetylcholine) in Alzheimer disease brain tissue supports the negative correlation between acetylcholine and the disease.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "The involvement of the cholinergic system in Alzheimer disease.",
+            "authors": [
+              "Cuello AC"
+            ],
+            "journal": "Handbook of clinical neurology",
+            "year": "2025",
+            "doi": "10.1016/B978-0-443-19088-9.00005-6",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00843#mechanism-of-action",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    },
+    {
+      "url": "https://www.uniprot.org/uniprot/P22303",
+      "type": "other",
+      "label": "uniprot.org — record source"
+    }
+  ],
+  "site": {
+    "id": "phase3__P20",
+    "record_id": "P20_DB00843_MESH_D000544",
+    "run": "phase3",
+    "run_label": "Phase-3 eval",
+    "source_file": "tests/phase3_eval_outputs/P20.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/phase3__P21.json b/web-revamp-mockup/data/records/phase3__P21.json
new file mode 100644
index 0000000..95dc006
--- /dev/null
+++ b/web-revamp-mockup/data/records/phase3__P21.json
@@ -0,0 +1,237 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P21_DB00563_MESH_D001172",
+    "drug": "Methotrexate",
+    "drug_mesh": "MESH:D008727",
+    "drugbank": "DB:DB00563",
+    "disease": "Rheumatoid Arthritis",
+    "disease_mesh": "MESH:D001172",
+    "summary": "Methotrexate → bifunctional purine biosynthesis protein ATIC → Adenosine → inflammatory response → Rheumatoid Arthritis"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D008727",
+      "name": "Methotrexate",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P31939",
+      "name": "bifunctional purine biosynthesis protein ATIC",
+      "label": "Protein"
+    },
+    {
+      "id": "MESH:D000241",
+      "name": "Adenosine",
+      "label": "ChemicalSubstance"
+    },
+    {
+      "id": "GO:0006954",
+      "name": "inflammatory response",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D001172",
+      "name": "Rheumatoid Arthritis",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D008727",
+      "target": "UniProt:P31939",
+      "evidence": [
+        {
+          "reference": "PMID:23464989",
+          "snippet": "intracellular MTX polyglutamates inhibit AICAR transformylase (ATIC) activity and thereby promote adenosine release",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Methotrexate polyglutamates (the active intracellular form of MTX) directly inhibit ATIC activity, the enzyme encoded by the ATIC gene (UniProt:P31939), thereby decreasing its catalytic function.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Fibroblasts from methotrexate-sensitive mice accumulate methotrexate polyglutamates but those from methotrexate-resistant mice do not.",
+            "authors": [
+              "You X",
+              "Williams A",
+              "Dervieux T",
+              "He W",
+              "Cronstein BN"
+            ],
+            "journal": "Clinical and experimental rheumatology",
+            "year": "2013",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "abundance",
+      "object_direction_qualifier": "decreased",
+      "source": "UniProt:P31939",
+      "target": "MESH:D000241",
+      "evidence": [
+        {
+          "reference": "PMID:23464989",
+          "snippet": "intracellular MTX polyglutamates inhibit AICAR transformylase (ATIC) activity and thereby promote adenosine release",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "This snippet establishes by contrapositive that ATIC activity limits adenosine release; when ATIC is inhibited, AICAR accumulates and promotes adenosine release, confirming that active ATIC decreases adenosine abundance.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Fibroblasts from methotrexate-sensitive mice accumulate methotrexate polyglutamates but those from methotrexate-resistant mice do not.",
+            "authors": [
+              "You X",
+              "Williams A",
+              "Dervieux T",
+              "He W",
+              "Cronstein BN"
+            ],
+            "journal": "Clinical and experimental rheumatology",
+            "year": "2013",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:40362255",
+          "snippet": "the pathway generating extracellular adenosine and its effects on promoting the immune regulation for the mechanism of MTX therapy of RA",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Confirms that extracellular adenosine generation is the key downstream effector in MTX-treated RA patients; ATIC inhibition is the upstream step that releases this brake on adenosine abundance.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Genetic Variants of the ATIC Gene and Therapeutic Response to Methotrexate in Patients with Rheumatoid Arthritis.",
+            "authors": [
+              "Gallardo-Moya SG",
+              "Gonzalez-Lopez L",
+              "Contreras-Haro B",
+              "Mireles-Ramirez MA",
+              "Villagomez-Vega A",
+              "Morán-Moguel MC",
+              "Méndez-Del Villar M",
+              "Vazquez-Villegas ML",
+              "Gamez-Nava JI",
+              "Saldaña-Cruz AM"
+            ],
+            "journal": "International journal of molecular sciences",
+            "year": "2025",
+            "doi": "10.3390/ijms26094013",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D000241",
+      "target": "GO:0006954",
+      "evidence": [
+        {
+          "reference": "PMID:12106498",
+          "snippet": "many of the anti-inflammatory effects of methotrexate are mediated by adenosine. This nucleoside, acting at one or more of its receptors, is a potent endogenous anti-inflammatory mediator.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Adenosine, acting via its cell-surface receptors, is a potent endogenous anti-inflammatory mediator that negatively regulates the inflammatory response; this review cites both animal and clinical studies confirming this.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Molecular action of methotrexate in inflammatory diseases.",
+            "authors": [
+              "Chan ES",
+              "Cronstein BN"
+            ],
+            "journal": "Arthritis research",
+            "year": "2002",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:30081197",
+          "snippet": "methotrexate increases adenosine levels and on engagement of adenosine with its extracellular receptors an intracellular cascade is activated promoting an overall anti-inflammatory state",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Adenosine engagement with extracellular receptors activates an intracellular cascade that promotes an overall anti-inflammatory state, directly supporting negatively regulates inflammatory response.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Methotrexate mechanism in treatment of rheumatoid arthritis.",
+            "authors": [
+              "Friedman B",
+              "Cronstein B"
+            ],
+            "journal": "Joint bone spine",
+            "year": "2019",
+            "doi": "10.1016/j.jbspin.2018.07.004",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "contributes to",
+      "source": "GO:0006954",
+      "target": "MESH:D001172",
+      "evidence": [
+        {
+          "reference": "PMID:42169647",
+          "snippet": "Rheumatoid arthritis (RA) is a chronic autoimmune disease characterized by synovial inflammation and joint destruction.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Synovial inflammation (i.e. the inflammatory response in joint tissue) is the defining pathological process of RA; the inflammatory response therefore contributes to the disease.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Role of the PI3K/AKT signaling pathway in regulating gene expression in rheumatoid arthritis (Review).",
+            "authors": [
+              "Cong C",
+              "Wang Y",
+              "Liu J",
+              "Jin C"
+            ],
+            "journal": "Molecular medicine reports",
+            "year": "2026",
+            "doi": "10.3892/mmr.2026.13915",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00563#mechanism-of-action",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    },
+    {
+      "url": "https://www.uniprot.org/uniprot/P31939",
+      "type": "other",
+      "label": "uniprot.org — record source"
+    }
+  ],
+  "site": {
+    "id": "phase3__P21",
+    "record_id": "P21_DB00563_MESH_D001172",
+    "run": "phase3",
+    "run_label": "Phase-3 eval",
+    "source_file": "tests/phase3_eval_outputs/P21.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/phase3__P22.json b/web-revamp-mockup/data/records/phase3__P22.json
new file mode 100644
index 0000000..4cb806e
--- /dev/null
+++ b/web-revamp-mockup/data/records/phase3__P22.json
@@ -0,0 +1,225 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P22_DB00065_MESH_D003424",
+    "drug": "Infliximab",
+    "drug_mesh": "MESH:D000069285",
+    "drugbank": "DB:DB00065",
+    "disease": "Crohn's disease",
+    "disease_mesh": "MESH:D003424",
+    "summary": "Infliximab → Tumor necrosis factor → NIK/NF-kappaB signaling → inflammatory response → Crohn's disease"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D000069285",
+      "name": "Infliximab",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P01375",
+      "name": "Tumor necrosis factor",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0038061",
+      "name": "NIK/NF-kappaB signaling",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "GO:0006954",
+      "name": "inflammatory response",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D003424",
+      "name": "Crohn's disease",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "directly physically interacts with",
+      "source": "MESH:D000069285",
+      "target": "UniProt:P01375",
+      "evidence": [
+        {
+          "reference": "PMID:34478145",
+          "snippet": "The mechanism of action (MOA) of infliximab involves its binding to soluble (s) and membrane (m) TNFα.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Infliximab's MoA is defined by its physical binding to both soluble and membrane-bound TNF-α, establishing a direct molecular interaction between the drug and its target protein.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Bioassays for the Evaluation of Target Neutralization and Complement-Dependent Cytotoxicity (CDC) of Therapeutic Antibodies.",
+            "authors": [
+              "Salinas-Jazmín N",
+              "Medina-Rivero E",
+              "Velasco-Velázquez MA"
+            ],
+            "journal": "Methods in molecular biology (Clifton, N.J.)",
+            "year": "2022",
+            "doi": "10.1007/978-1-0716-1450-1_17",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D000069285",
+      "target": "UniProt:P01375",
+      "evidence": [
+        {
+          "reference": "PMID:33614645",
+          "snippet": "Infliximab, adalimumab, and other anti-TNF antibodies neutralize TNFα, preventing interactions with its receptors and reducing the inflammatory response.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Infliximab neutralizes TNF-α, preventing it from engaging its receptors. Neutralization is equivalent to decreasing TNF-α functional activity.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Vedolizumab: Potential Mechanisms of Action for Reducing Pathological Inflammation in Inflammatory Bowel Diseases.",
+            "authors": [
+              "Luzentales-Simpson M",
+              "Pang YCF",
+              "Zhang A",
+              "Sousa JA",
+              "Sly LM"
+            ],
+            "journal": "Frontiers in cell and developmental biology",
+            "year": "2021",
+            "doi": "10.3389/fcell.2021.612830",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P01375",
+      "target": "GO:0038061",
+      "evidence": [
+        {
+          "reference": "PMID:33601000",
+          "snippet": "TNF-α activated the nuclear factor-κB (NF-κB) pathway, as confirmed by IκB-α degradation, and phosphorylation and nuclear migration of NF-κB p65.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "TNF-α directly activates NF-κB signaling (GO:0038061 NIK/NF-κB signaling), as shown by IκB-α degradation and NF-κB p65 nuclear translocation upon TNF-α stimulation.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Myricetin inhibits TNF-α-induced inflammation in A549 cells via the SIRT1/NF-κB pathway.",
+            "authors": [
+              "Chen M",
+              "Chen Z",
+              "Huang D",
+              "Sun C",
+              "Xie J",
+              "Chen T",
+              "Zhao X",
+              "Huang Y",
+              "Li D",
+              "Wu B",
+              "Wu D"
+            ],
+            "journal": "Pulmonary pharmacology & therapeutics",
+            "year": "2020",
+            "doi": "10.1016/j.pupt.2021.102000",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "GO:0038061",
+      "target": "GO:0006954",
+      "evidence": [
+        {
+          "reference": "PMID:42148126",
+          "snippet": "NF-κB signalling mediates intestinal inflammatory responses at different levels including cytokine secretion, inflammasome signalling, the recruiting of immune cells and antibody production.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "NF-κB signaling positively regulates the inflammatory response by driving cytokine secretion, inflammasome activation, and immune cell recruitment in the intestinal mucosa.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "All roads lead to NF-κB: the NF-κB pathway as a major target for intestinal inflammatory disorders.",
+            "authors": [
+              "Khasanov R",
+              "Boettcher M",
+              "Wessel LM",
+              "Schäfer KH",
+              "Tapia-Laliena MÁ"
+            ],
+            "journal": "Frontiers in immunology",
+            "year": "2026",
+            "doi": "10.3389/fimmu.2026.1816653",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "contributes to",
+      "source": "GO:0006954",
+      "target": "MESH:D003424",
+      "evidence": [
+        {
+          "reference": "PMID:42148126",
+          "snippet": "a dysregulated NF-κB signalling appears often in multiple chronic intestinal inflammatory conditions, such as Crohn's Disease (CD) and Ulcerative Colitis (UC), Celiac Disease (CeD) or microscopic colitis.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Chronic intestinal inflammatory response, driven by dysregulated NF-κB signaling, is a hallmark of Crohn's disease, establishing the inflammatory response as a contributor to CD pathogenesis.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "All roads lead to NF-κB: the NF-κB pathway as a major target for intestinal inflammatory disorders.",
+            "authors": [
+              "Khasanov R",
+              "Boettcher M",
+              "Wessel LM",
+              "Schäfer KH",
+              "Tapia-Laliena MÁ"
+            ],
+            "journal": "Frontiers in immunology",
+            "year": "2026",
+            "doi": "10.3389/fimmu.2026.1816653",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00065#mechanism-of-action",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    },
+    {
+      "url": "https://www.uniprot.org/uniprot/P01375#function",
+      "type": "other",
+      "label": "uniprot.org — record source"
+    }
+  ],
+  "site": {
+    "id": "phase3__P22",
+    "record_id": "P22_DB00065_MESH_D003424",
+    "run": "phase3",
+    "run_label": "Phase-3 eval",
+    "source_file": "tests/phase3_eval_outputs/P22.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/phase3__P23.json b/web-revamp-mockup/data/records/phase3__P23.json
new file mode 100644
index 0000000..323077f
--- /dev/null
+++ b/web-revamp-mockup/data/records/phase3__P23.json
@@ -0,0 +1,272 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P23_DB01611_MESH_D008180",
+    "drug": "Hydroxychloroquine",
+    "drug_mesh": "MESH:D006886",
+    "drugbank": "DB:DB01611",
+    "disease": "Systemic Lupus Erythematosus",
+    "disease_mesh": "MESH:D008180",
+    "summary": "Hydroxychloroquine → Toll-like receptor 9 → type I interferon production → Systemic Lupus Erythematosus"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D006886",
+      "name": "Hydroxychloroquine",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:Q9NR96",
+      "name": "Toll-like receptor 9",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0032606",
+      "name": "type I interferon production",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D008180",
+      "name": "Systemic Lupus Erythematosus",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D006886",
+      "target": "UniProt:Q9NR96",
+      "evidence": [
+        {
+          "reference": "PMID:24342772",
+          "snippet": "Our data also confirm an earlier report that this same mechanism may explain inhibition of TLR7 and 9 signaling by hydroxychloroquine",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Lamphier et al. confirm that hydroxychloroquine inhibits TLR7 and TLR9 signaling via accumulation in intracellular acidic compartments, the same mechanism as the novel small-molecule inhibitors studied.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Novel small molecule inhibitors of TLR7 and TLR9: mechanism of action and efficacy in vivo.",
+            "authors": [
+              "Lamphier M",
+              "Zheng W",
+              "Latz E",
+              "Spyvee M",
+              "Hansen H",
+              "Rose J",
+              "Genest M",
+              "Yang H",
+              "Shaffer C",
+              "Zhao Y",
+              "Shen Y",
+              "Liu C",
+              "Liu D",
+              "Mempel TR",
+              "Rowbottom C",
+              "Chow J",
+              "Twine NC",
+              "Yu M",
+              "Gusovsky F",
+              "Ishizaka ST"
+            ],
+            "journal": "Molecular pharmacology",
+            "year": "2014",
+            "doi": "10.1124/mol.113.089821",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:30846987",
+          "snippet": "clinically-relevant HCQ concentrations partially inhibit the pDC response to TLR9",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Gardet et al. show that blood HCQ levels in CLE patients correlate with reduced ex vivo pDC response to the TLR9 agonist CpG-A, confirming HCQ decreases TLR9 signaling activity in human clinical samples.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Effect of in vivo Hydroxychloroquine and ex vivo Anti-BDCA2 mAb Treatment on pDC IFNα Production From Patients Affected With Cutaneous Lupus Erythematosus.",
+            "authors": [
+              "Gardet A",
+              "Pellerin A",
+              "McCarl CA",
+              "Diwanji R",
+              "Wang W",
+              "Donaldson D",
+              "Franchimont N",
+              "Werth VP",
+              "Rabah D"
+            ],
+            "journal": "Frontiers in immunology",
+            "year": "2019",
+            "doi": "10.3389/fimmu.2019.00275",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:21448012",
+          "snippet": "antimalarials also appear to have an impact through inhibition of intracellular toll-like receptors (TLRs), particularly TLR9",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Katz and Russell review confirm that antimalarials including hydroxychloroquine act by inhibiting endosomal/intracellular TLRs, particularly TLR9.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Re-evaluation of antimalarials in treating rheumatic diseases: re-appreciation and insights into new mechanisms of action.",
+            "authors": [
+              "Katz SJ",
+              "Russell AS"
+            ],
+            "journal": "Current opinion in rheumatology",
+            "year": "2011",
+            "doi": "10.1097/BOR.0b013e32834456bf",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:Q9NR96",
+      "target": "GO:0032606",
+      "evidence": [
+        {
+          "reference": "PMID:30846987",
+          "snippet": "PDCs were the only producers of IFNα in response to CpG-A, R848, and ssRNA stimulation in PBMC cultures.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "CpG-A is a TLR9 agonist; that pDCs are the sole IFNα producers in response to CpG-A demonstrates that TLR9 signaling drives type I interferon (IFNα) production.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Effect of in vivo Hydroxychloroquine and ex vivo Anti-BDCA2 mAb Treatment on pDC IFNα Production From Patients Affected With Cutaneous Lupus Erythematosus.",
+            "authors": [
+              "Gardet A",
+              "Pellerin A",
+              "McCarl CA",
+              "Diwanji R",
+              "Wang W",
+              "Donaldson D",
+              "Franchimont N",
+              "Werth VP",
+              "Rabah D"
+            ],
+            "journal": "Frontiers in immunology",
+            "year": "2019",
+            "doi": "10.3389/fimmu.2019.00275",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:38914753",
+          "snippet": "IFN-I signaling is increased in pediatric SLE, largely due to the presence of plasmacytoid dendritic cells and pathways such as cyclic GMP-AMP synthase-stimulator of interferon genes-TANK-binding kinase 1 and Toll-like receptor (TLR)4/TLR9.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Zhou and Song's review identifies TLR9 as one of the primary pathways driving increased type I interferon signaling/production in SLE patients.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Type I interferon pathway in pediatric systemic lupus erythematosus.",
+            "authors": [
+              "Zhou Y",
+              "Song HM"
+            ],
+            "journal": "World journal of pediatrics : WJP",
+            "year": "2024",
+            "doi": "10.1007/s12519-024-00811-4",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "contributes to",
+      "source": "GO:0032606",
+      "target": "MESH:D008180",
+      "evidence": [
+        {
+          "reference": "PMID:30210502",
+          "snippet": "Aberrant and persistent production of interferon-α (IFN-α) by plasmacytoid dendritic cells (pDCs) is known to play a key role in the pathogenesis of systemic lupus erythematosus (SLE).",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Sakata et al. establish that aberrant type I interferon (IFNα) production is a key driver of SLE pathogenesis, confirming that the type I interferon production process contributes to SLE.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Up-Regulation of TLR7-Mediated IFN-α Production by Plasmacytoid Dendritic Cells in Patients With Systemic Lupus Erythematosus.",
+            "authors": [
+              "Sakata K",
+              "Nakayamada S",
+              "Miyazaki Y",
+              "Kubo S",
+              "Ishii A",
+              "Nakano K",
+              "Tanaka Y"
+            ],
+            "journal": "Frontiers in immunology",
+            "year": "2018",
+            "doi": "10.3389/fimmu.2018.01957",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:26953155",
+          "snippet": "nucleic acid-sensing Toll-like receptors (TLRs), and type I interferon can affect B-cell survival and decrease their threshold for activation",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Singh et al. confirm that type I interferon, produced downstream of nucleic-acid-sensing TLRs, contributes to aberrant B-cell activation that underlies SLE pathogenesis.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Interfering with baffled B cells at the lupus tollway: Promises, successes, and failed expectations.",
+            "authors": [
+              "Singh N",
+              "Kumar B",
+              "Aluri V",
+              "Lenert P"
+            ],
+            "journal": "The Journal of allergy and clinical immunology",
+            "year": "2016",
+            "doi": "10.1016/j.jaci.2015.12.1326",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB01611#mechanism-of-action",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    },
+    {
+      "url": "https://www.uniprot.org/uniprot/Q9NR96#function",
+      "type": "other",
+      "label": "uniprot.org — record source"
+    },
+    {
+      "url": "https://www.quickgo.org/term/GO:0032606",
+      "type": "other",
+      "label": "quickgo.org — record source"
+    }
+  ],
+  "site": {
+    "id": "phase3__P23",
+    "record_id": "P23_DB01611_MESH_D008180",
+    "run": "phase3",
+    "run_label": "Phase-3 eval",
+    "source_file": "tests/phase3_eval_outputs/P23.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/phase3__P24.json b/web-revamp-mockup/data/records/phase3__P24.json
new file mode 100644
index 0000000..0f98f38
--- /dev/null
+++ b/web-revamp-mockup/data/records/phase3__P24.json
@@ -0,0 +1,328 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P24_DB00688_MESH_D008181",
+    "drug": "Mycophenolate Mofetil",
+    "drug_mesh": "MESH:D000077732",
+    "drugbank": "DB:DB00688",
+    "disease": "Lupus Nephritis",
+    "disease_mesh": "MESH:D008181",
+    "summary": "Mycophenolate Mofetil → Mycophenolic acid → Inosine-5'-monophosphate dehydrogenase 2 → GMP biosynthetic process → lymphocyte proliferation → Lupus Nephritis"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D000077732",
+      "name": "Mycophenolate Mofetil",
+      "label": "Drug"
+    },
+    {
+      "id": "CHEBI:168618",
+      "name": "Mycophenolic acid",
+      "label": "ChemicalSubstance"
+    },
+    {
+      "id": "UniProt:P12268",
+      "name": "Inosine-5'-monophosphate dehydrogenase 2",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0006177",
+      "name": "GMP biosynthetic process",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "GO:0046651",
+      "name": "lymphocyte proliferation",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D008181",
+      "name": "Lupus Nephritis",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "has metabolite",
+      "source": "MESH:D000077732",
+      "target": "CHEBI:168618",
+      "evidence": [
+        {
+          "reference": "PMID:20823294",
+          "snippet": "Mycophenolate mofetil (MMF) is the ester prodrug of the immunosuppressant agent mycophenolic acid (MPA) and is rapidly activated by esterases after oral administration.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Confirms MMF is a prodrug of MPA, hydrolyzed by esterases to release the active metabolite MPA.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Involvement of carboxylesterase 1 and 2 in the hydrolysis of mycophenolate mofetil.",
+            "authors": [
+              "Fujiyama N",
+              "Miura M",
+              "Kato S",
+              "Sone T",
+              "Isobe M",
+              "Satoh S"
+            ],
+            "journal": "Drug metabolism and disposition: the biological fate of chemicals",
+            "year": "2010",
+            "doi": "10.1124/dmd.110.034249",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "CHEBI:168618",
+      "target": "UniProt:P12268",
+      "evidence": [
+        {
+          "reference": "PMID:19834629",
+          "snippet": "Mycophenolic acid (MPA) is a potent, selective, noncompetitive and reversible inhibitor of inosine-5'-monophosphate deshydrogenase (IMPDH).",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "MPA directly and selectively inhibits IMPDH2, decreasing its enzymatic activity.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Mycophenolate mofetil: An update.",
+            "authors": [
+              "Villarroel MC",
+              "Hidalgo M",
+              "Jimeno A"
+            ],
+            "journal": "Drugs of today (Barcelona, Spain : 1998)",
+            "year": "2009",
+            "doi": "10.1358/dot.2009.45.7.1384878",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:40142133",
+          "snippet": "MPA effectively inhibited IMPDH activity in a dose-dependent manner, with 94-96% inhibition at concentrations of 100 μM and above.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "In vitro demonstration of MPA dose-dependently inhibiting IMPDH activity, supporting decreases activity of edge.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Combination Effects of Aminolevulinic Acid and Mycophenolic Acid on Hacat Cell Proliferation and Inhibition of Inosine Monophosphate Dehydrogenase.",
+            "authors": [
+              "Venkatesh M",
+              "Capriglione N",
+              "Rehberg K",
+              "Voigt J",
+              "Hass MA"
+            ],
+            "journal": "Molecules (Basel, Switzerland)",
+            "year": "2025",
+            "doi": "10.3390/molecules30061359",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P12268",
+      "target": "GO:0006177",
+      "evidence": [
+        {
+          "reference": "PMID:12944494",
+          "snippet": "Inosine 5'-monophosphate dehydrogenase (IMPDH) is the critical, rate-limiting enzyme in the de novo biosynthesis pathway for guanine nucleotides.",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "explanation": "IMPDH is the rate-limiting enzyme for de novo guanine nucleotide (GMP) biosynthesis; its activity positively regulates the GMP biosynthetic process.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Targeted disruption of the inosine 5'-monophosphate dehydrogenase type I gene in mice.",
+            "authors": [
+              "Gu JJ",
+              "Tolin AK",
+              "Jain J",
+              "Huang H",
+              "Santiago L",
+              "Mitchell BS"
+            ],
+            "journal": "Molecular and cellular biology",
+            "year": "2003",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:19753127",
+          "snippet": "Mycophenolic acid (MPA) blocks the key enzyme inosine monophosphate dehydrogenase and the production of guanosine nucleotides required for DNA synthesis.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Blocking IMPDH prevents guanosine nucleotide production, confirming IMPDH positively regulates GMP biosynthesis.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Mycophenolic acid formulations in adult renal transplantation - update on efficacy and tolerability.",
+            "authors": [
+              "Golshayan D",
+              "Pascual M",
+              "Vogt B"
+            ],
+            "journal": "Therapeutics and clinical risk management",
+            "year": "2009",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "GO:0006177",
+      "target": "GO:0046651",
+      "evidence": [
+        {
+          "reference": "PMID:16051207",
+          "snippet": "The mechanism of action of mycophenolic acid (MPA) has been described as a blockade of inosine 5'-monophosphate dehydrogenase (IMPDH) and is thought to selectively influence T- and B-lymphocytes due to their strong dependency on guanine nucleotides synthesized via the de novo purine synthesis pathway.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "T and B lymphocytes depend on the de novo guanine nucleotide synthesis pathway for proliferation; GMP biosynthesis positively regulates lymphocyte proliferation.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Inosine 5'-monophosphate dehydrogenase inhibition by mycophenolic acid impairs maturation and function of dendritic cells.",
+            "authors": [
+              "Dubsky PC",
+              "Friedl J",
+              "Stift A",
+              "Bachleitner-Hofmann T",
+              "Jakesz R",
+              "Gnant MF",
+              "Weigel G"
+            ],
+            "journal": "Clinica chimica acta; international journal of clinical chemistry",
+            "year": "2006",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:19753127",
+          "snippet": "The description more than 30 years ago of the role of de novo purine synthesis in T and B lymphocytes clonal proliferation opened the possibility for selective immunosuppression by targeting specific enzymatic pathways.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "De novo purine (guanosine) synthesis is required for T and B lymphocyte clonal proliferation, supporting that GMP biosynthesis positively regulates lymphocyte proliferation.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Mycophenolic acid formulations in adult renal transplantation - update on efficacy and tolerability.",
+            "authors": [
+              "Golshayan D",
+              "Pascual M",
+              "Vogt B"
+            ],
+            "journal": "Therapeutics and clinical risk management",
+            "year": "2009",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "contributes to",
+      "source": "GO:0046651",
+      "target": "MESH:D008181",
+      "evidence": [
+        {
+          "reference": "PMID:22571761",
+          "snippet": "The thorough inhibition of B cell activation and plasma cell formation by MMF might explain the favorable outcomes of previous clinical trials in patients with SLE, since enhanced B cell proliferation is a hallmark of this disease.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Enhanced B cell proliferation is a hallmark of SLE/lupus nephritis; inhibiting it with MMF leads to favorable clinical outcomes, confirming lymphocyte proliferation contributes to lupus nephritis.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Mycophenolic acid counteracts B cell proliferation and plasmablast formation in patients with systemic lupus erythematosus.",
+            "authors": [
+              "Eickenberg S",
+              "Mickholz E",
+              "Jung E",
+              "Nofer JR",
+              "Pavenstadt HJ",
+              "Jacobi AM"
+            ],
+            "journal": "Arthritis research & therapy",
+            "year": "2012",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:21187439",
+          "snippet": "The most prevalent severe manifestation of systemic lupus erythematosus is nephritis, which is characterized by immune complex deposition, inflammation, and scarring in glomeruli and the tubulointerstitium.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Lupus nephritis is the most prevalent severe manifestation of SLE, driven by immune complex deposition from dysregulated lymphocyte activity.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "In situ B cell-mediated immune responses and tubulointerstitial inflammation in human lupus nephritis.",
+            "authors": [
+              "Chang A",
+              "Henderson SG",
+              "Brandt D",
+              "Liu N",
+              "Guttikonda R",
+              "Hsieh C",
+              "Kaverina N",
+              "Utset TO",
+              "Meehan SM",
+              "Quigg RJ",
+              "Meffre E",
+              "Clark MR"
+            ],
+            "journal": "Journal of immunology (Baltimore, Md. : 1950)",
+            "year": "2011",
+            "doi": "10.4049/jimmunol.1001983",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00688#mechanism-of-action",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    },
+    {
+      "url": "https://www.uniprot.org/uniprot/P12268",
+      "type": "other",
+      "label": "uniprot.org — record source"
+    }
+  ],
+  "site": {
+    "id": "phase3__P24",
+    "record_id": "P24_DB00688_MESH_D008181",
+    "run": "phase3",
+    "run_label": "Phase-3 eval",
+    "source_file": "tests/phase3_eval_outputs/P24.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/phase3__P25.json b/web-revamp-mockup/data/records/phase3__P25.json
new file mode 100644
index 0000000..b2f2e4d
--- /dev/null
+++ b/web-revamp-mockup/data/records/phase3__P25.json
@@ -0,0 +1,305 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P25_DB00051_MESH_D011565",
+    "drug": "Adalimumab",
+    "drug_mesh": "MESH:D000068879",
+    "drugbank": "DB:DB00051",
+    "disease": "Psoriasis",
+    "disease_mesh": "MESH:D011565",
+    "summary": "Adalimumab → Tumor necrosis factor → NIK/NF-kappaB signaling → Inflammatory response → Psoriasis"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D000068879",
+      "name": "Adalimumab",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P01375",
+      "name": "Tumor necrosis factor",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0038061",
+      "name": "NIK/NF-kappaB signaling",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "GO:0006954",
+      "name": "Inflammatory response",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D011565",
+      "name": "Psoriasis",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D000068879",
+      "target": "UniProt:P01375",
+      "evidence": [
+        {
+          "reference": "PMID:15046527",
+          "snippet": "Adalimumab (Humira) is a recombinant, fully human IgG1 monoclonal antibody that binds specifically to tumor necrosis factor (TNF)-alpha, thereby neutralizing the activity of the cytokine.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Pharmacology review confirming adalimumab binds TNF-alpha and neutralizes the cytokine's biological activity, directly decreasing its function.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Adalimumab: a review of its use in rheumatoid arthritis.",
+            "authors": [
+              "Bang LM",
+              "Keating GM"
+            ],
+            "journal": "BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy",
+            "year": "2004",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:17223742",
+          "snippet": "Adalimumab is a fully human monoclonal antibody that binds specifically to TNF-alpha, thereby neutralising its activity.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Expert review confirming adalimumab is a fully human anti-TNF-alpha monoclonal antibody that neutralizes TNF-alpha activity.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Adalimumab for rheumatoid arthritis.",
+            "authors": [
+              "Voulgari PV",
+              "Drosos AA"
+            ],
+            "journal": "Expert opinion on biological therapy",
+            "year": "2006",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P01375",
+      "target": "GO:0038061",
+      "evidence": [
+        {
+          "reference": "PMID:34362923",
+          "snippet": "Enhanced NF-κBp65 phosphorylation, induced by TNF and LPS in type-2 dendritic cells (DC) before therapy, significantly correlates with lack of clinical response after 12 weeks of treatment.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "TNF induces NF-κBp65 phosphorylation (activation of NIK/NF-kappaB signaling) in immune cells; this is established in psoriasis patients prior to adalimumab therapy.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Enhanced NF-κB signaling in type-2 dendritic cells at baseline predicts non-response to adalimumab in psoriasis.",
+            "authors": [
+              "Andres-Ejarque R",
+              "Ale HB",
+              "Grys K",
+              "Tosi I",
+              "Solanky S",
+              "Ainali C",
+              "Catak Z",
+              "Sreeneebus H",
+              "Saklatvala J",
+              "Dand N",
+              "de Rinaldis E",
+              "Chapman A",
+              "Nestle FO",
+              "Barnes MR",
+              "Warren RB",
+              "Reynolds NJ",
+              "Griffiths CEM",
+              "Barker JN",
+              "Smith CH",
+              "Di Meglio P",
+              "PSORT Consortium"
+            ],
+            "journal": "Nature communications",
+            "year": "2021",
+            "doi": "10.1038/s41467-021-25066-9",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:30321197",
+          "snippet": "suggesting that rhodomyrtone acts by modulating MAP kinase and NF-κB signaling pathways, rhodomyrtone inhibited TNF-induced ERK, JNK, p38, and NF-κBp65 phosphorylation.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "TNF induces NF-κBp65 phosphorylation in keratinocytes, demonstrating that TNF-alpha positively regulates NIK/NF-kappaB signaling in psoriasis-relevant cells.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "The small molecule rhodomyrtone suppresses TNF-α and IL-17A-induced keratinocyte inflammatory responses: A potential new therapeutic for psoriasis.",
+            "authors": [
+              "Chorachoo J",
+              "Lambert S",
+              "Furnholm T",
+              "Roberts L",
+              "Reingold L",
+              "Auepemkiate S",
+              "Voravuthikunchai SP",
+              "Johnston A"
+            ],
+            "journal": "PloS one",
+            "year": "2018",
+            "doi": "10.1371/journal.pone.0205340",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "GO:0038061",
+      "target": "GO:0006954",
+      "evidence": [
+        {
+          "reference": "PMID:36903321",
+          "snippet": "acenocoumarol attenuates the macrophage secretion of TNF-α, IL-6, IL-1β, and NO, inducing iNOS and COX-2 expression via the inhibition of the NF-κB and MAPK signaling pathways.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "NF-κB signaling drives secretion of pro-inflammatory cytokines (TNF-α, IL-6, IL-1β) and mediators (iNOS, COX-2), confirming NF-kappaB positively regulates the inflammatory response.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Acenocoumarol Exerts Anti-Inflammatory Activity via the Suppression of NF-κB and MAPK Pathways in RAW 264.7 Cells.",
+            "authors": [
+              "Han HJ",
+              "Hyun CG"
+            ],
+            "journal": "Molecules (Basel, Switzerland)",
+            "year": "2023",
+            "doi": "10.3390/molecules28052075",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:34929480",
+          "snippet": "POH significantly decreased the intracellular ROS levels and inhibited the phosphorylation of NF-κB and STAT3 in in-vitro.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Inhibiting NF-κB phosphorylation in keratinocytes reduces pro-inflammatory cytokines (TNF-α, IL-6, IL-1β) and inflammatory proteins, confirming NF-κB positively drives the inflammatory response in psoriasis.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Perillyl alcohol inhibits keratinocyte proliferation and attenuates imiquimod-induced psoriasis like skin-inflammation by modulating NF-κB and STAT3 signaling pathways.",
+            "authors": [
+              "Sudha Yalamarthi S",
+              "Puppala ER",
+              "Abubakar M",
+              "Saha P",
+              "Challa VS",
+              "Np S",
+              "Usn M",
+              "Gangasani JK",
+              "Naidu VGM"
+            ],
+            "journal": "International immunopharmacology",
+            "year": "2022",
+            "doi": "10.1016/j.intimp.2021.108436",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "causes",
+      "source": "GO:0006954",
+      "target": "MESH:D011565",
+      "evidence": [
+        {
+          "reference": "PMID:40243475",
+          "snippet": "Psoriasis is a chronic immune-mediated skin disease characterized by cytokine dysregulation. Pro-inflammatory mediators, including tumor necrosis factor-alpha (TNF-α), interleukin (IL)-17, and IL-23, play pivotal roles in the pathogenesis of psoriasis.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Psoriasis is defined by a chronic inflammatory response driven by pro-inflammatory mediators; the inflammatory response is the direct pathological driver (cause) of the disease.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Targeting Cytokine Dysregulation in Psoriasis: The Role of Dietary Interventions in Modulating the Immune Response.",
+            "authors": [
+              "Simancas-Racines D",
+              "Román-Galeano NM",
+              "Verde L",
+              "Annunziata G",
+              "Marchetti M",
+              "Matos A",
+              "Campuzano-Donoso M",
+              "Reytor-González C",
+              "Muscogiuri G",
+              "Barrea L",
+              "Frias-Toral E"
+            ],
+            "journal": "International journal of molecular sciences",
+            "year": "2025",
+            "doi": "10.3390/ijms26072895",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:41196583",
+          "snippet": "Psoriasis is characterized by increased levels of pro-inflammatory cytokines, including TNF-α, IL-1β, IL-17A, and NF-κB, as well as keratinocyte hyperproliferation and epidermal thickening.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Psoriasis is characterized by a state of elevated pro-inflammatory cytokines (hallmarks of inflammatory response) alongside the resulting keratinocyte hyperproliferation, confirming the inflammatory response causes psoriasis.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Exploring the therapeutic potential of syringaldehyde in imiquimod-induced psoriasis model in mice via NF-κB pathway inhibition.",
+            "authors": [
+              "Gosia M",
+              "Godad A",
+              "Pahelkar A",
+              "Doshi G"
+            ],
+            "journal": "Journal of immunoassay & immunochemistry",
+            "year": "2026",
+            "doi": "10.1080/15321819.2025.2584190",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00051#mechanism-of-action",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    },
+    {
+      "url": "https://www.uniprot.org/uniprot/P01375#function",
+      "type": "other",
+      "label": "uniprot.org — record source"
+    }
+  ],
+  "site": {
+    "id": "phase3__P25",
+    "record_id": "P25_DB00051_MESH_D011565",
+    "run": "phase3",
+    "run_label": "Phase-3 eval",
+    "source_file": "tests/phase3_eval_outputs/P25.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/phase3__P26.json b/web-revamp-mockup/data/records/phase3__P26.json
new file mode 100644
index 0000000..9b30c85
--- /dev/null
+++ b/web-revamp-mockup/data/records/phase3__P26.json
@@ -0,0 +1,268 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P26_DB00331_MESH_D003924",
+    "drug": "Metformin",
+    "drug_mesh": "MESH:D008687",
+    "drugbank": "DB:DB00331",
+    "disease": "Diabetes mellitus type 2",
+    "disease_mesh": "MESH:D003924",
+    "summary": "Metformin → 5'-AMP-activated protein kinase catalytic subunit alpha-1 → gluconeogenesis → Hyperglycemia → Diabetes mellitus type 2"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D008687",
+      "name": "Metformin",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:Q13131",
+      "name": "5'-AMP-activated protein kinase catalytic subunit alpha-1",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0006094",
+      "name": "gluconeogenesis",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "HP:0003074",
+      "name": "Hyperglycemia",
+      "label": "PhenotypicFeature"
+    },
+    {
+      "id": "MESH:D003924",
+      "name": "Diabetes mellitus type 2",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "increased",
+      "source": "MESH:D008687",
+      "target": "UniProt:Q13131",
+      "evidence": [
+        {
+          "reference": "PMID:31693892",
+          "snippet": "activation of AMPK by metformin improves mitochondrial respiration and hyperglycemia in obesity",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "explanation": "Metformin activates AMPK (whose α1 catalytic subunit is encoded by PRKAA1/UniProt:Q13131) in hepatocytes and in vivo, demonstrated by knockout of AMPKα1/2 abolishing metformin's glucose-lowering effect.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Metformin Improves Mitochondrial Respiratory Activity through Activation of AMPK.",
+            "authors": [
+              "Wang Y",
+              "An H",
+              "Liu T",
+              "Qin C",
+              "Sesaki H",
+              "Guo S",
+              "Radovick S",
+              "Hussain M",
+              "Maheshwari A",
+              "Wondisford FE",
+              "O'Rourke B",
+              "He L"
+            ],
+            "journal": "Cell reports",
+            "year": "2019",
+            "doi": "10.1016/j.celrep.2019.09.070",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:41819225",
+          "snippet": "raise cytosolic AMP and activate AMP-activated protein kinase (AMPK)",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Comprehensive review confirming that metformin raises cytosolic AMP, which activates AMPK (including the PRKAA1-containing heterotrimeric complex).",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Metformin: Antidiabetic actions from cells to tissues.",
+            "authors": [
+              "Bailey CJ",
+              "Gwilt M",
+              "Brand KMG"
+            ],
+            "journal": "Metabolism: clinical and experimental",
+            "year": "2026",
+            "doi": "10.1016/j.metabol.2026.156589",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "decreased",
+      "source": "UniProt:Q13131",
+      "target": "GO:0006094",
+      "evidence": [
+        {
+          "reference": "PMID:41924526",
+          "snippet": "activating the hepatic AMP-activated protein kinase (AMPK) pathway, thus suppressing hepatic gluconeogenesis",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "explanation": "AMPK activation (via the PRKAA1 catalytic subunit) suppresses hepatic gluconeogenesis, directly supporting the negatively regulates edge.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Mechanistic insights of hypoglycemic components from Polygonatum polysaccharide.",
+            "authors": [
+              "Ren Z",
+              "Chen S",
+              "Guo Z",
+              "Mei X",
+              "Tong Y",
+              "Liu Y",
+              "Gao Z",
+              "Chen X",
+              "Dai G"
+            ],
+            "journal": "Frontiers in endocrinology",
+            "year": "2026",
+            "doi": "10.3389/fendo.2026.1744730",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:36637190",
+          "snippet": "the main effect of AMPK activation pertinent to the control of hepatic gluconeogenesis is to antagonize glucagon signalling in the short-term",
+          "supports": "PARTIAL",
+          "evidence_source": "OTHER",
+          "explanation": "Review concludes AMPK activation's primary gluconeogenesis-relevant effect is antagonizing glucagon signalling; supports the directionality but notes the mechanism is indirect (via signalling cross-talk rather than direct transcriptional suppression).",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "AMPK inhibits liver gluconeogenesis: fact or fiction?",
+            "authors": [
+              "Johanns M",
+              "Hue L",
+              "Rider MH"
+            ],
+            "journal": "The Biochemical journal",
+            "year": "2023",
+            "doi": "10.1042/BCJ20220582",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "positively correlated with",
+      "source": "GO:0006094",
+      "target": "HP:0003074",
+      "evidence": [
+        {
+          "reference": "PMID:41819225",
+          "snippet": "It counters the effects of insulin resistance, improves glucose homeostasis, assists weight control and avoids overt hypoglycemia via reduced hepatic gluconeogenesis",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Reducing hepatic gluconeogenesis is a primary means by which metformin avoids hyperglycemia, establishing that elevated gluconeogenesis is positively correlated with hyperglycemia.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Metformin: Antidiabetic actions from cells to tissues.",
+            "authors": [
+              "Bailey CJ",
+              "Gwilt M",
+              "Brand KMG"
+            ],
+            "journal": "Metabolism: clinical and experimental",
+            "year": "2026",
+            "doi": "10.1016/j.metabol.2026.156589",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:41924526",
+          "snippet": "PP III administration significantly reduced hyperglycemia while enhancing insulin sensitivity. Transcriptomic sequencing analysis showed that PP III's mechanism involves gut microbiota-mediated short-chain fatty acid production (notably acetic acid and propionic acid), subsequently inhibiting hepatic gluconeogenesis.",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "explanation": "Inhibiting hepatic gluconeogenesis reduces hyperglycemia in db/db mice, establishing the positive correlation between gluconeogenesis activity and hyperglycemia.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Mechanistic insights of hypoglycemic components from Polygonatum polysaccharide.",
+            "authors": [
+              "Ren Z",
+              "Chen S",
+              "Guo Z",
+              "Mei X",
+              "Tong Y",
+              "Liu Y",
+              "Gao Z",
+              "Chen X",
+              "Dai G"
+            ],
+            "journal": "Frontiers in endocrinology",
+            "year": "2026",
+            "doi": "10.3389/fendo.2026.1744730",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "manifestation of",
+      "source": "HP:0003074",
+      "target": "MESH:D003924",
+      "evidence": [
+        {
+          "reference": "PMID:41819225",
+          "snippet": "Metformin (dimethyl biguanide) is a primary pharmacotherapy to treat hyperglycemia in type 2 diabetes.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Hyperglycemia is the defining metabolic manifestation of type 2 diabetes; metformin is prescribed specifically to reduce it.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Metformin: Antidiabetic actions from cells to tissues.",
+            "authors": [
+              "Bailey CJ",
+              "Gwilt M",
+              "Brand KMG"
+            ],
+            "journal": "Metabolism: clinical and experimental",
+            "year": "2026",
+            "doi": "10.1016/j.metabol.2026.156589",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00331#mechanism-of-action",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    },
+    {
+      "url": "https://www.uniprot.org/uniprot/Q13131",
+      "type": "other",
+      "label": "uniprot.org — record source"
+    }
+  ],
+  "site": {
+    "id": "phase3__P26",
+    "record_id": "P26_DB00331_MESH_D003924",
+    "run": "phase3",
+    "run_label": "Phase-3 eval",
+    "source_file": "tests/phase3_eval_outputs/P26.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/phase3__P27.json b/web-revamp-mockup/data/records/phase3__P27.json
new file mode 100644
index 0000000..3f03d09
--- /dev/null
+++ b/web-revamp-mockup/data/records/phase3__P27.json
@@ -0,0 +1,233 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P27_DB00030_MESH_D003922",
+    "drug": "Insulin Human",
+    "drug_mesh": "MESH:D007328",
+    "drugbank": "DB:DB00030",
+    "disease": "Diabetes mellitus type 1",
+    "disease_mesh": "MESH:D003922",
+    "summary": "Insulin Human → Insulin receptor → glucose import → Hyperglycemia → Diabetes mellitus type 1"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D007328",
+      "name": "Insulin Human",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P06213",
+      "name": "Insulin receptor",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0046323",
+      "name": "glucose import",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "HP:0003074",
+      "name": "Hyperglycemia",
+      "label": "PhenotypicFeature"
+    },
+    {
+      "id": "MESH:D003922",
+      "name": "Diabetes mellitus type 1",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "directly physically interacts with",
+      "source": "MESH:D007328",
+      "target": "UniProt:P06213",
+      "evidence": [
+        {
+          "reference": "PMID:28677502",
+          "snippet": "Its binding to insulin receptor on the surface of diverse cells allows glucose entry into cells, and activates a variety of cellular actions.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Insulin binds directly to the insulin receptor (INSR/UniProt:P06213) on cell surfaces; this molecular interaction is the initiating event of the insulin signalling cascade that lowers blood glucose.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "PTEN, Insulin Resistance and Cancer.",
+            "authors": [
+              "Li A",
+              "Qiu M",
+              "Zhou H",
+              "Wang T",
+              "Guo W"
+            ],
+            "journal": "Current pharmaceutical design",
+            "year": "2017",
+            "doi": "10.2174/1381612823666170704124611",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P06213",
+      "target": "GO:0046323",
+      "evidence": [
+        {
+          "reference": "PMID:37778516",
+          "snippet": "activated the insulin receptor substrate 1 (IRS1)/phosphatidylinositol 3-kinase (PI3K)/protein kinase B (AKT) signaling pathway, and enhanced the translocation of glucose transporter type 4 (GLUT4) and glucose uptake in adipocytes treated with palmitic acid.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Insulin receptor activation triggers the IRS1/PI3K/AKT cascade that drives GLUT4 translocation to the plasma membrane, thereby positively regulating glucose import (GO:0046323) into insulin-sensitive cells.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Esculin ameliorates obesity-induced insulin resistance by improving adipose tissue remodeling and activating the IRS1/PI3K/AKT/GLUT4 pathway.",
+            "authors": [
+              "Yang YY",
+              "Qi JJ",
+              "Jiang SY",
+              "Ye L"
+            ],
+            "journal": "Journal of ethnopharmacology",
+            "year": "2024",
+            "doi": "10.1016/j.jep.2023.117251",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:29686650",
+          "snippet": "impairments in the phosphoinositide 3-kinase (PI3K)/AKT signaling pathway, or perturbations in the trafficking of glucose transporters (GLUTs), which mediate the uptake of glucose into cells.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "The PI3K/AKT pathway downstream of INSR controls GLUT trafficking and glucose uptake into cells; disruption of this pathway impairs glucose import, confirming INSR positively regulates GO:0046323.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Glucose Transporters in Diabetic Kidney Disease-Friends or Foes?",
+            "authors": [
+              "Wasik AA",
+              "Lehtonen S"
+            ],
+            "journal": "Frontiers in endocrinology",
+            "year": "2018",
+            "doi": "10.3389/fendo.2018.00155",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "negatively correlated with",
+      "source": "GO:0046323",
+      "target": "HP:0003074",
+      "evidence": [
+        {
+          "reference": "PMID:42130086",
+          "snippet": "promoted glucose uptake in the liver and skeletal muscle, and upregulated hepatic Ghr and Igf1 levels to facilitate glucose homeostasis.",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "explanation": "Promoting cellular glucose import in liver and muscle facilitates glucose homeostasis, the inverse of hyperglycemia; the same study showed that this effect alleviated hyperglycemia in insulin-deficient models, confirming that glucose import (GO:0046323) is negatively correlated with hyperglycemia (HP:0003074).",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "The novel adipokine Placin regulates glucose homeostasis via insulin secretion and IGF1 receptor signaling.",
+            "authors": [
+              "Lo TH",
+              "Chan KY",
+              "Chen D",
+              "Deng CJ",
+              "Ting-Yuan Yeh S",
+              "Wu M",
+              "Cai Y",
+              "Xu A",
+              "Wong CM"
+            ],
+            "journal": "Molecular therapy : the journal of the American Society of Gene Therapy",
+            "year": "2026",
+            "doi": "10.1016/j.ymthe.2026.05.006",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "manifestation of",
+      "source": "HP:0003074",
+      "target": "MESH:D003922",
+      "evidence": [
+        {
+          "reference": "PMID:31378283",
+          "snippet": "In T1DM, the destruction of pancreatic β-cells leads to reduced insulin production or even absolute insulin deficiency, which consequently results in hyperglycemia.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Hyperglycemia is directly caused by the insulin deficiency that results from autoimmune beta-cell destruction in T1DM; it is therefore a manifestation of the disease.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Molecular imaging of β-cells: diabetes and beyond.",
+            "authors": [
+              "Wei W",
+              "Ehlerding EB",
+              "Lan X",
+              "Luo QY",
+              "Cai W"
+            ],
+            "journal": "Advanced drug delivery reviews",
+            "year": "2019",
+            "doi": "10.1016/j.addr.2018.06.022",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:27558810",
+          "snippet": "The autoimmune process leads to a deficiency in insulin production and resultant hyperglycemia requiring lifelong treatment with insulin administration.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "This clinical review confirms that hyperglycemia is a direct manifestation of T1DM caused by autoimmune insulin deficiency, and that insulin administration is the required treatment.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Immune Intervention and Preservation of Pancreatic Beta Cell Function in Type 1 Diabetes.",
+            "authors": [
+              "Simmons KM",
+              "Gottlieb PA",
+              "Michels AW"
+            ],
+            "journal": "Current diabetes reports",
+            "year": "2016",
+            "doi": "10.1007/s11892-016-0793-8",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00030#mechanism-of-action",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    },
+    {
+      "url": "https://www.uniprot.org/uniprot/P06213#function",
+      "type": "other",
+      "label": "uniprot.org — record source"
+    }
+  ],
+  "site": {
+    "id": "phase3__P27",
+    "record_id": "P27_DB00030_MESH_D003922",
+    "run": "phase3",
+    "run_label": "Phase-3 eval",
+    "source_file": "tests/phase3_eval_outputs/P27.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/phase3__P28.json b/web-revamp-mockup/data/records/phase3__P28.json
new file mode 100644
index 0000000..4f2d14d
--- /dev/null
+++ b/web-revamp-mockup/data/records/phase3__P28.json
@@ -0,0 +1,278 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P28_DB00451_MESH_D007037",
+    "drug": "Levothyroxine",
+    "drug_mesh": "MESH:D013974",
+    "drugbank": "DB:DB00451",
+    "disease": "Hypothyroidism",
+    "disease_mesh": "MESH:D007037",
+    "summary": "Levothyroxine → Triiodothyronine → Thyroid hormone receptor beta → Thyroid hormone mediated signaling pathway → Hypothyroidism"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D013974",
+      "name": "Levothyroxine",
+      "label": "Drug"
+    },
+    {
+      "id": "MESH:D014284",
+      "name": "Triiodothyronine",
+      "label": "ChemicalSubstance"
+    },
+    {
+      "id": "UniProt:P10828",
+      "name": "Thyroid hormone receptor beta",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0002154",
+      "name": "Thyroid hormone mediated signaling pathway",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D007037",
+      "name": "Hypothyroidism",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "has metabolite",
+      "source": "MESH:D013974",
+      "target": "MESH:D014284",
+      "evidence": [
+        {
+          "reference": "PMID:21292729",
+          "snippet": "The thyroid gland predominantly secretes the pro-hormone thyroxine (T(4)) that is converted to the active hormone 3,5,3'-l-triiodothyronine (T(3)) in target cells.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Levothyroxine is synthetic T4; upon administration it is converted to the active metabolite T3 by tissue deiodinases, establishing T3 as its active metabolite.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Deiodinases: the balance of thyroid hormone: local control of thyroid hormone action: role of type 2 deiodinase.",
+            "authors": [
+              "Williams GR",
+              "Bassett JH"
+            ],
+            "journal": "The Journal of endocrinology",
+            "year": "2011",
+            "doi": "10.1530/JOE-10-0448",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:23883148",
+          "snippet": "The monodeiodination of T4 to 3,3',5-triiodothyronine (T3) by selenium-containing deiodinases (ID-1, ID-2) is a key step in the activation of thyroid hormones.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Deiodination of T4 to T3 is the key activation step; administered levothyroxine (T4) is therefore a prodrug whose active form is T3.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Antithyroid drugs and their analogues: synthesis, structure, and mechanism of action.",
+            "authors": [
+              "Manna D",
+              "Roy G",
+              "Mugesh G"
+            ],
+            "journal": "Accounts of chemical research",
+            "year": "2013",
+            "doi": "10.1021/ar4001229",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "increased",
+      "source": "MESH:D014284",
+      "target": "UniProt:P10828",
+      "evidence": [
+        {
+          "reference": "PMID:23235186",
+          "snippet": "Thyroid hormone has to be transported into the cell, where it can bind to the thyroid hormone receptor (TR) in the nucleus to exert its effect on cellular gene-transcription.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "T3 binds nuclear thyroid hormone receptors (including TRβ/THRB) and activates them as transcription factors, directly increasing THRB activity.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Thyroid hormone receptors in health and disease.",
+            "authors": [
+              "Boelen A",
+              "Kwakkel J",
+              "Fliers E"
+            ],
+            "journal": "Minerva endocrinologica",
+            "year": "2012",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:21292729",
+          "snippet": "T(3) action in target tissues is determined by DIO2-regulated local availability of T(3) to its nuclear receptors, TRα and TRβ.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "T3 acts via its nuclear receptors TRα and TRβ (UniProt:P10828); local T3 availability drives receptor activity.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Deiodinases: the balance of thyroid hormone: local control of thyroid hormone action: role of type 2 deiodinase.",
+            "authors": [
+              "Williams GR",
+              "Bassett JH"
+            ],
+            "journal": "The Journal of endocrinology",
+            "year": "2011",
+            "doi": "10.1530/JOE-10-0448",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P10828",
+      "target": "GO:0002154",
+      "evidence": [
+        {
+          "reference": "PMID:38081939",
+          "snippet": "TRβ-deficiency blunts T3-regulated gene expression, indicating that TRβ confers transcriptional sensitivity.",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "explanation": "TRβ (THRB) is required for T3-regulated gene expression in the pituitary; its deficiency blunts the thyroid hormone mediated signaling pathway.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Thyroid hormone-regulated chromatin landscape and transcriptional sensitivity of the pituitary gland.",
+            "authors": [
+              "Cho YW",
+              "Fu Y",
+              "Huang CJ",
+              "Wu X",
+              "Ng L",
+              "Kelley KA",
+              "Vella KR",
+              "Berg AH",
+              "Hollenberg AN",
+              "Liu H",
+              "Forrest D"
+            ],
+            "journal": "Communications biology",
+            "year": "2023",
+            "doi": "10.1038/s42003-023-05546-y",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:29892814",
+          "snippet": "The thyroid hormones act through their nuclear receptor TRs that are T3-modulated transcription factors.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "TRs including THRB are T3-activated transcription factors that drive thyroid hormone-responsive gene expression, i.e. they positively regulate the thyroid hormone mediated signaling pathway.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "In Vitro Approaches to Identify Thyroid Hormone Receptor-Dependent Transcriptional Response.",
+            "authors": [
+              "Sirakov M",
+              "Plateroti M"
+            ],
+            "journal": "Methods in molecular biology (Clifton, N.J.)",
+            "year": "2018",
+            "doi": "10.1007/978-1-4939-7902-8_4",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "decreased",
+      "source": "GO:0002154",
+      "target": "MESH:D007037",
+      "evidence": [
+        {
+          "reference": "PMID:14751033",
+          "snippet": "optimal therapy for hypothyroidism requires replacement of the deficiency in thyroid hormone with synthetic levothyroxine",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Hypothyroidism is a state of deficient thyroid hormone signaling; restoring that signaling (via levothyroxine) treats the disease, confirming the pathway negatively regulates the disease state.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Evaluation of the therapeutic efficacy of different levothyroxine preparations in the treatment of human thyroid disease.",
+            "authors": [
+              "Klein I",
+              "Danzi S"
+            ],
+            "journal": "Thyroid : official journal of the American Thyroid Association",
+            "year": "2003",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:19491714",
+          "snippet": "Standard therapy for patients with hypothyroidism is replacement with synthetic thyroxine (T4).",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Synthetic T4 (levothyroxine) restores thyroid hormone mediated signaling, confirming that active signaling counteracts (negatively regulates) hypothyroidism.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Thyroxine alone or thyroxine plus triiodothyronine replacement therapy for hypothyroidism.",
+            "authors": [
+              "Ma C",
+              "Xie J",
+              "Huang X",
+              "Wang G",
+              "Wang Y",
+              "Wang X",
+              "Zuo S"
+            ],
+            "journal": "Nuclear medicine communications",
+            "year": "2009",
+            "doi": "10.1097/MNM.0b013e32832c79e0",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00451#mechanism-of-action",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    },
+    {
+      "url": "https://www.uniprot.org/uniprot/P10828",
+      "type": "other",
+      "label": "uniprot.org — record source"
+    }
+  ],
+  "site": {
+    "id": "phase3__P28",
+    "record_id": "P28_DB00451_MESH_D007037",
+    "run": "phase3",
+    "run_label": "Phase-3 eval",
+    "source_file": "tests/phase3_eval_outputs/P28.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/phase3__P29.json b/web-revamp-mockup/data/records/phase3__P29.json
new file mode 100644
index 0000000..826a298
--- /dev/null
+++ b/web-revamp-mockup/data/records/phase3__P29.json
@@ -0,0 +1,302 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P29_DB00437_MESH_D006073",
+    "drug": "Allopurinol",
+    "drug_mesh": "MESH:D000493",
+    "drugbank": "DB:DB00437",
+    "disease": "Gout",
+    "disease_mesh": "MESH:D006073",
+    "summary": "Allopurinol → Xanthine dehydrogenase/oxidase → uric acid biosynthetic process → uric acid → Gout"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D000493",
+      "name": "Allopurinol",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P47989",
+      "name": "Xanthine dehydrogenase/oxidase",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0002103",
+      "name": "uric acid biosynthetic process",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "CHEBI:27226",
+      "name": "uric acid",
+      "label": "ChemicalSubstance"
+    },
+    {
+      "id": "MESH:D006073",
+      "name": "Gout",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D000493",
+      "target": "UniProt:P47989",
+      "evidence": [
+        {
+          "reference": "PMID:41879452",
+          "snippet": "Allopurinol and its active metabolite, oxypurinol, reduce uric acid concentrations through xanthine oxidase inhibition by suppressing the conversion of hypoxanthine and xanthine.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Pharmacokinetic review confirming that allopurinol acts by inhibiting xanthine oxidase (XDH/XO), thereby suppressing conversion of hypoxanthine and xanthine to uric acid.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Population Pharmacokinetic Models of Oxypurinol in Adults: A Systematic Review.",
+            "authors": [
+              "Zairol Azwan FAA",
+              "Mohd Tahir NA",
+              "Mohd Saffian S",
+              "Makmor-Bakry M",
+              "Mohamed Said MS"
+            ],
+            "journal": "Current drug metabolism",
+            "year": "2026",
+            "doi": "10.2174/0113892002439476260101094935",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:41330172",
+          "snippet": "Both Feb and ALP inhibited the upregulation of xanthine dehydrogenas/xanthine oxidase (XDH/XOD), UA levels, and UA transporters (URAT1 and GLUT9) induced by MSU, with Feb having a more pronounced effect.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "In vitro study showing allopurinol (ALP) inhibits XDH/XOD activity and reduces uric acid (UA) levels in MSU-treated cells.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Febuxostat alleviates gout-associated hyperuricemia and inflammation by downregulating IL1A to modulate TLR2/TLR4/NF-κB signaling pathway.",
+            "authors": [
+              "Hu M",
+              "Zhou Y",
+              "Zhang Y",
+              "Pan F",
+              "Liu M"
+            ],
+            "journal": "International immunopharmacology",
+            "year": "2026",
+            "doi": "10.1016/j.intimp.2025.115935",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P47989",
+      "target": "GO:0002103",
+      "evidence": [
+        {
+          "reference": "PMID:41729472",
+          "snippet": "Xanthine dehydrogenase (XDH) is an enzyme that catalyzes the sequential conversion of hypoxanthine to xanthine, and of xanthine to urate.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "XDH catalyzes the final two steps of uric acid biosynthesis (hypoxanthine→xanthine→urate), directly driving the uric acid biosynthetic process.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Exploring the relationship between XDH gene variants and serum urate and xanthine dehydrogenase levels in gout.",
+            "authors": [
+              "Román-Olmos JA",
+              "Zamudio-Cuevas Y",
+              "Martínez-Flores K",
+              "Espinosa-Morales R",
+              "Fernández-Torres J"
+            ],
+            "journal": "Clinical rheumatology",
+            "year": "2026",
+            "doi": "10.1007/s10067-026-08002-4",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:41689938",
+          "snippet": "Xanthine oxidase (XO), the rate-limiting enzyme in uric acid production, represents a core therapeutic target for gout.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "XO/XDH is identified as the rate-limiting enzyme in uric acid production, confirming it positively regulates the uric acid biosynthetic process.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Xanthine oxidase inhibitors for gout: Applications and novel drug development.",
+            "authors": [
+              "Lyu W",
+              "Qin H",
+              "Zhou X",
+              "Zhang Y",
+              "Lu D",
+              "Shao Y",
+              "Chen Y",
+              "Liang M",
+              "Li Q",
+              "Chi X",
+              "Zhang L",
+              "Shi C",
+              "Liu Z"
+            ],
+            "journal": "European journal of medicinal chemistry",
+            "year": "2026",
+            "doi": "10.1016/j.ejmech.2026.118619",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "abundance",
+      "object_direction_qualifier": "increased",
+      "source": "GO:0002103",
+      "target": "CHEBI:27226",
+      "evidence": [
+        {
+          "reference": "PMID:41729472",
+          "snippet": "Xanthine dehydrogenase (XDH) is a key enzyme in urate biosynthesis, and genetic variations in its XDH gene can influence the amount or activity of the enzyme, as well as the levels of urate produced.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Urate biosynthesis driven by XDH produces uric acid (urate); increased XDH activity or expression correlates with higher urate levels, confirming the biosynthetic process increases uric acid abundance.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Exploring the relationship between XDH gene variants and serum urate and xanthine dehydrogenase levels in gout.",
+            "authors": [
+              "Román-Olmos JA",
+              "Zamudio-Cuevas Y",
+              "Martínez-Flores K",
+              "Espinosa-Morales R",
+              "Fernández-Torres J"
+            ],
+            "journal": "Clinical rheumatology",
+            "year": "2026",
+            "doi": "10.1007/s10067-026-08002-4",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:41879452",
+          "snippet": "Allopurinol and its active metabolite, oxypurinol, reduce uric acid concentrations through xanthine oxidase inhibition by suppressing the conversion of hypoxanthine and xanthine.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Blocking xanthine oxidase (the enzyme driving the uric acid biosynthetic process) reduces uric acid concentrations, confirming the biosynthetic process is the source of uric acid abundance.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Population Pharmacokinetic Models of Oxypurinol in Adults: A Systematic Review.",
+            "authors": [
+              "Zairol Azwan FAA",
+              "Mohd Tahir NA",
+              "Mohd Saffian S",
+              "Makmor-Bakry M",
+              "Mohamed Said MS"
+            ],
+            "journal": "Current drug metabolism",
+            "year": "2026",
+            "doi": "10.2174/0113892002439476260101094935",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "contributes to",
+      "source": "CHEBI:27226",
+      "target": "MESH:D006073",
+      "evidence": [
+        {
+          "reference": "PMID:42212135",
+          "snippet": "Gout is an aseptic inflammatory disease caused by monosodium urate (MSU) crystal deposition.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Elevated uric acid (monosodium urate) leads to crystal deposition, the direct cause of gouty inflammation, confirming uric acid contributes to gout.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Neutrophil extracellular traps in gout: from immune defense to pathological dynamic equilibrium.",
+            "authors": [
+              "Wang F",
+              "Tie N",
+              "Jin Y",
+              "Li H"
+            ],
+            "journal": "Frontiers in immunology",
+            "year": "2026",
+            "doi": "10.3389/fimmu.2026.1826191",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:41689938",
+          "snippet": "Xanthine oxidase (XO), the rate-limiting enzyme in uric acid production, represents a core therapeutic target for gout.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Uric acid production (via XO) is the core driver of gout pathogenesis, confirming that uric acid contributes to gout.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Xanthine oxidase inhibitors for gout: Applications and novel drug development.",
+            "authors": [
+              "Lyu W",
+              "Qin H",
+              "Zhou X",
+              "Zhang Y",
+              "Lu D",
+              "Shao Y",
+              "Chen Y",
+              "Liang M",
+              "Li Q",
+              "Chi X",
+              "Zhang L",
+              "Shi C",
+              "Liu Z"
+            ],
+            "journal": "European journal of medicinal chemistry",
+            "year": "2026",
+            "doi": "10.1016/j.ejmech.2026.118619",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00437#mechanism-of-action",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    },
+    {
+      "url": "https://www.uniprot.org/uniprot/P47989",
+      "type": "other",
+      "label": "uniprot.org — record source"
+    }
+  ],
+  "site": {
+    "id": "phase3__P29",
+    "record_id": "P29_DB00437_MESH_D006073",
+    "run": "phase3",
+    "run_label": "Phase-3 eval",
+    "source_file": "tests/phase3_eval_outputs/P29.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/phase3__P30.json b/web-revamp-mockup/data/records/phase3__P30.json
new file mode 100644
index 0000000..9e90b23
--- /dev/null
+++ b/web-revamp-mockup/data/records/phase3__P30.json
@@ -0,0 +1,259 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P30_DB09038_MESH_D003924",
+    "drug": "Empagliflozin",
+    "drug_mesh": "MESH:C000591311",
+    "drugbank": "DB:DB09038",
+    "disease": "Diabetes Mellitus, Type 2",
+    "disease_mesh": "MESH:D003924",
+    "summary": "Empagliflozin → Sodium/glucose cotransporter 2 → renal glucose absorption → Hyperglycemia → Diabetes Mellitus, Type 2"
+  },
+  "nodes": [
+    {
+      "id": "MESH:C000591311",
+      "name": "Empagliflozin",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P31639",
+      "name": "Sodium/glucose cotransporter 2",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0035623",
+      "name": "renal glucose absorption",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "HP:0003074",
+      "name": "Hyperglycemia",
+      "label": "PhenotypicFeature"
+    },
+    {
+      "id": "MESH:D003924",
+      "name": "Diabetes Mellitus, Type 2",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:C000591311",
+      "target": "UniProt:P31639",
+      "evidence": [
+        {
+          "reference": "PMID:38265382",
+          "snippet": "Empagliflozin is a selective SGLT2 inhibitor that works by constraining glucose reabsorption in the kidneys, causing increased urinary glucose elimination.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Pharmacological review confirming empagliflozin selectively inhibits SGLT2 activity, constraining its renal glucose reabsorption function.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Empagliflozin-A Sodium Glucose Co-transporter-2 Inhibitor: Overview ofits Chemistry, Pharmacology, and Toxicology.",
+            "authors": [
+              "Yadav J",
+              "Ahsan F",
+              "Panda P",
+              "Mahmood T",
+              "Ansari VA",
+              "Shamim A"
+            ],
+            "journal": "Current diabetes reviews",
+            "year": "2024",
+            "doi": "10.2174/0115733998271026231127051545",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P31639",
+      "target": "GO:0035623",
+      "evidence": [
+        {
+          "reference": "PMID:40041732",
+          "snippet": "Sodium-glucose cotransporter-2 (SGLT-2) acts as a key element in the reabsorption of glucose in the kidney.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "SGLT2 is the key transporter driving renal glucose reabsorption; it positively regulates this biological process.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "The effects of empagliflozin in patients with type 1 diabetes: Results of a 12-week, double-blind, randomized, placebo-controlled clinical trial.",
+            "authors": [
+              "Najafipour M",
+              "Najafipour F",
+              "Ostadrahimi A",
+              "Ghavami M",
+              "Razaghi Z",
+              "Tutunchi H",
+              "Mesri Alamdari N"
+            ],
+            "journal": "Health promotion perspectives",
+            "year": "2024",
+            "doi": "10.34172/hpp.42486",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:41477427",
+          "snippet": "work by blocking SGLT2 proteins in the proximal convoluted tubules of the nephrons, thereby preventing glucose reabsorption into the bloodstream.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Blocking SGLT2 prevents renal glucose reabsorption, confirming that SGLT2 positively regulates this process.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "The Effects of Sodium-Glucose Co-transporter 2 Inhibitors on Cardiovascular Outcomes in Heart Failure: A Systematic Review and Meta-Analysis.",
+            "authors": [
+              "Maharaj A",
+              "Bidhesi S",
+              "Grover D",
+              "Raghunath P",
+              "Lutchmedial RN",
+              "Khan AS",
+              "Maharaj MA",
+              "Heera PV",
+              "Maharaj R",
+              "Sookhan C",
+              "Kanhai CD",
+              "Marshall C",
+              "Calder AA"
+            ],
+            "journal": "Cureus",
+            "year": "2025",
+            "doi": "10.7759/cureus.98140",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "positively correlated with",
+      "source": "GO:0035623",
+      "target": "HP:0003074",
+      "evidence": [
+        {
+          "reference": "PMID:33085977",
+          "snippet": "SGLT2 inhibitors are a class of oral antidiabetic drugs that lower elevated plasma glucose levels by promoting the urinary excretion of excess glucose through the inhibition of renal glucose reuptake.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Inhibiting renal glucose reabsorption lowers plasma glucose, establishing that renal glucose reabsorption is positively correlated with blood glucose / hyperglycemia.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Mechanistic evaluation of the effect of sodium-dependent glucose transporter 2 inhibitors on delayed glucose absorption in patients with type 2 diabetes mellitus using a quantitative systems pharmacology model of human systemic glucose dynamics.",
+            "authors": [
+              "Mori-Anai K",
+              "Tashima Y",
+              "Nakada T",
+              "Nakamaru Y",
+              "Takahata T",
+              "Saito R"
+            ],
+            "journal": "Biopharmaceutics & drug disposition",
+            "year": "2020",
+            "doi": "10.1002/bdd.2253",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:34487707",
+          "snippet": "Ipragliflozin significantly lowered blood glucose levels in mice that had prefasted for 0, 6, or 12 h, but not 18 h or more.",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "explanation": "SGLT2 inhibitor-mediated reduction of renal glucose reabsorption lowers blood glucose in a blood glucose-dependent manner, supporting positive correlation between renal glucose absorption and hyperglycemia.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "SGLT2 inhibitor ipragliflozin exerts antihyperglycemic effects via the blood glucose-dependent increase in urinary glucose excretion in type 2 diabetic mice.",
+            "authors": [
+              "Tahara A"
+            ],
+            "journal": "European journal of pharmacology",
+            "year": "2021",
+            "doi": "10.1016/j.ejphar.2021.174486",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "manifestation of",
+      "source": "HP:0003074",
+      "target": "MESH:D003924",
+      "evidence": [
+        {
+          "reference": "PMID:24843435",
+          "snippet": "Diabetes mellitus is a group of diseases associated with various metabolic disorders, the main feature of which is chronic hyperglycemia due to insufficient insulin action.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Chronic hyperglycemia is the main feature (manifestation) of diabetes mellitus, including type 2 diabetes mellitus.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Report of the committee on the classification and diagnostic criteria of diabetes mellitus.",
+            "authors": [
+              "Committee of the Japan Diabetes Society on the Diagnostic Criteria of Diabetes Mellitus",
+              "Seino Y",
+              "Nanjo K",
+              "Tajima N",
+              "Kadowaki T",
+              "Kashiwagi A",
+              "Araki E",
+              "Ito C",
+              "Inagaki N",
+              "Iwamoto Y",
+              "Kasuga M",
+              "Hanafusa T",
+              "Haneda M",
+              "Ueki K"
+            ],
+            "journal": "Journal of diabetes investigation",
+            "year": "2010",
+            "doi": "10.1111/j.2040-1124.2010.00074.x",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB09038#mechanism-of-action",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    },
+    {
+      "url": "https://www.uniprot.org/uniprot/P31639#function",
+      "type": "other",
+      "label": "uniprot.org — record source"
+    },
+    {
+      "url": "https://en.wikipedia.org/wiki/Empagliflozin#Mechanism_of_action",
+      "type": "wiki",
+      "label": "en.wikipedia.org — record source"
+    }
+  ],
+  "site": {
+    "id": "phase3__P30",
+    "record_id": "P30_DB09038_MESH_D003924",
+    "run": "phase3",
+    "run_label": "Phase-3 eval",
+    "source_file": "tests/phase3_eval_outputs/P30.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/pilot__B02362_MESH_D003882_1.json b/web-revamp-mockup/data/records/pilot__B02362_MESH_D003882_1.json
new file mode 100644
index 0000000..6981b43
--- /dev/null
+++ b/web-revamp-mockup/data/records/pilot__B02362_MESH_D003882_1.json
@@ -0,0 +1,114 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "B02362_MESH_D003882_1",
+    "drug": "aminobenzoic acid",
+    "drug_mesh": "MESH:D010129",
+    "drugbank": "DB:B02362",
+    "disease": "Dermatomyositis",
+    "disease_mesh": "MESH:D003882",
+    "summary": "aminobenzoic acid → Glycosaminoglycans → Dermatomyositis"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D010129",
+      "name": "aminobenzoic acid",
+      "label": "Drug"
+    },
+    {
+      "id": "MESH:D006025",
+      "name": "Glycosaminoglycans",
+      "label": "ChemicalSubstance"
+    },
+    {
+      "id": "MESH:D003882",
+      "name": "Dermatomyositis",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "abundance",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D010129",
+      "target": "MESH:D006025",
+      "evidence": [
+        {
+          "reference": "PMID:1350132",
+          "snippet": "Monolayer cultures containing Potaba showed a dose-dependent inhibition...similar dose dependent inhibition of glycosaminoglycan secretion in all 3 groups",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Potaba (potassium para-aminobenzoate, the salt of aminobenzoic acid) dose-dependently inhibits glycosaminoglycan secretion by dermal fibroblasts.",
+          "source_type": "pubmed",
+          "paper": null
+        },
+        {
+          "reference": "PMID:155125",
+          "snippet": "Potassium para-aminobenzoate was tested for its ability to affect growth and macromolecule synthesis...Acid mucopolysaccharide secretion by rheumatoid synovial cells and scleroderma fibroblasts was inhibited even at 100 microgram/ml",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Acid mucopolysaccharides are glycosaminoglycans; their secretion by scleroderma fibroblasts is inhibited by potassium para-aminobenzoate within the therapeutic range.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    },
+    {
+      "key": "manifestation of",
+      "source": "MESH:D006025",
+      "target": "MESH:D003882",
+      "evidence": [
+        {
+          "reference": "PMID:17300236",
+          "snippet": "Dermal mucin is an amorphous gelatinous substance composed primarily of hyaluronan (HA) and sulphated glycosaminoglycans (GAGs)...deposition is associated with lupus erythematosus, dermatomyositis, scleroderma and granuloma annulare",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Dermal mucin, composed of glycosaminoglycans, is deposited in dermatomyositis lesions; this GAG deposition is a manifestation of the disease.",
+          "source_type": "pubmed",
+          "paper": null
+        },
+        {
+          "reference": "PMID:26322557",
+          "snippet": "deposition of glycosaminoglycans (mucin), either focally or diffusely within the dermis...secondary to several dermatoses, most notably lupus erythematous, scleroderma, and dermatomyositis",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Dermal mucinosis (glycosaminoglycan deposition) occurs secondary to dermatomyositis, i.e. as a manifestation of the disease.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://pubmed.ncbi.nlm.nih.gov/1350132/",
+      "type": "other",
+      "label": "pubmed.ncbi.nlm.nih.gov — record source"
+    },
+    {
+      "url": "https://pubmed.ncbi.nlm.nih.gov/155125/",
+      "type": "other",
+      "label": "pubmed.ncbi.nlm.nih.gov — record source"
+    },
+    {
+      "url": "https://pubmed.ncbi.nlm.nih.gov/17300236/",
+      "type": "other",
+      "label": "pubmed.ncbi.nlm.nih.gov — record source"
+    },
+    {
+      "url": "https://pubmed.ncbi.nlm.nih.gov/26322557/",
+      "type": "other",
+      "label": "pubmed.ncbi.nlm.nih.gov — record source"
+    }
+  ],
+  "site": {
+    "id": "pilot__B02362_MESH_D003882_1",
+    "record_id": "B02362_MESH_D003882_1",
+    "run": "pilot",
+    "run_label": "Pilot run",
+    "source_file": "experiments/pilot/outputs/B02362_MESH_D003882_1.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/pilot__B02362_MESH_D003882_1__r2.json b/web-revamp-mockup/data/records/pilot__B02362_MESH_D003882_1__r2.json
new file mode 100644
index 0000000..1775d48
--- /dev/null
+++ b/web-revamp-mockup/data/records/pilot__B02362_MESH_D003882_1__r2.json
@@ -0,0 +1,114 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "B02362_MESH_D003882_1",
+    "drug": "aminobenzoic acid",
+    "drug_mesh": "MESH:D010129",
+    "drugbank": "DB:B02362",
+    "disease": "Dermatomyositis",
+    "disease_mesh": "MESH:D003882",
+    "summary": "aminobenzoic acid → response to UV → apoptotic process → Dermatomyositis"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D010129",
+      "name": "aminobenzoic acid",
+      "label": "Drug"
+    },
+    {
+      "id": "GO:0009411",
+      "name": "response to UV",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "GO:0006915",
+      "name": "apoptotic process",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D003882",
+      "name": "Dermatomyositis",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D010129",
+      "target": "GO:0009411",
+      "evidence": [
+        {
+          "reference": "PMID:7205025",
+          "snippet": "Sunscreen preparations containing various chemical UV absorbers, para-aminobenzoic acid (PABA), 2 PABA derivatives, benzophenone or a combination of these were topically applied to the backs of C3H/HeN mice prior to their being irradiated with ultraviolet light in the UVB range. In all cases this treatment was effective in preventing the pathological skin changes associated with UVB irradiation.",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "explanation": "para-aminobenzoic acid (aminobenzoic acid) is a UV absorber that, applied before UVB exposure, prevents the pathological skin changes caused by UVB, i.e. it blunts the skin's response to ultraviolet radiation.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "GO:0009411",
+      "target": "GO:0006915",
+      "evidence": [
+        {
+          "reference": "PMID:11390206",
+          "snippet": "High-dose ultraviolet B (UVB) irradiation is known to induce apoptosis of keratinocytes",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Ultraviolet B irradiation directly induces apoptosis of keratinocytes.",
+          "source_type": "pubmed",
+          "paper": null
+        },
+        {
+          "reference": "PMID:9067700",
+          "snippet": "Irradiation with ultraviolet (UV) B light results in the formation of apoptotic keratinocytes called sunburn cells (SC).",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "UVB irradiation produces apoptotic keratinocytes (sunburn cells), so the response to ultraviolet radiation drives the apoptotic process.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    },
+    {
+      "key": "contributes to",
+      "source": "GO:0006915",
+      "target": "MESH:D003882",
+      "evidence": [
+        {
+          "reference": "PMID:16850099",
+          "snippet": "The defective regulation of apoptosis may play an important role in the development of cutaneous lesions of patients with dermatomyositis, in which the skin is a prominent target organ.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Apoptosis of epidermal keratinocytes contributes to the development of the cutaneous lesions of dermatomyositis.",
+          "source_type": "pubmed",
+          "paper": null
+        },
+        {
+          "reference": "PMID:10398142",
+          "snippet": "In DM and CLE skin, the number of apoptotic keratinocytes was significantly increased (p=0.008) compared with normal skin.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Apoptotic keratinocytes are significantly increased in dermatomyositis lesional skin, and this apoptosis mediates the epidermal lesions of the disease.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    }
+  ],
+  "references": [],
+  "site": {
+    "id": "pilot__B02362_MESH_D003882_1__r2",
+    "record_id": "B02362_MESH_D003882_1",
+    "run": "pilot",
+    "run_label": "Pilot run",
+    "source_file": "experiments/pilot/outputs/B02362_MESH_D003882_1__r2.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/pilot__B02362_MESH_D003882_1__r3.json b/web-revamp-mockup/data/records/pilot__B02362_MESH_D003882_1__r3.json
new file mode 100644
index 0000000..c939679
--- /dev/null
+++ b/web-revamp-mockup/data/records/pilot__B02362_MESH_D003882_1__r3.json
@@ -0,0 +1,104 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "B02362_MESH_D003882_1",
+    "drug": "aminobenzoic acid",
+    "drug_mesh": "MESH:D010129",
+    "drugbank": "DB:B02362",
+    "disease": "Dermatomyositis",
+    "disease_mesh": "MESH:D003882",
+    "summary": "aminobenzoic acid → Glycosaminoglycans → Dermatomyositis"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D010129",
+      "name": "aminobenzoic acid",
+      "label": "Drug"
+    },
+    {
+      "id": "MESH:D006025",
+      "name": "Glycosaminoglycans",
+      "label": "ChemicalSubstance"
+    },
+    {
+      "id": "MESH:D003882",
+      "name": "Dermatomyositis",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "abundance",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D010129",
+      "target": "MESH:D006025",
+      "evidence": [
+        {
+          "reference": "PMID:155125",
+          "snippet": "Acid mucopolysaccharide secretion by rheumatoid synovial cells and scleroderma fibroblasts was inhibited even at 100 microgram/ml, which is within the therapeutic range",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Potassium para-aminobenzoate (Potaba), the potassium salt of aminobenzoic acid, directly inhibits fibroblast secretion of acid mucopolysaccharides (glycosaminoglycans).",
+          "source_type": "pubmed",
+          "paper": null
+        },
+        {
+          "reference": "PMID:1350132",
+          "snippet": "There was a similar dose dependent inhibition of glycosaminoglycan secretion in all 3 groups",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Potaba (potassium para-aminobenzoate, the potassium salt of aminobenzoic acid) produces dose-dependent inhibition of glycosaminoglycan secretion by skin fibroblasts.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    },
+    {
+      "key": "manifestation of",
+      "source": "MESH:D006025",
+      "target": "MESH:D003882",
+      "evidence": [
+        {
+          "reference": "PMID:17300236",
+          "snippet": "Dermal mucin is an amorphous gelatinous substance composed primarily of hyaluronan (HA) and sulphated glycosaminoglycans (GAGs) ... deposition is associated with lupus erythematosus, dermatomyositis, scleroderma and granuloma annulare",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "The dermal mucin deposited in dermatomyositis is composed of hyaluronan and sulphated glycosaminoglycans, and its deposition is associated with dermatomyositis.",
+          "source_type": "pubmed",
+          "paper": null
+        },
+        {
+          "reference": "PMID:11328393",
+          "snippet": "Mucin deposition is a common feature in autoimmune collagen diseases including dermatomyositis.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Glycosaminoglycan-rich dermal mucin deposition is a characteristic feature of dermatomyositis.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://pubmed.ncbi.nlm.nih.gov/155125/",
+      "type": "other",
+      "label": "pubmed.ncbi.nlm.nih.gov — record source"
+    },
+    {
+      "url": "https://pubmed.ncbi.nlm.nih.gov/17300236/",
+      "type": "other",
+      "label": "pubmed.ncbi.nlm.nih.gov — record source"
+    }
+  ],
+  "site": {
+    "id": "pilot__B02362_MESH_D003882_1__r3",
+    "record_id": "B02362_MESH_D003882_1",
+    "run": "pilot",
+    "run_label": "Pilot run",
+    "source_file": "experiments/pilot/outputs/B02362_MESH_D003882_1__r3.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/pilot__DB00002_MESH_D003110_1.json b/web-revamp-mockup/data/records/pilot__DB00002_MESH_D003110_1.json
new file mode 100644
index 0000000..08791f5
--- /dev/null
+++ b/web-revamp-mockup/data/records/pilot__DB00002_MESH_D003110_1.json
@@ -0,0 +1,103 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "DB00002_MESH_D003110_1",
+    "drug": "cetuximab",
+    "drug_mesh": "MESH:D000068818",
+    "drugbank": "DB:DB00002",
+    "disease": "Malignant tumor of colon",
+    "disease_mesh": "MESH:D003110",
+    "summary": "cetuximab → Epidermal growth factor receptor → cell population proliferation → Malignant tumor of colon"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D000068818",
+      "name": "cetuximab",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P00533",
+      "name": "Epidermal growth factor receptor",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0008283",
+      "name": "cell population proliferation",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D003110",
+      "name": "Malignant tumor of colon",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D000068818",
+      "target": "UniProt:P00533",
+      "evidence": [
+        {
+          "reference": "PMID:39000238",
+          "snippet": "Cetuximab, a mouse-human chimeric monoclonal antibody (mAb), binds to the extracellular domain of EGFR thus impairing EGFR-mediated signaling and reducing cell proliferation.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Cetuximab binds the extracellular domain of EGFR and impairs EGFR-mediated signaling, i.e. decreases EGFR activity.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P00533",
+      "target": "GO:0008283",
+      "evidence": [
+        {
+          "reference": "PMID:39000238",
+          "snippet": "Cetuximab, a mouse-human chimeric monoclonal antibody (mAb), binds to the extracellular domain of EGFR thus impairing EGFR-mediated signaling and reducing cell proliferation.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Impairing EGFR-mediated signaling reduces cell proliferation, indicating EGFR signaling positively regulates cell proliferation.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    },
+    {
+      "key": "contributes to",
+      "source": "GO:0008283",
+      "target": "MESH:D003110",
+      "evidence": [
+        {
+          "reference": "PMID:41037865",
+          "snippet": "The second deadliest cancer in the world is colorectal cancer (CRC), which is caused by the uncontrolled proliferation of epithelial cells in the colon.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Colorectal cancer is caused by the uncontrolled proliferation of epithelial cells in the colon, establishing cell proliferation as a contributor to the colonic malignancy.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00002",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    }
+  ],
+  "site": {
+    "id": "pilot__DB00002_MESH_D003110_1",
+    "record_id": "DB00002_MESH_D003110_1",
+    "run": "pilot",
+    "run_label": "Pilot run",
+    "source_file": "experiments/pilot/outputs/DB00002_MESH_D003110_1.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/pilot__DB00002_MESH_D003110_1__r2.json b/web-revamp-mockup/data/records/pilot__DB00002_MESH_D003110_1__r2.json
new file mode 100644
index 0000000..b803b9b
--- /dev/null
+++ b/web-revamp-mockup/data/records/pilot__DB00002_MESH_D003110_1__r2.json
@@ -0,0 +1,138 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "DB00002_MESH_D003110_1",
+    "drug": "cetuximab",
+    "drug_mesh": "MESH:D000068818",
+    "drugbank": "DB:DB00002",
+    "disease": "Malignant tumor of colon",
+    "disease_mesh": "MESH:D003110",
+    "summary": "Cetuximab → Epidermal growth factor receptor → Cell proliferation → Malignant tumor of colon"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D000068818",
+      "name": "Cetuximab",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P00533",
+      "name": "Epidermal growth factor receptor",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0008283",
+      "name": "Cell proliferation",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D003110",
+      "name": "Malignant tumor of colon",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D000068818",
+      "target": "UniProt:P00533",
+      "evidence": [
+        {
+          "reference": "PMID:23723688",
+          "snippet": "binds with high affinity to the extracellular domain of the human EGFR, blocking ligand binding, resulting in inhibition of the receptor function",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Cetuximab binds the EGFR extracellular domain and inhibits receptor function.",
+          "source_type": "pubmed",
+          "paper": null
+        },
+        {
+          "reference": "PMID:20088790",
+          "snippet": "Cetuximab binding to the EGFR blocks phosphorylation and activation of receptor-associated kinases and their associated downstream signalling (MAPK, PI3K/Akt, Jak/Stat pathways)",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Cetuximab: from bench to bedside.",
+            "authors": [
+              "Vincenzi B",
+              "Zoccoli A",
+              "Pantano F",
+              "Venditti O",
+              "Galluzzo S"
+            ],
+            "journal": "Current cancer drug targets",
+            "year": "2010",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P00533",
+      "target": "GO:0008283",
+      "evidence": [
+        {
+          "reference": "PMID:15717942",
+          "snippet": "EGFR plays a fundamental role in regulating the proliferation and survival of malignant neoplasms",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "EGFR signaling drives proliferation of malignant cells.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Clinical experience with monoclonal antibodies to epidermal growth factor receptor.",
+            "authors": [
+              "Calvo E",
+              "Rowinsky EK"
+            ],
+            "journal": "Current oncology reports",
+            "year": "2005",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "contributes to",
+      "source": "GO:0008283",
+      "target": "MESH:D003110",
+      "evidence": [
+        {
+          "reference": "PMID:23803085",
+          "snippet": "cell proliferation of Ki-67 showed a significant contribution in colonic cancer progression",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "explanation": "Cell proliferation contributes to colonic cancer progression in an azoxymethane-induced rat model.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00002",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    }
+  ],
+  "site": {
+    "id": "pilot__DB00002_MESH_D003110_1__r2",
+    "record_id": "DB00002_MESH_D003110_1",
+    "run": "pilot",
+    "run_label": "Pilot run",
+    "source_file": "experiments/pilot/outputs/DB00002_MESH_D003110_1__r2.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/pilot__DB00002_MESH_D003110_1__r3.json b/web-revamp-mockup/data/records/pilot__DB00002_MESH_D003110_1__r3.json
new file mode 100644
index 0000000..23ed5ef
--- /dev/null
+++ b/web-revamp-mockup/data/records/pilot__DB00002_MESH_D003110_1__r3.json
@@ -0,0 +1,145 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "DB00002_MESH_D003110_1",
+    "drug": "cetuximab",
+    "drug_mesh": "MESH:D000068818",
+    "drugbank": "DB:DB00002",
+    "disease": "Malignant tumor of colon",
+    "disease_mesh": "MESH:D003110",
+    "summary": "cetuximab → Epidermal growth factor receptor → cell proliferation → Malignant tumor of colon"
+  },
+  "nodes": [
+    {
+      "id": "DB:DB00002",
+      "name": "cetuximab",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P00533",
+      "name": "Epidermal growth factor receptor",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0008283",
+      "name": "cell proliferation",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D003110",
+      "name": "Malignant tumor of colon",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "DB:DB00002",
+      "target": "UniProt:P00533",
+      "evidence": [
+        {
+          "reference": "PMID:42176792",
+          "snippet": "Cetuximab exerts its antitumor activity by blocking ligand-dependent EGFR signaling and by engaging immune effector mechanisms.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Cetuximab blocks ligand-dependent EGFR signaling, reducing EGFR activity.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "EGFR S442 ectodomain mutation confers cetuximab resistance that can be overcome by ERBB2 blockade with trastuzumab-deruxtecan.",
+            "authors": [
+              "Harmych SJ",
+              "Joshi N",
+              "Tanaka H",
+              "Bogatcheva G",
+              "Ramirez MA",
+              "Graves-Deal R",
+              "Tydings CW",
+              "Elia MT",
+              "Mueller HRL",
+              "Silvestri IM",
+              "Ti Ning K",
+              "Wahoski CC",
+              "Sievers CK",
+              "Higginbotham JN",
+              "Irudayam MJ",
+              "Revetta FL",
+              "Zhao Z",
+              "Franklin JL",
+              "Yilma B",
+              "O'Grady TM",
+              "Fragkogianni S",
+              "Ciampricotti M",
+              "Washington MK",
+              "Guo X",
+              "Lovly CM",
+              "Walker AS",
+              "Meiler J",
+              "Mudumbi KC",
+              "Liu Q",
+              "Coffey RJ",
+              "Rosenthal E",
+              "Singh B"
+            ],
+            "journal": "Cancer letters",
+            "year": "2026",
+            "doi": "10.1016/j.canlet.2026.218607",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P00533",
+      "target": "GO:0008283",
+      "evidence": [
+        {
+          "reference": "PMID:38958494",
+          "snippet": "EGFR plays an essential role in cellular signaling pathways that regulate cell growth, proliferation, and survival and is often dysregulated in cancer.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "EGFR signaling drives cell growth and proliferation.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    },
+    {
+      "key": "contributes to",
+      "source": "GO:0008283",
+      "target": "MESH:D003110",
+      "evidence": [
+        {
+          "reference": "PMID:22114026",
+          "snippet": "colorectal cancers (CRC) form a group of pathologies in which early steps of development are characterized by an aberrant expression of β-catenin and an uncontrolled proliferation of epithelial cells.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Uncontrolled proliferation of epithelial cells drives colorectal cancer development.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00002",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    }
+  ],
+  "site": {
+    "id": "pilot__DB00002_MESH_D003110_1__r3",
+    "record_id": "DB00002_MESH_D003110_1",
+    "run": "pilot",
+    "run_label": "Pilot run",
+    "source_file": "experiments/pilot/outputs/DB00002_MESH_D003110_1__r3.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/pilot__DB00005_MESH_D015535_1.json b/web-revamp-mockup/data/records/pilot__DB00005_MESH_D015535_1.json
new file mode 100644
index 0000000..c8b8cdb
--- /dev/null
+++ b/web-revamp-mockup/data/records/pilot__DB00005_MESH_D015535_1.json
@@ -0,0 +1,101 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "DB00005_MESH_D015535_1",
+    "drug": "Etanercept",
+    "drug_mesh": "MESH:D000068800",
+    "drugbank": "DB:DB00005",
+    "disease": "Psoriasis with arthropathy",
+    "disease_mesh": "MESH:D015535",
+    "summary": "Etanercept → Tumor necrosis factor → inflammatory response → Psoriasis with arthropathy"
+  },
+  "nodes": [
+    {
+      "id": "DB:DB00005",
+      "name": "Etanercept",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P01375",
+      "name": "Tumor necrosis factor",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0006954",
+      "name": "inflammatory response",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D015535",
+      "name": "Psoriasis with arthropathy",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "DB:DB00005",
+      "target": "UniProt:P01375",
+      "evidence": [
+        {
+          "reference": "PMID:22686544",
+          "snippet": "The mechanism of action of etanercept in psoriatic disease and other approved indications is mediated by the neutralization of soluble TNF-α",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Mechanism-of-action review; etanercept neutralizes soluble TNF-α, decreasing its activity.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    },
+    {
+      "key": "contributes to",
+      "source": "UniProt:P01375",
+      "target": "GO:0006954",
+      "evidence": [
+        {
+          "reference": "PMID:30293157",
+          "snippet": "Tumor necrosis factor (TNF)-α is a cytokine that plays a well-established, key role as a central mediator of inflammation and immune regulation.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    },
+    {
+      "key": "manifestation of",
+      "source": "GO:0006954",
+      "target": "MESH:D015535",
+      "evidence": [
+        {
+          "reference": "PMID:26523063",
+          "snippet": "Psoriatic arthritis (PsA) is a chronic inflammatory disease affecting peripheral and axial joints",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Joint inflammation is the defining pathological manifestation of psoriatic arthritis (psoriasis with arthropathy).",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00005",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    }
+  ],
+  "site": {
+    "id": "pilot__DB00005_MESH_D015535_1",
+    "record_id": "DB00005_MESH_D015535_1",
+    "run": "pilot",
+    "run_label": "Pilot run",
+    "source_file": "experiments/pilot/outputs/DB00005_MESH_D015535_1.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/pilot__DB00009_MESH_D011655_1.json b/web-revamp-mockup/data/records/pilot__DB00009_MESH_D011655_1.json
new file mode 100644
index 0000000..4ea644f
--- /dev/null
+++ b/web-revamp-mockup/data/records/pilot__DB00009_MESH_D011655_1.json
@@ -0,0 +1,104 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "DB00009_MESH_D011655_1",
+    "drug": "alteplase",
+    "drug_mesh": "MESH:D010959",
+    "drugbank": "DB:DB00009",
+    "disease": "Pulmonary embolism",
+    "disease_mesh": "MESH:D011655",
+    "summary": "alteplase → Plasminogen → Fibrin → Pulmonary embolism"
+  },
+  "nodes": [
+    {
+      "id": "DB:DB00009",
+      "name": "alteplase",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P00747",
+      "name": "Plasminogen",
+      "label": "Protein"
+    },
+    {
+      "id": "MESH:D005342",
+      "name": "Fibrin",
+      "label": "ChemicalSubstance"
+    },
+    {
+      "id": "MESH:D011655",
+      "name": "Pulmonary embolism",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "increased",
+      "source": "DB:DB00009",
+      "target": "UniProt:P00747",
+      "evidence": [
+        {
+          "reference": "PMID:3044205",
+          "snippet": "fibrin strikingly enhances the activation rate of plasminogen by t-PA",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Alteplase is recombinant human tissue-type plasminogen activator (t-PA), which activates the zymogen plasminogen.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    },
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "abundance",
+      "object_direction_qualifier": "decreased",
+      "source": "UniProt:P00747",
+      "target": "MESH:D005342",
+      "evidence": [
+        {
+          "reference": "PMID:3044205",
+          "snippet": "plasminogen, which can be converted to the active enzyme plasmin, which will degrade fibrin",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Activated plasminogen (plasmin) proteolytically degrades fibrin, reducing fibrin abundance in the clot.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    },
+    {
+      "key": "causes",
+      "source": "MESH:D005342",
+      "target": "MESH:D011655",
+      "evidence": [
+        {
+          "reference": "PMID:12845330",
+          "snippet": "fibrin microemboli aggregating in pulmonary vasculature",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "explanation": "Fibrin-rich emboli lodge in and obstruct the pulmonary vasculature, the pathologic basis of pulmonary embolism; degrading fibrin dissolves these clots.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00009",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    }
+  ],
+  "site": {
+    "id": "pilot__DB00009_MESH_D011655_1",
+    "record_id": "DB00009_MESH_D011655_1",
+    "run": "pilot",
+    "run_label": "Pilot run",
+    "source_file": "experiments/pilot/outputs/DB00009_MESH_D011655_1.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/pilot__DB00009_MESH_D011655_1__r2.json b/web-revamp-mockup/data/records/pilot__DB00009_MESH_D011655_1__r2.json
new file mode 100644
index 0000000..95d4318
--- /dev/null
+++ b/web-revamp-mockup/data/records/pilot__DB00009_MESH_D011655_1__r2.json
@@ -0,0 +1,151 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "DB00009_MESH_D011655_1",
+    "drug": "alteplase",
+    "drug_mesh": "MESH:D010959",
+    "drugbank": "DB:DB00009",
+    "disease": "Pulmonary embolism",
+    "disease_mesh": "MESH:D011655",
+    "summary": "alteplase → Plasminogen → Fibrinolysis → Thromboembolism → Pulmonary embolism"
+  },
+  "nodes": [
+    {
+      "id": "DB:DB00009",
+      "name": "alteplase",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P00747",
+      "name": "Plasminogen",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0042730",
+      "name": "Fibrinolysis",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "HP:0001907",
+      "name": "Thromboembolism",
+      "label": "PhenotypicFeature"
+    },
+    {
+      "id": "MESH:D011655",
+      "name": "Pulmonary embolism",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "increased",
+      "source": "DB:DB00009",
+      "target": "UniProt:P00747",
+      "evidence": [
+        {
+          "reference": "PMID:3117481",
+          "snippet": "Tissue plasminogen activator (t-PA) is a serine protease that binds to fibrin-plasminogen complex, catalyzing the conversion of plasminogen to plasmin",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Alteplase is the recombinant t-PA product (rt-PA, Activase) reviewed here; t-PA catalyzes conversion of plasminogen to active plasmin.",
+          "source_type": "pubmed",
+          "paper": null
+        },
+        {
+          "reference": "PMID:22079561",
+          "snippet": "the main function of tPA released from the endothelium is to convert fibrin-bound plasminogen into active plasmin, thus dissolving the fibrin meshwork of blood clots",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Alteplase is recombinant human tPA; tPA converts fibrin-bound plasminogen into active plasmin.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    },
+    {
+      "key": "participates in",
+      "source": "UniProt:P00747",
+      "target": "GO:0042730",
+      "evidence": [
+        {
+          "reference": "PMID:36942151",
+          "snippet": "convert plasminogen into plasmin to initiate fiber lysis",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Plasmin, generated from plasminogen, initiates fiber (fibrin) lysis, i.e. it drives fibrinolysis.",
+          "source_type": "pubmed",
+          "paper": null
+        },
+        {
+          "reference": "PMID:3126344",
+          "snippet": "a proenzyme, plasminogen, which can be converted to the active enzyme plasmin, which will degrade fibrin",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Active plasmin derived from plasminogen degrades fibrin, the proteolytic core of fibrinolysis.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    },
+    {
+      "key": "disrupts",
+      "source": "GO:0042730",
+      "target": "HP:0001907",
+      "evidence": [
+        {
+          "reference": "PMID:36942151",
+          "snippet": "This illustrated review focuses on fibrinolysis-the degradation of blood clots or thrombi",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Fibrinolysis is the degradation of blood clots/thrombi, i.e. the process itself disrupts the thromboembolus.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    },
+    {
+      "key": "causes",
+      "source": "HP:0001907",
+      "target": "MESH:D011655",
+      "evidence": [
+        {
+          "reference": "PMID:38299563",
+          "snippet": "thrombus that detaches and lodges in the pulmonary circulation being a cause of APE",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "A thrombus that detaches and lodges in the pulmonary circulation (a thromboembolus) is the cause of acute pulmonary embolism (APE).",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://pubmed.ncbi.nlm.nih.gov/3117481/",
+      "type": "other",
+      "label": "pubmed.ncbi.nlm.nih.gov — record source"
+    },
+    {
+      "url": "https://pubmed.ncbi.nlm.nih.gov/36942151/",
+      "type": "other",
+      "label": "pubmed.ncbi.nlm.nih.gov — record source"
+    },
+    {
+      "url": "https://pubmed.ncbi.nlm.nih.gov/38299563/",
+      "type": "other",
+      "label": "pubmed.ncbi.nlm.nih.gov — record source"
+    }
+  ],
+  "site": {
+    "id": "pilot__DB00009_MESH_D011655_1__r2",
+    "record_id": "DB00009_MESH_D011655_1",
+    "run": "pilot",
+    "run_label": "Pilot run",
+    "source_file": "experiments/pilot/outputs/DB00009_MESH_D011655_1__r2.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/pilot__DB00009_MESH_D011655_1__r3.json b/web-revamp-mockup/data/records/pilot__DB00009_MESH_D011655_1__r3.json
new file mode 100644
index 0000000..1f03136
--- /dev/null
+++ b/web-revamp-mockup/data/records/pilot__DB00009_MESH_D011655_1__r3.json
@@ -0,0 +1,120 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "DB00009_MESH_D011655_1",
+    "drug": "alteplase",
+    "drug_mesh": "MESH:D010959",
+    "drugbank": "DB:DB00009",
+    "disease": "Pulmonary embolism",
+    "disease_mesh": "MESH:D011655",
+    "summary": "Alteplase → Plasmin → Fibrin → Pulmonary embolism"
+  },
+  "nodes": [
+    {
+      "id": "DB:DB00009",
+      "name": "Alteplase",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P00747",
+      "name": "Plasmin",
+      "label": "Protein"
+    },
+    {
+      "id": "MESH:D005341",
+      "name": "Fibrin",
+      "label": "ChemicalSubstance"
+    },
+    {
+      "id": "MESH:D011655",
+      "name": "Pulmonary embolism",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "increased",
+      "source": "DB:DB00009",
+      "target": "UniProt:P00747",
+      "evidence": [
+        {
+          "reference": "PMID:38297113",
+          "snippet": "Fibrin-bound tissue plasminogen activator (tPA) converts nearby plasminogen into active plasmin",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Alteplase is recombinant human tissue plasminogen activator (tPA); it converts plasminogen into active plasmin, increasing plasmin activity.",
+          "source_type": "pubmed",
+          "paper": null
+        },
+        {
+          "reference": "PMID:26447340",
+          "snippet": "The therapeutic action of tissue plasminogen activator (t-PA) is a two-step process: (1) binding to lysine-rich fibrin (Km event) and (2) converting local plasminogen into plasmin (Kcat event).",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    },
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "abundance",
+      "object_direction_qualifier": "decreased",
+      "source": "UniProt:P00747",
+      "target": "MESH:D005341",
+      "evidence": [
+        {
+          "reference": "PMID:39299257",
+          "snippet": "plasmin then converts fibrin to fibrin degradation products (FDPs)",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Plasmin proteolytically degrades fibrin into fibrin degradation products, reducing fibrin abundance.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    },
+    {
+      "key": "contributes to",
+      "source": "MESH:D005341",
+      "target": "MESH:D011655",
+      "evidence": [
+        {
+          "reference": "PMID:32368694",
+          "snippet": "deligation of suture-induced spontaneous pulmonary emboli of fibrin-rich DVT",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "explanation": "Pulmonary emboli are fibrin-rich thrombi; fibrin is the main structural component of the embolus obstructing the pulmonary vasculature.",
+          "source_type": "pubmed",
+          "paper": null
+        },
+        {
+          "reference": "PMID:8205686",
+          "snippet": "Red, fibrin-rich thrombi within the thromboendarterectomy specimens were lined with a single layer of endothelial cells exhibiting high levels of PAI-1 antigen.",
+          "supports": "PARTIAL",
+          "evidence_source": "HUMAN_CLINICAL",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00009",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    }
+  ],
+  "site": {
+    "id": "pilot__DB00009_MESH_D011655_1__r3",
+    "record_id": "DB00009_MESH_D011655_1",
+    "run": "pilot",
+    "run_label": "Pilot run",
+    "source_file": "experiments/pilot/outputs/DB00009_MESH_D011655_1__r3.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/pilot__DB00010_MESH_D004393_1.json b/web-revamp-mockup/data/records/pilot__DB00010_MESH_D004393_1.json
new file mode 100644
index 0000000..2d5b3bd
--- /dev/null
+++ b/web-revamp-mockup/data/records/pilot__DB00010_MESH_D004393_1.json
@@ -0,0 +1,131 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "DB00010_MESH_D004393_1",
+    "drug": "sermorelin",
+    "drug_mesh": "MESH:D017337",
+    "drugbank": "DB:DB00010",
+    "disease": "Pituitary dwarfism",
+    "disease_mesh": "MESH:D004393",
+    "summary": "Sermorelin → Growth hormone-releasing hormone receptor → growth hormone secretion → Pituitary dwarfism"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D017337",
+      "name": "Sermorelin",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:Q02643",
+      "name": "Growth hormone-releasing hormone receptor",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0030252",
+      "name": "growth hormone secretion",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D004393",
+      "name": "Pituitary dwarfism",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "increased",
+      "source": "MESH:D017337",
+      "target": "UniProt:Q02643",
+      "evidence": [
+        {
+          "reference": "PMID:12446584",
+          "snippet": "GHRH stimulates GH secretion from somatotroph cells of the anterior pituitary via a pathway that involves GHRH receptor activation of adenylyl cyclase and increased cAMP production.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Sermorelin is the GHRH(1-29)NH2 agonist; like native GHRH it acts by activating the GHRH receptor, triggering adenylyl cyclase and cAMP signalling.",
+          "source_type": "pubmed",
+          "paper": null
+        },
+        {
+          "reference": "PMID:6236914",
+          "snippet": "GHRH(1-29)NH2 is equipotent to GHRH(1-40); increasing doses from 10-200 micrograms per subject augments the duration of stimulated growth hormone (GH) release",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Sermorelin (GHRH(1-29)NH2) is a full GHRH-receptor agonist, equipotent to full-length GHRH in stimulating GH release.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:Q02643",
+      "target": "GO:0030252",
+      "evidence": [
+        {
+          "reference": "PMID:8395283",
+          "snippet": "The growth hormone-releasing hormone receptor (GHRHR) is a member of the family of G protein-coupled receptors that is expressed on pituitary somatotrope cells and mediates the actions of GHRH in stimulating growth hormone (GH) synthesis and secretion.",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "explanation": "The GHRH receptor is the somatotroph G-protein-coupled receptor that mediates stimulation of growth hormone secretion.",
+          "source_type": "pubmed",
+          "paper": null
+        },
+        {
+          "reference": "PMID:12446584",
+          "snippet": "GHRH stimulates GH secretion from somatotroph cells of the anterior pituitary via a pathway that involves GHRH receptor activation of adenylyl cyclase and increased cAMP production.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Activation of the GHRH receptor drives the adenylyl-cyclase/cAMP pathway that stimulates GH secretion.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "decreased",
+      "source": "GO:0030252",
+      "target": "MESH:D004393",
+      "evidence": [
+        {
+          "reference": "PMID:10549302",
+          "snippet": "We describe a recently identified new form of dwarfism due to isolated growth hormone (GH) deficiency, secondary to inactivating mutations in the GH-releasing hormone receptor (GHRHR) gene.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Pituitary dwarfism arises from deficient growth hormone secretion; adequate GH secretion therefore opposes the disease, so raising GH secretion (via sermorelin) nets to reducing dwarfism.",
+          "source_type": "pubmed",
+          "paper": null
+        },
+        {
+          "reference": "PMID:8395283",
+          "snippet": "Mice homozygous for this mutation have reduced GH secretion and a dwarf phenotype.",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "explanation": "Loss of GHRH-receptor function reduces GH secretion and produces the dwarf phenotype, confirming the inverse relationship between GH secretion and dwarfism.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00010",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    }
+  ],
+  "site": {
+    "id": "pilot__DB00010_MESH_D004393_1",
+    "record_id": "DB00010_MESH_D004393_1",
+    "run": "pilot",
+    "run_label": "Pilot run",
+    "source_file": "experiments/pilot/outputs/DB00010_MESH_D004393_1.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/pilot__DB00013_MESH_D011655_1.json b/web-revamp-mockup/data/records/pilot__DB00013_MESH_D011655_1.json
new file mode 100644
index 0000000..9211508
--- /dev/null
+++ b/web-revamp-mockup/data/records/pilot__DB00013_MESH_D011655_1.json
@@ -0,0 +1,124 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "DB00013_MESH_D011655_1",
+    "drug": "urokinase",
+    "drug_mesh": "MESH:D014568",
+    "disease": "Pulmonary thromboembolism",
+    "disease_mesh": "MESH:D011655",
+    "summary": "Urokinase → Plasminogen → Fibrin → Thrombosis → Pulmonary embolism"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D014568",
+      "name": "Urokinase",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P00747",
+      "name": "Plasminogen",
+      "label": "Protein"
+    },
+    {
+      "id": "MESH:D005341",
+      "name": "Fibrin",
+      "label": "ChemicalSubstance"
+    },
+    {
+      "id": "MESH:D013927",
+      "name": "Thrombosis",
+      "label": "Disease"
+    },
+    {
+      "id": "MESH:D011655",
+      "name": "Pulmonary embolism",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "increased",
+      "source": "MESH:D014568",
+      "target": "UniProt:P00747",
+      "evidence": [
+        {
+          "reference": "PMID:3044205",
+          "snippet": "Plasminogen activation is mediated by plasminogen activators which are classified as either tissue-type plasminogen activator (t-PA) or urokinase-type plasminogen activator (u-PA).",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Urokinase (u-PA) is a plasminogen activator that activates plasminogen, converting it to active plasmin.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    },
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "abundance",
+      "object_direction_qualifier": "decreased",
+      "source": "UniProt:P00747",
+      "target": "MESH:D005341",
+      "evidence": [
+        {
+          "reference": "PMID:3044205",
+          "snippet": "The mammalian fibrinolytic system comprises a proenzyme, plasminogen, which can be converted to the active enzyme plasmin, which will degrade fibrin.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Plasminogen, once converted to plasmin, degrades fibrin, reducing fibrin abundance.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    },
+    {
+      "key": "contributes to",
+      "source": "MESH:D005341",
+      "target": "MESH:D013927",
+      "evidence": [
+        {
+          "reference": "PMID:29225327",
+          "snippet": "Fibrin formed as a result of fibrinogen polymerization is the main protein component of a clot in a test tube and intravascular thrombi in vivo.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Fibrin is the main protein component of intravascular thrombi, contributing to thrombus formation.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    },
+    {
+      "key": "causes",
+      "source": "MESH:D013927",
+      "target": "MESH:D011655",
+      "evidence": [
+        {
+          "reference": "PMID:29798363",
+          "snippet": "is caused by deep vein thrombosis embolism pulmonary artery trunk or branch pulmonary disorder",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "A thrombus (deep vein thrombosis) that embolizes to the pulmonary artery causes pulmonary embolism.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://www.ncbi.nlm.nih.gov/mesh/68014568",
+      "type": "other",
+      "label": "ncbi.nlm.nih.gov — record source"
+    }
+  ],
+  "site": {
+    "id": "pilot__DB00013_MESH_D011655_1",
+    "record_id": "DB00013_MESH_D011655_1",
+    "run": "pilot",
+    "run_label": "Pilot run",
+    "source_file": "experiments/pilot/outputs/DB00013_MESH_D011655_1.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/pilot__DB00026_MESH_D056587_1.json b/web-revamp-mockup/data/records/pilot__DB00026_MESH_D056587_1.json
new file mode 100644
index 0000000..42a1bdf
--- /dev/null
+++ b/web-revamp-mockup/data/records/pilot__DB00026_MESH_D056587_1.json
@@ -0,0 +1,121 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "DB00026_MESH_D056587_1",
+    "drug": "anakinra",
+    "drug_mesh": "MESH:D053590",
+    "drugbank": "DB:DB00026",
+    "disease": "Cryopyrin-associated periodic syndrome",
+    "disease_mesh": "MESH:D056587",
+    "summary": "anakinra → Interleukin-1 receptor type 1 → inflammatory response → Cryopyrin-associated periodic syndrome"
+  },
+  "nodes": [
+    {
+      "id": "DB:DB00026",
+      "name": "anakinra",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P14778",
+      "name": "Interleukin-1 receptor type 1",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0006954",
+      "name": "inflammatory response",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D056587",
+      "name": "Cryopyrin-associated periodic syndrome",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "DB:DB00026",
+      "target": "UniProt:P14778",
+      "evidence": [
+        {
+          "reference": "PMID:27790031",
+          "snippet": "Anakinra is an interleukin (IL) receptor antagonist that works by blocking the biological activity of IL-1 by competitively inhibiting binding of IL-1 to the type 1 interleukin receptor.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Anakinra competitively inhibits binding of IL-1 to the type 1 IL-1 receptor, decreasing the receptor's signaling activity.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P14778",
+      "target": "GO:0006954",
+      "evidence": [
+        {
+          "reference": "PMID:26140469",
+          "snippet": "IL-1 inhibitors block the IL-1 signaling cascade, thereby preventing systemic inflammation in CAPS.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Signaling through the IL-1 receptor (the IL-1 signaling cascade) drives the systemic inflammation of CAPS; blocking it prevents that inflammation.",
+          "source_type": "pubmed",
+          "paper": null
+        },
+        {
+          "reference": "PMID:31524632",
+          "snippet": "IL-1α and IL-1β are upstream components of a signaling pathway, including IL-1R1 and downstream SPDEF and ERN2, that generate a positive feedback cycle capable of producing persistent mucus hyperconcentration and IL-1α and/or IL-1β-mediated neutrophilic inflammation in the absence of infection in CF airways.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "IL-1R1 is named as the signaling receptor within the IL-1 pathway that produces IL-1-mediated inflammation.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    },
+    {
+      "key": "causes",
+      "source": "GO:0006954",
+      "target": "MESH:D056587",
+      "evidence": [
+        {
+          "reference": "PMID:22288581",
+          "snippet": "Both CAPS and FMF are characterized by increased inflammasome activity and overproduction of IL-1β which is ultimately responsible for disease manifestations.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "IL-1β-driven inflammation is ultimately responsible for the clinical manifestations of CAPS.",
+          "source_type": "pubmed",
+          "paper": null
+        },
+        {
+          "reference": "PMID:26140469",
+          "snippet": "It is not only a pro-inflammatory cytokine responsible for features such as fever, rash, and arthritis, but is also a major mediator in the central pathways of fatigue.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "IL-1-driven inflammation is responsible for the characteristic CAPS features of fever, rash, and arthritis.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00026",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    }
+  ],
+  "site": {
+    "id": "pilot__DB00026_MESH_D056587_1",
+    "record_id": "DB00026_MESH_D056587_1",
+    "run": "pilot",
+    "run_label": "Pilot run",
+    "source_file": "experiments/pilot/outputs/DB00026_MESH_D056587_1.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/pilot__DB00030_MESH_D003922_1.json b/web-revamp-mockup/data/records/pilot__DB00030_MESH_D003922_1.json
new file mode 100644
index 0000000..860c5c9
--- /dev/null
+++ b/web-revamp-mockup/data/records/pilot__DB00030_MESH_D003922_1.json
@@ -0,0 +1,148 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "DB00030_MESH_D003922_1",
+    "drug": "insulin human",
+    "drug_mesh": "MESH:D007328",
+    "drugbank": "DB:DB00030",
+    "disease": "Diabetes Mellitus, Type 1",
+    "disease_mesh": "MESH:D003922",
+    "summary": "insulin human → Insulin receptor → glucose import → Hyperglycemia → Diabetes Mellitus, Type 1"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D007328",
+      "name": "insulin human",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P06213",
+      "name": "Insulin receptor",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0046323",
+      "name": "glucose import",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "HP:0003074",
+      "name": "Hyperglycemia",
+      "label": "PhenotypicFeature"
+    },
+    {
+      "id": "MESH:D003922",
+      "name": "Diabetes Mellitus, Type 1",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "increased",
+      "source": "MESH:D007328",
+      "target": "UniProt:P06213",
+      "evidence": [
+        {
+          "reference": "PMID:9932214",
+          "snippet": "The binding of insulin to its receptor induces autophosphorylation of the receptor on tyrosine residues and thereby stimulates its tyrosine kinase activity towards intracellular substrates such as Shc or IRS1.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Insulin binding activates the insulin receptor tyrosine kinase.",
+          "source_type": "pubmed",
+          "paper": null
+        },
+        {
+          "reference": "PMID:20526383",
+          "snippet": "Insulin action involves a series of signaling cascades initiated by insulin binding to its receptor, eliciting receptor autophosphorylation and activation of the receptor tyrosine kinase, resulting in tyrosine phosphorylation of insulin receptor substrates (IRSs).",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P06213",
+      "target": "GO:0046323",
+      "evidence": [
+        {
+          "reference": "PMID:20526383",
+          "snippet": "Phosphorylation of IRSs leads to activation of phosphatidylinositol 3-kinase (PI3K) and, subsequently, to activation of Akt and its downstream mediator AS160, all of which are important steps for stimulating glucose transport induced by insulin.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "The insulin-receptor-initiated signaling cascade stimulates cellular glucose transport/uptake.",
+          "source_type": "pubmed",
+          "paper": null
+        },
+        {
+          "reference": "PMID:9932214",
+          "snippet": "is involved in several of the metabolic effects of the hormone, such as glucose transport, glycolysis and glycogen synthesis.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "decreased",
+      "source": "GO:0046323",
+      "target": "HP:0003074",
+      "evidence": [
+        {
+          "reference": "PMID:12542844",
+          "snippet": "Increased glucose disposal by tissues engineered to overexpress key regulatory genes in glucose transport or phosphorylation can reduce diabetic hyperglycemia.",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "explanation": "Increased cellular glucose uptake/disposal lowers hyperglycemia.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    },
+    {
+      "key": "manifestation of",
+      "source": "HP:0003074",
+      "target": "MESH:D003922",
+      "evidence": [
+        {
+          "reference": "PMID:39918671",
+          "snippet": "Type 1 diabetes (T1D) is a chronic autoimmune disorder characterized by the destruction of insulin-producing beta cells in the pancreas, leading to insulin deficiency and chronic hyperglycemia.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "source_type": "pubmed",
+          "paper": null
+        },
+        {
+          "reference": "PMID:39211721",
+          "snippet": "Type 1 diabetes is an autoimmune disorder characterized by the destruction of pancreatic beta cells, leading to insulin deficiency and hyperglycemia.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00030",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    }
+  ],
+  "site": {
+    "id": "pilot__DB00030_MESH_D003922_1",
+    "record_id": "DB00030_MESH_D003922_1",
+    "run": "pilot",
+    "run_label": "Pilot run",
+    "source_file": "experiments/pilot/outputs/DB00030_MESH_D003922_1.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/pilot__DB00035_MESH_D006467_1.json b/web-revamp-mockup/data/records/pilot__DB00035_MESH_D006467_1.json
new file mode 100644
index 0000000..9bf34d0
--- /dev/null
+++ b/web-revamp-mockup/data/records/pilot__DB00035_MESH_D006467_1.json
@@ -0,0 +1,185 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "DB00035_MESH_D006467_1",
+    "drug": "desmopressin",
+    "drug_mesh": "MESH:D003894",
+    "drugbank": "DB:DB00035",
+    "disease": "Hereditary factor VIII deficiency disease",
+    "disease_mesh": "MESH:D006467",
+    "summary": "desmopressin → Arginine vasopressin receptor 2 → von Willebrand factor → Coagulation factor VIII → Hereditary factor VIII deficiency disease"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D003894",
+      "name": "desmopressin",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P30518",
+      "name": "Arginine vasopressin receptor 2",
+      "label": "Protein"
+    },
+    {
+      "id": "UniProt:P04275",
+      "name": "von Willebrand factor",
+      "label": "Protein"
+    },
+    {
+      "id": "UniProt:P00451",
+      "name": "Coagulation factor VIII",
+      "label": "Protein"
+    },
+    {
+      "id": "MESH:D006467",
+      "name": "Hereditary factor VIII deficiency disease",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "increased",
+      "source": "MESH:D003894",
+      "target": "UniProt:P30518",
+      "evidence": [
+        {
+          "reference": "PMID:8232694",
+          "snippet": "the selective V2-vasopressin receptor agonist 1-desamino-8-D-arginine vasopressin (DDAVP, 400 ng/kg in 10 min)",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Desmopressin (DDAVP) is a selective agonist of the vasopressin V2 receptor, activating the receptor.",
+          "source_type": "pubmed",
+          "paper": null
+        },
+        {
+          "reference": "PMID:12871401",
+          "snippet": "a direct action on the endothelium, via activation of endothelial vasopressin V2R receptor and cAMP-mediated signaling",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "DDAVP acts via activation of the endothelial vasopressin V2 receptor.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Cellular mechanisms of the hemostatic effects of desmopressin (DDAVP).",
+            "authors": [
+              "Kaufmann JE",
+              "Vischer UM"
+            ],
+            "journal": "Journal of thrombosis and haemostasis : JTH",
+            "year": "2003",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "abundance",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P30518",
+      "target": "UniProt:P04275",
+      "evidence": [
+        {
+          "reference": "PMID:12871401",
+          "snippet": "activation of endothelial vasopressin V2R receptor and cAMP-mediated signaling. This leads to exocytosis from Weibel Palade bodies where both VWF and t-PA are stored",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "V2 receptor activation drives exocytosis of Weibel-Palade bodies, releasing stored von Willebrand factor and raising its plasma level.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Cellular mechanisms of the hemostatic effects of desmopressin (DDAVP).",
+            "authors": [
+              "Kaufmann JE",
+              "Vischer UM"
+            ],
+            "journal": "Journal of thrombosis and haemostasis : JTH",
+            "year": "2003",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "abundance",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P04275",
+      "target": "UniProt:P00451",
+      "evidence": [
+        {
+          "reference": "PMID:16150043",
+          "snippet": "von Willebrand factor (VWF), the natural stabilizing carrier protein of FVIII",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "von Willebrand factor is the stabilizing carrier of factor VIII, prolonging its half-life and thereby increasing circulating factor VIII abundance.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Extra-hepatic factor VIII expression in porcine fulminant hepatic failure.",
+            "authors": [
+              "Hollestelle MJ",
+              "Poyck PP",
+              "Hollestelle JM",
+              "Marsman HA",
+              "Mourik JA",
+              "Gulik TM"
+            ],
+            "journal": "Journal of thrombosis and haemostasis : JTH",
+            "year": "2005",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "negatively correlated with",
+      "source": "UniProt:P00451",
+      "target": "MESH:D006467",
+      "evidence": [
+        {
+          "reference": "PMID:34349063",
+          "snippet": "FVIII deficiency causes hemophilia A",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Deficiency of factor VIII causes the disease (hemophilia A / hereditary factor VIII deficiency); factor VIII levels are inversely related to disease severity, so raising factor VIII counters the deficiency.",
+          "source_type": "pubmed",
+          "paper": null
+        },
+        {
+          "reference": "PMID:32248973",
+          "snippet": "for which deficiency results in the bleeding disorder hemophilia A",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Factor VIII deficiency results in hemophilia A; restoring factor VIII opposes the disease state.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00035",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    }
+  ],
+  "site": {
+    "id": "pilot__DB00035_MESH_D006467_1",
+    "record_id": "DB00035_MESH_D006467_1",
+    "run": "pilot",
+    "run_label": "Pilot run",
+    "source_file": "experiments/pilot/outputs/DB00035_MESH_D006467_1.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/pilot__DB00038_MESH_D013921_1.json b/web-revamp-mockup/data/records/pilot__DB00038_MESH_D013921_1.json
new file mode 100644
index 0000000..7b07b44
--- /dev/null
+++ b/web-revamp-mockup/data/records/pilot__DB00038_MESH_D013921_1.json
@@ -0,0 +1,142 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "DB00038_MESH_D013921_1",
+    "drug": "oprelvekin",
+    "drug_mesh": "MESH:C105308",
+    "drugbank": "DB:DB00038",
+    "disease": "Thrombocytopenic disorder",
+    "disease_mesh": "MESH:D013921",
+    "summary": "oprelvekin → Interleukin-11 receptor subunit alpha → megakaryocyte differentiation → platelet formation → Thrombocytopenic disorder"
+  },
+  "nodes": [
+    {
+      "id": "DB:DB00038",
+      "name": "oprelvekin",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:Q14626",
+      "name": "Interleukin-11 receptor subunit alpha",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0030219",
+      "name": "megakaryocyte differentiation",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "GO:0030220",
+      "name": "platelet formation",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D013921",
+      "name": "Thrombocytopenic disorder",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "increased",
+      "source": "DB:DB00038",
+      "target": "UniProt:Q14626",
+      "evidence": [
+        {
+          "reference": "PMID:12919066",
+          "snippet": "IL-11 signalling is dependent on the formation of a tripartite ligand-receptor complex consisting of IL-11, the IL-11R (IL-11 receptor) alpha subunit (responsible for the specificity of the interaction) and gp130 (glycoprotein 130) receptor beta subunit (responsible for signal transduction).",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Oprelvekin is recombinant human interleukin-11 (IL-11); its binding to the IL-11 receptor alpha subunit forms the signalling complex that activates receptor signal transduction.",
+          "source_type": "pubmed",
+          "paper": null
+        },
+        {
+          "reference": "PMID:26551279",
+          "snippet": "A pre-requisite for signal transduction is the initial binding of the cytokines to their unique α-receptors, IL-6R and IL-11R.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:Q14626",
+      "target": "GO:0030219",
+      "evidence": [
+        {
+          "reference": "PMID:9354656",
+          "snippet": "We determined that MKs can be direct targets of rhIL-11 by showing the expression of functional IL-11 receptor on these cells.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Megakaryocytes express a functional IL-11 receptor, making receptor-alpha signalling the direct mediator of rhIL-11-induced megakaryocytopoiesis.",
+          "source_type": "pubmed",
+          "paper": null
+        },
+        {
+          "reference": "PMID:9354656",
+          "snippet": "After a short exposure of purified BM MKs to rhIL-11, enhanced phosphorylation of both its signal transduction subunit, gp130, and the transcription factor, STAT3 was detected, showing a direct activation of receptor signaling by the cytokine.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Activation of IL-11 receptor signalling (gp130/STAT3) in megakaryocytes directly promotes megakaryocytopoiesis/megakaryocyte differentiation.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "GO:0030219",
+      "target": "GO:0030220",
+      "evidence": [
+        {
+          "reference": "PMID:34943811",
+          "snippet": "platelets are released in the circulation by mature megakaryocytes generated by hematopoietic stem cells by giving rise to lineage-restricted progenitor cells and then to morphologically recognizable megakaryocyte precursors, which undergo a process of terminal maturation.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Terminal maturation/differentiation of megakaryocytes is what produces (releases) platelets.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    },
+    {
+      "key": "negatively correlated with",
+      "source": "GO:0030220",
+      "target": "MESH:D013921",
+      "evidence": [
+        {
+          "reference": "PMID:6683869",
+          "snippet": "the pathogenesis of thrombocytopenia can be due not only to the peripheral destruction of platelets, but also to a deficient platelet production by megakaryocytes.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Deficient platelet production (impaired platelet formation) causes thrombocytopenia, so platelet formation is inversely related to the disorder; oprelvekin's stimulation of platelet formation therefore suppresses the thrombocytopenic disorder.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00038",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    }
+  ],
+  "site": {
+    "id": "pilot__DB00038_MESH_D013921_1",
+    "record_id": "DB00038_MESH_D013921_1",
+    "run": "pilot",
+    "run_label": "Pilot run",
+    "source_file": "experiments/pilot/outputs/DB00038_MESH_D013921_1.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/pilot__DB00152_MESH_D001361_1.json b/web-revamp-mockup/data/records/pilot__DB00152_MESH_D001361_1.json
new file mode 100644
index 0000000..0aec86c
--- /dev/null
+++ b/web-revamp-mockup/data/records/pilot__DB00152_MESH_D001361_1.json
@@ -0,0 +1,58 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "DB00152_MESH_D001361_1",
+    "drug": "Thiamine",
+    "drug_mesh": "MESH:D013831",
+    "drugbank": "DB:DB00152",
+    "disease": "Avitaminosis",
+    "disease_mesh": "MESH:D001361",
+    "summary": "Thiamine → Avitaminosis"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D013831",
+      "name": "Thiamine",
+      "label": "Drug"
+    },
+    {
+      "id": "MESH:D001361",
+      "name": "Avitaminosis",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "treats",
+      "source": "MESH:D013831",
+      "target": "MESH:D001361",
+      "evidence": [
+        {
+          "reference": "PMID:19892133",
+          "snippet": "the therapeutic benefits of thiamin for Wernicke-Korsakoff syndrome and beriberi were demonstrated.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Historical/review narrative (Handbook of Clinical Neurology), not a primary clinical study, hence evidence_source OTHER. Thiamine is a replacement therapy whose mode of action is vitamin repletion. The assigned disease node is Avitaminosis (MESH:D001361); thiamine treats specifically the thiamine-deficiency avitaminoses (beriberi, Wernicke-Korsakoff syndrome), a subtype of avitaminosis, and cannot be narrowed further because the curated (drug, disease) pair fixes MESH:D001361. No downstream molecular mechanism distinct from replacement of the depleted vitamin can be sourced for this indication.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://www.ncbi.nlm.nih.gov/pubmed/19892133",
+      "type": "other",
+      "label": "ncbi.nlm.nih.gov — record source"
+    }
+  ],
+  "site": {
+    "id": "pilot__DB00152_MESH_D001361_1",
+    "record_id": "DB00152_MESH_D001361_1",
+    "run": "pilot",
+    "run_label": "Pilot run",
+    "source_file": "experiments/pilot/outputs/DB00152_MESH_D001361_1.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/pilot__DB00152_MESH_D001361_1__r2.json b/web-revamp-mockup/data/records/pilot__DB00152_MESH_D001361_1__r2.json
new file mode 100644
index 0000000..31d7fd8
--- /dev/null
+++ b/web-revamp-mockup/data/records/pilot__DB00152_MESH_D001361_1__r2.json
@@ -0,0 +1,128 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "DB00152_MESH_D001361_1",
+    "drug": "Thiamine",
+    "drug_mesh": "MESH:D013831",
+    "drugbank": "DB:DB00152",
+    "disease": "Avitaminosis",
+    "disease_mesh": "MESH:D001361",
+    "summary": "Thiamine → Thiamine pyrophosphate → Transketolase → Carbohydrate metabolism → Avitaminosis"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D013831",
+      "name": "Thiamine",
+      "label": "Drug"
+    },
+    {
+      "id": "MESH:D013835",
+      "name": "Thiamine pyrophosphate",
+      "label": "ChemicalSubstance"
+    },
+    {
+      "id": "UniProt:P29401",
+      "name": "Transketolase",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0005975",
+      "name": "Carbohydrate metabolism",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D001361",
+      "name": "Avitaminosis",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "has metabolite",
+      "source": "MESH:D013831",
+      "target": "MESH:D013835",
+      "evidence": [
+        {
+          "reference": "PMID:21288652",
+          "snippet": "Once thiamine enters the cells it is phosphorylated by thiamine pyrophosphokinase (TPPK), and converted into the coenzyme thiamine pyrophosphate (TPP), the active form of thiamine.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Thiamine is phosphorylated intracellularly and converted into its active metabolite, thiamine pyrophosphate.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    },
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "increased",
+      "source": "MESH:D013835",
+      "target": "UniProt:P29401",
+      "evidence": [
+        {
+          "reference": "PMID:21288652",
+          "snippet": "TPP is a relevant cofactor for transketolase (TK), α-ketoglutarate dehydrogenase (αKDH), and pyruvate dehydrogenase (PDH), all these enzymes are fundamental for glucose metabolism.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Thiamine pyrophosphate serves as the coenzyme/cofactor required for transketolase activity.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    },
+    {
+      "key": "participates in",
+      "source": "UniProt:P29401",
+      "target": "GO:0005975",
+      "evidence": [
+        {
+          "reference": "PMID:21288652",
+          "snippet": "TPP is a relevant cofactor for transketolase (TK), α-ketoglutarate dehydrogenase (αKDH), and pyruvate dehydrogenase (PDH), all these enzymes are fundamental for glucose metabolism.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Transketolase is one of the thiamine-dependent enzymes fundamental for glucose/carbohydrate metabolism.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    },
+    {
+      "key": "negatively correlated with",
+      "source": "GO:0005975",
+      "target": "MESH:D001361",
+      "evidence": [
+        {
+          "reference": "PMID:27440134",
+          "snippet": "Thiamine is an essential cofactor in carbohydrate metabolism, and deficiency can therefore cause various organ dysfunctions.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Functional thiamine-dependent carbohydrate metabolism is inversely related to the deficiency disease: it is the loss/impairment of this metabolism when thiamine is deficient (avitaminosis) that produces the organ dysfunctions constituting the disease.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://pubmed.ncbi.nlm.nih.gov/21288652/",
+      "type": "other",
+      "label": "pubmed.ncbi.nlm.nih.gov — record source"
+    },
+    {
+      "url": "https://pubmed.ncbi.nlm.nih.gov/27440134/",
+      "type": "other",
+      "label": "pubmed.ncbi.nlm.nih.gov — record source"
+    }
+  ],
+  "site": {
+    "id": "pilot__DB00152_MESH_D001361_1__r2",
+    "record_id": "DB00152_MESH_D001361_1",
+    "run": "pilot",
+    "run_label": "Pilot run",
+    "source_file": "experiments/pilot/outputs/DB00152_MESH_D001361_1__r2.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/pilot__DB00152_MESH_D001361_1__r3.json b/web-revamp-mockup/data/records/pilot__DB00152_MESH_D001361_1__r3.json
new file mode 100644
index 0000000..a3f0e33
--- /dev/null
+++ b/web-revamp-mockup/data/records/pilot__DB00152_MESH_D001361_1__r3.json
@@ -0,0 +1,102 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "DB00152_MESH_D001361_1",
+    "drug": "thiamine",
+    "drug_mesh": "MESH:D013831",
+    "drugbank": "DB:DB00152",
+    "disease": "Avitaminosis",
+    "disease_mesh": "MESH:D001361",
+    "summary": "Thiamine → Thiamine pyrophosphate → Transketolase activity → Avitaminosis"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D013831",
+      "name": "Thiamine",
+      "label": "Drug"
+    },
+    {
+      "id": "MESH:D013835",
+      "name": "Thiamine pyrophosphate",
+      "label": "ChemicalSubstance"
+    },
+    {
+      "id": "GO:0004802",
+      "name": "Transketolase activity",
+      "label": "MolecularActivity"
+    },
+    {
+      "id": "MESH:D001361",
+      "name": "Avitaminosis",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "has metabolite",
+      "source": "MESH:D013831",
+      "target": "MESH:D013835",
+      "evidence": [
+        {
+          "reference": "PMID:39470204",
+          "snippet": "Thiamine is metabolized into thiamine pyrophosphate (TPP), an essential enzyme cofactor.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Thiamine is the precursor metabolized to its active coenzyme form, thiamine pyrophosphate (TPP); repletion with thiamine raises TPP, the vitamin form whose depletion defines the thiamine-deficiency state.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    },
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "increased",
+      "source": "MESH:D013835",
+      "target": "GO:0004802",
+      "evidence": [
+        {
+          "reference": "PMID:22152682",
+          "snippet": "Thiamine pyrophosphate (TPP) is an essential cofactor of the cytosolic transketolase and of three mitochondrial enzymes involved in the oxidative decarboxylation of either pyruvate, α-ketoglutarate or branched chain amino acids.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "TPP is the essential coenzyme required for transketolase and the TPP-dependent dehydrogenases; supplying TPP increases their catalytic activity.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    },
+    {
+      "key": "negatively correlated with",
+      "source": "GO:0004802",
+      "target": "MESH:D001361",
+      "evidence": [
+        {
+          "reference": "PMID:38696890",
+          "snippet": "Deficiency for thiamine (vitamin B1), traditionally assessed via the activity of the thiamine-dependent enzyme erythrocyte transketolase",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Erythrocyte transketolase activity is the classic functional index of thiamine status and is inversely related to the thiamine-deficiency state (a form of avitaminosis); low transketolase activity marks the deficiency and rises when thiamine is repleted.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00152",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    }
+  ],
+  "site": {
+    "id": "pilot__DB00152_MESH_D001361_1__r3",
+    "record_id": "DB00152_MESH_D001361_1",
+    "run": "pilot",
+    "run_label": "Pilot run",
+    "source_file": "experiments/pilot/outputs/DB00152_MESH_D001361_1__r3.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/pilot__DB00258_MESH_D006996_1.json b/web-revamp-mockup/data/records/pilot__DB00258_MESH_D006996_1.json
new file mode 100644
index 0000000..cffb955
--- /dev/null
+++ b/web-revamp-mockup/data/records/pilot__DB00258_MESH_D006996_1.json
@@ -0,0 +1,86 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "DB00258_MESH_D006996_1",
+    "drug": "calcium acetate",
+    "drug_mesh": "MESH:C120662",
+    "drugbank": "DB:DB00258",
+    "disease": "Hypocalcemia",
+    "disease_mesh": "MESH:D006996",
+    "summary": "calcium acetate → Calcium → Hypocalcemia"
+  },
+  "nodes": [
+    {
+      "id": "MESH:C120662",
+      "name": "calcium acetate",
+      "label": "Drug"
+    },
+    {
+      "id": "MESH:D002118",
+      "name": "Calcium",
+      "label": "ChemicalSubstance"
+    },
+    {
+      "id": "MESH:D006996",
+      "name": "Hypocalcemia",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "abundance",
+      "object_direction_qualifier": "increased",
+      "source": "MESH:C120662",
+      "target": "MESH:D002118",
+      "evidence": [
+        {
+          "reference": "PMID:23625273",
+          "snippet": "The average daily dose of calcium acetate or carbonate prescribed in the randomised controlled trials to control hyperphosphataemia in dialysis patients ranges between 1.2 and 2.3 g of elemental calcium. Such doses are greater than the recommended dietary calcium intake and can lead to a positive calcium balance.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Calcium acetate delivers elemental calcium and, at typical doses, produces a positive calcium balance, i.e., it increases the amount of calcium in the body.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    },
+    {
+      "key": "negatively correlated with",
+      "source": "MESH:D002118",
+      "target": "MESH:D006996",
+      "evidence": [
+        {
+          "reference": "PMID:30551988",
+          "snippet": "The goal of the clinical management of hypoparathyroidism is to correct acute and chronic hypocalcemia....The treatment cornerstones of chronic hypoparathyroidism are oral supplementation of calcium and/or active vitamin D",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Supplying calcium corrects hypocalcemia; increasing available calcium is inversely related to the low-serum-calcium disease state.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://www.ncbi.nlm.nih.gov/pubmed/23625273",
+      "type": "other",
+      "label": "ncbi.nlm.nih.gov — record source"
+    },
+    {
+      "url": "https://www.ncbi.nlm.nih.gov/pubmed/30551988",
+      "type": "other",
+      "label": "ncbi.nlm.nih.gov — record source"
+    }
+  ],
+  "site": {
+    "id": "pilot__DB00258_MESH_D006996_1",
+    "record_id": "DB00258_MESH_D006996_1",
+    "run": "pilot",
+    "run_label": "Pilot run",
+    "source_file": "experiments/pilot/outputs/DB00258_MESH_D006996_1.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/pilot__DB00290_MESH_D002294_1.json b/web-revamp-mockup/data/records/pilot__DB00290_MESH_D002294_1.json
new file mode 100644
index 0000000..a3b5499
--- /dev/null
+++ b/web-revamp-mockup/data/records/pilot__DB00290_MESH_D002294_1.json
@@ -0,0 +1,123 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "DB00290_MESH_D002294_1",
+    "drug": "bleomycin",
+    "drug_mesh": "MESH:D001761",
+    "drugbank": "DB:DB00290",
+    "disease": "Squamous cell carcinoma",
+    "disease_mesh": "MESH:D002294",
+    "summary": "bleomycin → Reactive oxygen species → DNA damage → apoptotic process → Squamous cell carcinoma"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D001761",
+      "name": "bleomycin",
+      "label": "Drug"
+    },
+    {
+      "id": "MESH:D017382",
+      "name": "Reactive oxygen species",
+      "label": "ChemicalSubstance"
+    },
+    {
+      "id": "MESH:D004249",
+      "name": "DNA damage",
+      "label": "ChemicalSubstance"
+    },
+    {
+      "id": "GO:0006915",
+      "name": "apoptotic process",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D002294",
+      "name": "Squamous cell carcinoma",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "abundance",
+      "object_direction_qualifier": "increased",
+      "source": "MESH:D001761",
+      "target": "MESH:D017382",
+      "evidence": [
+        {
+          "reference": "PMID:18234257",
+          "snippet": "Bleomycin (BLM) has been found to induce 8-oxoguanine and DNA strand breaks through producing oxidative free radicals",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Bleomycin generates oxidative free radicals (reactive oxygen species) inside tumor cells.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    },
+    {
+      "key": "causes",
+      "source": "MESH:D017382",
+      "target": "MESH:D004249",
+      "evidence": [
+        {
+          "reference": "PMID:37491116",
+          "snippet": "reactive oxygen species (ROS) are important mediators of Pt- and BLM-induced DNA damage",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Reactive oxygen species mediate the DNA damage produced by bleomycin (BLM).",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    },
+    {
+      "key": "causes",
+      "source": "MESH:D004249",
+      "target": "GO:0006915",
+      "evidence": [
+        {
+          "reference": "PMID:17879944",
+          "snippet": "Bleomycin induces single- and double-stranded breaks in DNA, with consequent mitochondrial membrane aberrations that lead to the apoptotic cell death.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Bleomycin-induced DNA strand breaks (DNA damage) trigger the apoptotic cell death program in human squamous carcinoma cells.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    },
+    {
+      "key": "disrupts",
+      "source": "GO:0006915",
+      "target": "MESH:D002294",
+      "evidence": [
+        {
+          "reference": "PMID:28459216",
+          "snippet": "combating oral cancer through targeting self-renewability of orospheres via reactive oxygen species-mediated apoptosis",
+          "supports": "PARTIAL",
+          "evidence_source": "IN_VITRO",
+          "explanation": "The apoptotic process is the named effector that combats (disrupts) oral squamous cell carcinoma by eliminating its neoplastic cells. Marked PARTIAL because the direct evidence is for the oral SCC subtype, whereas the edge object is squamous cell carcinoma generally.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00290",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    }
+  ],
+  "site": {
+    "id": "pilot__DB00290_MESH_D002294_1",
+    "record_id": "DB00290_MESH_D002294_1",
+    "run": "pilot",
+    "run_label": "Pilot run",
+    "source_file": "experiments/pilot/outputs/DB00290_MESH_D002294_1.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/pilot__DB00619_MESH_D015464_1.json b/web-revamp-mockup/data/records/pilot__DB00619_MESH_D015464_1.json
new file mode 100644
index 0000000..5907a24
--- /dev/null
+++ b/web-revamp-mockup/data/records/pilot__DB00619_MESH_D015464_1.json
@@ -0,0 +1,103 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "DB00619_MESH_D015464_1",
+    "drug": "imatinib",
+    "drug_mesh": "MESH:D000068877",
+    "drugbank": "DB:DB00619",
+    "disease": "Chronic myeloid leukemia",
+    "disease_mesh": "MESH:D015464",
+    "summary": "imatinib → BCR/ABL fusion protein → cell population proliferation → Chronic myeloid leukemia"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D000068877",
+      "name": "imatinib",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:A9UF07",
+      "name": "BCR/ABL fusion protein",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0008283",
+      "name": "cell population proliferation",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D015464",
+      "name": "Chronic myeloid leukemia",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D000068877",
+      "target": "UniProt:A9UF07",
+      "evidence": [
+        {
+          "reference": "PMID:38627294",
+          "snippet": "Imatinib mesylate was the first representative BCR-ABL1 tyrosine kinase inhibitor (TKI) class for the treatment of chronic myeloid leukemia.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Imatinib is a BCR-ABL1 tyrosine kinase inhibitor, i.e. it decreases the activity of the BCR-ABL fusion kinase.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:A9UF07",
+      "target": "GO:0008283",
+      "evidence": [
+        {
+          "reference": "PMID:42174092",
+          "snippet": "This alteration gives rise to the BCR::ABL1 fusion oncogene, whose constitutive tyrosine kinase activity promotes uncontrolled proliferation and survival of leukemic cells.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "The constitutive tyrosine kinase activity of the BCR-ABL fusion promotes uncontrolled proliferation of leukemic cells.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    },
+    {
+      "key": "manifestation of",
+      "source": "GO:0008283",
+      "target": "MESH:D015464",
+      "evidence": [
+        {
+          "reference": "PMID:41353321",
+          "snippet": "Chronic myeloid leukemia (CML) is a myeloproliferative malignancy marked through the excessive proliferative growth of functional myeloid cells.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Excessive proliferative growth of myeloid cells is the defining manifestation of CML.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00619",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    }
+  ],
+  "site": {
+    "id": "pilot__DB00619_MESH_D015464_1",
+    "record_id": "DB00619_MESH_D015464_1",
+    "run": "pilot",
+    "run_label": "Pilot run",
+    "source_file": "experiments/pilot/outputs/DB00619_MESH_D015464_1.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/pilot__DB00619_MESH_D015464_1__r2.json b/web-revamp-mockup/data/records/pilot__DB00619_MESH_D015464_1__r2.json
new file mode 100644
index 0000000..5aea9e5
--- /dev/null
+++ b/web-revamp-mockup/data/records/pilot__DB00619_MESH_D015464_1__r2.json
@@ -0,0 +1,86 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "DB00619_MESH_D015464_1",
+    "drug": "imatinib",
+    "drug_mesh": "MESH:D000068877",
+    "drugbank": "DB:DB00619",
+    "disease": "Chronic myeloid leukemia, BCR-ABL positive",
+    "disease_mesh": "MESH:D015464",
+    "summary": "imatinib → BCR/ABL fusion protein → Chronic myeloid leukemia, BCR-ABL positive"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D000068877",
+      "name": "imatinib",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:A9UF07",
+      "name": "BCR/ABL fusion protein",
+      "label": "Protein"
+    },
+    {
+      "id": "MESH:D015464",
+      "name": "Chronic myeloid leukemia, BCR-ABL positive",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D000068877",
+      "target": "UniProt:A9UF07",
+      "evidence": [
+        {
+          "reference": "PMID:12663457",
+          "snippet": "The tyrosine kinase inhibitor STI571 (imatinib) binds competitively to the adenosine triphosphate (ATP) binding site of the ABL kinase, thereby inhibiting auto- and substrate phosphorylation of the oncogenic protein BCR-ABL and preventing the activation of downstream signaling pathways.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "STI571 is the developmental name for imatinib; the sentence states it binds the ATP site of the ABL kinase and inhibits phosphorylation of BCR-ABL.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    },
+    {
+      "key": "causes",
+      "source": "UniProt:A9UF07",
+      "target": "MESH:D015464",
+      "evidence": [
+        {
+          "reference": "PMID:32711219",
+          "snippet": "Chronic myeloid leukemia (CML) is a kind of myeloproliferative disorder caused by a constitutively active BCR-ABL tyrosine kinase.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Background disease-mechanism statement establishing constitutively active BCR-ABL as the cause of CML.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://pubmed.ncbi.nlm.nih.gov/12663457/",
+      "type": "other",
+      "label": "pubmed.ncbi.nlm.nih.gov — record source"
+    },
+    {
+      "url": "https://pubmed.ncbi.nlm.nih.gov/32711219/",
+      "type": "other",
+      "label": "pubmed.ncbi.nlm.nih.gov — record source"
+    }
+  ],
+  "site": {
+    "id": "pilot__DB00619_MESH_D015464_1__r2",
+    "record_id": "DB00619_MESH_D015464_1",
+    "run": "pilot",
+    "run_label": "Pilot run",
+    "source_file": "experiments/pilot/outputs/DB00619_MESH_D015464_1__r2.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/pilot__DB00619_MESH_D015464_1__r3.json b/web-revamp-mockup/data/records/pilot__DB00619_MESH_D015464_1__r3.json
new file mode 100644
index 0000000..3d14b08
--- /dev/null
+++ b/web-revamp-mockup/data/records/pilot__DB00619_MESH_D015464_1__r3.json
@@ -0,0 +1,109 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "DB00619_MESH_D015464_1",
+    "drug": "imatinib",
+    "drug_mesh": "MESH:D000068877",
+    "drugbank": "DB:DB00619",
+    "disease": "Chronic myelogenous leukemia, BCR-ABL positive",
+    "disease_mesh": "MESH:D015464",
+    "summary": "imatinib → BCR/ABL fusion protein → Leukemia, Myelogenous, Chronic, BCR-ABL Positive"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D000068877",
+      "name": "imatinib",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:A9UF07",
+      "name": "BCR/ABL fusion protein",
+      "label": "Protein"
+    },
+    {
+      "id": "MESH:D015464",
+      "name": "Leukemia, Myelogenous, Chronic, BCR-ABL Positive",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D000068877",
+      "target": "UniProt:A9UF07",
+      "evidence": [
+        {
+          "reference": "PMID:12200353",
+          "snippet": "Imatinib is an orally administered, potent inhibitor of the Bcr-Abl tyrosine kinase.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    },
+    {
+      "key": "causes",
+      "source": "UniProt:A9UF07",
+      "target": "MESH:D015464",
+      "evidence": [
+        {
+          "reference": "PMID:11287972",
+          "snippet": "BCR-ABL is a constitutively activated tyrosine kinase that causes chronic myeloid leukemia (CML).",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Efficacy and safety of a specific inhibitor of the BCR-ABL tyrosine kinase in chronic myeloid leukemia.",
+            "authors": [
+              "Druker BJ",
+              "Talpaz M",
+              "Resta DJ",
+              "Peng B",
+              "Buchdunger E",
+              "Ford JM",
+              "Lydon NB",
+              "Kantarjian H",
+              "Capdeville R",
+              "Ohno-Jones S",
+              "Sawyers CL"
+            ],
+            "journal": "The New England journal of medicine",
+            "year": "2001",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:42174092",
+          "snippet": "This alteration gives rise to the BCR::ABL1 fusion oncogene, whose constitutive tyrosine kinase activity promotes uncontrolled proliferation and survival of leukemic cells.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Corroborates that the BCR-ABL fusion drives the leukemic phenotype of CML.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00619",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    }
+  ],
+  "site": {
+    "id": "pilot__DB00619_MESH_D015464_1__r3",
+    "record_id": "DB00619_MESH_D015464_1",
+    "run": "pilot",
+    "run_label": "Pilot run",
+    "source_file": "experiments/pilot/outputs/DB00619_MESH_D015464_1__r3.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/pilot__DB00843_MESH_D000544_1.json b/web-revamp-mockup/data/records/pilot__DB00843_MESH_D000544_1.json
new file mode 100644
index 0000000..21d3fc6
--- /dev/null
+++ b/web-revamp-mockup/data/records/pilot__DB00843_MESH_D000544_1.json
@@ -0,0 +1,112 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "DB00843_MESH_D000544_1",
+    "drug": "donepezil",
+    "drug_mesh": "MESH:C076946",
+    "drugbank": "DB:DB00843",
+    "disease": "Alzheimer's disease",
+    "disease_mesh": "MESH:D000544",
+    "summary": "Donepezil → Acetylcholinesterase → Acetylcholine → Alzheimer's disease"
+  },
+  "nodes": [
+    {
+      "id": "MESH:C076946",
+      "name": "Donepezil",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P22303",
+      "name": "Acetylcholinesterase",
+      "label": "Protein"
+    },
+    {
+      "id": "CHEBI:15355",
+      "name": "Acetylcholine",
+      "label": "ChemicalSubstance"
+    },
+    {
+      "id": "MESH:D000544",
+      "name": "Alzheimer's disease",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:C076946",
+      "target": "UniProt:P22303",
+      "evidence": [
+        {
+          "reference": "PMID:39037949",
+          "snippet": "donepezil, a well-known AChE inhibitor used in Alzheimer's disease treatment",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Donepezil directly inhibits acetylcholinesterase (AChE).",
+          "source_type": "pubmed",
+          "paper": null
+        },
+        {
+          "reference": "PMID:34893996",
+          "snippet": "The most commonly used drug, donepezil, is a cholinesterase inhibitor.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    },
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "abundance",
+      "object_direction_qualifier": "decreased",
+      "source": "UniProt:P22303",
+      "target": "CHEBI:15355",
+      "evidence": [
+        {
+          "reference": "PMID:39037949",
+          "snippet": "acetylcholinesterase (AChE) is a critical enzyme in the nervous system, responsible for breaking down the neurotransmitter acetylcholine",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "AChE degrades acetylcholine; donepezil's inhibition of AChE therefore raises synaptic acetylcholine.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    },
+    {
+      "key": "negatively correlated with",
+      "source": "CHEBI:15355",
+      "target": "MESH:D000544",
+      "evidence": [
+        {
+          "reference": "PMID:37242234",
+          "snippet": "the cholinergic hypothesis proposes that AD symptoms are a result of reduced synthesis of acetylcholine (ACh)",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Per the cholinergic hypothesis, acetylcholine is inversely related to Alzheimer's disease symptoms (reduced acetylcholine produces symptoms); donepezil raising acetylcholine therefore opposes the disease.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00843",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    }
+  ],
+  "site": {
+    "id": "pilot__DB00843_MESH_D000544_1",
+    "record_id": "DB00843_MESH_D000544_1",
+    "run": "pilot",
+    "run_label": "Pilot run",
+    "source_file": "experiments/pilot/outputs/DB00843_MESH_D000544_1.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/pilot__DB00993_MESH_D001172_1.json b/web-revamp-mockup/data/records/pilot__DB00993_MESH_D001172_1.json
new file mode 100644
index 0000000..a3691bf
--- /dev/null
+++ b/web-revamp-mockup/data/records/pilot__DB00993_MESH_D001172_1.json
@@ -0,0 +1,162 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "DB00993_MESH_D001172_1",
+    "drug": "azathioprine",
+    "drug_mesh": "MESH:D001379",
+    "drugbank": "DB:DB00993",
+    "disease": "Rheumatoid arthritis",
+    "disease_mesh": "MESH:D001172",
+    "summary": "Azathioprine → Mercaptopurine → purine nucleotide biosynthetic process → T cell proliferation → Rheumatoid arthritis"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D001379",
+      "name": "Azathioprine",
+      "label": "Drug"
+    },
+    {
+      "id": "MESH:D008774",
+      "name": "Mercaptopurine",
+      "label": "ChemicalSubstance"
+    },
+    {
+      "id": "GO:0006164",
+      "name": "purine nucleotide biosynthetic process",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "GO:0042098",
+      "name": "T cell proliferation",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D001172",
+      "name": "Rheumatoid arthritis",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "has metabolite",
+      "source": "MESH:D001379",
+      "target": "MESH:D008774",
+      "evidence": [
+        {
+          "reference": "PMID:12697733",
+          "snippet": "Azathioprine and its metabolite 6-mercaptopurine (6-MP) are immunosuppressive drugs that are used in organ transplantation and autoimmune and chronic inflammatory diseases such as Crohn disease.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Azathioprine is a prodrug metabolized to 6-mercaptopurine.",
+          "source_type": "pubmed",
+          "paper": null
+        },
+        {
+          "reference": "PMID:11683683",
+          "snippet": "The thioguanine derivative, azathioprine, is a prodrug of 6-mercaptopurine that is further metabolized by various enzymes present in the liver and gut.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D008774",
+      "target": "GO:0006164",
+      "evidence": [
+        {
+          "reference": "PMID:11683683",
+          "snippet": "The mode of action of azathioprine is thought to be multifactorial, including conversion to 6-mercaptopurine (which acts as a purine antimetabolite), possible blockade of thiol groups by alkylation, inhibition of several pathways in nucleic acid biosynthesis (preventing proliferation of cells involved in the determination and amplification of the immune response) and damage to DNA through the incorporation of thiopurine analogues.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "6-Mercaptopurine acts as a purine antimetabolite, inhibiting purine nucleotide biosynthesis.",
+          "source_type": "pubmed",
+          "paper": null
+        },
+        {
+          "reference": "PMID:10878284",
+          "snippet": "Azathioprine metabolites inhibit several enzymes of purine synthesis.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "source_type": "pubmed",
+          "paper": null
+        },
+        {
+          "reference": "PMID:12734342",
+          "snippet": "This was investigated in the present study by using well-known purine (mycophenolic acid, 6-mercaptopurine) and pyrimidine (methotrexate, 5-fluorouracil) inhibitors, which are used in neoplastic diseases or as immunosuppressive agents.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "6-Mercaptopurine is a purine synthesis inhibitor.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "GO:0006164",
+      "target": "GO:0042098",
+      "evidence": [
+        {
+          "reference": "PMID:12734342",
+          "snippet": "We showed that synthesis of both purine and pyrimidine nucleotides is required for T cell proliferation.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "De novo purine nucleotide synthesis is required for proliferation of activated T lymphocytes.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    },
+    {
+      "key": "contributes to",
+      "source": "GO:0042098",
+      "target": "MESH:D001172",
+      "evidence": [
+        {
+          "reference": "PMID:8013988",
+          "snippet": "Two promising new therapeutic approaches are being developed, one aimed at specifically reducing the proliferation of activated T cell clones, and the second designed to modulate the activity of the cytokines involved in the inflammatory process.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Proliferation of activated T cell clones drives the inflammatory process of rheumatoid arthritis and is a therapeutic target.",
+          "source_type": "pubmed",
+          "paper": null
+        },
+        {
+          "reference": "PMID:29581356",
+          "snippet": "For the initiation of CIA, the Tyr181-based SH2-binding motif of ICOS that is known to activate PI3K was critical for Ab production and expansion of inflammatory T cells.",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "explanation": "In collagen-induced arthritis, a murine model of rheumatoid arthritis, expansion (proliferation) of inflammatory T cells is critical for disease initiation.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://pubmed.ncbi.nlm.nih.gov/12697733/",
+      "type": "other",
+      "label": "pubmed.ncbi.nlm.nih.gov — record source"
+    },
+    {
+      "url": "https://pubmed.ncbi.nlm.nih.gov/12734342/",
+      "type": "other",
+      "label": "pubmed.ncbi.nlm.nih.gov — record source"
+    }
+  ],
+  "site": {
+    "id": "pilot__DB00993_MESH_D001172_1",
+    "record_id": "DB00993_MESH_D001172_1",
+    "run": "pilot",
+    "run_label": "Pilot run",
+    "source_file": "experiments/pilot/outputs/DB00993_MESH_D001172_1.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/pilot__DB01076_MESH_D006937_1.json b/web-revamp-mockup/data/records/pilot__DB01076_MESH_D006937_1.json
new file mode 100644
index 0000000..95e316a
--- /dev/null
+++ b/web-revamp-mockup/data/records/pilot__DB01076_MESH_D006937_1.json
@@ -0,0 +1,178 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "DB01076_MESH_D006937_1",
+    "drug": "atorvastatin",
+    "drug_mesh": "MESH:D000069059",
+    "drugbank": "DB:DB01076",
+    "disease": "Hypercholesterolemia",
+    "disease_mesh": "MESH:D006937",
+    "summary": "atorvastatin → 3-hydroxy-3-methylglutaryl-coenzyme A reductase → Cholesterol → Low-density lipoprotein receptor → Low-density lipoprotein cholesterol → Hypercholesterolemia"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D000069059",
+      "name": "atorvastatin",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P04035",
+      "name": "3-hydroxy-3-methylglutaryl-coenzyme A reductase",
+      "label": "Protein"
+    },
+    {
+      "id": "MESH:D002784",
+      "name": "Cholesterol",
+      "label": "ChemicalSubstance"
+    },
+    {
+      "id": "UniProt:P01130",
+      "name": "Low-density lipoprotein receptor",
+      "label": "Protein"
+    },
+    {
+      "id": "MESH:D008078",
+      "name": "Low-density lipoprotein cholesterol",
+      "label": "ChemicalSubstance"
+    },
+    {
+      "id": "MESH:D006937",
+      "name": "Hypercholesterolemia",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D000069059",
+      "target": "UniProt:P04035",
+      "evidence": [
+        {
+          "reference": "PMID:10582478",
+          "snippet": "the inhibition of HMG Co-A reductase, the key enzyme in cholesterol synthesis, which leads to the increase of LDL receptors.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Atorvastatin's mechanism of action is inhibition of HMG-CoA reductase.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    },
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "abundance",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P04035",
+      "target": "MESH:D002784",
+      "evidence": [
+        {
+          "reference": "PMID:10582478",
+          "snippet": "HMG Co-A reductase, the key enzyme in cholesterol synthesis",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "HMG-CoA reductase is the rate-limiting enzyme of cholesterol biosynthesis, so its activity increases cellular cholesterol.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D002784",
+      "target": "UniProt:P01130",
+      "evidence": [
+        {
+          "reference": "PMID:12829694",
+          "snippet": "LDL receptor levels are subject to negative feedback regulation by cellular cholesterol through sterol regulatory element-binding protein-2 (SREBP-2).",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Cellular cholesterol negatively feedback-regulates LDL receptor levels via SREBP-2; statin-lowered cholesterol therefore raises LDL receptor expression.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Thyroid hormone regulation and cholesterol metabolism are connected through Sterol Regulatory Element-Binding Protein-2 (SREBP-2).",
+            "authors": [
+              "Shin DJ",
+              "Osborne TF"
+            ],
+            "journal": "The Journal of biological chemistry",
+            "year": "2003",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "abundance",
+      "object_direction_qualifier": "decreased",
+      "source": "UniProt:P01130",
+      "target": "MESH:D008078",
+      "evidence": [
+        {
+          "reference": "PMID:32109664",
+          "snippet": "Hepatic low density lipoprotein receptor (LDLR) pathway, as the major mechanism for clearing circulating low density lipoprotein cholesterol (LDL-C) in bloodstream, is a pivotal therapeutic target to treat hypercholesterolemia and atherosclerosis.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "The hepatic LDL receptor is the major route for clearing circulating LDL cholesterol, reducing its plasma abundance.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Hsa-miR-140-5p down-regulates LDL receptor and attenuates LDL-C uptake in human hepatocytes.",
+            "authors": [
+              "Xu Y",
+              "Gao J",
+              "Gong Y",
+              "Chen M",
+              "Chen J",
+              "Zhao W",
+              "Tan S"
+            ],
+            "journal": "Atherosclerosis",
+            "year": "2020",
+            "doi": "10.1016/j.atherosclerosis.2020.02.004",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "causes",
+      "source": "MESH:D008078",
+      "target": "MESH:D006937",
+      "evidence": [
+        {
+          "reference": "PMID:10591675",
+          "snippet": "marked hypercholesterolemia (up to 3- to 4-fold over nontransgenics), characterized by an increase in low density lipoprotein (LDL) cholesterol",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "explanation": "Elevated LDL cholesterol produces the hypercholesterolemic state.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB01076",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    }
+  ],
+  "site": {
+    "id": "pilot__DB01076_MESH_D006937_1",
+    "record_id": "DB01076_MESH_D006937_1",
+    "run": "pilot",
+    "run_label": "Pilot run",
+    "source_file": "experiments/pilot/outputs/DB01076_MESH_D006937_1.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/pilot__DB01527_MESH_D000856_1.json b/web-revamp-mockup/data/records/pilot__DB01527_MESH_D000856_1.json
new file mode 100644
index 0000000..aa34f5c
--- /dev/null
+++ b/web-revamp-mockup/data/records/pilot__DB01527_MESH_D000856_1.json
@@ -0,0 +1,88 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "DB01527_MESH_D000856_1",
+    "drug": "clortermine",
+    "drugbank": "DB:DB01527",
+    "disease": "Anorexia",
+    "disease_mesh": "MESH:D000856",
+    "summary": "Clortermine → Feeding behavior → Anorexia"
+  },
+  "nodes": [
+    {
+      "id": "DB:DB01527",
+      "name": "Clortermine",
+      "label": "Drug"
+    },
+    {
+      "id": "GO:0007631",
+      "name": "Feeding behavior",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D000856",
+      "name": "Anorexia",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "decreased",
+      "source": "DB:DB01527",
+      "target": "GO:0007631",
+      "evidence": [
+        {
+          "reference": "PMID:3620005",
+          "snippet": "All drugs reduced food intake in a dose-related manner.",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "explanation": "In rhesus monkeys the anorectics benzphetamine, chlorphentermine, clortermine, mazindol, phendimetrazine and phenmetrazine were compared; clortermine is explicitly one of the drugs that reduced food intake.",
+          "source_type": "pubmed",
+          "paper": null
+        },
+        {
+          "reference": "PMID:826970",
+          "snippet": "Increasing self-infused doses of all drugs produced a substantial suppression of concurrent food-maintained behavior.",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "explanation": "Clortermine is one of the eight phenylethylamines tested in baboons whose increasing doses suppressed food-maintained behavior.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    },
+    {
+      "key": "manifestation of",
+      "source": "GO:0007631",
+      "target": "MESH:D000856",
+      "evidence": [
+        {
+          "reference": "PMID:8637056",
+          "snippet": "a reduction in food consumption (anorexia)",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "A reduction in food consumption is equated with anorexia (loss of appetite / reduced food intake); the suppressed feeding behavior is the manifestation of anorexia.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB01527",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    }
+  ],
+  "site": {
+    "id": "pilot__DB01527_MESH_D000856_1",
+    "record_id": "DB01527_MESH_D000856_1",
+    "run": "pilot",
+    "run_label": "Pilot run",
+    "source_file": "experiments/pilot/outputs/DB01527_MESH_D000856_1.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/pilot__DB09038_MESH_D003924_1.json b/web-revamp-mockup/data/records/pilot__DB09038_MESH_D003924_1.json
new file mode 100644
index 0000000..30c3d41
--- /dev/null
+++ b/web-revamp-mockup/data/records/pilot__DB09038_MESH_D003924_1.json
@@ -0,0 +1,161 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "DB09038_MESH_D003924_1",
+    "drug": "empagliflozin",
+    "drug_mesh": "MESH:C570240",
+    "drugbank": "DB:DB09038",
+    "disease": "Diabetes Mellitus, Type 2",
+    "disease_mesh": "MESH:D003924",
+    "summary": "empagliflozin → Sodium/glucose cotransporter 2 → renal glucose absorption → Glycosuria → Hyperglycemia → Diabetes Mellitus, Type 2"
+  },
+  "nodes": [
+    {
+      "id": "DB:DB09038",
+      "name": "empagliflozin",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P31639",
+      "name": "Sodium/glucose cotransporter 2",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0035623",
+      "name": "renal glucose absorption",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "HP:0003076",
+      "name": "Glycosuria",
+      "label": "PhenotypicFeature"
+    },
+    {
+      "id": "HP:0003074",
+      "name": "Hyperglycemia",
+      "label": "PhenotypicFeature"
+    },
+    {
+      "id": "MESH:D003924",
+      "name": "Diabetes Mellitus, Type 2",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "DB:DB09038",
+      "target": "UniProt:P31639",
+      "evidence": [
+        {
+          "reference": "PMID:24152604",
+          "snippet": "Empagliflozin is an orally available, potent and highly selective inhibitor of the sodium glucose cotransporter 2 (SGLT2).",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P31639",
+      "target": "GO:0035623",
+      "evidence": [
+        {
+          "reference": "PMID:38171209",
+          "snippet": "Sodium-dependent glucose cotransporter 2 (SGLT2) mediates glucose reabsorption in the renal proximal tubules",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Inhibition of Sodium-Glucose Cotransporter-2 during Serum Deprivation Increases Hepatic Gluconeogenesis via the AMPK/AKT/FOXO Signaling Pathway.",
+            "authors": [
+              "Lee J",
+              "Hong SW",
+              "Kim MJ",
+              "Lim YM",
+              "Moon SJ",
+              "Kwon H",
+              "Park SE",
+              "Rhee EJ",
+              "Lee WY"
+            ],
+            "journal": "Endocrinology and metabolism (Seoul, Korea)",
+            "year": "2024",
+            "doi": "10.3803/EnM.2023.1786",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "negatively correlated with",
+      "source": "GO:0035623",
+      "target": "HP:0003076",
+      "evidence": [
+        {
+          "reference": "PMID:31951170",
+          "snippet": "The SGLT2 inhibitors by inhibiting the SGLT2 in the proximal nephron, helps in reducing the reabsorption of approximately 90% of the filtered glucose and increased urinary glucose excretion (UGE).",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Reduced renal glucose reabsorption is accompanied by increased urinary glucose excretion (glycosuria), i.e. the two are inversely related.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    },
+    {
+      "key": "negatively correlated with",
+      "source": "HP:0003076",
+      "target": "HP:0003074",
+      "evidence": [
+        {
+          "reference": "PMID:24455799",
+          "snippet": "SGLT2-inhibitors are a new class of oral antidiabetics, which reduce hyperglycemia by increasing urinary glucose excretion independently of insulin secretion or action.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Increasing urinary glucose excretion (glycosuria) lowers blood glucose, reducing hyperglycemia.",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    },
+    {
+      "key": "manifestation of",
+      "source": "HP:0003074",
+      "target": "MESH:D003924",
+      "evidence": [
+        {
+          "reference": "PMID:42356484",
+          "snippet": "Type 2 Diabetes Mellitus (T2DM) is characterized by insulin resistance and chronic hyperglycemia, which significantly impair vascular function.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "source_type": "pubmed",
+          "paper": null
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB09038",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    }
+  ],
+  "site": {
+    "id": "pilot__DB09038_MESH_D003924_1",
+    "record_id": "DB09038_MESH_D003924_1",
+    "run": "pilot",
+    "run_label": "Pilot run",
+    "source_file": "experiments/pilot/outputs/DB09038_MESH_D003924_1.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/sonnet__P01.json b/web-revamp-mockup/data/records/sonnet__P01.json
new file mode 100644
index 0000000..4c27e34
--- /dev/null
+++ b/web-revamp-mockup/data/records/sonnet__P01.json
@@ -0,0 +1,256 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P01_DB00945_MESH_D009203",
+    "drug": "Aspirin",
+    "drug_mesh": "MESH:D001241",
+    "drugbank": "DB:DB00945",
+    "disease": "Myocardial Infarction",
+    "disease_mesh": "MESH:D009203",
+    "summary": "Aspirin → Cyclooxygenase-1 → Thromboxane A2 → platelet aggregation → Myocardial Infarction"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D001241",
+      "name": "Aspirin",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P23219",
+      "name": "Cyclooxygenase-1",
+      "label": "Protein"
+    },
+    {
+      "id": "MESH:D013931",
+      "name": "Thromboxane A2",
+      "label": "ChemicalSubstance"
+    },
+    {
+      "id": "GO:0070527",
+      "name": "platelet aggregation",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D009203",
+      "name": "Myocardial Infarction",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D001241",
+      "target": "UniProt:P23219",
+      "evidence": [
+        {
+          "reference": "PMID:18855644",
+          "snippet": "Aspirin works by irreversibly acetylating the cyclooxygenase (COX-1) enzyme, thus suppressing the production of thromboxane A(2) (TxA(2)) and inhibiting platelet activation and aggregation.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Directly states aspirin irreversibly acetylates COX-1, decreasing its activity.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Clopidogrel and aspirin in cardiovascular medicine: responders or not--current best available evidence.",
+            "authors": [
+              "Tourmousoglou CE",
+              "Rokkas CK"
+            ],
+            "journal": "Cardiovascular & hematological agents in medicinal chemistry",
+            "year": "2008",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:26139061",
+          "snippet": "Inactivation of platelet cyclooxygenase (COX)-1 by low-dose aspirin leads to long-lasting suppression of thromboxane (TX) A2 production and TXA2-mediated platelet activation and aggregation.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "States that aspirin inactivates COX-1, confirming decreases activity of relationship.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "The Multifaceted Clinical Readouts of Platelet Inhibition by Low-Dose Aspirin.",
+            "authors": [
+              "Patrono C"
+            ],
+            "journal": "Journal of the American College of Cardiology",
+            "year": "2015",
+            "doi": "10.1016/j.jacc.2015.05.012",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P23219",
+      "target": "MESH:D013931",
+      "evidence": [
+        {
+          "reference": "PMID:11552047",
+          "snippet": "Cox-1 catalyzes the synthesis of thromboxane A2 (Tx-A2), which causes platelet activation, vasoconstriction, and smooth muscle proliferation.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Directly states COX-1 catalyzes synthesis of TXA2, establishing COX-1 positively regulates TXA2 production.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Vascular biology of thrombosis: platelet-vessel wall interactions and aspirin effects.",
+            "authors": [
+              "Catella-Lawson F"
+            ],
+            "journal": "Neurology",
+            "year": "2001",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:19110389",
+          "snippet": "Aspirin irreversibly inhibits cyclooxygenase (COX) 1 involved in the platelet production of thromboxane (TX) A(2), an inducer of vasoconstriction and a platelet activating agent.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "States COX-1 is involved in platelet production of TXA2, supporting positive regulation.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "[Variable platelet response to aspirin and new therapeutic targets].",
+            "authors": [
+              "Richard S",
+              "Toussaint-Hacquard M",
+              "Lecompte T"
+            ],
+            "journal": "Journal des maladies vasculaires",
+            "year": "2009",
+            "doi": "10.1016/j.jmv.2008.10.009",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "MESH:D013931",
+      "target": "GO:0070527",
+      "evidence": [
+        {
+          "reference": "PMID:32721526",
+          "snippet": "Thromboxane A2 (TXA2) is implicated in graft failure by inducing vasoconstriction and platelet aggregation.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Directly states TXA2 induces platelet aggregation, supporting positive regulation.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Mechanism of thromboxane receptor-induced vasoconstriction in human saphenous vein.",
+            "authors": [
+              "Ozen G",
+              "Aljesri K",
+              "Celik Z",
+              "Turkyılmaz G",
+              "Turkyılmaz S",
+              "Teskin O",
+              "Norel X",
+              "Topal G"
+            ],
+            "journal": "Prostaglandins & other lipid mediators",
+            "year": "2020",
+            "doi": "10.1016/j.prostaglandins.2020.106476",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:19110389",
+          "snippet": "Aspirin irreversibly inhibits cyclooxygenase (COX) 1 involved in the platelet production of thromboxane (TX) A(2), an inducer of vasoconstriction and a platelet activating agent.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Describes TXA2 as a platelet activating agent, supporting its role in positively regulating platelet aggregation.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "[Variable platelet response to aspirin and new therapeutic targets].",
+            "authors": [
+              "Richard S",
+              "Toussaint-Hacquard M",
+              "Lecompte T"
+            ],
+            "journal": "Journal des maladies vasculaires",
+            "year": "2009",
+            "doi": "10.1016/j.jmv.2008.10.009",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "contributes to",
+      "source": "GO:0070527",
+      "target": "MESH:D009203",
+      "evidence": [
+        {
+          "reference": "PMID:24558405",
+          "snippet": "Excessive aggregation of platelets at the site of plaque rupture on the coronary artery led to the formation of thrombus which is reported to precipitate acute myocardial infarction (AMI).",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Directly states platelet aggregation at plaque rupture precipitates acute myocardial infarction.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Reduction of death rate due to acute myocardial infarction in subjects with cancers through systemic restoration of impaired nitric oxide.",
+            "authors": [
+              "Ghosh R",
+              "Ray U",
+              "Jana P",
+              "Bhattacharya R",
+              "Banerjee D",
+              "Sinha A"
+            ],
+            "journal": "PloS one",
+            "year": "2014",
+            "doi": "10.1371/journal.pone.0088639",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://www.drugbank.ca/drugs/DB00945",
+      "type": "drugbank",
+      "label": "drugbank.ca — record source"
+    },
+    {
+      "url": "https://meshb.nlm.nih.gov/record/ui?ui=D001241",
+      "type": "other",
+      "label": "meshb.nlm.nih.gov — record source"
+    },
+    {
+      "url": "https://meshb.nlm.nih.gov/record/ui?ui=D009203",
+      "type": "other",
+      "label": "meshb.nlm.nih.gov — record source"
+    }
+  ],
+  "site": {
+    "id": "sonnet__P01",
+    "record_id": "P01_DB00945_MESH_D009203",
+    "run": "sonnet",
+    "run_label": "Sonnet (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/sonnet/outputs/P01.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/sonnet__P02.json b/web-revamp-mockup/data/records/sonnet__P02.json
new file mode 100644
index 0000000..1298a1d
--- /dev/null
+++ b/web-revamp-mockup/data/records/sonnet__P02.json
@@ -0,0 +1,206 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P02_DB01076_MESH_D006937",
+    "drug": "atorvastatin",
+    "drug_mesh": "MESH:D000069059",
+    "drugbank": "DB:DB01076",
+    "disease": "Hypercholesterolemia",
+    "disease_mesh": "MESH:D006937",
+    "summary": "atorvastatin → HMG-CoA reductase → cholesterol biosynthetic process → LDL receptor → Hypercholesterolemia"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D000069059",
+      "name": "atorvastatin",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P04035",
+      "name": "HMG-CoA reductase",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0006695",
+      "name": "cholesterol biosynthetic process",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "UniProt:P01130",
+      "name": "LDL receptor",
+      "label": "Protein"
+    },
+    {
+      "id": "MESH:D006937",
+      "name": "Hypercholesterolemia",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D000069059",
+      "target": "UniProt:P04035",
+      "evidence": [
+        {
+          "reference": "PMID:42112329",
+          "snippet": "Atorvastatin, a widely used statin, primarily functions by inhibiting 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase, the rate-limiting enzyme in the mevalonate pathway, thereby lowering cholesterol.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Directly states atorvastatin inhibits HMG-CoA reductase (HMGCR).",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Atorvastatin as a pleiotropic anticancer agent: mechanisms, evidence, and therapeutic repurposing potential.",
+            "authors": [
+              "Su J",
+              "Ji C",
+              "Niu X",
+              "Wu Z",
+              "Shi L",
+              "Kang L",
+              "Li D",
+              "Ma Y",
+              "Pang G",
+              "Ma X",
+              "Zhou CM",
+              "Jiang X",
+              "Pang B"
+            ],
+            "journal": "Frontiers in immunology",
+            "year": "2026",
+            "doi": "10.3389/fimmu.2026.1808729",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:12486413",
+          "snippet": "HMGR is the target of compounds (HMGR inhibitors, commonly referred to as statins) that are very effective in lowering serum cholesterol levels. These inhibitors have K(i) values in the nanomolar range and are widely prescribed in the treatment of hypercholesterolemia.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Confirms statins including atorvastatin inhibit HMGCR with nanomolar Ki values.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Structural mechanism for statin inhibition of 3-hydroxy-3-methylglutaryl coenzyme A reductase.",
+            "authors": [
+              "Istvan ES"
+            ],
+            "journal": "American heart journal",
+            "year": "2002",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "participates in",
+      "source": "UniProt:P04035",
+      "target": "GO:0006695",
+      "evidence": [
+        {
+          "reference": "PMID:12486413",
+          "snippet": "3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase (HMGR) catalyzes the committed step in cholesterol biosynthesis.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "HMG-CoA reductase catalyzes the committed (rate-limiting) step in the cholesterol biosynthetic process.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Structural mechanism for statin inhibition of 3-hydroxy-3-methylglutaryl coenzyme A reductase.",
+            "authors": [
+              "Istvan ES"
+            ],
+            "journal": "American heart journal",
+            "year": "2002",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "decreased",
+      "source": "GO:0006695",
+      "target": "UniProt:P01130",
+      "evidence": [
+        {
+          "reference": "PMID:17910517",
+          "snippet": "By inhibiting 3-hydroxy-3-methylglutaryl coenzyme-A (HMG-CoA) reductase, the statins reduce hepatocyte cholesterol levels, which results in up-regulation of low-density lipoprotein (LDL) receptors and, consequently, increased clearance of LDL-cholesterol (LDL-C) from the plasma.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Reduced cholesterol biosynthesis (via HMGCR inhibition) leads to LDL receptor upregulation, demonstrating that the cholesterol biosynthetic process negatively regulates LDL receptor expression.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Atorvastatin: pharmacological characteristics and lipid-lowering effects.",
+            "authors": [
+              "Poli A"
+            ],
+            "journal": "Drugs",
+            "year": "2007",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "decreased",
+      "source": "UniProt:P01130",
+      "target": "MESH:D006937",
+      "evidence": [
+        {
+          "reference": "PMID:23074505",
+          "snippet": "The reduced number or absence of functional LDL receptors results in impaired hepatic clearance of circulating low-density lipoprotein cholesterol (LDL-C) particles, which results in extremely high levels of LDL-C in the bloodstream.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Loss of LDL receptor function causes hypercholesterolemia (extremely high LDL-C), demonstrating that the LDL receptor negatively regulates hypercholesterolemia.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Low-density lipoprotein apheresis: an evidence-based analysis.",
+            "authors": [
+              "Medical Advisory Secretariat"
+            ],
+            "journal": "Ontario health technology assessment series",
+            "year": "2007",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://www.drugbank.ca/drugs/DB01076",
+      "type": "drugbank",
+      "label": "drugbank.ca — record source"
+    },
+    {
+      "url": "https://meshb.nlm.nih.gov/record/ui?ui=D006937",
+      "type": "other",
+      "label": "meshb.nlm.nih.gov — record source"
+    }
+  ],
+  "site": {
+    "id": "sonnet__P02",
+    "record_id": "P02_DB01076_MESH_D006937",
+    "run": "sonnet",
+    "run_label": "Sonnet (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/sonnet/outputs/P02.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/sonnet__P03.json b/web-revamp-mockup/data/records/sonnet__P03.json
new file mode 100644
index 0000000..f278516
--- /dev/null
+++ b/web-revamp-mockup/data/records/sonnet__P03.json
@@ -0,0 +1,273 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P03_DB00722_MESH_D006973",
+    "drug": "Lisinopril",
+    "drug_mesh": "MESH:D017706",
+    "drugbank": "DB:DB00722",
+    "disease": "Hypertension",
+    "disease_mesh": "MESH:D006973",
+    "summary": "Lisinopril → Angiotensin-converting enzyme → Angiotensin II → vasoconstriction → Hypertension"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D017706",
+      "name": "Lisinopril",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P12821",
+      "name": "Angiotensin-converting enzyme",
+      "label": "Protein"
+    },
+    {
+      "id": "MESH:D000804",
+      "name": "Angiotensin II",
+      "label": "ChemicalSubstance"
+    },
+    {
+      "id": "GO:0042310",
+      "name": "vasoconstriction",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D006973",
+      "name": "Hypertension",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D017706",
+      "target": "UniProt:P12821",
+      "evidence": [
+        {
+          "reference": "PMID:28629525",
+          "snippet": "ACE inhibitors, to prevent Ang I processing to Ang II",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Lisinopril is an ACE inhibitor that decreases the activity of angiotensin-converting enzyme, thereby preventing the conversion of angiotensin I to angiotensin II.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Erythropoietin Regulation by Angiotensin II.",
+            "authors": [
+              "Kim YC",
+              "Mungunsukh O",
+              "Day RM"
+            ],
+            "journal": "Vitamins and hormones",
+            "year": "2017",
+            "doi": "10.1016/bs.vh.2017.02.001",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:16614314",
+          "snippet": "Inhibition of the angiotensin-converting enzyme (ACE) protects against the progression of several cardiovascular diseases. Because of its dual role in regulating angiotensin II and bradykinin levels, the positive clinical effects of ACE inhibitors were thought to be the consequence of concomitant reductions in the production of angiotensin II",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Signaling by the angiotensin-converting enzyme.",
+            "authors": [
+              "Fleming I"
+            ],
+            "journal": "Circulation research",
+            "year": "2006",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P12821",
+      "target": "MESH:D000804",
+      "evidence": [
+        {
+          "reference": "PMID:28629525",
+          "snippet": "angiotensin II (Ang II) that has a variety of biological functions in the cells is converted from Ang I through removal of two-C-terminal residues by ACE",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "ACE cleaves angiotensin I to produce angiotensin II by removing the C-terminal dipeptide.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Erythropoietin Regulation by Angiotensin II.",
+            "authors": [
+              "Kim YC",
+              "Mungunsukh O",
+              "Day RM"
+            ],
+            "journal": "Vitamins and hormones",
+            "year": "2017",
+            "doi": "10.1016/bs.vh.2017.02.001",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:32799009",
+          "snippet": "induced angiotensin-converting enzyme (ACE) expression and the consequent conversion from Ang I to Ang II",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Multiple pathophysiological roles of midkine in human disease.",
+            "authors": [
+              "Cai YQ",
+              "Lv Y",
+              "Mo ZC",
+              "Lei J",
+              "Zhu JL",
+              "Zhong QQ"
+            ],
+            "journal": "Cytokine",
+            "year": "2020",
+            "doi": "10.1016/j.cyto.2020.155242",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "causes",
+      "source": "MESH:D000804",
+      "target": "GO:0042310",
+      "evidence": [
+        {
+          "reference": "PMID:28384411",
+          "snippet": "angiotensin II (Ang II), that causes vasoconstriction, sodium retention, and structural alterations of the heart and the arteries",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Angiotensin II directly causes vasoconstriction, which raises peripheral vascular resistance.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Kallikrein-kinin system as the dominant mechanism to counteract hyperactive renin-angiotensin system.",
+            "authors": [
+              "Regoli D",
+              "Gobeil F"
+            ],
+            "journal": "Canadian journal of physiology and pharmacology",
+            "year": "2017",
+            "doi": "10.1139/cjpp-2016-0619",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:39385670",
+          "snippet": "angiotensin (Ang) II is an essential vasoconstrictive peptide",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Pyridoxal-5'-phosphate: A cost-effective treatment candidate for hypertensive patients?",
+            "authors": [
+              "Lellig M",
+              "Rodríguez M",
+              "López-Baltanás R",
+              "Hermann J",
+              "Wollenhaupt J",
+              "Noels H",
+              "Zidek W",
+              "Tepel M",
+              "Mahfoud F",
+              "Jankowski J",
+              "Muñoz-Castañeda JR",
+              "Jankowski V"
+            ],
+            "journal": "Journal of internal medicine",
+            "year": "2024",
+            "doi": "10.1111/joim.20015",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "causes",
+      "source": "GO:0042310",
+      "target": "MESH:D006973",
+      "evidence": [
+        {
+          "reference": "PMID:28629525",
+          "snippet": "The physiological effects of Ang II are due to Ang II signaling through specific receptor binding, resulting in muscle contraction leading to increased blood pressure and volume.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Vasoconstriction from angiotensin II-mediated smooth muscle contraction increases peripheral resistance leading to elevated blood pressure (hypertension).",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Erythropoietin Regulation by Angiotensin II.",
+            "authors": [
+              "Kim YC",
+              "Mungunsukh O",
+              "Day RM"
+            ],
+            "journal": "Vitamins and hormones",
+            "year": "2017",
+            "doi": "10.1016/bs.vh.2017.02.001",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:28384411",
+          "snippet": "The renin-angiotensin system (RAS) generates, maintains, and makes worse hypertension and cardiovascular diseases (CVDs) through its biologically active component angiotensin II (Ang II), that causes vasoconstriction",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Kallikrein-kinin system as the dominant mechanism to counteract hyperactive renin-angiotensin system.",
+            "authors": [
+              "Regoli D",
+              "Gobeil F"
+            ],
+            "journal": "Canadian journal of physiology and pharmacology",
+            "year": "2017",
+            "doi": "10.1139/cjpp-2016-0619",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://www.drugbank.ca/drugs/DB00722",
+      "type": "drugbank",
+      "label": "drugbank.ca — record source"
+    },
+    {
+      "url": "https://www.ncbi.nlm.nih.gov/mesh/D017706",
+      "type": "other",
+      "label": "ncbi.nlm.nih.gov — record source"
+    }
+  ],
+  "site": {
+    "id": "sonnet__P03",
+    "record_id": "P03_DB00722_MESH_D006973",
+    "run": "sonnet",
+    "run_label": "Sonnet (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/sonnet/outputs/P03.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/sonnet__P04.json b/web-revamp-mockup/data/records/sonnet__P04.json
new file mode 100644
index 0000000..781d32c
--- /dev/null
+++ b/web-revamp-mockup/data/records/sonnet__P04.json
@@ -0,0 +1,271 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P04_DB00264_MESH_D006333",
+    "drug": "Metoprolol",
+    "drug_mesh": "MESH:D008790",
+    "drugbank": "DB:DB00264",
+    "disease": "Heart Failure",
+    "disease_mesh": "MESH:D006333",
+    "summary": "Metoprolol → Beta-1 adrenergic receptor → apoptotic process → Heart Failure"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D008790",
+      "name": "Metoprolol",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P08588",
+      "name": "Beta-1 adrenergic receptor",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0006915",
+      "name": "apoptotic process",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D006333",
+      "name": "Heart Failure",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D008790",
+      "target": "UniProt:P08588",
+      "evidence": [
+        {
+          "reference": "PMID:23300817",
+          "snippet": "This effect could be blocked by the selective β(1)-adrenergic receptor antagonist metoprolol, PKA inhibitor H89, and p38 MAPK inhibitor SB203580.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Metoprolol is identified as a selective beta-1 adrenergic receptor antagonist, blocking (decreasing) receptor activity.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "β1-Adrenoceptor autoantibodies from DCM patients enhance the proliferation of T lymphocytes through the β1-AR/cAMP/PKA and p38 MAPK pathways.",
+            "authors": [
+              "Du Y",
+              "Yan L",
+              "Wang J",
+              "Zhan W",
+              "Song K",
+              "Han X",
+              "Li X",
+              "Cao J",
+              "Liu H"
+            ],
+            "journal": "PloS one",
+            "year": "2012",
+            "doi": "10.1371/journal.pone.0052911",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:20888833",
+          "snippet": "prolonged treatment with of β(2) AR agonist, fenoterol, in combination with a β(1) AR blocker, metoprolol, is more effective than β(1) AR blocker alone",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "explanation": "Metoprolol is a beta-1 adrenergic receptor blocker, decreasing receptor activity.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "β₂ AR agonists in treatment of chronic heart failure: long path to translation.",
+            "authors": [
+              "Talan MI",
+              "Ahmet I",
+              "Xiao RP",
+              "Lakatta EG"
+            ],
+            "journal": "Journal of molecular and cellular cardiology",
+            "year": "2011",
+            "doi": "10.1016/j.yjmcc.2010.09.019",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P08588",
+      "target": "GO:0006915",
+      "evidence": [
+        {
+          "reference": "PMID:20888833",
+          "snippet": "selective stimulation of β(1) AR activates the proapoptotic signaling pathways, while selective stimulation of β(2) AR is antiapoptotic",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Activation of beta-1 adrenergic receptor triggers pro-apoptotic signaling pathways in cardiomyocytes.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "β₂ AR agonists in treatment of chronic heart failure: long path to translation.",
+            "authors": [
+              "Talan MI",
+              "Ahmet I",
+              "Xiao RP",
+              "Lakatta EG"
+            ],
+            "journal": "Journal of molecular and cellular cardiology",
+            "year": "2011",
+            "doi": "10.1016/j.yjmcc.2010.09.019",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:23104882",
+          "snippet": "PKA inhibition protected myocytes from death induced by β1-adrenergic receptor agonists by preventing cytosolic and sarcoplasmic reticulum Ca(2+) overload and calcium/calmodulin-dependent kinase II activation.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Beta-1 adrenergic receptor agonists drive myocyte death through PKA and CaMKII pathways.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Cardiotoxic and cardioprotective features of chronic β-adrenergic signaling.",
+            "authors": [
+              "Zhang X",
+              "Szeto C",
+              "Gao E",
+              "Tang M",
+              "Jin J",
+              "Fu Q",
+              "Makarewich C",
+              "Ai X",
+              "Li Y",
+              "Tang A",
+              "Wang J",
+              "Gao H",
+              "Wang F",
+              "Ge XJ",
+              "Kunapuli SP",
+              "Zhou L",
+              "Zeng C",
+              "Xiang KY",
+              "Chen X"
+            ],
+            "journal": "Circulation research",
+            "year": "2013",
+            "doi": "10.1161/CIRCRESAHA.112.273896",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "contributes to",
+      "source": "GO:0006915",
+      "target": "MESH:D006333",
+      "evidence": [
+        {
+          "reference": "PMID:20888833",
+          "snippet": "Loss of cardiomyocytes due to apoptosis is one mechanism that undoubtedly contributes to cardiac remodeling and functional deterioration associated with dilated cardiomyopathy (DCM).",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Cardiomyocyte apoptosis contributes to progressive cardiac remodeling and functional deterioration seen in heart failure.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "β₂ AR agonists in treatment of chronic heart failure: long path to translation.",
+            "authors": [
+              "Talan MI",
+              "Ahmet I",
+              "Xiao RP",
+              "Lakatta EG"
+            ],
+            "journal": "Journal of molecular and cellular cardiology",
+            "year": "2011",
+            "doi": "10.1016/j.yjmcc.2010.09.019",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "treats",
+      "source": "MESH:D008790",
+      "target": "MESH:D006333",
+      "evidence": [
+        {
+          "reference": "PMID:11181074",
+          "snippet": "Selective beta(1)-blockade with high dose of metoprolol initiated in the early postinfarct phase improves myocardial energy metabolism and function and prevents overactivation of sympathetic system.",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "explanation": "Metoprolol treatment improves cardiac function and energy metabolism in a heart failure model.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Selective beta(1)-blockade improves cardiac bioenergetics and function and decreases neuroendocrine activation in rats during early postinfarct remodeling.",
+            "authors": [
+              "Omerovic E",
+              "Bollano E",
+              "Mobini R",
+              "Madhu B",
+              "Kujacic V",
+              "Soussi B",
+              "Hjalmarson A",
+              "Waagstein F"
+            ],
+            "journal": "Biochemical and biophysical research communications",
+            "year": "2001",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:26488593",
+          "snippet": "Several well designed, large scale randomized clinical trials including CIBS-II (bisoprolol), MERIT-HF (metoprolol succinate), and Copernicus (carvedilol) among others, have been conducted in patients with HFRef and demonstrated an improvement in cardiac mortality and morbidity.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Multiple large clinical trials demonstrate that metoprolol succinate improves cardiac mortality and morbidity in heart failure.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "The safety and tolerability of beta blockers in heart failure with reduced ejection fraction: is the current underutilization of this evidence-based therapy justified?",
+            "authors": [
+              "Kiel RG",
+              "Deedwania P"
+            ],
+            "journal": "Expert opinion on drug safety",
+            "year": "2015",
+            "doi": "10.1517/14740338.2015.1102225",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://www.drugbank.ca/drugs/DB00264",
+      "type": "drugbank",
+      "label": "drugbank.ca — record source"
+    },
+    {
+      "url": "https://meshb.nlm.nih.gov/record/ui?ui=D006333",
+      "type": "other",
+      "label": "meshb.nlm.nih.gov — record source"
+    }
+  ],
+  "site": {
+    "id": "sonnet__P04",
+    "record_id": "P04_DB00264_MESH_D006333",
+    "run": "sonnet",
+    "run_label": "Sonnet (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/sonnet/outputs/P04.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/sonnet__P05.json b/web-revamp-mockup/data/records/sonnet__P05.json
new file mode 100644
index 0000000..833c3c7
--- /dev/null
+++ b/web-revamp-mockup/data/records/sonnet__P05.json
@@ -0,0 +1,249 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P05_DB00758_MESH_D020521",
+    "drug": "Clopidogrel",
+    "drug_mesh": "MESH:D000077144",
+    "drugbank": "DB:DB00758",
+    "disease": "Stroke",
+    "disease_mesh": "MESH:D020521",
+    "summary": "Clopidogrel → Clopidogrel active metabolite → P2Y12 receptor → platelet aggregation → Stroke"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D000077144",
+      "name": "Clopidogrel",
+      "label": "Drug"
+    },
+    {
+      "id": "CHEBI:174738",
+      "name": "Clopidogrel active metabolite",
+      "label": "ChemicalSubstance"
+    },
+    {
+      "id": "UniProt:Q9H244",
+      "name": "P2Y12 receptor",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0070527",
+      "name": "platelet aggregation",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D020521",
+      "name": "Stroke",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "has metabolite",
+      "source": "MESH:D000077144",
+      "target": "CHEBI:174738",
+      "evidence": [
+        {
+          "reference": "PMID:22221409",
+          "snippet": "Clopidogrel is an antithrombotic prodrug, whose active metabolite inhibits platelet function by irreversibly binding to the platelet receptor for adenosine diphosphate, P2Y(12).",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Establishes that clopidogrel is a prodrug that generates an active metabolite responsible for its antiplatelet effect.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Response variability to clopidogrel: is tailored treatment, based on laboratory testing, the right solution?",
+            "authors": [
+              "Cattaneo M"
+            ],
+            "journal": "Journal of thrombosis and haemostasis : JTH",
+            "year": "2012",
+            "doi": "10.1111/j.1538-7836.2011.04602.x",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "CHEBI:174738",
+      "target": "UniProt:Q9H244",
+      "evidence": [
+        {
+          "reference": "PMID:23885646",
+          "snippet": "Clopidogrel is a thienopyridine that selectively and irreversibly inhibits the ADP purinergic receptor P2Y12 and the subsequent ADP-mediated platelet activation.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Directly states clopidogrel (via its active metabolite) irreversibly inhibits the P2Y12 receptor.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Clopidogrel generic formulations in the era of new antiplatelets: a systematic review.",
+            "authors": [
+              "Tsoumani ME",
+              "Kalantzi KI",
+              "Goudevenos IA",
+              "Tselepis AD"
+            ],
+            "journal": "Current vascular pharmacology",
+            "year": "2014",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:22221409",
+          "snippet": "Clopidogrel is an antithrombotic prodrug, whose active metabolite inhibits platelet function by irreversibly binding to the platelet receptor for adenosine diphosphate, P2Y(12).",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Response variability to clopidogrel: is tailored treatment, based on laboratory testing, the right solution?",
+            "authors": [
+              "Cattaneo M"
+            ],
+            "journal": "Journal of thrombosis and haemostasis : JTH",
+            "year": "2012",
+            "doi": "10.1111/j.1538-7836.2011.04602.x",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:Q9H244",
+      "target": "GO:0070527",
+      "evidence": [
+        {
+          "reference": "PMID:29439388",
+          "snippet": "Adenosine diphosphate (ADP) is the major platelet agonist, which is important in the shape changes, stability, and growth of the thrombus.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "P2Y12 is an ADP receptor; ADP acting through P2Y12 positively regulates platelet aggregation. The pharmacologic blockade of P2Y12 reduces platelet aggregation (per the same paper).",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Inhibitory Effect of Flavonolignans on the P2Y12 Pathway in Blood Platelets.",
+            "authors": [
+              "Bijak M",
+              "Szelenberger R",
+              "Dziedzic A",
+              "Saluk-Bijak J"
+            ],
+            "journal": "Molecules (Basel, Switzerland)",
+            "year": "2018",
+            "doi": "10.3390/molecules23020374",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:23885646",
+          "snippet": "Clopidogrel is a thienopyridine that selectively and irreversibly inhibits the ADP purinergic receptor P2Y12 and the subsequent ADP-mediated platelet activation.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Shows that P2Y12 mediates ADP-driven platelet activation, supporting that P2Y12 positively regulates platelet aggregation.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Clopidogrel generic formulations in the era of new antiplatelets: a systematic review.",
+            "authors": [
+              "Tsoumani ME",
+              "Kalantzi KI",
+              "Goudevenos IA",
+              "Tselepis AD"
+            ],
+            "journal": "Current vascular pharmacology",
+            "year": "2014",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "contributes to",
+      "source": "GO:0070527",
+      "target": "MESH:D020521",
+      "evidence": [
+        {
+          "reference": "PMID:22393298",
+          "snippet": "Platelet activation and aggregation play a seminal role in the arterial thrombus formation that precipitates acute manifestations of atherothrombotic disease.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Establishes platelet aggregation as contributing to arterial thrombus formation, which causes ischemic stroke (an atherothrombotic disease manifestation).",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Oral antiplatelet therapy for atherothrombotic disease: overview of current and emerging treatment options.",
+            "authors": [
+              "Fintel DJ"
+            ],
+            "journal": "Vascular health and risk management",
+            "year": "2012",
+            "doi": "10.2147/VHRM.S26030",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:35094598",
+          "snippet": "An abundance of evidence supports aspirin and clopidogrel use for secondary stroke prevention.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Clinical evidence that antiplatelet therapy (clopidogrel) prevents stroke, implicating platelet aggregation in stroke pathogenesis.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Antiplatelet Use in Ischemic Stroke.",
+            "authors": [
+              "Kamarova M",
+              "Baig S",
+              "Patel H",
+              "Monks K",
+              "Wasay M",
+              "Ali A",
+              "Redgrave J",
+              "Majid A",
+              "Bell SM"
+            ],
+            "journal": "The Annals of pharmacotherapy",
+            "year": "2022",
+            "doi": "10.1177/10600280211073009",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://www.drugbank.ca/drugs/DB00758",
+      "type": "drugbank",
+      "label": "drugbank.ca — record source"
+    },
+    {
+      "url": "https://pubchem.ncbi.nlm.nih.gov/compound/60606",
+      "type": "other",
+      "label": "pubchem.ncbi.nlm.nih.gov — record source"
+    }
+  ],
+  "site": {
+    "id": "sonnet__P05",
+    "record_id": "P05_DB00758_MESH_D020521",
+    "run": "sonnet",
+    "run_label": "Sonnet (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/sonnet/outputs/P05.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/sonnet__P06.json b/web-revamp-mockup/data/records/sonnet__P06.json
new file mode 100644
index 0000000..143b7a2
--- /dev/null
+++ b/web-revamp-mockup/data/records/sonnet__P06.json
@@ -0,0 +1,230 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P06_DB00675_MESH_D001943",
+    "drug": "Tamoxifen",
+    "drug_mesh": "MESH:D013629",
+    "drugbank": "DB:DB00675",
+    "disease": "Breast Cancer",
+    "disease_mesh": "MESH:D001943",
+    "summary": "Tamoxifen → 4-Hydroxytamoxifen → Estrogen receptor alpha → cell proliferation → Breast Cancer"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D013629",
+      "name": "Tamoxifen",
+      "label": "Drug"
+    },
+    {
+      "id": "CHEBI:44616",
+      "name": "4-Hydroxytamoxifen",
+      "label": "ChemicalSubstance"
+    },
+    {
+      "id": "UniProt:P03372",
+      "name": "Estrogen receptor alpha",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0008283",
+      "name": "cell proliferation",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D001943",
+      "name": "Breast Cancer",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "has metabolite",
+      "source": "MESH:D013629",
+      "target": "CHEBI:44616",
+      "evidence": [
+        {
+          "reference": "PMID:19574470",
+          "snippet": "Tamoxifen requires enzymatic activation by cytochrome P450 (CYP) enzymes for the formation of active metabolites 4-hydroxytamoxifen and endoxifen.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Tamoxifen is metabolised by CYP enzymes to form the active metabolite 4-hydroxytamoxifen.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Pharmacogenomics of tamoxifen therapy.",
+            "authors": [
+              "Brauch H",
+              "Mürdter TE",
+              "Eichelbaum M",
+              "Schwab M"
+            ],
+            "journal": "Clinical chemistry",
+            "year": "2009",
+            "doi": "10.1373/clinchem.2008.121756",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "CHEBI:44616",
+      "target": "UniProt:P03372",
+      "evidence": [
+        {
+          "reference": "PMID:19574470",
+          "snippet": "both metabolites have an approximately 100-fold greater affinity for the estrogen receptor and the ability to inhibit cell proliferation",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "4-Hydroxytamoxifen binds estrogen receptor alpha with ~100-fold greater affinity than tamoxifen and inhibits its activity.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Pharmacogenomics of tamoxifen therapy.",
+            "authors": [
+              "Brauch H",
+              "Mürdter TE",
+              "Eichelbaum M",
+              "Schwab M"
+            ],
+            "journal": "Clinical chemistry",
+            "year": "2009",
+            "doi": "10.1373/clinchem.2008.121756",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:22041137",
+          "snippet": "4-hydroxytamoxifen and endoxifen, which have 30- to 100-fold greater affinity to the estrogen receptor and the potency to suppress estrogen-dependent breast cancer cell proliferation",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Active tamoxifen metabolites including 4-hydroxytamoxifen have high affinity for the estrogen receptor and suppress its proliferative activity.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Pharmacogenomics of tamoxifen: roles of drug metabolizing enzymes and transporters.",
+            "authors": [
+              "Kiyotani K",
+              "Mushiroda T",
+              "Nakamura Y",
+              "Zembutsu H"
+            ],
+            "journal": "Drug metabolism and pharmacokinetics",
+            "year": "2012",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P03372",
+      "target": "GO:0008283",
+      "evidence": [
+        {
+          "reference": "PMID:19369047",
+          "snippet": "About two thirds of breast cancers in women are hormone-dependent and require estrogen for growth, its effects being mainly mediated through estrogen receptor alpha (ERalpha).",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Estrogen receptor alpha mediates estrogen-driven growth of hormone-dependent breast cancer cells.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Docosahexaenoic acid induces proteasome-dependent degradation of estrogen receptor alpha and inhibits the downstream signaling target in MCF-7 breast cancer cells.",
+            "authors": [
+              "Lu IF",
+              "Hasio AC",
+              "Hu MC",
+              "Yang FM",
+              "Su HM"
+            ],
+            "journal": "The Journal of nutritional biochemistry",
+            "year": "2010",
+            "doi": "10.1016/j.jnutbio.2009.02.009",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:20103625",
+          "snippet": "RBCK1 regulates cell cycle progression and proliferation of ERalpha-positive breast cancer cells by supporting transcription of ERalpha and cyclin B1",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "ERα supports cell cycle progression and proliferation in ER-positive breast cancer cells.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "RBCK1 drives breast cancer cell proliferation by promoting transcription of estrogen receptor alpha and cyclin B1.",
+            "authors": [
+              "Gustafsson N",
+              "Zhao C",
+              "Gustafsson JA",
+              "Dahlman-Wright K"
+            ],
+            "journal": "Cancer research",
+            "year": "2010",
+            "doi": "10.1158/0008-5472.CAN-09-2674",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "contributes to",
+      "source": "GO:0008283",
+      "target": "MESH:D001943",
+      "evidence": [
+        {
+          "reference": "PMID:33190190",
+          "snippet": "inhibit tumor cell proliferation by targeting ER signaling",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Endocrine therapies treat breast cancer by inhibiting tumor cell proliferation, demonstrating that cell proliferation contributes to breast cancer.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Clinical Challenges in the Management of Hormone Receptor-Positive, Human Epidermal Growth Factor Receptor 2-Negative Metastatic Breast Cancer: A Literature Review.",
+            "authors": [
+              "Nagaraj G",
+              "Ma CX"
+            ],
+            "journal": "Advances in therapy",
+            "year": "2021",
+            "doi": "10.1007/s12325-020-01552-2",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://www.drugbank.ca/drugs/DB00675",
+      "type": "drugbank",
+      "label": "drugbank.ca — record source"
+    },
+    {
+      "url": "https://www.ncbi.nlm.nih.gov/mesh/D013629",
+      "type": "other",
+      "label": "ncbi.nlm.nih.gov — record source"
+    }
+  ],
+  "site": {
+    "id": "sonnet__P06",
+    "record_id": "P06_DB00675_MESH_D001943",
+    "run": "sonnet",
+    "run_label": "Sonnet (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/sonnet/outputs/P06.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/sonnet__P07.json b/web-revamp-mockup/data/records/sonnet__P07.json
new file mode 100644
index 0000000..c06aa68
--- /dev/null
+++ b/web-revamp-mockup/data/records/sonnet__P07.json
@@ -0,0 +1,327 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P07_DB00619_MESH_D015464",
+    "drug": "Imatinib",
+    "drug_mesh": "MESH:D000068877",
+    "drugbank": "DB:DB00619",
+    "disease": "Chronic Myeloid Leukemia",
+    "disease_mesh": "MESH:D015464",
+    "summary": "Imatinib → BCR-ABL fusion protein → cell proliferation → Chronic Myeloid Leukemia"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D000068877",
+      "name": "Imatinib",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P00519",
+      "name": "BCR-ABL fusion protein",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0008283",
+      "name": "cell proliferation",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "GO:0006915",
+      "name": "apoptotic process",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D015464",
+      "name": "Chronic Myeloid Leukemia",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D000068877",
+      "target": "UniProt:P00519",
+      "evidence": [
+        {
+          "reference": "PMID:38280275",
+          "snippet": "imatinib, effectively target BCR-ABL's tyrosine kinase activity by binding near the active site, disrupting ATP binding, and inhibiting downstream protein phosphorylation",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "The impact of the BCR-ABL oncogene in the pathology and treatment of chronic myeloid leukemia.",
+            "authors": [
+              "El-Tanani M",
+              "Nsairat H",
+              "Matalka II",
+              "Lee YF",
+              "Rizzo M",
+              "Aljabali AA",
+              "Mishra V",
+              "Mishra Y",
+              "Hromić-Jahjefendić A",
+              "Tambuwala MM"
+            ],
+            "journal": "Pathology, research and practice",
+            "year": "2024",
+            "doi": "10.1016/j.prp.2024.155161",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:11831067",
+          "snippet": "STI571 was shown to be a competitive inhibitor at the ATP-binding site of the Bcr-Abl tyrosine kinase",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "[Bcr-Abl inhibition as molecular therapy approach in chronic myeloid leukemia].",
+            "authors": [
+              "Buchdunger E"
+            ],
+            "journal": "Medizinische Klinik (Munich, Germany : 1983)",
+            "year": "2002",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P00519",
+      "target": "GO:0008283",
+      "evidence": [
+        {
+          "reference": "PMID:16113647",
+          "snippet": "constitutive activation of Abl tyrosine kinase, which in turn induces growth-factor-independent proliferation and cell survival",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Bcr-Abl activates the AKT/Fox O3 signalling pathway to restrict transforming growth factor-beta-mediated cytostatic signals.",
+            "authors": [
+              "Atfi A",
+              "Abécassis L",
+              "Bourgeade MF"
+            ],
+            "journal": "EMBO reports",
+            "year": "2005",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:35313299",
+          "snippet": "Chronic myeloid leukaemia (CML) is a myeloproliferative neoplasm characterized by constitutive activity of the tyrosine kinase BCR-ABL1",
+          "supports": "PARTIAL",
+          "evidence_source": "HUMAN_CLINICAL",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "MiR-199a-3p Overexpression Suppressed Cell Proliferation and Sensitized Chronic Myeloid Leukaemia Cells to Imatinib by Inhibiting mTOR Signalling.",
+            "authors": [
+              "Liu X",
+              "Cui MM",
+              "Zhu HZ",
+              "Fu PY",
+              "Wang GC",
+              "Huang L"
+            ],
+            "journal": "Acta haematologica",
+            "year": "2022",
+            "doi": "10.1159/000524158",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "decreased",
+      "source": "UniProt:P00519",
+      "target": "GO:0006915",
+      "evidence": [
+        {
+          "reference": "PMID:16113647",
+          "snippet": "Bcr-Abl-expressing cells are resistant to growth inhibition and apoptosis mediated by transforming growth factor-beta",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Bcr-Abl activates the AKT/Fox O3 signalling pathway to restrict transforming growth factor-beta-mediated cytostatic signals.",
+            "authors": [
+              "Atfi A",
+              "Abécassis L",
+              "Bourgeade MF"
+            ],
+            "journal": "EMBO reports",
+            "year": "2005",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:9111865",
+          "snippet": "The identification of various genetic abnormalities which influence apoptosis in leukaemic cells (e.g., mutant p53, Bcr-Abl and over-expression of Bcl-2), suggests that the acquisition of an anti-apoptotic lesions is an important event in the multi-step evolution of hematological malignancies",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Functional aspects of apoptosis in hematopoiesis and consequences of failure.",
+            "authors": [
+              "McKenna SL",
+              "Cotter TG"
+            ],
+            "journal": "Advances in cancer research",
+            "year": "1997",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "contributes to",
+      "source": "GO:0008283",
+      "target": "MESH:D015464",
+      "evidence": [
+        {
+          "reference": "PMID:38280275",
+          "snippet": "In CML, the BCR-ABL fusion protein disrupts the first exon of Abl, leading to sustained activation of tyrosine kinase and resistance to deactivation mechanisms",
+          "supports": "PARTIAL",
+          "evidence_source": "HUMAN_CLINICAL",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "The impact of the BCR-ABL oncogene in the pathology and treatment of chronic myeloid leukemia.",
+            "authors": [
+              "El-Tanani M",
+              "Nsairat H",
+              "Matalka II",
+              "Lee YF",
+              "Rizzo M",
+              "Aljabali AA",
+              "Mishra V",
+              "Mishra Y",
+              "Hromić-Jahjefendić A",
+              "Tambuwala MM"
+            ],
+            "journal": "Pathology, research and practice",
+            "year": "2024",
+            "doi": "10.1016/j.prp.2024.155161",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:11831067",
+          "snippet": "In vitro studies and studies in animal models have shown, that Bcr-Abl is the molecular cause CML",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "[Bcr-Abl inhibition as molecular therapy approach in chronic myeloid leukemia].",
+            "authors": [
+              "Buchdunger E"
+            ],
+            "journal": "Medizinische Klinik (Munich, Germany : 1983)",
+            "year": "2002",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "contributes to",
+      "source": "GO:0006915",
+      "target": "MESH:D015464",
+      "evidence": [
+        {
+          "reference": "PMID:9111865",
+          "snippet": "ineffective apoptosis has been associated with the development of inflammation, autoimmunity and hematological malignancies",
+          "supports": "PARTIAL",
+          "evidence_source": "OTHER",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Functional aspects of apoptosis in hematopoiesis and consequences of failure.",
+            "authors": [
+              "McKenna SL",
+              "Cotter TG"
+            ],
+            "journal": "Advances in cancer research",
+            "year": "1997",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:22207735",
+          "snippet": "SIRT1 activation promotes CML cell survival and proliferation associated with deacetylation of multiple SIRT1 substrates",
+          "supports": "PARTIAL",
+          "evidence_source": "IN_VITRO",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Activation of stress response gene SIRT1 by BCR-ABL promotes leukemogenesis.",
+            "authors": [
+              "Yuan H",
+              "Wang Z",
+              "Li L",
+              "Zhang H",
+              "Modi H",
+              "Horne D",
+              "Bhatia R",
+              "Chen W"
+            ],
+            "journal": "Blood",
+            "year": "2012",
+            "doi": "10.1182/blood-2011-06-361691",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://www.drugbank.ca/drugs/DB00619",
+      "type": "drugbank",
+      "label": "drugbank.ca — record source"
+    },
+    {
+      "url": "https://www.ncbi.nlm.nih.gov/mesh/D015464",
+      "type": "other",
+      "label": "ncbi.nlm.nih.gov — record source"
+    }
+  ],
+  "site": {
+    "id": "sonnet__P07",
+    "record_id": "P07_DB00619_MESH_D015464",
+    "run": "sonnet",
+    "run_label": "Sonnet (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/sonnet/outputs/P07.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/sonnet__P08.json b/web-revamp-mockup/data/records/sonnet__P08.json
new file mode 100644
index 0000000..fc4f433
--- /dev/null
+++ b/web-revamp-mockup/data/records/sonnet__P08.json
@@ -0,0 +1,236 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P08_DB00002_MESH_D015179",
+    "drug": "Cetuximab",
+    "drug_mesh": "MESH:D000068818",
+    "drugbank": "DB:DB00002",
+    "disease": "Colorectal Cancer",
+    "disease_mesh": "MESH:D015179",
+    "summary": "Cetuximab → Epidermal growth factor receptor → cell population proliferation → Colorectal Cancer"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D000068818",
+      "name": "Cetuximab",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P00533",
+      "name": "Epidermal growth factor receptor",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0008283",
+      "name": "cell population proliferation",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D015179",
+      "name": "Colorectal Cancer",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "directly physically interacts with",
+      "source": "MESH:D000068818",
+      "target": "UniProt:P00533",
+      "evidence": [
+        {
+          "reference": "PMID:20088790",
+          "snippet": "Cetuximab (IMC-C225, Erbitux ImClone Systems Inc, New York, NY) is a recombinant, human/mouse chimeric monoclonal antibody (MAb) that binds specifically to the extracellular domain of the human epidermal growth factor receptor (EGFR) on both normal and tumor cells, and competitively inhibits the binding of epidermal growth factor (EGF) as well as other ligands.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Cetuximab binds specifically to the extracellular domain of EGFR (UniProt:P00533).",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Cetuximab: from bench to bedside.",
+            "authors": [
+              "Vincenzi B",
+              "Zoccoli A",
+              "Pantano F",
+              "Venditti O",
+              "Galluzzo S"
+            ],
+            "journal": "Current cancer drug targets",
+            "year": "2010",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D000068818",
+      "target": "UniProt:P00533",
+      "evidence": [
+        {
+          "reference": "PMID:20088790",
+          "snippet": "Cetuximab binding to the EGFR blocks phosphorylation and activation of receptor-associated kinases and their associated downstream signalling (MAPK, PI3K/Akt, Jak/Stat pathways) resulting in inhibition of many cellular processes such as induction of apoptosis, cell growth, decreased Matrix Metallo-Proteinase (MMPs) and vascular endothelial growth factor (VEGF) production.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Cetuximab binding blocks EGFR phosphorylation and downstream kinase activation, thereby decreasing EGFR signaling activity.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Cetuximab: from bench to bedside.",
+            "authors": [
+              "Vincenzi B",
+              "Zoccoli A",
+              "Pantano F",
+              "Venditti O",
+              "Galluzzo S"
+            ],
+            "journal": "Current cancer drug targets",
+            "year": "2010",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P00533",
+      "target": "GO:0008283",
+      "evidence": [
+        {
+          "reference": "PMID:15341677",
+          "snippet": "When activated, EGFR phosphorylates and activates other intracellular proteins that affect cell signaling pathways, cellular proliferation, control of apoptosis and angiogenesis.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Activated EGFR drives cellular proliferation through downstream signaling cascades.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "The epidermal growth factor receptor as a target for gastrointestinal cancer therapy.",
+            "authors": [
+              "Tedesco KL",
+              "Lockhart AC",
+              "Berlin JD"
+            ],
+            "journal": "Current treatment options in oncology",
+            "year": "2004",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:19747140",
+          "snippet": "EGFR signaling pathway is implicated in the control of cell survival, proliferation, metastasis and angiogenesis.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "EGFR positively regulates cell proliferation as part of its canonical signaling activity.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Targeting epidermal growth factor receptor in solid tumors: critical evaluation of the biological importance of therapeutic monoclonal antibodies.",
+            "authors": [
+              "Gialeli Ch",
+              "Kletsas D",
+              "Mavroudis D",
+              "Kalofonos HP",
+              "Tzanakakis GN",
+              "Karamanos NK"
+            ],
+            "journal": "Current medicinal chemistry",
+            "year": "2009",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "contributes to",
+      "source": "GO:0008283",
+      "target": "MESH:D015179",
+      "evidence": [
+        {
+          "reference": "PMID:15717942",
+          "snippet": "The strategy of using monoclonal antibodies (mAbs) to block ligand binding to the extracellular domain of the EGFR has led to the development of therapeutics that robustly arrest malignant cell proliferation and, in some cases, induce profound tumor regression.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Blocking EGFR-driven malignant cell proliferation produces tumor regression, indicating that cell proliferation contributes to colorectal cancer progression.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Clinical experience with monoclonal antibodies to epidermal growth factor receptor.",
+            "authors": [
+              "Calvo E",
+              "Rowinsky EK"
+            ],
+            "journal": "Current oncology reports",
+            "year": "2005",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:33989949",
+          "snippet": "cetuximab inhibits the EGFR signaling pathway, inhibiting proliferation and inducing apoptosis.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Inhibiting proliferation by cetuximab is associated with anti-tumor effects in colorectal cancer.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Avelumab and cetuximab as a therapeutic combination: An overview of scientific rationale and current clinical trials in cancer.",
+            "authors": [
+              "Bourhis J",
+              "Stein A",
+              "Paul de Boer J",
+              "Van Den Eynde M",
+              "Gold KA",
+              "Stintzing S",
+              "Becker JC",
+              "Moran M",
+              "Schroeder A",
+              "Pennock G",
+              "Salmio S",
+              "Esser R",
+              "Ciardiello F"
+            ],
+            "journal": "Cancer treatment reviews",
+            "year": "2021",
+            "doi": "10.1016/j.ctrv.2021.102172",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://www.drugbank.ca/drugs/DB00002",
+      "type": "drugbank",
+      "label": "drugbank.ca — record source"
+    },
+    {
+      "url": "https://www.ncbi.nlm.nih.gov/mesh/D000068818",
+      "type": "other",
+      "label": "ncbi.nlm.nih.gov — record source"
+    }
+  ],
+  "site": {
+    "id": "sonnet__P08",
+    "record_id": "P08_DB00002_MESH_D015179",
+    "run": "sonnet",
+    "run_label": "Sonnet (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/sonnet/outputs/P08.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/sonnet__P09.json b/web-revamp-mockup/data/records/sonnet__P09.json
new file mode 100644
index 0000000..48df097
--- /dev/null
+++ b/web-revamp-mockup/data/records/sonnet__P09.json
@@ -0,0 +1,281 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P09_DB00563_MESH_D054198",
+    "drug": "Methotrexate",
+    "drug_mesh": "MESH:D008727",
+    "drugbank": "DB:DB00563",
+    "disease": "Acute Lymphoblastic Leukemia",
+    "disease_mesh": "MESH:D054198",
+    "summary": "Methotrexate → Dihydrofolate reductase → dTMP biosynthetic process → DNA biosynthetic process"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D008727",
+      "name": "Methotrexate",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P00374",
+      "name": "Dihydrofolate reductase",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0006231",
+      "name": "dTMP biosynthetic process",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "GO:0071897",
+      "name": "DNA biosynthetic process",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D054198",
+      "name": "Acute Lymphoblastic Leukemia",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D008727",
+      "target": "UniProt:P00374",
+      "evidence": [
+        {
+          "reference": "PMID:37941559",
+          "snippet": "Working by inhibiting dihydrofolate reductase and thereby preventing eventual formation of tetrahydrofolate, methotrexate inhibits synthesis of purines and thymidylate, therefore disabling a malignant cell's ability to replicate.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Methotrexate directly inhibits DHFR, preventing tetrahydrofolate formation.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Case Report: Serum methotrexate monitoring by immunoassay: confusion by by-product, confusion by antidote.",
+            "authors": [
+              "Sharma A",
+              "Benoit P",
+              "Lansigan F",
+              "Nierenberg D"
+            ],
+            "journal": "Frontiers in oncology",
+            "year": "2023",
+            "doi": "10.3389/fonc.2023.1237178",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:19959110",
+          "snippet": "the role of dihydrofolate reductase (DHFR), the principal target of aminopterin, has been studied extensively",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "DHFR is established as the principal target of antifolates including methotrexate.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Cancer research: from folate antagonism to molecular targets.",
+            "authors": [
+              "Bertino JR"
+            ],
+            "journal": "Best practice & research. Clinical haematology",
+            "year": "2009",
+            "doi": "10.1016/j.beha.2009.09.004",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "participates in",
+      "source": "UniProt:P00374",
+      "target": "GO:0006231",
+      "evidence": [
+        {
+          "reference": "PMID:10623528",
+          "snippet": "Dihydrofolate reductase (DHFR) catalyzes the NADPH-dependent reduction of dihydrofolate to tetrahydrofolate and is essential for the synthesis of thymidylate, purines and several amino acids.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "DHFR provides the tetrahydrofolate cofactor required for thymidylate (dTMP) biosynthesis.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Three-dimensional structure of M. tuberculosis dihydrofolate reductase reveals opportunities for the design of novel tuberculosis drugs.",
+            "authors": [
+              "Li R",
+              "Sirawaraporn R",
+              "Chitnumsub P",
+              "Sirawaraporn W",
+              "Wooden J",
+              "Athappilly F",
+              "Turley S",
+              "Hol WG"
+            ],
+            "journal": "Journal of molecular biology",
+            "year": "2000",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "participates in",
+      "source": "GO:0006231",
+      "target": "GO:0071897",
+      "evidence": [
+        {
+          "reference": "PMID:14529544",
+          "snippet": "inhibition of both dTMP synthesis and de novo purine synthesis, secondary to DHFR inhibition, led to DNA synthesis inhibition and subsequent cell death",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "dTMP biosynthesis is required for DNA synthesis; inhibiting dTMP synthesis directly inhibits DNA replication.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Anticancer antifolates: current status and future directions.",
+            "authors": [
+              "McGuire JJ"
+            ],
+            "journal": "Current pharmaceutical design",
+            "year": "2003",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D008727",
+      "target": "GO:0071897",
+      "evidence": [
+        {
+          "reference": "PMID:37941559",
+          "snippet": "methotrexate inhibits synthesis of purines and thymidylate, therefore disabling a malignant cell's ability to replicate.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Methotrexate ultimately inhibits DNA synthesis through its effect on folate-dependent nucleotide biosynthesis.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Case Report: Serum methotrexate monitoring by immunoassay: confusion by by-product, confusion by antidote.",
+            "authors": [
+              "Sharma A",
+              "Benoit P",
+              "Lansigan F",
+              "Nierenberg D"
+            ],
+            "journal": "Frontiers in oncology",
+            "year": "2023",
+            "doi": "10.3389/fonc.2023.1237178",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:10623528",
+          "snippet": "Inhibition of the enzyme's activity leads to arrest of DNA synthesis and cell death.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "DHFR inhibition by methotrexate arrests DNA synthesis and leads to cell death.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Three-dimensional structure of M. tuberculosis dihydrofolate reductase reveals opportunities for the design of novel tuberculosis drugs.",
+            "authors": [
+              "Li R",
+              "Sirawaraporn R",
+              "Chitnumsub P",
+              "Sirawaraporn W",
+              "Wooden J",
+              "Athappilly F",
+              "Turley S",
+              "Hol WG"
+            ],
+            "journal": "Journal of molecular biology",
+            "year": "2000",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "treats",
+      "source": "MESH:D008727",
+      "target": "MESH:D054198",
+      "evidence": [
+        {
+          "reference": "PMID:19959110",
+          "snippet": "Aminopterin was the first drug reported to cause remissions in children with acute lymphocytic leukaemia, and methotrexate (MTX), the antifolate that has supplemented aminopterin in the clinic",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Methotrexate is an established treatment for acute lymphoblastic leukemia, having replaced aminopterin in clinical practice.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Cancer research: from folate antagonism to molecular targets.",
+            "authors": [
+              "Bertino JR"
+            ],
+            "journal": "Best practice & research. Clinical haematology",
+            "year": "2009",
+            "doi": "10.1016/j.beha.2009.09.004",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:30706807",
+          "snippet": "MTX acts on a variety of target enzymes in the folates cycle, as well as being transported out and into of the cell by several transmembrane proteins.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Methotrexate is a pivotal drug in ALL treatment protocols.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Clinical Implications of Methotrexate Pharmacogenetics in Childhood Acute Lymphoblastic Leukaemia.",
+            "authors": [
+              "Gervasini G",
+              "Mota-Zamorano S"
+            ],
+            "journal": "Current drug metabolism",
+            "year": "2019",
+            "doi": "10.2174/1389200220666190130161758",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://www.drugbank.ca/drugs/DB00563",
+      "type": "drugbank",
+      "label": "drugbank.ca — record source"
+    },
+    {
+      "url": "https://www.ncbi.nlm.nih.gov/books/NBK8000/",
+      "type": "other",
+      "label": "ncbi.nlm.nih.gov — record source"
+    }
+  ],
+  "site": {
+    "id": "sonnet__P09",
+    "record_id": "P09_DB00563_MESH_D054198",
+    "run": "sonnet",
+    "run_label": "Sonnet (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/sonnet/outputs/P09.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/sonnet__P10.json b/web-revamp-mockup/data/records/sonnet__P10.json
new file mode 100644
index 0000000..85d3d95
--- /dev/null
+++ b/web-revamp-mockup/data/records/sonnet__P10.json
@@ -0,0 +1,190 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P10_DB00072_MESH_D001943",
+    "drug": "Trastuzumab",
+    "drug_mesh": "MESH:D000068878",
+    "drugbank": "DB:DB00072",
+    "disease": "HER2-positive Breast Cancer",
+    "disease_mesh": "MESH:D001943",
+    "summary": "Trastuzumab → HER2 → AKT1 → cell proliferation → HER2-positive Breast Cancer"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D000068878",
+      "name": "Trastuzumab",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P04626",
+      "name": "HER2",
+      "label": "Protein"
+    },
+    {
+      "id": "UniProt:P31749",
+      "name": "AKT1",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0008283",
+      "name": "cell proliferation",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D001943",
+      "name": "HER2-positive Breast Cancer",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D000068878",
+      "target": "UniProt:P04626",
+      "evidence": [
+        {
+          "reference": "PMID:19884552",
+          "snippet": "At least five potential extracellular and intracellular antitumor mechanisms of trastuzumab have been identified in the preclinical setting. These include activation of antibody-dependent cellular cytotoxicity, inhibition of extracellular domain cleavage, abrogation of intracellular signaling, reduction of angiogenesis, and decreased DNA repair.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Trastuzumab abrogates intracellular signaling downstream of HER2, effectively decreasing HER2-mediated signaling activity.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Understanding the mechanisms behind trastuzumab therapy for human epidermal growth factor receptor 2-positive breast cancer.",
+            "authors": [
+              "Spector NL",
+              "Blackwell KL"
+            ],
+            "journal": "Journal of clinical oncology : official journal of the American Society of Clinical Oncology",
+            "year": "2009",
+            "doi": "10.1200/JCO.2009.22.1507",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P04626",
+      "target": "UniProt:P31749",
+      "evidence": [
+        {
+          "reference": "PMID:12853564",
+          "snippet": "ErbB3's role, which is to couple active ErbB2 to the phosphatidylinositol 3-kinase/protein kinase B pathway. Thus, the ErbB2/ErbB3 dimer functions as an oncogenic unit to drive breast tumor cell proliferation.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "HER2 (ErbB2) activates the PI3K/AKT (protein kinase B) pathway, demonstrating HER2 positively regulates AKT1 signaling.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "The ErbB2/ErbB3 heterodimer functions as an oncogenic unit: ErbB2 requires ErbB3 to drive breast tumor cell proliferation.",
+            "authors": [
+              "Holbro T",
+              "Beerli RR",
+              "Maurer F",
+              "Koziczak M",
+              "Barbas CF",
+              "Hynes NE"
+            ],
+            "journal": "Proceedings of the National Academy of Sciences of the United States of America",
+            "year": "2003",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P31749",
+      "target": "GO:0008283",
+      "evidence": [
+        {
+          "reference": "PMID:42207644",
+          "snippet": "Functionally, AKT1 glutarylation inhibits cell proliferation and tumor growth, whereas GCDH promotes these oncogenic functions by suppressing glutarylation.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "AKT1 activity promotes cell proliferation; glutarylation-mediated inhibition of AKT1 blocks proliferation, confirming AKT1 positively regulates cell proliferation.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "AKT1 glutarylation regulated by GCDH and SIRT5 suppresses oncogenic signaling.",
+            "authors": [
+              "Bai L",
+              "Liao R",
+              "Zhang Y",
+              "Jia Y",
+              "Shi L",
+              "Xu H",
+              "Liang L",
+              "Feng Y",
+              "Dong C"
+            ],
+            "journal": "Cell reports",
+            "year": "2026",
+            "doi": "10.1016/j.celrep.2026.117394",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "contributes to",
+      "source": "GO:0008283",
+      "target": "MESH:D001943",
+      "evidence": [
+        {
+          "reference": "PMID:22865781",
+          "snippet": "Approximately 15%-23% of breast cancers overexpress human epidermal growth factor receptor 2 (HER2), which leads to the activation of signaling pathways that stimulate cell proliferation and survival.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "HER2 overexpression-driven cell proliferation contributes to the development and progression of HER2-positive breast cancer.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Overcoming resistance and restoring sensitivity to HER2-targeted therapies in breast cancer.",
+            "authors": [
+              "Mohd Sharial MSN",
+              "Crown J",
+              "Hennessy BT"
+            ],
+            "journal": "Annals of oncology : official journal of the European Society for Medical Oncology",
+            "year": "2012",
+            "doi": "10.1093/annonc/mds200",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://www.drugbank.ca/drugs/DB00072",
+      "type": "drugbank",
+      "label": "drugbank.ca — record source"
+    },
+    {
+      "url": "https://go.drugbank.com/drugs/DB00072",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    }
+  ],
+  "site": {
+    "id": "sonnet__P10",
+    "record_id": "P10_DB00072_MESH_D001943",
+    "run": "sonnet",
+    "run_label": "Sonnet (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/sonnet/outputs/P10.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/sonnet__P11.json b/web-revamp-mockup/data/records/sonnet__P11.json
new file mode 100644
index 0000000..fc924a5
--- /dev/null
+++ b/web-revamp-mockup/data/records/sonnet__P11.json
@@ -0,0 +1,303 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P11_DB01045_MESH_D014397",
+    "drug": "Rifampicin",
+    "drug_mesh": "MESH:D012293",
+    "drugbank": "DB:DB01045",
+    "disease": "Pulmonary Tuberculosis",
+    "disease_mesh": "MESH:D014397",
+    "summary": "Rifampicin → DNA-directed RNA polymerase subunit beta → DNA-templated transcription"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D012293",
+      "name": "Rifampicin",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P9WKP4",
+      "name": "DNA-directed RNA polymerase subunit beta",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0006351",
+      "name": "DNA-templated transcription",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D014397",
+      "name": "Pulmonary Tuberculosis",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D012293",
+      "target": "UniProt:P9WKP4",
+      "evidence": [
+        {
+          "reference": "PMID:33877820",
+          "snippet": "Rifamycins act by binding to the β-subunit of bacterial RNA polymerase, inhibiting transcription, which results in cell death.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Rifampicin (a rifamycin) binds to and inhibits the beta-subunit of bacterial RNA polymerase (RpoB, UniProt:P9WKP4 in M. tuberculosis).",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "The Enzymes of the Rifamycin Antibiotic Resistome.",
+            "authors": [
+              "Surette MD",
+              "Spanogiannopoulos P",
+              "Wright GD"
+            ],
+            "journal": "Accounts of chemical research",
+            "year": "2021",
+            "doi": "10.1021/acs.accounts.1c00048",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:28392175",
+          "snippet": "Rif functions by a steric-occlusion mechanism that prevents extension of RNA.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Structural studies confirm rifampin binding to and inhibiting the function of M. tuberculosis RNAP, whose beta subunit is RpoB.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Structural Basis of Mycobacterium tuberculosis Transcription and Transcription Inhibition.",
+            "authors": [
+              "Lin W",
+              "Mandal S",
+              "Degen D",
+              "Liu Y",
+              "Ebright YW",
+              "Li S",
+              "Feng Y",
+              "Zhang Y",
+              "Mandal S",
+              "Jiang Y",
+              "Liu S",
+              "Gigliotti M",
+              "Talaue M",
+              "Connell N",
+              "Das K",
+              "Arnold E",
+              "Ebright RH"
+            ],
+            "journal": "Molecular cell",
+            "year": "2017",
+            "doi": "10.1016/j.molcel.2017.03.001",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "participates in",
+      "source": "UniProt:P9WKP4",
+      "target": "GO:0006351",
+      "evidence": [
+        {
+          "reference": "PMID:33877820",
+          "snippet": "Rifamycins act by binding to the β-subunit of bacterial RNA polymerase, inhibiting transcription, which results in cell death.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "The RNA polymerase beta subunit (RpoB) is a core catalytic component of the bacterial RNA polymerase complex that carries out DNA-templated transcription.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "The Enzymes of the Rifamycin Antibiotic Resistome.",
+            "authors": [
+              "Surette MD",
+              "Spanogiannopoulos P",
+              "Wright GD"
+            ],
+            "journal": "Accounts of chemical research",
+            "year": "2021",
+            "doi": "10.1021/acs.accounts.1c00048",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:28392175",
+          "snippet": "Rif functions by a steric-occlusion mechanism that prevents extension of RNA.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "RpoB is the subunit through which RNA extension (transcription) occurs; rifampicin blocks this activity by steric occlusion.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Structural Basis of Mycobacterium tuberculosis Transcription and Transcription Inhibition.",
+            "authors": [
+              "Lin W",
+              "Mandal S",
+              "Degen D",
+              "Liu Y",
+              "Ebright YW",
+              "Li S",
+              "Feng Y",
+              "Zhang Y",
+              "Mandal S",
+              "Jiang Y",
+              "Liu S",
+              "Gigliotti M",
+              "Talaue M",
+              "Connell N",
+              "Das K",
+              "Arnold E",
+              "Ebright RH"
+            ],
+            "journal": "Molecular cell",
+            "year": "2017",
+            "doi": "10.1016/j.molcel.2017.03.001",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D012293",
+      "target": "GO:0006351",
+      "evidence": [
+        {
+          "reference": "PMID:41339746",
+          "snippet": "Rifampicin, a cornerstone of first-line therapy, inhibits transcription during promoter escape",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Rifampicin negatively regulates bacterial DNA-templated transcription by blocking the RNA polymerase during promoter escape.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Transcription co-inhibition alters drug resistance evolution and enhances Mycobacterium tuberculosis clearance from granulomas.",
+            "authors": [
+              "Bosch B",
+              "Munsamy-Govender V",
+              "Sarathy J",
+              "Lilic M",
+              "Olinares PDB",
+              "Eckartt KA",
+              "Nalam P",
+              "Lang M",
+              "Simon M",
+              "Richter A",
+              "Rock JM",
+              "Campbell EA"
+            ],
+            "journal": "Nature microbiology",
+            "year": "2026",
+            "doi": "10.1038/s41564-025-02201-6",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:33877820",
+          "snippet": "Rifamycins act by binding to the β-subunit of bacterial RNA polymerase, inhibiting transcription, which results in cell death.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "The Enzymes of the Rifamycin Antibiotic Resistome.",
+            "authors": [
+              "Surette MD",
+              "Spanogiannopoulos P",
+              "Wright GD"
+            ],
+            "journal": "Accounts of chemical research",
+            "year": "2021",
+            "doi": "10.1021/acs.accounts.1c00048",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "treats",
+      "source": "MESH:D012293",
+      "target": "MESH:D014397",
+      "evidence": [
+        {
+          "reference": "PMID:33877820",
+          "snippet": "These antibiotics are primarily used to treat mycobacterial infections, including tuberculosis.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Rifampicin (a rifamycin antibiotic) is used to treat tuberculosis, including pulmonary tuberculosis.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "The Enzymes of the Rifamycin Antibiotic Resistome.",
+            "authors": [
+              "Surette MD",
+              "Spanogiannopoulos P",
+              "Wright GD"
+            ],
+            "journal": "Accounts of chemical research",
+            "year": "2021",
+            "doi": "10.1021/acs.accounts.1c00048",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:28392175",
+          "snippet": "Mtb RNA polymerase (RNAP) is the target of the first-line antituberculosis drug rifampin (Rif).",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Rifampin (rifampicin) is a first-line antituberculosis drug used to treat pulmonary tuberculosis caused by M. tuberculosis.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Structural Basis of Mycobacterium tuberculosis Transcription and Transcription Inhibition.",
+            "authors": [
+              "Lin W",
+              "Mandal S",
+              "Degen D",
+              "Liu Y",
+              "Ebright YW",
+              "Li S",
+              "Feng Y",
+              "Zhang Y",
+              "Mandal S",
+              "Jiang Y",
+              "Liu S",
+              "Gigliotti M",
+              "Talaue M",
+              "Connell N",
+              "Das K",
+              "Arnold E",
+              "Ebright RH"
+            ],
+            "journal": "Molecular cell",
+            "year": "2017",
+            "doi": "10.1016/j.molcel.2017.03.001",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [],
+  "site": {
+    "id": "sonnet__P11",
+    "record_id": "P11_DB01045_MESH_D014397",
+    "run": "sonnet",
+    "run_label": "Sonnet (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/sonnet/outputs/P11.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/sonnet__P12.json b/web-revamp-mockup/data/records/sonnet__P12.json
new file mode 100644
index 0000000..cbb6773
--- /dev/null
+++ b/web-revamp-mockup/data/records/sonnet__P12.json
@@ -0,0 +1,236 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P12_DB00951_MESH_D014397",
+    "drug": "Isoniazid",
+    "drug_mesh": "MESH:D007538",
+    "drugbank": "DB:DB00951",
+    "disease": "Pulmonary Tuberculosis",
+    "disease_mesh": "MESH:D014397",
+    "summary": "Isoniazid → InhA → mycolic acid biosynthetic process → Mycobacterium tuberculosis → Pulmonary Tuberculosis"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D007538",
+      "name": "Isoniazid",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P0A5Q9",
+      "name": "InhA",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0001560",
+      "name": "mycolic acid biosynthetic process",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "NCBITaxon:1773",
+      "name": "Mycobacterium tuberculosis",
+      "label": "OrganismTaxon"
+    },
+    {
+      "id": "MESH:D014397",
+      "name": "Pulmonary Tuberculosis",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D007538",
+      "target": "UniProt:P0A5Q9",
+      "evidence": [
+        {
+          "reference": "PMID:9949810",
+          "snippet": "A reactive form of isoniazid inhibits InhA by reacting with the NAD(H) cofactor bound to the enzyme active site forming a covalent adduct (isonicotinic acyl NADH) that is apt to bind with high affinity.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Isoniazid is a prodrug activated by the mycobacterial catalase-peroxidase KatG; the resulting isonicotinoyl-NAD adduct inhibits InhA (enoyl-ACP reductase).",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Mechanisms for isoniazid action and resistance.",
+            "authors": [
+              "Miesel L",
+              "Rozwarski DA",
+              "Sacchettini JC",
+              "Jacobs WR"
+            ],
+            "journal": "Novartis Foundation symposium",
+            "year": "1998",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:29765372",
+          "snippet": "This isonicotinyl-NAD adduct inhibits the activity of 2-trans-enoyl-ACP(CoA) reductase (InhA), which plays a role in mycolic acid biosynthesis.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Is IQG-607 a Potential Metallodrug or Metallopro-Drug With a Defined Molecular Target in Mycobacterium tuberculosis?",
+            "authors": [
+              "Abbadi BL",
+              "Rodrigues-Junior VDS",
+              "Dadda ADS",
+              "Pissinate K",
+              "Villela AD",
+              "Campos MM",
+              "Lopes LGF",
+              "Bizarro CV",
+              "Machado P",
+              "Sousa EHS",
+              "Basso LA"
+            ],
+            "journal": "Frontiers in microbiology",
+            "year": "2018",
+            "doi": "10.3389/fmicb.2018.00880",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "participates in",
+      "source": "UniProt:P0A5Q9",
+      "target": "GO:0001560",
+      "evidence": [
+        {
+          "reference": "PMID:21143326",
+          "snippet": "InhA, an essential enzyme of the mycolic acid biosynthetic pathway and the primary target of the anti-tubercular drug isoniazid",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "explanation": "InhA is an enoyl-ACP reductase essential for the mycolic acid biosynthetic pathway.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Phosphorylation of InhA inhibits mycolic acid biosynthesis and growth of Mycobacterium tuberculosis.",
+            "authors": [
+              "Molle V",
+              "Gulten G",
+              "Vilchèze C",
+              "Veyron-Churlet R",
+              "Zanella-Cléon I",
+              "Sacchettini JC",
+              "Jacobs WR",
+              "Kremer L"
+            ],
+            "journal": "Molecular microbiology",
+            "year": "2010",
+            "doi": "10.1111/j.1365-2958.2010.07446.x",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:16842188",
+          "snippet": "InhA is a member of the mycobacterial Type II fatty acid biosynthesis system, which elongates acyl fatty acid precursors of mycolic acids.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Slow-onset inhibition of 2-trans-enoyl-ACP (CoA) reductase from Mycobacterium tuberculosis by an inorganic complex.",
+            "authors": [
+              "Oliveira JS",
+              "de Sousa EH",
+              "de Souza ON",
+              "Moreira IS",
+              "Santos DS",
+              "Basso LA"
+            ],
+            "journal": "Current pharmaceutical design",
+            "year": "2006",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "occurs in",
+      "source": "GO:0001560",
+      "target": "NCBITaxon:1773",
+      "evidence": [
+        {
+          "reference": "PMID:34634381",
+          "snippet": "Mycobacterium tuberculosis has a complex cell wall containing mycolic acids (MA), which play an important role in pathogenesis, virulence, and survival by protecting the cell against harsh environments.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Mycolic acid biosynthesis is an essential process unique to Mycobacterium tuberculosis; disrupting it kills the bacterium.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Genomic characterization of variants on mycolic acid metabolism genes in Mycobacterium tuberculosis isolates from Santa Catarina, Southern Brazil.",
+            "authors": [
+              "Medeiros TF",
+              "Scheffer MC",
+              "Verza M",
+              "Salvato RS",
+              "Schörner MA",
+              "Barazzetti FH",
+              "Rovaris DB",
+              "Bazzo ML"
+            ],
+            "journal": "Infection, genetics and evolution : journal of molecular epidemiology and evolutionary genetics in infectious diseases",
+            "year": "2021",
+            "doi": "10.1016/j.meegid.2021.105107",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "causes",
+      "source": "NCBITaxon:1773",
+      "target": "MESH:D014397",
+      "evidence": [
+        {
+          "reference": "PMID:16842188",
+          "snippet": "Tuberculosis (TB) remains the leading cause of mortality due to a bacterial pathogen, Mycobacterium tuberculosis.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Mycobacterium tuberculosis is the causative agent of tuberculosis, including pulmonary tuberculosis.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Slow-onset inhibition of 2-trans-enoyl-ACP (CoA) reductase from Mycobacterium tuberculosis by an inorganic complex.",
+            "authors": [
+              "Oliveira JS",
+              "de Sousa EH",
+              "de Souza ON",
+              "Moreira IS",
+              "Santos DS",
+              "Basso LA"
+            ],
+            "journal": "Current pharmaceutical design",
+            "year": "2006",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [],
+  "site": {
+    "id": "sonnet__P12",
+    "record_id": "P12_DB00951_MESH_D014397",
+    "run": "sonnet",
+    "run_label": "Sonnet (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/sonnet/outputs/P12.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/sonnet__P13.json b/web-revamp-mockup/data/records/sonnet__P13.json
new file mode 100644
index 0000000..a89cecc
--- /dev/null
+++ b/web-revamp-mockup/data/records/sonnet__P13.json
@@ -0,0 +1,171 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P13_DB00512_MESH_D055624",
+    "drug": "Vancomycin",
+    "drug_mesh": "MESH:D014640",
+    "drugbank": "DB:DB00512",
+    "disease": "MRSA Infection",
+    "disease_mesh": "MESH:D055624",
+    "summary": "Vancomycin → Lipid II → peptidoglycan biosynthetic process → Staphylococcus aureus"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D014640",
+      "name": "Vancomycin",
+      "label": "Drug"
+    },
+    {
+      "id": "CHEBI:83419",
+      "name": "Lipid II",
+      "label": "ChemicalSubstance"
+    },
+    {
+      "id": "GO:0009252",
+      "name": "peptidoglycan biosynthetic process",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "NCBITaxon:1280",
+      "name": "Staphylococcus aureus",
+      "label": "OrganismTaxon"
+    },
+    {
+      "id": "MESH:D055624",
+      "name": "MRSA Infection",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "directly physically interacts with",
+      "source": "MESH:D014640",
+      "target": "CHEBI:83419",
+      "evidence": [
+        {
+          "reference": "PMID:33458529",
+          "snippet": "Vancomycin inhibits cell wall biosynthesis by targeting lipid II, which is the membrane-bound peptidoglycan precursor. The heptapeptide aglycon structure of vancomycin binds to the d-Ala-d-Ala of the pentapeptide stem structure in lipid II.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Vancomycin binds the D-Ala-D-Ala terminus of the peptidoglycan precursor lipid II.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Molecular Dynamics Simulation of Atomic Interactions in the Vancomycin Binding Site.",
+            "authors": [
+              "Olademehin OP",
+              "Kim SJ",
+              "Shuford KL"
+            ],
+            "journal": "ACS omega",
+            "year": "2021",
+            "doi": "10.1021/acsomega.0c05353",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "decreased",
+      "source": "CHEBI:83419",
+      "target": "GO:0009252",
+      "evidence": [
+        {
+          "reference": "PMID:31899563",
+          "snippet": "Vancomycin forms an intricate network of hydrogen bonds with the d-Ala-d-Ala region of Lipid II, interfering with the peptidoglycan layer maturation process.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Vancomycin binding to Lipid II interferes with peptidoglycan layer maturation (biosynthetic process).",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Molecular mechanisms of vancomycin resistance.",
+            "authors": [
+              "Stogios PJ",
+              "Savchenko A"
+            ],
+            "journal": "Protein science : a publication of the Protein Society",
+            "year": "2020",
+            "doi": "10.1002/pro.3819",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "decreased",
+      "source": "GO:0009252",
+      "target": "NCBITaxon:1280",
+      "evidence": [
+        {
+          "reference": "PMID:19576226",
+          "snippet": "Our results show the accumulation of peptidoglycan precursors after vancomycin treatment, consistent with transglycosylase inhibition",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Inhibition of peptidoglycan biosynthesis (transglycosylase inhibition) leads to accumulation of precursors and impaired Staphylococcus aureus cell wall synthesis.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Vancomycin and oritavancin have different modes of action in Enterococcus faecium.",
+            "authors": [
+              "Patti GJ",
+              "Kim SJ",
+              "Yu TY",
+              "Dietrich E",
+              "Tanaka KS",
+              "Parr TR",
+              "Far AR",
+              "Schaefer J"
+            ],
+            "journal": "Journal of molecular biology",
+            "year": "2009",
+            "doi": "10.1016/j.jmb.2009.06.064",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "treats",
+      "source": "MESH:D014640",
+      "target": "MESH:D055624",
+      "evidence": [
+        {
+          "reference": "PMID:20353147",
+          "snippet": "Vancomycin is the first-line agent for MRSA in hospitalized patients",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Vancomycin is the standard first-line treatment for MRSA infections in hospitalized patients.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Skin and soft tissue infections in immunocompetent patients.",
+            "authors": [
+              "Breen JO"
+            ],
+            "journal": "American family physician",
+            "year": "2010",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [],
+  "site": {
+    "id": "sonnet__P13",
+    "record_id": "P13_DB00512_MESH_D055624",
+    "run": "sonnet",
+    "run_label": "Sonnet (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/sonnet/outputs/P13.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/sonnet__P14.json b/web-revamp-mockup/data/records/sonnet__P14.json
new file mode 100644
index 0000000..c767073
--- /dev/null
+++ b/web-revamp-mockup/data/records/sonnet__P14.json
@@ -0,0 +1,288 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P14_DB00198_MESH_D007251",
+    "drug": "Oseltamivir",
+    "drug_mesh": "MESH:D053139",
+    "drugbank": "DB:DB00198",
+    "disease": "Influenza",
+    "disease_mesh": "MESH:D007251",
+    "summary": "Oseltamivir → Oseltamivir carboxylate → Neuraminidase → viral release from host cell → Influenza"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D053139",
+      "name": "Oseltamivir",
+      "label": "Drug"
+    },
+    {
+      "id": "CHEBI:67200",
+      "name": "Oseltamivir carboxylate",
+      "label": "ChemicalSubstance"
+    },
+    {
+      "id": "UniProt:P03472",
+      "name": "Neuraminidase",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0019076",
+      "name": "viral release from host cell",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D007251",
+      "name": "Influenza",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "has metabolite",
+      "source": "MESH:D053139",
+      "target": "CHEBI:67200",
+      "evidence": [
+        {
+          "reference": "PMID:21803598",
+          "snippet": "Oseltamivir phosphate (OP; tamiflu) is an antiviral pro-drug, which is hydrolyzed hepatically to the active metabolite oseltamivir carboxylate (OC).",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Study on the interaction of tamiflu and oseltamivir carboxylate with human serum albumin.",
+            "authors": [
+              "Nafisi S",
+              "Vishkaee TS"
+            ],
+            "journal": "Journal of photochemistry and photobiology. B, Biology",
+            "year": "2011",
+            "doi": "10.1016/j.jphotobiol.2011.06.008",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:27228223",
+          "snippet": "Oseltamivir, an inactive anti-influenza virus prodrug, is activated (hydrolysed) in vivo by carboxylesterase 1 (CES1) to its active metabolite oseltamivir carboxylate.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Association of Oseltamivir Activation with Gender and Carboxylesterase 1 Genetic Polymorphisms.",
+            "authors": [
+              "Shi J",
+              "Wang X",
+              "Eyler RF",
+              "Liang Y",
+              "Liu L",
+              "Mueller BA",
+              "Zhu HJ"
+            ],
+            "journal": "Basic & clinical pharmacology & toxicology",
+            "year": "2016",
+            "doi": "10.1111/bcpt.12625",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "CHEBI:67200",
+      "target": "UniProt:P03472",
+      "evidence": [
+        {
+          "reference": "PMID:18694948",
+          "snippet": "Oseltamivir (Tamiflu) and zanamivir (Relenza), two extensively used clinically effective anti-influenza drugs, are viral sialidase (also known as neuraminidase) inhibitors that prevent the release of progeny virions and thereby limit the spread of infection.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Limited inhibitory effects of oseltamivir and zanamivir on human sialidases.",
+            "authors": [
+              "Hata K",
+              "Koseki K",
+              "Yamaguchi K",
+              "Moriya S",
+              "Suzuki Y",
+              "Yingsakmongkon S",
+              "Hirai G",
+              "Sodeoka M",
+              "von Itzstein M",
+              "Miyagi T"
+            ],
+            "journal": "Antimicrobial agents and chemotherapy",
+            "year": "2008",
+            "doi": "10.1128/AAC.00344-08",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:22340192",
+          "snippet": "Anti influenza drugs such as Oseltamivir target a highly conserved active site of NA, which comprises of 8 functional residues (R118, D151, R152, R224, E276, R292, R371 and Y406) to restrict viral release from host cells, thus inhibiting its ability to cleave sialic acid residues on the cell membrane.",
+          "supports": "SUPPORT",
+          "evidence_source": "COMPUTATIONAL",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "In-Silico screening of Pleconaril and its novel substituted derivatives with Neuraminidase of H1N1 Influenza strain.",
+            "authors": [
+              "Hussain Basha S",
+              "Prasad RN"
+            ],
+            "journal": "BMC research notes",
+            "year": "2012",
+            "doi": "10.1186/1756-0500-5-105",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P03472",
+      "target": "GO:0019076",
+      "evidence": [
+        {
+          "reference": "PMID:10711940",
+          "snippet": "Neuraminidase promotes influenza virus release from infected cells and facilitates virus spread within the respiratory tract.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Influenza virus neuraminidase inhibitors.",
+            "authors": [
+              "Gubareva LV",
+              "Kaiser L",
+              "Hayden FG"
+            ],
+            "journal": "Lancet (London, England)",
+            "year": "2000",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:27845731",
+          "snippet": "A neuraminidase located on the surface of the virus plays an important role in viral reproduction by contributing to the release of viruses from infected host cells.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Influenza Neuraminidase Inhibitors: Synthetic Approaches, Derivatives and Biological Activity.",
+            "authors": [
+              "Laborda P",
+              "Wang SY",
+              "Voglmeir J"
+            ],
+            "journal": "Molecules (Basel, Switzerland)",
+            "year": "2016",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "contributes to",
+      "source": "GO:0019076",
+      "target": "MESH:D007251",
+      "evidence": [
+        {
+          "reference": "PMID:23028967",
+          "snippet": "Influenza virus neuraminidase (NA) cleaves terminal sialic acid residues on oligosaccharide chains that are receptors for virus binding, thus playing an important role in the release of virions from infected cells to promote the spread of cell-to-cell infection.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Bacterial neuraminidase rescues influenza virus replication from inhibition by a neuraminidase inhibitor.",
+            "authors": [
+              "Nishikawa T",
+              "Shimizu K",
+              "Tanaka T",
+              "Kuroda K",
+              "Takayama T",
+              "Yamamoto T",
+              "Hanada N",
+              "Hamada Y"
+            ],
+            "journal": "PloS one",
+            "year": "2012",
+            "doi": "10.1371/journal.pone.0045371",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:25934861",
+          "snippet": "Viral neuraminidase inhibitors, which inhibit viral release from the infected cell, are currently the only approved drugs for influenza",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "A novel lung explant model for the ex vivo study of efficacy and mechanisms of anti-influenza drugs.",
+            "authors": [
+              "Nicholas B",
+              "Staples KJ",
+              "Moese S",
+              "Meldrum E",
+              "Ward J",
+              "Dennison P",
+              "Havelock T",
+              "Hinks TS",
+              "Amer K",
+              "Woo E",
+              "Chamberlain M",
+              "Singh N",
+              "North M",
+              "Pink S",
+              "Wilkinson TM",
+              "Djukanović R"
+            ],
+            "journal": "Journal of immunology (Baltimore, Md. : 1950)",
+            "year": "2015",
+            "doi": "10.4049/jimmunol.1402283",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://www.drugbank.ca/drugs/DB00198",
+      "type": "drugbank",
+      "label": "drugbank.ca — record source"
+    },
+    {
+      "url": "https://meshb.nlm.nih.gov/record/ui?ui=D007251",
+      "type": "other",
+      "label": "meshb.nlm.nih.gov — record source"
+    }
+  ],
+  "site": {
+    "id": "sonnet__P14",
+    "record_id": "P14_DB00198_MESH_D007251",
+    "run": "sonnet",
+    "run_label": "Sonnet (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/sonnet/outputs/P14.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/sonnet__P15.json b/web-revamp-mockup/data/records/sonnet__P15.json
new file mode 100644
index 0000000..489df49
--- /dev/null
+++ b/web-revamp-mockup/data/records/sonnet__P15.json
@@ -0,0 +1,221 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P15_DB00787_MESH_D006561",
+    "drug": "Acyclovir",
+    "drug_mesh": "MESH:D000212",
+    "drugbank": "DB:DB00787",
+    "disease": "Herpes Simplex",
+    "disease_mesh": "MESH:D006561",
+    "summary": "Acyclovir → Acyclovir triphosphate → DNA polymerase (HSV-1 UL30) → viral DNA genome replication → Herpes Simplex"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D000212",
+      "name": "Acyclovir",
+      "label": "Drug"
+    },
+    {
+      "id": "CHEBI:16624",
+      "name": "Acyclovir triphosphate",
+      "label": "ChemicalSubstance"
+    },
+    {
+      "id": "UniProt:P04293",
+      "name": "DNA polymerase (HSV-1 UL30)",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0039693",
+      "name": "viral DNA genome replication",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D006561",
+      "name": "Herpes Simplex",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "has metabolite",
+      "source": "MESH:D000212",
+      "target": "CHEBI:16624",
+      "evidence": [
+        {
+          "reference": "PMID:6313600",
+          "snippet": "Acyclovir monophosphate is subsequently converted to a triphosphate which is a more potent inhibitor of herpes virus DNA polymerases than of cellular DNA polymerases.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Acyclovir is phosphorylated by viral thymidine kinase to the monophosphate, which is then converted by cellular kinases to the active triphosphate metabolite.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "The biochemistry and mechanism of action of acyclovir.",
+            "authors": [
+              "Elion GB"
+            ],
+            "journal": "The Journal of antimicrobial chemotherapy",
+            "year": "1983",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "CHEBI:16624",
+      "target": "UniProt:P04293",
+      "evidence": [
+        {
+          "reference": "PMID:6291456",
+          "snippet": "ACVTP inhibition was competitive with dGTP with Ki values of 0.03, 0.15, 9.8 and 11.9 microM for HSV-1 DNA polymerase, DNA polymerase alpha, EBV DNA polymerase and DNA polymerase beta, respectively.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Acyclovir triphosphate (ACVTP) potently and competitively inhibits HSV-1 DNA polymerase UL30 with respect to dGTP.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Mode of action of acyclovir triphosphate on herpesviral and cellular DNA polymerases.",
+            "authors": [
+              "Allaudeen HS",
+              "Descamps J",
+              "Sehgal RK"
+            ],
+            "journal": "Antiviral research",
+            "year": "1982",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:26836009",
+          "snippet": "the ability of acyclovir and Foscarnet to block dNTP polymerization without impacting exonuclease activity raises the possibility that their effects on herpes replication may involve both direct inhibition of dNTP polymerization and exonuclease-mediated destruction of herpes DNA.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Acyclovir triphosphate blocks dNTP polymerization by the HSV-1 DNA polymerase UL30 (encoded by UL30 gene).",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Effects of Acyclovir, Foscarnet, and Ribonucleotides on Herpes Simplex Virus-1 DNA Polymerase: Mechanistic Insights and a Novel Mechanism for Preventing Stable Incorporation of Ribonucleotides into DNA.",
+            "authors": [
+              "Vashishtha AK",
+              "Kuchta RD"
+            ],
+            "journal": "Biochemistry",
+            "year": "2016",
+            "doi": "10.1021/acs.biochem.6b00065",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "participates in",
+      "source": "UniProt:P04293",
+      "target": "GO:0039693",
+      "evidence": [
+        {
+          "reference": "PMID:6291456",
+          "snippet": "it appeared to act as a chain terminator in DNA replication catalyzed by either HSV-1 DNA polymerase or DNA polymerase alpha.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "HSV-1 DNA polymerase catalyzes viral DNA genome replication; acyclovir triphosphate terminates DNA chains during this process.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Mode of action of acyclovir triphosphate on herpesviral and cellular DNA polymerases.",
+            "authors": [
+              "Allaudeen HS",
+              "Descamps J",
+              "Sehgal RK"
+            ],
+            "journal": "Antiviral research",
+            "year": "1982",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:29896665",
+          "snippet": "Acyclovir and penciclovir are phosphorylated by viral thymidine kinase and are incorporated into the DNA chain by viral DNA polymerase, resulting in chain termination.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "The viral DNA polymerase participates in viral genome replication and incorporates acyclovir triphosphate causing chain termination.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Antiviral Drugs Against Alphaherpesvirus.",
+            "authors": [
+              "Shiraki K"
+            ],
+            "journal": "Advances in experimental medicine and biology",
+            "year": "2018",
+            "doi": "10.1007/978-981-10-7230-7_6",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "causes",
+      "source": "GO:0039693",
+      "target": "MESH:D006561",
+      "evidence": [
+        {
+          "reference": "PMID:33705354",
+          "snippet": "Anti-HSV-1 drugs, such as acyclovir, target thymidine kinase and viral DNA polymerase.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Viral DNA genome replication is essential for HSV pathogenesis; inhibiting it (via acyclovir targeting TK and DNA polymerase) treats Herpes Simplex disease.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Antiviral activity of 1,4-disubstituted-1,2,3-triazoles against HSV-1 in vitro.",
+            "authors": [
+              "Viegas DJ",
+              "da Silva VD",
+              "Buarque CD",
+              "Bloom DC",
+              "Abreu PA"
+            ],
+            "journal": "Antiviral therapy",
+            "year": "2020",
+            "doi": "10.3851/IMP3387",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://www.drugbank.ca/drugs/DB00787",
+      "type": "drugbank",
+      "label": "drugbank.ca — record source"
+    },
+    {
+      "url": "https://pubchem.ncbi.nlm.nih.gov/compound/2022",
+      "type": "other",
+      "label": "pubchem.ncbi.nlm.nih.gov — record source"
+    }
+  ],
+  "site": {
+    "id": "sonnet__P15",
+    "record_id": "P15_DB00787_MESH_D006561",
+    "run": "sonnet",
+    "run_label": "Sonnet (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/sonnet/outputs/P15.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/sonnet__P16.json b/web-revamp-mockup/data/records/sonnet__P16.json
new file mode 100644
index 0000000..2cc7b64
--- /dev/null
+++ b/web-revamp-mockup/data/records/sonnet__P16.json
@@ -0,0 +1,256 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P16_DB01235_MESH_D010300",
+    "drug": "Levodopa",
+    "drug_mesh": "MESH:D007980",
+    "drugbank": "DB:DB01235",
+    "disease": "Parkinson's Disease",
+    "disease_mesh": "MESH:D010300",
+    "summary": "Levodopa → Dopamine → D(2) dopamine receptor"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D007980",
+      "name": "Levodopa",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P20711",
+      "name": "Aromatic-L-amino-acid decarboxylase",
+      "label": "Protein"
+    },
+    {
+      "id": "MESH:D004298",
+      "name": "Dopamine",
+      "label": "ChemicalSubstance"
+    },
+    {
+      "id": "UniProt:P14416",
+      "name": "D(2) dopamine receptor",
+      "label": "Protein"
+    },
+    {
+      "id": "MESH:D010300",
+      "name": "Parkinson's Disease",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "increased",
+      "source": "MESH:D007980",
+      "target": "UniProt:P20711",
+      "evidence": [
+        {
+          "reference": "PMID:28166239",
+          "snippet": "aromatic L-amino acid decarboxylase (AADC) is the rate-limiting enzyme in the conversion of L-DOPA (Sinemet) to dopamine (DA)",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Levodopa is the substrate for AADC (DDC), the enzyme that converts it to dopamine. The enzyme activity is the key step in levodopa's mechanism.\n",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Depletion of AADC activity in caudate nucleus and putamen of Parkinson's disease patients; implications for ongoing AAV2-AADC gene therapy trial.",
+            "authors": [
+              "Ciesielska A",
+              "Samaranch L",
+              "San Sebastian W",
+              "Dickson DW",
+              "Goldman S",
+              "Forsayeth J",
+              "Bankiewicz KS"
+            ],
+            "journal": "PloS one",
+            "year": "2017",
+            "doi": "10.1371/journal.pone.0169965",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "has metabolite",
+      "source": "MESH:D007980",
+      "target": "MESH:D004298",
+      "evidence": [
+        {
+          "reference": "PMID:30077198",
+          "snippet": "Replenishment of dopamine by oral supplementation of its precursor, the levodopa (L-DOPA), remains the primary mode of treatment of PD",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Levodopa is converted to dopamine in the brain, replenishing dopamine levels in Parkinson's disease patients.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Garcinol, an effective monoamine oxidase-B inhibitor for the treatment of Parkinson's disease.",
+            "authors": [
+              "Mazumder MK",
+              "Paul R",
+              "Phukan BC",
+              "Dutta A",
+              "Chakrabarty J",
+              "Bhattacharya P",
+              "Borah A"
+            ],
+            "journal": "Medical hypotheses",
+            "year": "2018",
+            "doi": "10.1016/j.mehy.2018.06.009",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:16829205",
+          "snippet": "Dopamine, the major neurotransmitter depleted in Parkinson disease, can be synthesized and regulated in vivo with a combination of intrastriatal AAV-hAADC gene therapy and administration of the dopamine precursor l-Dopa.",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "explanation": "Confirms levodopa is a dopamine precursor and its conversion to dopamine is central to its therapeutic effect.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Long-term clinical improvement in MPTP-lesioned primates after gene therapy with AAV-hAADC.",
+            "authors": [
+              "Bankiewicz KS",
+              "Forsayeth J",
+              "Eberling JL",
+              "Sanchez-Pernaute R",
+              "Pivirotto P",
+              "Bringas J",
+              "Herscovitch P",
+              "Carson RE",
+              "Eckelman W",
+              "Reutter B",
+              "Cunningham J"
+            ],
+            "journal": "Molecular therapy : the journal of the American Society of Gene Therapy",
+            "year": "2006",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "increased",
+      "source": "MESH:D004298",
+      "target": "UniProt:P14416",
+      "evidence": [
+        {
+          "reference": "PMID:22133327",
+          "snippet": "Although the resulting dopamine deficiency is the cause of the typical motor features of Parkinson's disease (bradykinesia, rigidity, tremor)",
+          "supports": "PARTIAL",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Dopamine deficiency underlies Parkinson's motor symptoms; replenishment of dopamine (from levodopa) restores stimulation of dopamine receptors including DRD2, which modulates motor control.\n",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Monoamine oxidase B inhibitors for the treatment of Parkinson's disease: a review of symptomatic and potential disease-modifying effects.",
+            "authors": [
+              "Schapira AH"
+            ],
+            "journal": "CNS drugs",
+            "year": "2011",
+            "doi": "10.2165/11596310-000000000-00000",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:36403747",
+          "snippet": "a decrease in dopamine levels in the striatum causes abnormal circuit activity in the basal ganglia, resulting in increased output via the substantia nigra pars reticulata (SNr)",
+          "supports": "PARTIAL",
+          "evidence_source": "MODEL_ORGANISM",
+          "explanation": "Depletion of dopamine disrupts basal ganglia activity; restoration of dopamine by levodopa acts through dopamine receptors to normalize this circuit.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Amino acid transporter Asc-1 (SLC7A10) expression is altered in basal ganglia in experimental Parkinsonism and L-dopa-induced dyskinesia model mice.",
+            "authors": [
+              "Nakahara K",
+              "Okuda H",
+              "Isonishi A",
+              "Kawabe Y",
+              "Tanaka T",
+              "Tatsumi K",
+              "Wanaka A"
+            ],
+            "journal": "Journal of chemical neuroanatomy",
+            "year": "2023",
+            "doi": "10.1016/j.jchemneu.2022.102191",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "treats",
+      "source": "MESH:D007980",
+      "target": "MESH:D010300",
+      "evidence": [
+        {
+          "reference": "PMID:34268560",
+          "snippet": "l-DOPA treatment ameliorated PD signs, particularly akinesia/bradykinesia, and normalized cortically evoked responses in both the GPi and GPe",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "explanation": "L-DOPA directly ameliorates the motor signs of Parkinson's disease by restoring dopaminergic signaling in the basal ganglia.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Altered Dynamic Information Flow through the Cortico-Basal Ganglia Pathways Mediates Parkinson's Disease Symptoms.",
+            "authors": [
+              "Chiken S",
+              "Takada M",
+              "Nambu A"
+            ],
+            "journal": "Cerebral cortex (New York, N.Y. : 1991)",
+            "year": "2021",
+            "doi": "10.1093/cercor/bhab164",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:17894650",
+          "snippet": "The most effective treatment for this disease continues to be the dopamine replacement therapy with levodopa together with an inhibitor of aromatic amino acid decarboxylase (AADC)",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Levodopa is the gold-standard treatment for Parkinson's disease.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Catechol-O-methyltransferase and its inhibitors in Parkinson's disease.",
+            "authors": [
+              "Bonifácio MJ",
+              "Palma PN",
+              "Almeida L",
+              "Soares-da-Silva P"
+            ],
+            "journal": "CNS drug reviews",
+            "year": "2007",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [],
+  "site": {
+    "id": "sonnet__P16",
+    "record_id": "P16_DB01235_MESH_D010300",
+    "run": "sonnet",
+    "run_label": "Sonnet (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/sonnet/outputs/P16.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/sonnet__P17.json b/web-revamp-mockup/data/records/sonnet__P17.json
new file mode 100644
index 0000000..9fbf08f
--- /dev/null
+++ b/web-revamp-mockup/data/records/sonnet__P17.json
@@ -0,0 +1,199 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P17_DB00472_MESH_D003865",
+    "drug": "fluoxetine",
+    "drug_mesh": "MESH:D005473",
+    "drugbank": "DB:DB00472",
+    "disease": "Major Depressive Disorder",
+    "disease_mesh": "MESH:D003865",
+    "summary": "fluoxetine → Serotonin transporter → Serotonin → serotonin receptor signaling pathway → Major Depressive Disorder"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D005473",
+      "name": "fluoxetine",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P31645",
+      "name": "Serotonin transporter",
+      "label": "Protein"
+    },
+    {
+      "id": "MESH:D012701",
+      "name": "Serotonin",
+      "label": "ChemicalSubstance"
+    },
+    {
+      "id": "GO:0007210",
+      "name": "serotonin receptor signaling pathway",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D003865",
+      "name": "Major Depressive Disorder",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D005473",
+      "target": "UniProt:P31645",
+      "evidence": [
+        {
+          "reference": "PMID:31480244",
+          "snippet": "Their primary mechanism of action is considered to be the increased synaptic concentration of serotonin through blockade of the serotonin transporter (SERT).",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Fluoxetine, as a representative SSRI, blocks SERT to increase synaptic serotonin.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Fluoxetine Suppresses Glutamate- and GABA-Mediated Neurotransmission by Altering SNARE Complex.",
+            "authors": [
+              "Lazarevic V",
+              "Mantas I",
+              "Flais I",
+              "Svenningsson P"
+            ],
+            "journal": "International journal of molecular sciences",
+            "year": "2019",
+            "doi": "10.3390/ijms20174247",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:19587851",
+          "snippet": "The primary SSRIs pharmacological action's mechanism consists in the presynaptic inhibition on the serotonin reuptake, with an increased availability of this amine into the synaptic cleft.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "SSRIs including fluoxetine inhibit presynaptic serotonin reuptake via SERT blockade.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Selective serotonin reuptake inhibitors: a review of its effects on intraocular pressure.",
+            "authors": [
+              "Costagliola C",
+              "Parmeggiani F",
+              "Semeraro F",
+              "Sebastiani A"
+            ],
+            "journal": "Current neuropharmacology",
+            "year": "2008",
+            "doi": "10.2174/157015908787386104",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "decreased",
+      "source": "UniProt:P31645",
+      "target": "MESH:D012701",
+      "evidence": [
+        {
+          "reference": "PMID:31480244",
+          "snippet": "by virtue of its inhibition at SERT, fluoxetine increases extracellular serotonin levels",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "SERT normally removes serotonin from the synapse; its inhibition leads to increased extracellular serotonin.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Fluoxetine Suppresses Glutamate- and GABA-Mediated Neurotransmission by Altering SNARE Complex.",
+            "authors": [
+              "Lazarevic V",
+              "Mantas I",
+              "Flais I",
+              "Svenningsson P"
+            ],
+            "journal": "International journal of molecular sciences",
+            "year": "2019",
+            "doi": "10.3390/ijms20174247",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "MESH:D012701",
+      "target": "GO:0007210",
+      "evidence": [
+        {
+          "reference": "PMID:19587851",
+          "snippet": "Serotonin produces its effects as a consequence of interactions with appropriate receptors.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Increased synaptic serotonin activates postsynaptic receptors, enhancing serotonin receptor signaling.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Selective serotonin reuptake inhibitors: a review of its effects on intraocular pressure.",
+            "authors": [
+              "Costagliola C",
+              "Parmeggiani F",
+              "Semeraro F",
+              "Sebastiani A"
+            ],
+            "journal": "Current neuropharmacology",
+            "year": "2008",
+            "doi": "10.2174/157015908787386104",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "decreased",
+      "source": "GO:0007210",
+      "target": "MESH:D003865",
+      "evidence": [
+        {
+          "reference": "PMID:19587851",
+          "snippet": "The increase in serotonin (5-HT) neurotransmission is considered to be one of the most efficacious medical approach to depression and its related disorders.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Enhanced serotonin receptor signaling is a key mechanism for alleviating major depressive disorder.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Selective serotonin reuptake inhibitors: a review of its effects on intraocular pressure.",
+            "authors": [
+              "Costagliola C",
+              "Parmeggiani F",
+              "Semeraro F",
+              "Sebastiani A"
+            ],
+            "journal": "Current neuropharmacology",
+            "year": "2008",
+            "doi": "10.2174/157015908787386104",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [],
+  "site": {
+    "id": "sonnet__P17",
+    "record_id": "P17_DB00472_MESH_D003865",
+    "run": "sonnet",
+    "run_label": "Sonnet (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/sonnet/outputs/P17.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/sonnet__P18.json b/web-revamp-mockup/data/records/sonnet__P18.json
new file mode 100644
index 0000000..33700e5
--- /dev/null
+++ b/web-revamp-mockup/data/records/sonnet__P18.json
@@ -0,0 +1,246 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P18_DB01356_MESH_D001714",
+    "drug": "Lithium",
+    "drug_mesh": "MESH:D008094",
+    "drugbank": "DB:DB01356",
+    "disease": "Bipolar Disorder",
+    "disease_mesh": "MESH:D001714",
+    "summary": "Lithium → Glycogen synthase kinase-3 beta → Apoptotic process → Bipolar Disorder"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D008094",
+      "name": "Lithium",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P49841",
+      "name": "Glycogen synthase kinase-3 beta",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0006915",
+      "name": "Apoptotic process",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D001714",
+      "name": "Bipolar Disorder",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D008094",
+      "target": "UniProt:P49841",
+      "evidence": [
+        {
+          "reference": "PMID:12071511",
+          "snippet": "lithium has been identified as a selective and direct inhibitor of GSK-3beta",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Lithium directly inhibits GSK-3beta activity, a key mechanism underlying its mood-stabilizing effects in bipolar disorder.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Glycogen synthase kinase-3beta, mood stabilizers, and neuroprotection.",
+            "authors": [
+              "Li X",
+              "Bijur GN",
+              "Jope RS"
+            ],
+            "journal": "Bipolar disorders",
+            "year": "2002",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:27128528",
+          "snippet": "The mood stabilizer lithium, the first-line treatment for bipolar disorder, is hypothesized to exert its effects through direct inhibition of glycogen synthase kinase 3 (GSK3)",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Lithium is hypothesized to exert its therapeutic effects through direct inhibition of GSK3.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Inhibitors of Glycogen Synthase Kinase 3 with Exquisite Kinome-Wide Selectivity and Their Functional Effects.",
+            "authors": [
+              "Wagner FF",
+              "Bishop JA",
+              "Gale JP",
+              "Shi X",
+              "Walk M",
+              "Ketterman J",
+              "Patnaik D",
+              "Barker D",
+              "Walpita D",
+              "Campbell AJ",
+              "Nguyen S",
+              "Lewis M",
+              "Ross L",
+              "Weïwer M",
+              "An WF",
+              "Germain AR",
+              "Nag PP",
+              "Metkar S",
+              "Kaya T",
+              "Dandapani S",
+              "Olson DE",
+              "Barbe AL",
+              "Lazzaro F",
+              "Sacher JR",
+              "Cheah JH",
+              "Fei D",
+              "Perez J",
+              "Munoz B",
+              "Palmer M",
+              "Stegmaier K",
+              "Schreiber SL",
+              "Scolnick E",
+              "Zhang YL",
+              "Haggarty SJ",
+              "Holson EB",
+              "Pan JQ"
+            ],
+            "journal": "ACS chemical biology",
+            "year": "2016",
+            "doi": "10.1021/acschembio.6b00306",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P49841",
+      "target": "GO:0006915",
+      "evidence": [
+        {
+          "reference": "PMID:12071511",
+          "snippet": "GSK-3beta is a pro-apoptotic enzyme",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "GSK-3beta promotes apoptosis; inhibition of its pro-apoptotic activity is linked to neuroprotection in bipolar disorder.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Glycogen synthase kinase-3beta, mood stabilizers, and neuroprotection.",
+            "authors": [
+              "Li X",
+              "Bijur GN",
+              "Jope RS"
+            ],
+            "journal": "Bipolar disorders",
+            "year": "2002",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:11527574",
+          "snippet": "GSK3beta also regulates cell survival, as it facilitates a variety of apoptotic mechanisms",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "GSK3beta positively regulates apoptotic processes in neuronal cells.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "The multifaceted roles of glycogen synthase kinase 3beta in cellular signaling.",
+            "authors": [
+              "Grimes CA",
+              "Jope RS"
+            ],
+            "journal": "Progress in neurobiology",
+            "year": "2001",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "contributes to",
+      "source": "GO:0006915",
+      "target": "MESH:D001714",
+      "evidence": [
+        {
+          "reference": "PMID:33732117",
+          "snippet": "neuronal apoptosis, contributing to chronic neuroinflammation",
+          "supports": "PARTIAL",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Neuronal apoptosis is a feature of bipolar disorder pathophysiology; the abstract describes BD as characterized by neuronal apoptosis contributing to neuroinflammation in BD.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Concepts of Neuroinflammation and Their Relationship With Impaired Mitochondrial Functions in Bipolar Disorder.",
+            "authors": [
+              "Cyrino LAR",
+              "Delwing-de Lima D",
+              "Ullmann OM",
+              "Maia TP"
+            ],
+            "journal": "Frontiers in behavioral neuroscience",
+            "year": "2021",
+            "doi": "10.3389/fnbeh.2021.609487",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:12071511",
+          "snippet": "dysregulation of GSK-3beta may contribute to the pathophysiology of bipolar disorder",
+          "supports": "PARTIAL",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Drugs that inhibit the pro-apoptotic effects of GSK-3beta are therapeutic for bipolar disorder, linking apoptotic process dysregulation to bipolar disorder pathophysiology.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Glycogen synthase kinase-3beta, mood stabilizers, and neuroprotection.",
+            "authors": [
+              "Li X",
+              "Bijur GN",
+              "Jope RS"
+            ],
+            "journal": "Bipolar disorders",
+            "year": "2002",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://www.drugbank.ca/drugs/DB01356",
+      "type": "drugbank",
+      "label": "drugbank.ca — record source"
+    },
+    {
+      "url": "https://www.ncbi.nlm.nih.gov/mesh/D001714",
+      "type": "other",
+      "label": "ncbi.nlm.nih.gov — record source"
+    }
+  ],
+  "site": {
+    "id": "sonnet__P18",
+    "record_id": "P18_DB01356_MESH_D001714",
+    "run": "sonnet",
+    "run_label": "Sonnet (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/sonnet/outputs/P18.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/sonnet__P19.json b/web-revamp-mockup/data/records/sonnet__P19.json
new file mode 100644
index 0000000..95f85f3
--- /dev/null
+++ b/web-revamp-mockup/data/records/sonnet__P19.json
@@ -0,0 +1,227 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P19_DB00996_MESH_D004827",
+    "drug": "Gabapentin",
+    "drug_mesh": "MESH:D000077306",
+    "drugbank": "DB:DB00996",
+    "disease": "Epilepsy",
+    "disease_mesh": "MESH:D004827",
+    "summary": "Gabapentin → Voltage-dependent calcium channel subunit alpha-2/delta-1 → Voltage-dependent P/Q-type calcium channel subunit alpha-1A → neurotransmitter secretion → Epilepsy"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D000077306",
+      "name": "Gabapentin",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P54289",
+      "name": "Voltage-dependent calcium channel subunit alpha-2/delta-1",
+      "label": "Protein"
+    },
+    {
+      "id": "UniProt:O00555",
+      "name": "Voltage-dependent P/Q-type calcium channel subunit alpha-1A",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0007269",
+      "name": "neurotransmitter secretion",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D004827",
+      "name": "Epilepsy",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D000077306",
+      "target": "UniProt:P54289",
+      "evidence": [
+        {
+          "reference": "PMID:18590620",
+          "snippet": "alpha(2)delta, auxiliary subunits of voltage-gated calcium channels through which the gabapentinoids gabapentin and pregabalin exert their anticonvulsant and analgesic actions",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Gabapentin exerts its anticonvulsant action by binding to and modulating the alpha-2-delta auxiliary subunit of voltage-gated calcium channels.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "New molecular targets for antiepileptic drugs: alpha(2)delta, SV2A, and K(v)7/KCNQ/M potassium channels.",
+            "authors": [
+              "Rogawski MA",
+              "Bazil CW"
+            ],
+            "journal": "Current neurology and neuroscience reports",
+            "year": "2008",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:38794193",
+          "snippet": "binding to the alpha-2-delta protein subunit of voltage-gated calcium channels in the central nervous system, thereby blocking the excitatory influx of calcium",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Molecular Mechanisms and Therapeutic Potential of Gabapentin with a Focus on Topical Formulations to Treat Ocular Surface Diseases.",
+            "authors": [
+              "Rusciano D"
+            ],
+            "journal": "Pharmaceuticals (Basel, Switzerland)",
+            "year": "2024",
+            "doi": "10.3390/ph17050623",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "UniProt:P54289",
+      "target": "UniProt:O00555",
+      "evidence": [
+        {
+          "reference": "PMID:11804619",
+          "snippet": "Gabapentin and pregabalin may bind to the Ca(2+) channel alpha 2 delta subunit to selectively attenuate depolarization-induced Ca(2+) influx of presynaptic P/Q-type Ca(2+) channels",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "The alpha-2-delta subunit modulated by gabapentin decreases activity of the P/Q-type voltage-gated calcium channel, reducing Ca2+ influx.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Inhibition of neuronal Ca(2+) influx by gabapentin and pregabalin in the human neocortex.",
+            "authors": [
+              "Fink K",
+              "Dooley DJ",
+              "Meder WP",
+              "Suman-Chauhan N",
+              "Duffy S",
+              "Clusmann H",
+              "Göthert M"
+            ],
+            "journal": "Neuropharmacology",
+            "year": "2002",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "decreased",
+      "source": "UniProt:O00555",
+      "target": "GO:0007269",
+      "evidence": [
+        {
+          "reference": "PMID:11804619",
+          "snippet": "this results in decreased glutamate/aspartate release from excitatory amino acid nerve terminals",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Reduced P/Q-type Ca2+ channel activity leads to decreased presynaptic calcium influx, which negatively regulates neurotransmitter secretion.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Inhibition of neuronal Ca(2+) influx by gabapentin and pregabalin in the human neocortex.",
+            "authors": [
+              "Fink K",
+              "Dooley DJ",
+              "Meder WP",
+              "Suman-Chauhan N",
+              "Duffy S",
+              "Clusmann H",
+              "Göthert M"
+            ],
+            "journal": "Neuropharmacology",
+            "year": "2002",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:29793598",
+          "snippet": "They inhibit calcium mediated neurotransmitter release through effects on α2δ-1 subunits",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Analgesic mechanisms of gabapentinoids and effects in experimental pain models: a narrative review.",
+            "authors": [
+              "Chincholkar M"
+            ],
+            "journal": "British journal of anaesthesia",
+            "year": "2018",
+            "doi": "10.1016/j.bja.2018.02.066",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "contributes to",
+      "source": "GO:0007269",
+      "target": "MESH:D004827",
+      "evidence": [
+        {
+          "reference": "PMID:18590620",
+          "snippet": "Functionally, all of the new targets modulate neurotransmitter output at synapses, focusing attention on presynaptic terminals as critical sites of action for AEDs.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Excessive neurotransmitter secretion at synapses contributes to neuronal hyperexcitability and seizure generation in epilepsy; modulation of presynaptic neurotransmitter output is the key mechanism through which AEDs including gabapentin treat epilepsy.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "New molecular targets for antiepileptic drugs: alpha(2)delta, SV2A, and K(v)7/KCNQ/M potassium channels.",
+            "authors": [
+              "Rogawski MA",
+              "Bazil CW"
+            ],
+            "journal": "Current neurology and neuroscience reports",
+            "year": "2008",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://www.drugbank.ca/drugs/DB00996",
+      "type": "drugbank",
+      "label": "drugbank.ca — record source"
+    },
+    {
+      "url": "https://meshb.nlm.nih.gov/record/ui?ui=D004827",
+      "type": "other",
+      "label": "meshb.nlm.nih.gov — record source"
+    }
+  ],
+  "site": {
+    "id": "sonnet__P19",
+    "record_id": "P19_DB00996_MESH_D004827",
+    "run": "sonnet",
+    "run_label": "Sonnet (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/sonnet/outputs/P19.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/sonnet__P20.json b/web-revamp-mockup/data/records/sonnet__P20.json
new file mode 100644
index 0000000..4bd8b30
--- /dev/null
+++ b/web-revamp-mockup/data/records/sonnet__P20.json
@@ -0,0 +1,187 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P20_DB00843_MESH_D000544",
+    "drug": "Donepezil",
+    "drug_mesh": "MESH:D000077856",
+    "drugbank": "DB:DB00843",
+    "disease": "Alzheimer's Disease",
+    "disease_mesh": "MESH:D000544",
+    "summary": "Donepezil → Acetylcholinesterase → Acetylcholine → Synaptic transmission, cholinergic → Alzheimer's Disease"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D000077856",
+      "name": "Donepezil",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P22303",
+      "name": "Acetylcholinesterase",
+      "label": "Protein"
+    },
+    {
+      "id": "MESH:D000109",
+      "name": "Acetylcholine",
+      "label": "ChemicalSubstance"
+    },
+    {
+      "id": "GO:0007271",
+      "name": "Synaptic transmission, cholinergic",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D000544",
+      "name": "Alzheimer's Disease",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D000077856",
+      "target": "UniProt:P22303",
+      "evidence": [
+        {
+          "reference": "PMID:22245562",
+          "snippet": "blocking acetylcholinesterase (AChE) and thus increases the concentration of extracellular acetylcholine",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Donepezil acts by blocking AChE, increasing extracellular acetylcholine concentrations.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Inhibition of acetylcholinesterase and phosphodiesterase-9A has differential effects on hippocampal early and late LTP.",
+            "authors": [
+              "Kroker KS",
+              "Rast G",
+              "Giovannini R",
+              "Marti A",
+              "Dorner-Ciossek C",
+              "Rosenbrock H"
+            ],
+            "journal": "Neuropharmacology",
+            "year": "2012",
+            "doi": "10.1016/j.neuropharm.2011.12.021",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "abundance",
+      "object_direction_qualifier": "decreased",
+      "source": "UniProt:P22303",
+      "target": "MESH:D000109",
+      "evidence": [
+        {
+          "reference": "PMID:34609711",
+          "snippet": "Acetylcholinesterase (AChE) hydrolyses ACh and inhibits the cholinergic transmission",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "AChE hydrolyzes acetylcholine, thereby reducing its availability at the synapse.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "ABCpred: a webserver for the discovery of acetyl- and butyryl-cholinesterase inhibitors.",
+            "authors": [
+              "Malik AA",
+              "Ojha SC",
+              "Schaduangrat N",
+              "Nantasenamat C"
+            ],
+            "journal": "Molecular diversity",
+            "year": "2022",
+            "doi": "10.1007/s11030-021-10292-6",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "MESH:D000109",
+      "target": "GO:0007271",
+      "evidence": [
+        {
+          "reference": "PMID:34609711",
+          "snippet": "The deficiency of the cholinergic neurotransmitter known as acetylcholine (ACh) is associated with AD",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Acetylcholine is the key neurotransmitter of cholinergic synaptic transmission; its deficiency impairs this process.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "ABCpred: a webserver for the discovery of acetyl- and butyryl-cholinesterase inhibitors.",
+            "authors": [
+              "Malik AA",
+              "Ojha SC",
+              "Schaduangrat N",
+              "Nantasenamat C"
+            ],
+            "journal": "Molecular diversity",
+            "year": "2022",
+            "doi": "10.1007/s11030-021-10292-6",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "negatively correlated with",
+      "source": "GO:0007271",
+      "target": "MESH:D000544",
+      "evidence": [
+        {
+          "reference": "PMID:21145918",
+          "snippet": "In presenile (early onset), and in the advanced stages of late-onset Alzheimer's disease (AD), a severe loss of cortical cholinergic innervation has extensively been documented",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "Loss of cholinergic neurotransmission is a hallmark of Alzheimer's disease progression.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "The cholinergic system in aging and neuronal degeneration.",
+            "authors": [
+              "Schliebs R",
+              "Arendt T"
+            ],
+            "journal": "Behavioural brain research",
+            "year": "2011",
+            "doi": "10.1016/j.bbr.2010.11.058",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://www.drugbank.ca/drugs/DB00843",
+      "type": "drugbank",
+      "label": "drugbank.ca — record source"
+    },
+    {
+      "url": "https://www.ncbi.nlm.nih.gov/mesh/D000077856",
+      "type": "other",
+      "label": "ncbi.nlm.nih.gov — record source"
+    }
+  ],
+  "site": {
+    "id": "sonnet__P20",
+    "record_id": "P20_DB00843_MESH_D000544",
+    "run": "sonnet",
+    "run_label": "Sonnet (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/sonnet/outputs/P20.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/sonnet__P21.json b/web-revamp-mockup/data/records/sonnet__P21.json
new file mode 100644
index 0000000..10e052c
--- /dev/null
+++ b/web-revamp-mockup/data/records/sonnet__P21.json
@@ -0,0 +1,273 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P21_DB00563_MESH_D001172",
+    "drug": "Methotrexate",
+    "drug_mesh": "MESH:D008727",
+    "drugbank": "DB:DB00563",
+    "disease": "Rheumatoid Arthritis",
+    "disease_mesh": "MESH:D001172",
+    "summary": "Methotrexate → 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase → Adenosine → Adenosine receptor A2a → Rheumatoid Arthritis"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D008727",
+      "name": "Methotrexate",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P00374",
+      "name": "Dihydrofolate reductase",
+      "label": "Protein"
+    },
+    {
+      "id": "UniProt:P31939",
+      "name": "5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase",
+      "label": "Protein"
+    },
+    {
+      "id": "MESH:D000241",
+      "name": "Adenosine",
+      "label": "ChemicalSubstance"
+    },
+    {
+      "id": "UniProt:P29274",
+      "name": "Adenosine receptor A2a",
+      "label": "Protein"
+    },
+    {
+      "id": "MESH:D001172",
+      "name": "Rheumatoid Arthritis",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D008727",
+      "target": "UniProt:P00374",
+      "evidence": [
+        {
+          "reference": "PMID:16280378",
+          "snippet": "Methotrexate (MTX), a synthetic folate analog, is a tight-binding inhibitor of dihydrofolate reductase (DHFR), a key enzyme for the biosynthesis of purines, thymidylate, and several amino acids.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "The effects of methotrexate on Drosophila development, female fecundity, and gene expression.",
+            "authors": [
+              "Affleck JG",
+              "Neumann K",
+              "Wong L",
+              "Walker VK"
+            ],
+            "journal": "Toxicological sciences : an official journal of the Society of Toxicology",
+            "year": "2006",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D008727",
+      "target": "UniProt:P31939",
+      "evidence": [
+        {
+          "reference": "PMID:7510620",
+          "snippet": "The polyglutamated derivatives of methotrexate are potent inhibitors of various enzymes, including dihydrofolate reductase and 5-aminoimidazole-4-carboxamide ribonucleotide transformylase.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Methotrexate in rheumatoid arthritis. An update.",
+            "authors": [
+              "Bannwarth B",
+              "Labat L",
+              "Moride Y",
+              "Schaeverbeke T"
+            ],
+            "journal": "Drugs",
+            "year": "1994",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:23464989",
+          "snippet": "intracellular MTX polyglutamates inhibit AICAR transformylase (ATIC) activity and thereby promote adenosine release",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Fibroblasts from methotrexate-sensitive mice accumulate methotrexate polyglutamates but those from methotrexate-resistant mice do not.",
+            "authors": [
+              "You X",
+              "Williams A",
+              "Dervieux T",
+              "He W",
+              "Cronstein BN"
+            ],
+            "journal": "Clinical and experimental rheumatology",
+            "year": "2013",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "decreased",
+      "source": "UniProt:P31939",
+      "target": "MESH:D000241",
+      "evidence": [
+        {
+          "reference": "PMID:23464989",
+          "snippet": "ATIC activity was inhibited following MTX treatment in DF from BALBc mice",
+          "supports": "PARTIAL",
+          "evidence_source": "IN_VITRO",
+          "explanation": "ATIC normally consumes AICAR in purine synthesis; its inhibition leads to AICAR accumulation and downstream adenosine release. The snippet confirms ATIC inhibition by MTX treatment; increased adenosine production was also demonstrated in the same paper.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Fibroblasts from methotrexate-sensitive mice accumulate methotrexate polyglutamates but those from methotrexate-resistant mice do not.",
+            "authors": [
+              "You X",
+              "Williams A",
+              "Dervieux T",
+              "He W",
+              "Cronstein BN"
+            ],
+            "journal": "Clinical and experimental rheumatology",
+            "year": "2013",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:15476202",
+          "snippet": "The blockade of purine nucleotide biosynthesis by MTX at the AICA ribonucleotide transformylase-catalyzed step may be related to the efficacy of MTX, and this blockade is effectively relieved by folinic acid, but not by folic acid, supplementation.",
+          "supports": "PARTIAL",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "ATIC inhibition (blockade at AICA ribonucleotide transformylase step) leads to AICAR accumulation and adenosine release; this sentence describes the blockade and its clinical significance.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "The effect of folic acid and folinic acid supplements on purine metabolism in methotrexate-treated rheumatoid arthritis.",
+            "authors": [
+              "Morgan SL",
+              "Oster RA",
+              "Lee JY",
+              "Alarcón GS",
+              "Baggott JE"
+            ],
+            "journal": "Arthritis and rheumatism",
+            "year": "2004",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "MESH:D000241",
+      "target": "UniProt:P29274",
+      "evidence": [
+        {
+          "reference": "PMID:12528125",
+          "snippet": "adenosine, acting at one or more of its receptors, mediates the antiinflammatory effects of methotrexate in animal models of both acute and chronic inflammation",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Adenosine A2A or A3 receptors are required for inhibition of inflammation by methotrexate and its analog MX-68.",
+            "authors": [
+              "Montesinos MC",
+              "Desai A",
+              "Delano D",
+              "Chen JF",
+              "Fink JS",
+              "Jacobson MA",
+              "Cronstein BN"
+            ],
+            "journal": "Arthritis and rheumatism",
+            "year": "2003",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "treats",
+      "source": "UniProt:P29274",
+      "target": "MESH:D001172",
+      "evidence": [
+        {
+          "reference": "PMID:12528125",
+          "snippet": "these results provide strong evidence that adenosine, acting at either or both of these receptors, mediates the antiinflammatory effects of methotrexate and its analog MX-68",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Adenosine A2A or A3 receptors are required for inhibition of inflammation by methotrexate and its analog MX-68.",
+            "authors": [
+              "Montesinos MC",
+              "Desai A",
+              "Delano D",
+              "Chen JF",
+              "Fink JS",
+              "Jacobson MA",
+              "Cronstein BN"
+            ],
+            "journal": "Arthritis and rheumatism",
+            "year": "2003",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://www.drugbank.ca/drugs/DB00563",
+      "type": "drugbank",
+      "label": "drugbank.ca — record source"
+    },
+    {
+      "url": "https://www.ncbi.nlm.nih.gov/mesh/D001172",
+      "type": "other",
+      "label": "ncbi.nlm.nih.gov — record source"
+    }
+  ],
+  "site": {
+    "id": "sonnet__P21",
+    "record_id": "P21_DB00563_MESH_D001172",
+    "run": "sonnet",
+    "run_label": "Sonnet (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/sonnet/outputs/P21.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/sonnet__P23.json b/web-revamp-mockup/data/records/sonnet__P23.json
new file mode 100644
index 0000000..1a1fd92
--- /dev/null
+++ b/web-revamp-mockup/data/records/sonnet__P23.json
@@ -0,0 +1,390 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P23_DB01611_MESH_D008180",
+    "drug": "Hydroxychloroquine",
+    "drug_mesh": "MESH:D006886",
+    "drugbank": "DB:DB01611",
+    "disease": "Systemic Lupus Erythematosus",
+    "disease_mesh": "MESH:D008180",
+    "summary": "Hydroxychloroquine → Toll-like receptor 7 → type I interferon production → Systemic Lupus Erythematosus"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D006886",
+      "name": "Hydroxychloroquine",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:Q9NYK1",
+      "name": "Toll-like receptor 7",
+      "label": "Protein"
+    },
+    {
+      "id": "UniProt:Q9NR96",
+      "name": "Toll-like receptor 9",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0032606",
+      "name": "type I interferon production",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D008180",
+      "name": "Systemic Lupus Erythematosus",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D006886",
+      "target": "UniProt:Q9NYK1",
+      "evidence": [
+        {
+          "reference": "PMID:21398612",
+          "snippet": "We conclude that the direct binding of inhibitors to nucleic acids mask their TLR-binding epitope and may explain the efficiency of those compounds in the treatment of autoimmune diseases.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "The study demonstrates that antimalarial drugs including hydroxychloroquine inhibit endosomal TLR activation by directly binding to nucleic acids and masking their TLR-binding epitope, including TLR7.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Mechanism of endosomal TLR inhibition by antimalarial drugs and imidazoquinolines.",
+            "authors": [
+              "Kuznik A",
+              "Bencina M",
+              "Svajger U",
+              "Jeras M",
+              "Rozman B",
+              "Jerala R"
+            ],
+            "journal": "Journal of immunology (Baltimore, Md. : 1950)",
+            "year": "2011",
+            "doi": "10.4049/jimmunol.1000702",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:24342772",
+          "snippet": "Our data also confirm an earlier report that this same mechanism may explain inhibition of TLR7 and 9 signaling by hydroxychloroquine (Plaquenil; Sanofi-Aventis, Bridgewater, NJ), a drug commonly prescribed to treat lupus.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Novel small molecule inhibitors of TLR7 and TLR9: mechanism of action and efficacy in vivo.",
+            "authors": [
+              "Lamphier M",
+              "Zheng W",
+              "Latz E",
+              "Spyvee M",
+              "Hansen H",
+              "Rose J",
+              "Genest M",
+              "Yang H",
+              "Shaffer C",
+              "Zhao Y",
+              "Shen Y",
+              "Liu C",
+              "Liu D",
+              "Mempel TR",
+              "Rowbottom C",
+              "Chow J",
+              "Twine NC",
+              "Yu M",
+              "Gusovsky F",
+              "Ishizaka ST"
+            ],
+            "journal": "Molecular pharmacology",
+            "year": "2014",
+            "doi": "10.1124/mol.113.089821",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D006886",
+      "target": "UniProt:Q9NR96",
+      "evidence": [
+        {
+          "reference": "PMID:21398612",
+          "snippet": "Endosomal TLRs play an important role in innate immune response as well as in autoimmune processes. In the therapy of systemic lupus erythematosus, antimalarial drugs chloroquine, hydroxychloroquine, and quinacrine have been used for a long time. Their suppression of endosomal TLR activation has been attributed to the inhibition of endosomal acidification, which is a prerequisite for the activation of these receptors.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "The study demonstrates antimalarial drugs including hydroxychloroquine inhibit endosomal TLR9 activation.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Mechanism of endosomal TLR inhibition by antimalarial drugs and imidazoquinolines.",
+            "authors": [
+              "Kuznik A",
+              "Bencina M",
+              "Svajger U",
+              "Jeras M",
+              "Rozman B",
+              "Jerala R"
+            ],
+            "journal": "Journal of immunology (Baltimore, Md. : 1950)",
+            "year": "2011",
+            "doi": "10.4049/jimmunol.1000702",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:24342772",
+          "snippet": "Our data also confirm an earlier report that this same mechanism may explain inhibition of TLR7 and 9 signaling by hydroxychloroquine (Plaquenil; Sanofi-Aventis, Bridgewater, NJ), a drug commonly prescribed to treat lupus.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Novel small molecule inhibitors of TLR7 and TLR9: mechanism of action and efficacy in vivo.",
+            "authors": [
+              "Lamphier M",
+              "Zheng W",
+              "Latz E",
+              "Spyvee M",
+              "Hansen H",
+              "Rose J",
+              "Genest M",
+              "Yang H",
+              "Shaffer C",
+              "Zhao Y",
+              "Shen Y",
+              "Liu C",
+              "Liu D",
+              "Mempel TR",
+              "Rowbottom C",
+              "Chow J",
+              "Twine NC",
+              "Yu M",
+              "Gusovsky F",
+              "Ishizaka ST"
+            ],
+            "journal": "Molecular pharmacology",
+            "year": "2014",
+            "doi": "10.1124/mol.113.089821",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:Q9NYK1",
+      "target": "GO:0032606",
+      "evidence": [
+        {
+          "reference": "PMID:36622335",
+          "snippet": "Increased Toll-like receptor 7 (TLR-7) signaling leading to the production of type I interferon (IFN) is an important contributor to human systemic lupus erythematosus (SLE).",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "De Novo PACSIN1 Gene Variant Found in Childhood Lupus and a Role for PACSIN1/TRAF4 Complex in Toll-like Receptor 7 Activation.",
+            "authors": [
+              "Xie C",
+              "Zhou H",
+              "Athanasopoulos V",
+              "Shen Q",
+              "Zhang Y",
+              "Meng X",
+              "Burgio G",
+              "Arsov T",
+              "Lungu AC",
+              "Zhang P",
+              "Qin Y",
+              "Ma J",
+              "Wu X",
+              "Jiang X",
+              "Ding H",
+              "Meng Y",
+              "Shen N",
+              "He Y",
+              "Vinuesa CG"
+            ],
+            "journal": "Arthritis & rheumatology (Hoboken, N.J.)",
+            "year": "2023",
+            "doi": "10.1002/art.42416",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:30846987",
+          "snippet": "PDCs were the only producers of IFNα in response to CpG-A, R848, and ssRNA stimulation in PBMC cultures. CLE patients with higher levels of blood HCQ showed lower ex vivo pDC responses to CpG-A, but not R848 or ssRNA.",
+          "supports": "PARTIAL",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "CpG-A stimulates TLR9 and R848/ssRNA stimulate TLR7/8; the pDC IFNα production is shown to be downstream of TLR activation.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Effect of in vivo Hydroxychloroquine and ex vivo Anti-BDCA2 mAb Treatment on pDC IFNα Production From Patients Affected With Cutaneous Lupus Erythematosus.",
+            "authors": [
+              "Gardet A",
+              "Pellerin A",
+              "McCarl CA",
+              "Diwanji R",
+              "Wang W",
+              "Donaldson D",
+              "Franchimont N",
+              "Werth VP",
+              "Rabah D"
+            ],
+            "journal": "Frontiers in immunology",
+            "year": "2019",
+            "doi": "10.3389/fimmu.2019.00275",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:Q9NR96",
+      "target": "GO:0032606",
+      "evidence": [
+        {
+          "reference": "PMID:32714335",
+          "snippet": "They are also known to interfere with endosomal Toll-like receptors signaling and cytosolic sensors of nucleic acids, which result in a decreased cellular activation and thereby a lower type I interferons and inflammatory cytokine secretion.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Blocking endosomal TLR signaling (including TLR9) reduces type I IFN production, confirming TLR9 positively regulates type I IFN production.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Beyond Anti-viral Effects of Chloroquine/Hydroxychloroquine.",
+            "authors": [
+              "Gies V",
+              "Bekaddour N",
+              "Dieudonné Y",
+              "Guffroy A",
+              "Frenger Q",
+              "Gros F",
+              "Rodero MP",
+              "Herbeuval JP",
+              "Korganow AS"
+            ],
+            "journal": "Frontiers in immunology",
+            "year": "2020",
+            "doi": "10.3389/fimmu.2020.01409",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:30846987",
+          "snippet": "Our findings reveal that clinically-relevant HCQ concentrations partially inhibit the pDC response to TLR9 and weakly affect the response to TLR7/8 stimulation.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "HCQ inhibits pDC IFNα production via TLR9, confirming TLR9 drives type I IFN production.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Effect of in vivo Hydroxychloroquine and ex vivo Anti-BDCA2 mAb Treatment on pDC IFNα Production From Patients Affected With Cutaneous Lupus Erythematosus.",
+            "authors": [
+              "Gardet A",
+              "Pellerin A",
+              "McCarl CA",
+              "Diwanji R",
+              "Wang W",
+              "Donaldson D",
+              "Franchimont N",
+              "Werth VP",
+              "Rabah D"
+            ],
+            "journal": "Frontiers in immunology",
+            "year": "2019",
+            "doi": "10.3389/fimmu.2019.00275",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "contributes to",
+      "source": "GO:0032606",
+      "target": "MESH:D008180",
+      "evidence": [
+        {
+          "reference": "PMID:26099519",
+          "snippet": "One of the most prominent features, shared by the majority of patients with SLE, is a continuous activation of the type I interferon (IFN) system, which manifests as increased serum levels of IFNα and/or an increased expression of type I IFN-induced genes, a so-called type I IFN signature.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Systemic Lupus Erythematosus--A Disease with A Dysregulated Type I Interferon System.",
+            "authors": [
+              "Hagberg N",
+              "Rönnblom L"
+            ],
+            "journal": "Scandinavian journal of immunology",
+            "year": "2015",
+            "doi": "10.1111/sji.12330",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:32185249",
+          "snippet": "Type I interferons secreted by plasmacytoid dendritic cells (pDCs) play a crucial role in the pathogenesis of systemic lupus erythematosus by driving the formation of autoantibodies against nuclear debris.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Interferon targeted therapies in systemic lupus erythematosus.",
+            "authors": [
+              "Misra DP",
+              "Negi VS"
+            ],
+            "journal": "Mediterranean journal of rheumatology",
+            "year": "2017",
+            "doi": "10.31138/mjr.28.1.13",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://www.drugbank.ca/drugs/DB01611",
+      "type": "drugbank",
+      "label": "drugbank.ca — record source"
+    },
+    {
+      "url": "https://meshb.nlm.nih.gov/record/ui?ui=D006886",
+      "type": "other",
+      "label": "meshb.nlm.nih.gov — record source"
+    }
+  ],
+  "site": {
+    "id": "sonnet__P23",
+    "record_id": "P23_DB01611_MESH_D008180",
+    "run": "sonnet",
+    "run_label": "Sonnet (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/sonnet/outputs/P23.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/sonnet__P24.json b/web-revamp-mockup/data/records/sonnet__P24.json
new file mode 100644
index 0000000..0d75c3f
--- /dev/null
+++ b/web-revamp-mockup/data/records/sonnet__P24.json
@@ -0,0 +1,247 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P24_DB00688_MESH_D008181",
+    "drug": "Mycophenolate Mofetil",
+    "drug_mesh": "MESH:D000077732",
+    "drugbank": "DB:DB00688",
+    "disease": "Lupus Nephritis",
+    "disease_mesh": "MESH:D008181",
+    "summary": "Mycophenolate Mofetil → Mycophenolic Acid → Inosine-5'-monophosphate dehydrogenase 2 → lymphocyte proliferation → Lupus Nephritis"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D000077732",
+      "name": "Mycophenolate Mofetil",
+      "label": "Drug"
+    },
+    {
+      "id": "MESH:D009173",
+      "name": "Mycophenolic Acid",
+      "label": "ChemicalSubstance"
+    },
+    {
+      "id": "UniProt:P12268",
+      "name": "Inosine-5'-monophosphate dehydrogenase 2",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0046651",
+      "name": "lymphocyte proliferation",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D008181",
+      "name": "Lupus Nephritis",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "has metabolite",
+      "source": "MESH:D000077732",
+      "target": "MESH:D009173",
+      "evidence": [
+        {
+          "reference": "PMID:19834629",
+          "snippet": "Mycophenolate mofetil (MMF) is a prodrug of MPA that was developed to improve the bioavailability of MPA. After oral administration, MMF is completely metabolized to MPA.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "MMF is a prodrug that is completely hydrolyzed to the active metabolite mycophenolic acid (MPA) after oral administration.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Mycophenolate mofetil: An update.",
+            "authors": [
+              "Villarroel MC",
+              "Hidalgo M",
+              "Jimeno A"
+            ],
+            "journal": "Drugs of today (Barcelona, Spain : 1998)",
+            "year": "2009",
+            "doi": "10.1358/dot.2009.45.7.1384878",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D009173",
+      "target": "UniProt:P12268",
+      "evidence": [
+        {
+          "reference": "PMID:19834629",
+          "snippet": "Mycophenolic acid (MPA) is a potent, selective, noncompetitive and reversible inhibitor of inosine-5'-monophosphate deshydrogenase (IMPDH).",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "MPA is a well-characterized potent inhibitor of IMPDH (type II isoform, UniProt P12268), the rate-limiting enzyme in de novo guanosine nucleotide biosynthesis.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Mycophenolate mofetil: An update.",
+            "authors": [
+              "Villarroel MC",
+              "Hidalgo M",
+              "Jimeno A"
+            ],
+            "journal": "Drugs of today (Barcelona, Spain : 1998)",
+            "year": "2009",
+            "doi": "10.1358/dot.2009.45.7.1384878",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:17100698",
+          "snippet": "Mycophenolic acid (MPA) is a highly selective, non-competitive and reversible inhibitor of the inosine monophosphate dehydrogenase (IMPDH), the rate-limiting enzyme in the de novo biosynthesis of guanosine nucleotides.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Antifibrotic actions of mycophenolic acid.",
+            "authors": [
+              "Morath C",
+              "Schwenger V",
+              "Beimler J",
+              "Mehrabi A",
+              "Schmidt J",
+              "Zeier M",
+              "Muranyi W"
+            ],
+            "journal": "Clinical transplantation",
+            "year": "2006",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P12268",
+      "target": "GO:0046651",
+      "evidence": [
+        {
+          "reference": "PMID:11233304",
+          "snippet": "As T and B-lymphocytes almost exclusively use the de novo pathway of purine synthesis, these cells are particularly sensitive to the inhibitory action of MMF.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "IMPDH catalyzes the rate-limiting step in de novo guanosine nucleotide synthesis, which T and B lymphocytes depend upon for proliferation; its activity thus positively regulates lymphocyte proliferation.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "[Pharmacological profiles of mycophenolate mofetil (CellCept), a new immunosuppressive agent].",
+            "authors": [
+              "Yashima Y",
+              "Ohgane T"
+            ],
+            "journal": "Nihon yakurigaku zasshi. Folia pharmacologica Japonica",
+            "year": "2001",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:19436616",
+          "snippet": "It preferentially inhibits denovo pathway of guanosine nucleotide synthesis in T and B-lymphocytes and prevents their proliferation, thereby suppresses both cell mediated and humoral immune responses.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Mycophenolate mofetil: safety and efficacy in the prophylaxis of acute kidney transplantation rejection.",
+            "authors": [
+              "Dalal P",
+              "Grafals M",
+              "Chhabra D",
+              "Gallon L"
+            ],
+            "journal": "Therapeutics and clinical risk management",
+            "year": "2009",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "contributes to",
+      "source": "GO:0046651",
+      "target": "MESH:D008181",
+      "evidence": [
+        {
+          "reference": "PMID:10361247",
+          "snippet": "the number of immunoglobulin-producing B cells and serum levels of IgG and IgG anti-dsDNA antibodies were reduced after MMF and CYC treatment. MMF treatment significantly reduced the extent of deposition of C3 in glomeruli.",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "explanation": "Lymphocyte proliferation drives production of pathogenic anti-dsDNA antibodies and immune complex/complement deposition in glomeruli in lupus nephritis; inhibiting lymphocyte proliferation with MMF reduces disease severity.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Beneficial effect of the inosine monophosphate dehydrogenase inhibitor mycophenolate mofetil on survival and severity of glomerulonephritis in systemic lupus erythematosus (SLE)-prone MRLlpr/lpr mice.",
+            "authors": [
+              "Jonsson CA",
+              "Svensson L",
+              "Carlsten H"
+            ],
+            "journal": "Clinical and experimental immunology",
+            "year": "1999",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:12538032",
+          "snippet": "since activated B lymphocytes play a central role in lupus and our results show that B cells are targets for MPA, we propose that direct effects on B cells may be an important mechanism for the ameliorating effects of MMF in SLE.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Mycophenolic acid inhibits inosine 5'-monophosphate dehydrogenase and suppresses immunoglobulin and cytokine production of B cells.",
+            "authors": [
+              "Jonsson CA",
+              "Carlsten H"
+            ],
+            "journal": "International immunopharmacology",
+            "year": "2003",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://www.drugbank.ca/drugs/DB00688",
+      "type": "drugbank",
+      "label": "drugbank.ca — record source"
+    },
+    {
+      "url": "https://meshb.nlm.nih.gov/record/ui?ui=D008181",
+      "type": "other",
+      "label": "meshb.nlm.nih.gov — record source"
+    }
+  ],
+  "site": {
+    "id": "sonnet__P24",
+    "record_id": "P24_DB00688_MESH_D008181",
+    "run": "sonnet",
+    "run_label": "Sonnet (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/sonnet/outputs/P24.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/sonnet__P25.json b/web-revamp-mockup/data/records/sonnet__P25.json
new file mode 100644
index 0000000..ee6f303
--- /dev/null
+++ b/web-revamp-mockup/data/records/sonnet__P25.json
@@ -0,0 +1,186 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P25_DB00051_MESH_D011565",
+    "drug": "Adalimumab",
+    "drug_mesh": "MESH:D000068879",
+    "drugbank": "DB:DB00051",
+    "disease": "Psoriasis",
+    "disease_mesh": "MESH:D011565",
+    "summary": "Adalimumab → Tumor necrosis factor → I-kappaB kinase/NF-kappaB signaling → Psoriasis"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D000068879",
+      "name": "Adalimumab",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P01375",
+      "name": "Tumor necrosis factor",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0007249",
+      "name": "I-kappaB kinase/NF-kappaB signaling",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D011565",
+      "name": "Psoriasis",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "directly physically interacts with",
+      "source": "MESH:D000068879",
+      "target": "UniProt:P01375",
+      "evidence": [
+        {
+          "reference": "PMID:19799828",
+          "snippet": "Adalimumab, a fully human monoclonal antibody, binds to and neutralizes tumor necrosis factor.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Adalimumab in the treatment of psoriasis: pooled efficacy and safety results from three pivotal studies.",
+            "authors": [
+              "Papp K",
+              "Okun M",
+              "Vender R"
+            ],
+            "journal": "Journal of cutaneous medicine and surgery",
+            "year": "2009",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D000068879",
+      "target": "UniProt:P01375",
+      "evidence": [
+        {
+          "reference": "PMID:21573251",
+          "snippet": "Adalimumab is a fully recombinant human immunoglobulin G1 monoclonal antibody that specifically binds with high affinity to human TNF-α and inhibits its binding to TNF receptors.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Adalimumab for the treatment of immune-mediated diseases: an update on old and recent indications.",
+            "authors": [
+              "Murdaca G",
+              "Colombo BM",
+              "Puppo F"
+            ],
+            "journal": "Drugs of today (Barcelona, Spain : 1998)",
+            "year": "2011",
+            "doi": "10.1358/dot.2011.47.4.1576692",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P01375",
+      "target": "GO:0007249",
+      "evidence": [
+        {
+          "reference": "PMID:17302610",
+          "snippet": "TNF-alpha and NF-kappaB expressions were significantly higher in psoriatic epidermis than in normal epidermis (p < 0.05).",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Nature of cell kinetics in psoriatic epidermis.",
+            "authors": [
+              "Doger FK",
+              "Dikicioglu E",
+              "Ergin F",
+              "Unal E",
+              "Sendur N",
+              "Uslu M"
+            ],
+            "journal": "Journal of cutaneous pathology",
+            "year": "2007",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "GO:0007249",
+      "target": "MESH:D011565",
+      "evidence": [
+        {
+          "reference": "PMID:35213752",
+          "snippet": "disease-relevant changes in morphology, gene transcription and cytokine production were robustly attenuated by pharmacologically blocking TNFα/IL-17A-induced NF-κB activation with IKK-2 inhibitor IV.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Cytokine induced 3-D organotypic psoriasis skin model demonstrates distinct roles for NF-κB and JAK pathways in disease pathophysiology.",
+            "authors": [
+              "Todorović V",
+              "McDonald HA",
+              "Hoover P",
+              "Wetter JB",
+              "Marinopoulos AE",
+              "Woody CL",
+              "Miller L",
+              "Finkielsztein A",
+              "Dunstan RW",
+              "Paller AS",
+              "Honore P",
+              "Getsios S",
+              "Scott VE"
+            ],
+            "journal": "Experimental dermatology",
+            "year": "2022",
+            "doi": "10.1111/exd.14551",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://www.drugbank.ca/drugs/DB00051",
+      "type": "drugbank",
+      "label": "drugbank.ca — record source"
+    },
+    {
+      "url": "https://www.ncbi.nlm.nih.gov/mesh/D011565",
+      "type": "other",
+      "label": "ncbi.nlm.nih.gov — record source"
+    }
+  ],
+  "site": {
+    "id": "sonnet__P25",
+    "record_id": "P25_DB00051_MESH_D011565",
+    "run": "sonnet",
+    "run_label": "Sonnet (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/sonnet/outputs/P25.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/sonnet__P26.json b/web-revamp-mockup/data/records/sonnet__P26.json
new file mode 100644
index 0000000..c25cf88
--- /dev/null
+++ b/web-revamp-mockup/data/records/sonnet__P26.json
@@ -0,0 +1,288 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P26_DB00331_MESH_D003924",
+    "drug": "Metformin",
+    "drug_mesh": "MESH:D008687",
+    "drugbank": "DB:DB00331",
+    "disease": "Type 2 Diabetes Mellitus",
+    "disease_mesh": "MESH:D003924",
+    "summary": "Metformin → NADH-ubiquinone oxidoreductase chain 1 → 5'-AMP-activated protein kinase catalytic subunit alpha-1 → gluconeogenesis → Diabetes Mellitus, Type 2"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D008687",
+      "name": "Metformin",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P03886",
+      "name": "NADH-ubiquinone oxidoreductase chain 1",
+      "label": "Protein"
+    },
+    {
+      "id": "UniProt:Q13131",
+      "name": "5'-AMP-activated protein kinase catalytic subunit alpha-1",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0006094",
+      "name": "gluconeogenesis",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D003924",
+      "name": "Diabetes Mellitus, Type 2",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D008687",
+      "target": "UniProt:P03886",
+      "evidence": [
+        {
+          "reference": "PMID:31886264",
+          "snippet": "action on complex I of the respiratory chain of mitochondria",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Metformin acts on complex I of the respiratory chain of mitochondria, establishing direct inhibition.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Role of Metformin on Osteoblast Differentiation in Type 2 Diabetes.",
+            "authors": [
+              "Jiating L",
+              "Buyun J",
+              "Yinchang Z"
+            ],
+            "journal": "BioMed research international",
+            "year": "2019",
+            "doi": "10.1155/2019/9203934",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:19664596",
+          "snippet": "Both metformin and rotenone, an inhibitor of respiratory chain complex I, suppressed glucose-6-phosphatase (G6pc), a rate limiting enzyme of liver glucose production, mRNA expression in a rat hepatoma cell line accompanied by a reduction of intracellular ATP concentration and an activation of AMP-activated protein kinase (AMPK).",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Metformin behaves like an inhibitor of respiratory chain complex I.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Metformin suppresses glucose-6-phosphatase expression by a complex I inhibition and AMPK activation-independent mechanism.",
+            "authors": [
+              "Ota S",
+              "Horigome K",
+              "Ishii T",
+              "Nakai M",
+              "Hayashi K",
+              "Kawamura T",
+              "Kishino A",
+              "Taiji M",
+              "Kimura T"
+            ],
+            "journal": "Biochemical and biophysical research communications",
+            "year": "2009",
+            "doi": "10.1016/j.bbrc.2009.07.164",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "causes",
+      "source": "UniProt:P03886",
+      "target": "UniProt:Q13131",
+      "evidence": [
+        {
+          "reference": "PMID:31886264",
+          "snippet": "These changes activate the cellular energy sensor AMP-activated protein kinase (AMPK). Thus, the increased cellular AMP/ATP ratio causes a dramatic and progressive activation",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Inhibition of complex I raises the AMP/ATP ratio, which activates AMPK.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Role of Metformin on Osteoblast Differentiation in Type 2 Diabetes.",
+            "authors": [
+              "Jiating L",
+              "Buyun J",
+              "Yinchang Z"
+            ],
+            "journal": "BioMed research international",
+            "year": "2019",
+            "doi": "10.1155/2019/9203934",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:23710432",
+          "snippet": "These drugs, such as metformin and STZ, inhibit ATP synthesis in mitochondria to raise AMP/ATP ratio in the process of AMPK activation.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Complex I inhibition by metformin raises AMP/ATP ratio and activates AMPK.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Mitochondrial inhibitor as a new class of insulin sensitizer.",
+            "authors": [
+              "Zhang Y",
+              "Ye J"
+            ],
+            "journal": "Acta pharmaceutica Sinica. B",
+            "year": "2012",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "decreased",
+      "source": "UniProt:Q13131",
+      "target": "GO:0006094",
+      "evidence": [
+        {
+          "reference": "PMID:16308421",
+          "snippet": "TORC2 is a critical target of LKB1/AMPK signals in the regulation of gluconeogenesis. Finally, we show that metformin, one of the most widely prescribed type 2 diabetes therapeutics, requires LKB1 in the liver to lower blood glucose levels.",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "explanation": "AMPK (activated via LKB1) negatively regulates gluconeogenesis via TORC2 suppression.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "The kinase LKB1 mediates glucose homeostasis in liver and therapeutic effects of metformin.",
+            "authors": [
+              "Shaw RJ",
+              "Lamia KA",
+              "Vasquez D",
+              "Koo SH",
+              "Bardeesy N",
+              "Depinho RA",
+              "Montminy M",
+              "Cantley LC"
+            ],
+            "journal": "Science (New York, N.Y.)",
+            "year": "2005",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:34502359",
+          "snippet": "Metformin, which is widely prescribed for type 2 diabetes mellitus (T2DM) patients, regulates blood sugar by inhibiting hepatic gluconeogenesis and promoting insulin sensitivity to facilitate glucose uptake by cells.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "explanation": "AMPK activation by metformin is responsible for inhibiting hepatic gluconeogenesis.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "New Insight into the Effects of Metformin on Diabetic Retinopathy, Aging and Cancer: Nonapoptotic Cell Death, Immunosuppression, and Effects beyond the AMPK Pathway.",
+            "authors": [
+              "Hsu SK",
+              "Cheng KC",
+              "Mgbeahuruike MO",
+              "Lin YH",
+              "Wu CY",
+              "Wang HD",
+              "Yen CH",
+              "Chiu CC",
+              "Sheu SJ"
+            ],
+            "journal": "International journal of molecular sciences",
+            "year": "2021",
+            "doi": "10.3390/ijms22179453",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "treats",
+      "source": "GO:0006094",
+      "target": "MESH:D003924",
+      "evidence": [
+        {
+          "reference": "PMID:25849133",
+          "snippet": "Metformin lowers blood glucose levels by inhibiting hepatic glucose production (HGP), an effect originally postulated to be due to a hepatic AMP-activated protein kinase (AMPK)-dependent mechanism.",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "explanation": "Inhibition of gluconeogenesis (hepatic glucose production) by the AMPK pathway lowers blood glucose, treating type 2 diabetes.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Metformin activates a duodenal Ampk-dependent pathway to lower hepatic glucose production in rats.",
+            "authors": [
+              "Duca FA",
+              "Côté CD",
+              "Rasmussen BA",
+              "Zadeh-Tahmasebi M",
+              "Rutter GA",
+              "Filippi BM",
+              "Lam TK"
+            ],
+            "journal": "Nature medicine",
+            "year": "2015",
+            "doi": "10.1038/nm.3787",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:15669880",
+          "snippet": "reduce hepatic glucose production (biguanides)",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Biguanides like metformin treat type 2 diabetes by reducing hepatic glucose production, establishing the link between gluconeogenesis inhibition and disease treatment.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Oral antidiabetic agents: current role in type 2 diabetes mellitus.",
+            "authors": [
+              "Krentz AJ",
+              "Bailey CJ"
+            ],
+            "journal": "Drugs",
+            "year": "2005",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://www.drugbank.ca/drugs/DB00331",
+      "type": "drugbank",
+      "label": "drugbank.ca — record source"
+    },
+    {
+      "url": "https://www.ncbi.nlm.nih.gov/mesh/D003924",
+      "type": "other",
+      "label": "ncbi.nlm.nih.gov — record source"
+    }
+  ],
+  "site": {
+    "id": "sonnet__P26",
+    "record_id": "P26_DB00331_MESH_D003924",
+    "run": "sonnet",
+    "run_label": "Sonnet (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/sonnet/outputs/P26.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/sonnet__P29.json b/web-revamp-mockup/data/records/sonnet__P29.json
new file mode 100644
index 0000000..33a934c
--- /dev/null
+++ b/web-revamp-mockup/data/records/sonnet__P29.json
@@ -0,0 +1,162 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P29_DB00437_MESH_D006073",
+    "drug": "Allopurinol",
+    "drug_mesh": "MESH:D000493",
+    "drugbank": "DB:DB00437",
+    "disease": "Gout",
+    "disease_mesh": "MESH:D006073",
+    "summary": "Allopurinol → Xanthine oxidoreductase → Uric Acid → Gout"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D000493",
+      "name": "Allopurinol",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P47989",
+      "name": "Xanthine oxidoreductase",
+      "label": "Protein"
+    },
+    {
+      "id": "MESH:D014527",
+      "name": "Uric Acid",
+      "label": "ChemicalSubstance"
+    },
+    {
+      "id": "MESH:D006073",
+      "name": "Gout",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D000493",
+      "target": "UniProt:P47989",
+      "evidence": [
+        {
+          "reference": "PMID:39149682",
+          "snippet": "Allopurinol lowers urate production through the inhibition of xanthine oxidase.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Allopurinol directly inhibits xanthine oxidase, reducing urate production.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Allopurinol: Clinical Considerations in the Development and Treatment of Stevens-Johnson Syndrome, Toxic Epidermal Necrolysis, and Other Associated Drug Reactions.",
+            "authors": [
+              "Dillman KM",
+              "Hawkins AM",
+              "Ragland AR",
+              "Wester GC",
+              "Greene DR",
+              "Varrassi G",
+              "Moore P",
+              "Behara R",
+              "Ahmadzadeh S",
+              "Siddaiah H",
+              "Shekoohi S",
+              "Kaye AD"
+            ],
+            "journal": "Cureus",
+            "year": "2024",
+            "doi": "10.7759/cureus.64654",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P47989",
+      "target": "MESH:D014527",
+      "evidence": [
+        {
+          "reference": "PMID:28478180",
+          "snippet": "Xanthine oxidase (XO), a versatile metalloflavoprotein enzyme, catalyzes the oxidative hydroxylation of hypoxanthine and xanthine to uric acid in purine catabolism while simultaneously producing reactive oxygen species.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Xanthine oxidase catalyzes the final steps of purine catabolism, producing uric acid from hypoxanthine and xanthine.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Xanthine oxidase inhibitors beyond allopurinol and febuxostat; an overview and selection of potential leads based on in silico calculated physico-chemical properties, predicted pharmacokinetics and toxicity.",
+            "authors": [
+              "Šmelcerović A",
+              "Tomović K",
+              "Šmelcerović Ž",
+              "Petronijević Ž",
+              "Kocić G",
+              "Tomašič T",
+              "Jakopin Ž",
+              "Anderluh M"
+            ],
+            "journal": "European journal of medicinal chemistry",
+            "year": "2017",
+            "doi": "10.1016/j.ejmech.2017.04.031",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "causes",
+      "source": "MESH:D014527",
+      "target": "MESH:D006073",
+      "evidence": [
+        {
+          "reference": "PMID:33671646",
+          "snippet": "It results from sustained hyperuricemia that leads to monosodium urate crystal deposition in joint structures and soft tissue.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Elevated uric acid (hyperuricemia) leads to monosodium urate crystal deposition in joints, causing gout.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Role of Vitamin C in Prophylaxis and Treatment of Gout-A Literature Review.",
+            "authors": [
+              "Brzezińska O",
+              "Styrzyński F",
+              "Makowska J",
+              "Walczak K"
+            ],
+            "journal": "Nutrients",
+            "year": "2021",
+            "doi": "10.3390/nu13020701",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://www.drugbank.ca/drugs/DB00437",
+      "type": "drugbank",
+      "label": "drugbank.ca — record source"
+    },
+    {
+      "url": "https://meshb.nlm.nih.gov/record/ui?ui=D006073",
+      "type": "other",
+      "label": "meshb.nlm.nih.gov — record source"
+    }
+  ],
+  "site": {
+    "id": "sonnet__P29",
+    "record_id": "P29_DB00437_MESH_D006073",
+    "run": "sonnet",
+    "run_label": "Sonnet (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/sonnet/outputs/P29.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/sonnet__P30.json b/web-revamp-mockup/data/records/sonnet__P30.json
new file mode 100644
index 0000000..6a8bf81
--- /dev/null
+++ b/web-revamp-mockup/data/records/sonnet__P30.json
@@ -0,0 +1,251 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P30_DB09038_MESH_D003924",
+    "drug": "Empagliflozin",
+    "drug_mesh": "MESH:C000591311",
+    "drugbank": "DB:DB09038",
+    "disease": "Type 2 Diabetes Mellitus",
+    "disease_mesh": "MESH:D003924",
+    "summary": "Empagliflozin → Sodium/glucose cotransporter 2 (SGLT2) → renal glucose absorption → Hyperglycemia → Type 2 Diabetes Mellitus"
+  },
+  "nodes": [
+    {
+      "id": "MESH:C000591311",
+      "name": "Empagliflozin",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P31639",
+      "name": "Sodium/glucose cotransporter 2 (SGLT2)",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0070293",
+      "name": "renal glucose absorption",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "HP:0003074",
+      "name": "Hyperglycemia",
+      "label": "PhenotypicFeature"
+    },
+    {
+      "id": "MESH:D003924",
+      "name": "Type 2 Diabetes Mellitus",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:C000591311",
+      "target": "UniProt:P31639",
+      "evidence": [
+        {
+          "reference": "PMID:26638450",
+          "snippet": "Empagliflozin is a new inhibitor of sodiumglucose cotransporters type 2 (SGLT2) for the treatment of type 2 diabetes mellitus (T2DM). Its specific action inhibits glucose reabsorption in renal tubules and thus promotes glucosuria.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Empagliflozin directly inhibits the SGLT2 cotransporter, reducing its activity.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "[EMPAGLIFLOZIN (JARDIANCE) :Nw SGLT2 COTRANSPORTER INHIBITOR FOR TREATING TYPE 2 DIABETES].",
+            "authors": [
+              "Scheen AJ"
+            ],
+            "journal": "Revue medicale de Liege",
+            "year": "2015",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:32006266",
+          "snippet": "By inhibiting these proteins, SGLT2 inhibitors increase urinary glucose excretion (UGE) that leads to fall in plasma glucose concentrations and improvement in all glycemic parameters.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Confirms SGLT2 inhibition as the mechanism of action of empagliflozin.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Glucose Lowering Efficacy and Pleiotropic Effects of Sodium-Glucose Cotransporter 2 Inhibitors.",
+            "authors": [
+              "Kuchay MS",
+              "Farooqui KJ",
+              "Mishra SK",
+              "Mithal A"
+            ],
+            "journal": "Advances in experimental medicine and biology",
+            "year": "2021",
+            "doi": "10.1007/5584_2020_479",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P31639",
+      "target": "GO:0070293",
+      "evidence": [
+        {
+          "reference": "PMID:33409652",
+          "snippet": "Inhibitors of sodium/glucose co-transporter 2 (SGLT2) are currently in clinical use for type 2 diabetes (T2D) treatment due to their anti-hyperglycemic effect exerted by the inhibition of glucose reabsorption in the kidney.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "SGLT2 drives renal glucose reabsorption; its inhibition reduces this process.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Impact of an SGLT2-loss of function mutation on renal architecture, histology, and glucose homeostasis.",
+            "authors": [
+              "Hughes CB",
+              "Mussman GM",
+              "Ray P",
+              "Bunn RC",
+              "Cornea V",
+              "Thrailkill KM",
+              "Fowlkes JL",
+              "Popescu I"
+            ],
+            "journal": "Cell and tissue research",
+            "year": "2021",
+            "doi": "10.1007/s00441-020-03358-8",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:25805666",
+          "snippet": "SGLT2 cotransporters are responsible for reabsorption of 90 % of the glucose filtered by the kidney.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "SGLT2 is the primary transporter responsible for renal glucose reabsorption.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Pharmacokinetics, Pharmacodynamics and Clinical Use of SGLT2 Inhibitors in Patients with Type 2 Diabetes Mellitus and Chronic Kidney Disease.",
+            "authors": [
+              "Scheen AJ"
+            ],
+            "journal": "Clinical pharmacokinetics",
+            "year": "2015",
+            "doi": "10.1007/s40262-015-0264-4",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "decreased",
+      "source": "GO:0070293",
+      "target": "HP:0003074",
+      "evidence": [
+        {
+          "reference": "PMID:26513131",
+          "snippet": "These agents reduce hyperglycemia by decreasing the renal glucose threshold and thereby increasing urinary glucose excretion.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Reduced renal glucose reabsorption increases urinary glucose excretion and lowers plasma glucose, thereby reducing hyperglycemia.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "SGLT2 inhibition: efficacy and safety in type 2 diabetes treatment.",
+            "authors": [
+              "Scheen AJ"
+            ],
+            "journal": "Expert opinion on drug safety",
+            "year": "2015",
+            "doi": "10.1517/14740338.2015.1100167",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:29963920",
+          "snippet": "Sodium-glucose cotransporter 2 inhibitors medications lower plasma glucose by inhibiting glucose reabsorption in the proximal tubule of the kidney independent of insulin.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Inhibiting renal glucose reabsorption lowers plasma glucose (reduces hyperglycemia).",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Effects of sodium glucose co-transporter 2 inhibitors on the kidney.",
+            "authors": [
+              "de Albuquerque Rocha N",
+              "Neeland IJ",
+              "McCullough PA",
+              "Toto RD",
+              "McGuire DK"
+            ],
+            "journal": "Diabetes & vascular disease research",
+            "year": "2018",
+            "doi": "10.1177/1479164118783756",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "manifestation of",
+      "source": "HP:0003074",
+      "target": "MESH:D003924",
+      "evidence": [
+        {
+          "reference": "PMID:32006266",
+          "snippet": "In type 2 diabetes, the maladaptive upregulation of sodium-glucose cotransporter 2 (SGLT2) protein expression and activity contribute to the maintenance of hyperglycemia.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Hyperglycemia is a cardinal manifestation of type 2 diabetes mellitus.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Glucose Lowering Efficacy and Pleiotropic Effects of Sodium-Glucose Cotransporter 2 Inhibitors.",
+            "authors": [
+              "Kuchay MS",
+              "Farooqui KJ",
+              "Mishra SK",
+              "Mithal A"
+            ],
+            "journal": "Advances in experimental medicine and biology",
+            "year": "2021",
+            "doi": "10.1007/5584_2020_479",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://www.drugbank.ca/drugs/DB09038",
+      "type": "drugbank",
+      "label": "drugbank.ca — record source"
+    },
+    {
+      "url": "https://meshb.nlm.nih.gov/record/ui?ui=D003924",
+      "type": "other",
+      "label": "meshb.nlm.nih.gov — record source"
+    }
+  ],
+  "site": {
+    "id": "sonnet__P30",
+    "record_id": "P30_DB09038_MESH_D003924",
+    "run": "sonnet",
+    "run_label": "Sonnet (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/sonnet/outputs/P30.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/sonnet__P31.json b/web-revamp-mockup/data/records/sonnet__P31.json
new file mode 100644
index 0000000..70431ba
--- /dev/null
+++ b/web-revamp-mockup/data/records/sonnet__P31.json
@@ -0,0 +1,273 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P31_DB00067_MESH_D006467",
+    "drug": "Vasopressin",
+    "drug_mesh": "MESH:C016671",
+    "drugbank": "DB:DB00067",
+    "disease": "Hemophilia A",
+    "disease_mesh": "MESH:D006467",
+    "summary": "Vasopressin → Vasopressin V2 receptor → cAMP-mediated signaling → Weibel-Palade body exocytosis → von Willebrand factor → Coagulation factor VIII → Hemophilia A"
+  },
+  "nodes": [
+    {
+      "id": "MESH:C016671",
+      "name": "Vasopressin",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P30518",
+      "name": "Vasopressin V2 receptor",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0019933",
+      "name": "cAMP-mediated signaling",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "GO:0099132",
+      "name": "Weibel-Palade body exocytosis",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "UniProt:P04275",
+      "name": "von Willebrand factor",
+      "label": "Protein"
+    },
+    {
+      "id": "UniProt:P00451",
+      "name": "Coagulation factor VIII",
+      "label": "Protein"
+    },
+    {
+      "id": "MESH:D006467",
+      "name": "Hemophilia A",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "increased",
+      "source": "MESH:C016671",
+      "target": "UniProt:P30518",
+      "evidence": [
+        {
+          "reference": "PMID:12871401",
+          "snippet": "Its effect on VWF and t-PA as well as its vasodilatory effect are likely explained by a direct action on the endothelium, via activation of endothelial vasopressin V2R receptor and cAMP-mediated signaling.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "DDAVP (the synthetic vasopressin analogue) activates the endothelial vasopressin V2 receptor (AVPR2), initiating cAMP-mediated signaling.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Cellular mechanisms of the hemostatic effects of desmopressin (DDAVP).",
+            "authors": [
+              "Kaufmann JE",
+              "Vischer UM"
+            ],
+            "journal": "Journal of thrombosis and haemostasis : JTH",
+            "year": "2003",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P30518",
+      "target": "GO:0019933",
+      "evidence": [
+        {
+          "reference": "PMID:12871401",
+          "snippet": "via activation of endothelial vasopressin V2R receptor and cAMP-mediated signaling. This leads to exocytosis from Weibel Palade bodies where both VWF and t-PA are stored",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Activation of the V2 receptor increases cAMP-mediated signaling, which drives Weibel-Palade body exocytosis.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Cellular mechanisms of the hemostatic effects of desmopressin (DDAVP).",
+            "authors": [
+              "Kaufmann JE",
+              "Vischer UM"
+            ],
+            "journal": "Journal of thrombosis and haemostasis : JTH",
+            "year": "2003",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "GO:0019933",
+      "target": "GO:0099132",
+      "evidence": [
+        {
+          "reference": "PMID:12871401",
+          "snippet": "via activation of endothelial vasopressin V2R receptor and cAMP-mediated signaling. This leads to exocytosis from Weibel Palade bodies where both VWF and t-PA are stored",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "cAMP-mediated signaling downstream of V2 receptor activation leads to exocytosis from Weibel-Palade bodies.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Cellular mechanisms of the hemostatic effects of desmopressin (DDAVP).",
+            "authors": [
+              "Kaufmann JE",
+              "Vischer UM"
+            ],
+            "journal": "Journal of thrombosis and haemostasis : JTH",
+            "year": "2003",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "GO:0099132",
+      "target": "UniProt:P04275",
+      "evidence": [
+        {
+          "reference": "PMID:26473492",
+          "snippet": "VWF is synthesized in megakaryocytes and endothelial cells, and is stored and secreted from platelet alpha granules and Weibel-Palade bodies of endothelial cells.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Weibel-Palade body exocytosis releases stored VWF into plasma, raising circulating VWF levels.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Factor VIII Is Synthesized in Human Endothelial Cells, Packaged in Weibel-Palade Bodies and Secreted Bound to ULVWF Strings.",
+            "authors": [
+              "Turner NA",
+              "Moake JL"
+            ],
+            "journal": "PloS one",
+            "year": "2015",
+            "doi": "10.1371/journal.pone.0140740",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:40290674",
+          "snippet": "DDAVP elicits the release of von Willebrand Factor (VWF) from endothelial cells, thereby increasing the levels of circulating VWF and coagulation factor (F)VIII.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Plasma proteomics in patients with von Willebrand disease and hemophilia A highlights von Willebrand factor as main determinant of response to desmopressin treatment.",
+            "authors": [
+              "Alferez JDC",
+              "Smit ER",
+              "Meijer AB",
+              "Fijnvandraat K",
+              "Kruip MJHA",
+              "van Duijl TT",
+              "van den Biggelaar M"
+            ],
+            "journal": "Research and practice in thrombosis and haemostasis",
+            "year": "2025",
+            "doi": "10.1016/j.rpth.2025.102738",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P04275",
+      "target": "UniProt:P00451",
+      "evidence": [
+        {
+          "reference": "PMID:26473492",
+          "snippet": "FVIII stability and half-life is dependent on non-covalent complex formation with von Willebrand factor (VWF) to avoid proteolysis and clearance.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "VWF forms a non-covalent complex with FVIII, stabilizing it against proteolysis and prolonging its half-life in circulation.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Factor VIII Is Synthesized in Human Endothelial Cells, Packaged in Weibel-Palade Bodies and Secreted Bound to ULVWF Strings.",
+            "authors": [
+              "Turner NA",
+              "Moake JL"
+            ],
+            "journal": "PloS one",
+            "year": "2015",
+            "doi": "10.1371/journal.pone.0140740",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "treats",
+      "source": "UniProt:P00451",
+      "target": "MESH:D006467",
+      "evidence": [
+        {
+          "reference": "PMID:20829683",
+          "snippet": "Owing to its ability to raise plasma levels of factor VIII and von Willebrand factor levels, the synthetic vasopressin analogue desmopressin has become the mainstay of treatment for type 1 von Willebrand disease and mild hemophilia A.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Raising plasma factor VIII levels is the mechanism by which desmopressin/vasopressin treats mild hemophilia A.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "The use of desmopressin in mild hemophilia A.",
+            "authors": [
+              "Franchini M",
+              "Zaffanello M",
+              "Lippi G"
+            ],
+            "journal": "Blood coagulation & fibrinolysis : an international journal in haemostasis and thrombosis",
+            "year": "2010",
+            "doi": "10.1097/MBC.0b013e32833c2bb5",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://www.drugbank.ca/drugs/DB00067",
+      "type": "drugbank",
+      "label": "drugbank.ca — record source"
+    },
+    {
+      "url": "https://meshb.nlm.nih.gov/record/ui?ui=D006467",
+      "type": "other",
+      "label": "meshb.nlm.nih.gov — record source"
+    }
+  ],
+  "site": {
+    "id": "sonnet__P31",
+    "record_id": "P31_DB00067_MESH_D006467",
+    "run": "sonnet",
+    "run_label": "Sonnet (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/sonnet/outputs/P31.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/sonnet__P32.json b/web-revamp-mockup/data/records/sonnet__P32.json
new file mode 100644
index 0000000..56d8519
--- /dev/null
+++ b/web-revamp-mockup/data/records/sonnet__P32.json
@@ -0,0 +1,213 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P32_DB00126_MESH_D001206",
+    "drug": "Ascorbic acid",
+    "drug_mesh": "MESH:D001205",
+    "drugbank": "DB:DB00126",
+    "disease": "Ascorbic acid deficiency",
+    "disease_mesh": "MESH:D001206",
+    "summary": "Ascorbic acid → Prolyl 4-hydroxylase subunit alpha-1 → collagen biosynthetic process → Ascorbic acid deficiency"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D001205",
+      "name": "Ascorbic acid",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P13674",
+      "name": "Prolyl 4-hydroxylase subunit alpha-1",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0032964",
+      "name": "collagen biosynthetic process",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D001206",
+      "name": "Ascorbic acid deficiency",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "increased",
+      "source": "MESH:D001205",
+      "target": "UniProt:P13674",
+      "evidence": [
+        {
+          "reference": "PMID:17325743",
+          "snippet": "This enzyme, in turn, requires ascorbic acid to maintain the enzyme-bound iron in its reduced state.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Ascorbic acid (vitamin C) acts as a cofactor for prolyl hydroxylase by maintaining the enzyme-bound iron in its ferrous (reduced) state, thereby sustaining enzymatic activity.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Depletion of ascorbic acid restricts angiogenesis and retards tumor growth in a mouse model.",
+            "authors": [
+              "Telang S",
+              "Clem AL",
+              "Eaton JW",
+              "Chesney J"
+            ],
+            "journal": "Neoplasia (New York, N.Y.)",
+            "year": "2007",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:10329688",
+          "snippet": "vitamin C is an essential co-factor of the enzyme prolyl 4-hydroxylase",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Intracellular retention of procollagen within the endoplasmic reticulum is mediated by prolyl 4-hydroxylase.",
+            "authors": [
+              "Walmsley AR",
+              "Batten MR",
+              "Lad U",
+              "Bulleid NJ"
+            ],
+            "journal": "The Journal of biological chemistry",
+            "year": "1999",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "participates in",
+      "source": "UniProt:P13674",
+      "target": "GO:0032964",
+      "evidence": [
+        {
+          "reference": "PMID:41980618",
+          "snippet": "Ascorbic acid (AA) is known to act as a cofactor for collagen-modifying enzymes (collagen prolyl and lysyl hydroxylases) and is vital for collagen thermal stability, proper folding, and fibrillogenesis.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Prolyl 4-hydroxylase catalyzes the hydroxylation of proline residues in procollagen, an essential step in collagen biosynthesis required for thermal stability and triple helix formation.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Hypoxia and ascorbic acid: two interconnected microenvironmental factors driving collagen biosynthesis.",
+            "authors": [
+              "Ricol M",
+              "Lipinski O",
+              "Moali C",
+              "Sée V"
+            ],
+            "journal": "Matrix biology : journal of the International Society for Matrix Biology",
+            "year": "2026",
+            "doi": "10.1016/j.matbio.2026.102007",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:10329688",
+          "snippet": "The accumulation of these partially folded intermediates occurs during vitamin C deficiency due to incomplete proline hydroxylation, as vitamin C is an essential co-factor of the enzyme prolyl 4-hydroxylase.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Intracellular retention of procollagen within the endoplasmic reticulum is mediated by prolyl 4-hydroxylase.",
+            "authors": [
+              "Walmsley AR",
+              "Batten MR",
+              "Lad U",
+              "Bulleid NJ"
+            ],
+            "journal": "The Journal of biological chemistry",
+            "year": "1999",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "negatively correlated with",
+      "source": "GO:0032964",
+      "target": "MESH:D001206",
+      "evidence": [
+        {
+          "reference": "PMID:39494043",
+          "snippet": "vitamin C deficiency, impairing collagen synthesis and leading to typical scurvy symptoms",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Deficiency in collagen synthesis caused by insufficient ascorbic acid leads to the clinical manifestations of scurvy (ascorbic acid deficiency disease).",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Clinical Diagnosis and Treatment of Scurvy in a Young Adult With Poor Dietary Habits: A Case Report and Literature Review.",
+            "authors": [
+              "Saeid L",
+              "Hussein Al-Janabi M",
+              "Hassan F"
+            ],
+            "journal": "Case reports in dermatological medicine",
+            "year": "2024",
+            "doi": "10.1155/2024/2779253",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:32517792",
+          "snippet": "Severe vitamin C deficiency, or scurvy, encompasses a syndrome of multisystem abnormalities due to defective collagen synthesis and antioxidative functions.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Vitamin C deficiency mimicking inflammatory bone disease of the hand.",
+            "authors": [
+              "Liebling EJ",
+              "Sze RW",
+              "Behrens EM"
+            ],
+            "journal": "Pediatric rheumatology online journal",
+            "year": "2020",
+            "doi": "10.1186/s12969-020-00439-4",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://www.drugbank.ca/drugs/DB00126",
+      "type": "drugbank",
+      "label": "drugbank.ca — record source"
+    },
+    {
+      "url": "https://meshb.nlm.nih.gov/record/ui?ui=D001206",
+      "type": "other",
+      "label": "meshb.nlm.nih.gov — record source"
+    }
+  ],
+  "site": {
+    "id": "sonnet__P32",
+    "record_id": "P32_DB00126_MESH_D001206",
+    "run": "sonnet",
+    "run_label": "Sonnet (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/sonnet/outputs/P32.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/sonnet__P34.json b/web-revamp-mockup/data/records/sonnet__P34.json
new file mode 100644
index 0000000..4340ede
--- /dev/null
+++ b/web-revamp-mockup/data/records/sonnet__P34.json
@@ -0,0 +1,217 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P34_DB00004_MESH_D016410",
+    "drug": "Denileukin diftitox",
+    "drug_mesh": "MESH:C078456",
+    "drugbank": "DB:DB00004",
+    "disease": "Primary cutaneous T-cell lymphoma",
+    "disease_mesh": "MESH:D016410",
+    "summary": "Denileukin diftitox → Eukaryotic translation elongation factor 2 (EEF2) → translation → apoptotic process"
+  },
+  "nodes": [
+    {
+      "id": "MESH:C078456",
+      "name": "Denileukin diftitox",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P01589",
+      "name": "Interleukin-2 receptor subunit alpha (CD25)",
+      "label": "Protein"
+    },
+    {
+      "id": "UniProt:P13639",
+      "name": "Eukaryotic translation elongation factor 2 (EEF2)",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0006412",
+      "name": "translation",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "GO:0006915",
+      "name": "apoptotic process",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D016410",
+      "name": "Primary cutaneous T-cell lymphoma",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "MESH:C078456",
+      "target": "UniProt:P01589",
+      "evidence": [
+        {
+          "reference": "PMID:36047157",
+          "snippet": "DD binds to IL-2 receptor (IL-2R) expressed on tumor cells and is taken up into the cells.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "[Preclinical and clinical researches of Denileukin Diftitox (Genetical Recombination) (Remitoro®), a novel agent for T-cell lymphoma].",
+            "authors": [
+              "Shiiba H",
+              "Takechi A",
+              "Asakura S",
+              "Kawaguchi T",
+              "Sato M"
+            ],
+            "journal": "Nihon yakurigaku zasshi. Folia pharmacologica Japonica",
+            "year": "2022",
+            "doi": "10.1254/fpj.22032",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:11707818",
+          "snippet": "DAB(389)IL-2 is internalized into IL-2 receptor-bearing cells by endocytosis.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "DAB(389)IL-2 (ONTAK): a novel fusion toxin therapy for lymphoma.",
+            "authors": [
+              "Foss FM"
+            ],
+            "journal": "Clinical lymphoma",
+            "year": "2000",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:C078456",
+      "target": "UniProt:P13639",
+      "evidence": [
+        {
+          "reference": "PMID:19707452",
+          "snippet": "the internalized fragment A catalyzes the cleavage of nicotinamide adenine dinucleotide (NAD) to nicotinamide resulting in a transfer of ADP to elongation factor-2 (EF-2). This ADP-ribosylation of EF-2 causes inhibition of mRNA prolongation and ultimately inhibition of protein synthesis.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "source_tier": "FULL_TEXT",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Denileukin diftitox for the treatment of cutaneous T-cell lymphoma.",
+            "authors": [
+              "Kaminetzky D",
+              "Hymes KB"
+            ],
+            "journal": "Biologics : targets & therapy",
+            "year": "2008",
+            "doi": null,
+            "pmcid": "PMC2727893",
+            "license": null
+          }
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "decreased",
+      "source": "UniProt:P13639",
+      "target": "GO:0006412",
+      "evidence": [
+        {
+          "reference": "PMID:23853096",
+          "snippet": "ADP(R) of eEF2 resulted in a decrease in total protein synthesis consistent with a defect in translation elongation.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "ADP-ribosylation of translation elongation factor 2 by diphtheria toxin in yeast inhibits translation and cell separation.",
+            "authors": [
+              "Mateyak MK",
+              "Kinzy TG"
+            ],
+            "journal": "The Journal of biological chemistry",
+            "year": "2013",
+            "doi": "10.1074/jbc.M113.488783",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "decreased",
+      "source": "GO:0006412",
+      "target": "GO:0006915",
+      "evidence": [
+        {
+          "reference": "PMID:11707818",
+          "snippet": "The ADP-ribosyltransferase activity of diphtheria toxin is cleaved in the endosome and is translocated into the cytosol where it inhibits protein synthesis, leading to apoptosis.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "DAB(389)IL-2 (ONTAK): a novel fusion toxin therapy for lymphoma.",
+            "authors": [
+              "Foss FM"
+            ],
+            "journal": "Clinical lymphoma",
+            "year": "2000",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "treats",
+      "source": "MESH:C078456",
+      "target": "MESH:D016410",
+      "evidence": [
+        {
+          "reference": "PMID:19707452",
+          "snippet": "Denileukin diftitox (DD, Ontak(R)) is a targeted immunotoxin which has biological activity against malignancies expressing the IL-2 receptor. CTCL/MF has been found be particularly susceptible to treatment with this agent.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "source_tier": "FULL_TEXT",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Denileukin diftitox for the treatment of cutaneous T-cell lymphoma.",
+            "authors": [
+              "Kaminetzky D",
+              "Hymes KB"
+            ],
+            "journal": "Biologics : targets & therapy",
+            "year": "2008",
+            "doi": null,
+            "pmcid": "PMC2727893",
+            "license": null
+          }
+        }
+      ]
+    }
+  ],
+  "references": [],
+  "site": {
+    "id": "sonnet__P34",
+    "record_id": "P34_DB00004_MESH_D016410",
+    "run": "sonnet",
+    "run_label": "Sonnet (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/sonnet/outputs/P34.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/sonnet__P35.json b/web-revamp-mockup/data/records/sonnet__P35.json
new file mode 100644
index 0000000..c455da6
--- /dev/null
+++ b/web-revamp-mockup/data/records/sonnet__P35.json
@@ -0,0 +1,331 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P35_DB00008_MESH_D019698",
+    "drug": "Peginterferon alfa-2a",
+    "drug_mesh": "MESH:C100416",
+    "drugbank": "DB:DB00008",
+    "disease": "Chronic hepatitis C",
+    "disease_mesh": "MESH:D019698",
+    "summary": "Peginterferon alfa-2a → JAK1 → STAT1 → cellular response to interferon-beta → response to virus → Chronic hepatitis C"
+  },
+  "nodes": [
+    {
+      "id": "MESH:C100416",
+      "name": "Peginterferon alfa-2a",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P23458",
+      "name": "JAK1",
+      "label": "Protein"
+    },
+    {
+      "id": "UniProt:P29597",
+      "name": "TYK2",
+      "label": "Protein"
+    },
+    {
+      "id": "UniProt:P42224",
+      "name": "STAT1",
+      "label": "Protein"
+    },
+    {
+      "id": "UniProt:P52630",
+      "name": "STAT2",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0035458",
+      "name": "cellular response to interferon-beta",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "GO:0009615",
+      "name": "response to virus",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D019698",
+      "name": "Chronic hepatitis C",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "increased",
+      "source": "MESH:C100416",
+      "target": "UniProt:P23458",
+      "evidence": [
+        {
+          "reference": "PMID:16324217",
+          "snippet": "When IFN-alpha binds its receptor, two receptor associated tyrosine kinases, Tyk2 and Jak1 become activated by phosphorylation",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Peginterferon alfa-2a (an IFN-alpha) activates JAK1 through receptor engagement.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Effect of ethanol on innate antiviral pathways and HCV replication in human liver cells.",
+            "authors": [
+              "Plumlee CR",
+              "Lazaro CA",
+              "Fausto N",
+              "Polyak SJ"
+            ],
+            "journal": "Virology journal",
+            "year": "2005",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "increased",
+      "source": "MESH:C100416",
+      "target": "UniProt:P29597",
+      "evidence": [
+        {
+          "reference": "PMID:16324217",
+          "snippet": "When IFN-alpha binds its receptor, two receptor associated tyrosine kinases, Tyk2 and Jak1 become activated by phosphorylation",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Peginterferon alfa-2a (an IFN-alpha) activates TYK2 through receptor engagement.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Effect of ethanol on innate antiviral pathways and HCV replication in human liver cells.",
+            "authors": [
+              "Plumlee CR",
+              "Lazaro CA",
+              "Fausto N",
+              "Polyak SJ"
+            ],
+            "journal": "Virology journal",
+            "year": "2005",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P23458",
+      "target": "UniProt:P42224",
+      "evidence": [
+        {
+          "reference": "PMID:16324217",
+          "snippet": "Tyk2 and Jak1 become activated by phosphorylation, and phosphorylate Stat1 and Stat2 on conserved tyrosine residues",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Activated JAK1 phosphorylates STAT1 on conserved tyrosine residues.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Effect of ethanol on innate antiviral pathways and HCV replication in human liver cells.",
+            "authors": [
+              "Plumlee CR",
+              "Lazaro CA",
+              "Fausto N",
+              "Polyak SJ"
+            ],
+            "journal": "Virology journal",
+            "year": "2005",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P29597",
+      "target": "UniProt:P52630",
+      "evidence": [
+        {
+          "reference": "PMID:16324217",
+          "snippet": "Tyk2 and Jak1 become activated by phosphorylation, and phosphorylate Stat1 and Stat2 on conserved tyrosine residues",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Activated TYK2 phosphorylates STAT2 on conserved tyrosine residues.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Effect of ethanol on innate antiviral pathways and HCV replication in human liver cells.",
+            "authors": [
+              "Plumlee CR",
+              "Lazaro CA",
+              "Fausto N",
+              "Polyak SJ"
+            ],
+            "journal": "Virology journal",
+            "year": "2005",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P42224",
+      "target": "GO:0035458",
+      "evidence": [
+        {
+          "reference": "PMID:16324217",
+          "snippet": "Stat1 and Stat2 combine with the IRF-9 protein to form the transcription factor interferon stimulated gene factor 3 (ISGF-3), which binds to the interferon stimulated response element (ISRE), and induces transcription of IFN-alpha-induced genes (ISG)",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "STAT1 forms ISGF3 complex that drives interferon-stimulated gene transcription, representing the cellular response to interferon.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Effect of ethanol on innate antiviral pathways and HCV replication in human liver cells.",
+            "authors": [
+              "Plumlee CR",
+              "Lazaro CA",
+              "Fausto N",
+              "Polyak SJ"
+            ],
+            "journal": "Virology journal",
+            "year": "2005",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P52630",
+      "target": "GO:0035458",
+      "evidence": [
+        {
+          "reference": "PMID:16324217",
+          "snippet": "Stat1 and Stat2 combine with the IRF-9 protein to form the transcription factor interferon stimulated gene factor 3 (ISGF-3), which binds to the interferon stimulated response element (ISRE), and induces transcription of IFN-alpha-induced genes (ISG)",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "STAT2 forms ISGF3 complex that drives interferon-stimulated gene transcription, representing the cellular response to interferon.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Effect of ethanol on innate antiviral pathways and HCV replication in human liver cells.",
+            "authors": [
+              "Plumlee CR",
+              "Lazaro CA",
+              "Fausto N",
+              "Polyak SJ"
+            ],
+            "journal": "Virology journal",
+            "year": "2005",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "GO:0035458",
+      "target": "GO:0009615",
+      "evidence": [
+        {
+          "reference": "PMID:16108059",
+          "snippet": "Interferon (IFN) alpha inhibits hepatitis C virus (HCV) replication both clinically and in vitro",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "IFN-alpha-induced ISG expression (cellular interferon response) leads to an antiviral response against HCV.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Analysis of ISG expression in chronic hepatitis C identifies viperin as a potential antiviral effector.",
+            "authors": [
+              "Helbig KJ",
+              "Lau DT",
+              "Semendric L",
+              "Harley HA",
+              "Beard MR"
+            ],
+            "journal": "Hepatology (Baltimore, Md.)",
+            "year": "2005",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "decreased",
+      "source": "GO:0009615",
+      "target": "MESH:D019698",
+      "evidence": [
+        {
+          "reference": "PMID:16108059",
+          "snippet": "even in the face of a persistent HCV infection, there is an active ISG antiviral cellular response, highlighting the complexity of the host viral relationship",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Antiviral ISG-driven response limits HCV replication, reducing chronic hepatitis C.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Analysis of ISG expression in chronic hepatitis C identifies viperin as a potential antiviral effector.",
+            "authors": [
+              "Helbig KJ",
+              "Lau DT",
+              "Semendric L",
+              "Harley HA",
+              "Beard MR"
+            ],
+            "journal": "Hepatology (Baltimore, Md.)",
+            "year": "2005",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://www.drugbank.ca/drugs/DB00008",
+      "type": "drugbank",
+      "label": "drugbank.ca — record source"
+    },
+    {
+      "url": "https://pubchem.ncbi.nlm.nih.gov/compound/peginterferon-alfa-2a",
+      "type": "other",
+      "label": "pubchem.ncbi.nlm.nih.gov — record source"
+    }
+  ],
+  "site": {
+    "id": "sonnet__P35",
+    "record_id": "P35_DB00008_MESH_D019698",
+    "run": "sonnet",
+    "run_label": "Sonnet (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/sonnet/outputs/P35.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/sonnet__P36.json b/web-revamp-mockup/data/records/sonnet__P36.json
new file mode 100644
index 0000000..2a50094
--- /dev/null
+++ b/web-revamp-mockup/data/records/sonnet__P36.json
@@ -0,0 +1,258 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P36_DB00027_MESH_D003234",
+    "drug": "Gramicidin",
+    "drug_mesh": "MESH:D006096",
+    "drugbank": "DB:DB00027",
+    "disease": "Bacterial conjunctivitis",
+    "disease_mesh": "MESH:D003234",
+    "summary": "Gramicidin → Plasma membrane → Ion transport → Killing of cells of other organism → Bacterial conjunctivitis"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D006096",
+      "name": "Gramicidin",
+      "label": "Drug"
+    },
+    {
+      "id": "GO:0005886",
+      "name": "Plasma membrane",
+      "label": "CellularComponent"
+    },
+    {
+      "id": "GO:0006811",
+      "name": "Ion transport",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "GO:0031640",
+      "name": "Killing of cells of other organism",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D003234",
+      "name": "Bacterial conjunctivitis",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "disrupts",
+      "source": "MESH:D006096",
+      "target": "GO:0005886",
+      "evidence": [
+        {
+          "reference": "PMID:35872830",
+          "snippet": "1 folds into a β6.3-helix in a lipid bilayer and forms a head-to-head dimer to function as a transmembrane channel for monovalent cations (H+, Na+, and K+)",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Gramicidin A inserts into the lipid bilayer and forms transmembrane ion channels, thereby disrupting the plasma membrane barrier function.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Gramicidin A accumulates in mitochondria, reduces ATP levels, induces mitophagy, and inhibits cancer cell growth.",
+            "authors": [
+              "Xue YW",
+              "Itoh H",
+              "Dan S",
+              "Inoue M"
+            ],
+            "journal": "Chemical science",
+            "year": "2022",
+            "doi": "10.1039/d2sc02024f",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:29501941",
+          "snippet": "upon insertion into membranes, it forms channels that disrupts ion gradients",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Design, synthesis, and biological evaluation of stable β6.3-Helices: Discovery of non-hemolytic antibacterial peptides.",
+            "authors": [
+              "Reddy DN",
+              "Singh S",
+              "Ho CMW",
+              "Patel J",
+              "Schlesinger P",
+              "Rodgers S",
+              "Doctor A",
+              "Marshall GR"
+            ],
+            "journal": "European journal of medicinal chemistry",
+            "year": "2018",
+            "doi": "10.1016/j.ejmech.2018.02.057",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "participates in",
+      "source": "GO:0005886",
+      "target": "GO:0006811",
+      "evidence": [
+        {
+          "reference": "PMID:35872830",
+          "snippet": "Compound 1 not only disrupted the ion concentration gradients of the plasma membrane",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "The gramicidin-permeabilized plasma membrane participates in aberrant ion transport; monovalent cations flow freely through gramicidin channels, dissipating normal ion concentration gradients.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Gramicidin A accumulates in mitochondria, reduces ATP levels, induces mitophagy, and inhibits cancer cell growth.",
+            "authors": [
+              "Xue YW",
+              "Itoh H",
+              "Dan S",
+              "Inoue M"
+            ],
+            "journal": "Chemical science",
+            "year": "2022",
+            "doi": "10.1039/d2sc02024f",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "causes",
+      "source": "GO:0006811",
+      "target": "GO:0031640",
+      "evidence": [
+        {
+          "reference": "PMID:24356337",
+          "snippet": "Changes in the conductance of membranes for ions will lead to cell death",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "pH dependent transfer of nano-pores into membrane of cancer cells to induce apoptosis.",
+            "authors": [
+              "Wijesinghe D",
+              "Arachchige MC",
+              "Lu A",
+              "Reshetnyak YK",
+              "Andreev OA"
+            ],
+            "journal": "Scientific reports",
+            "year": "2013",
+            "doi": "10.1038/srep03560",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:24356337",
+          "snippet": "Gramicidin channels inserted into the cancer cells open flux of protons into the cytoplasm and disrupt balance of other monovalent cations, which induces cell apoptosis",
+          "supports": "PARTIAL",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Gramicidin-mediated uncontrolled ion transport through the membrane causes cell death. Evidence shown in cancer cells but the ion-channel-disruption mechanism applies to bacterial cells.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "pH dependent transfer of nano-pores into membrane of cancer cells to induce apoptosis.",
+            "authors": [
+              "Wijesinghe D",
+              "Arachchige MC",
+              "Lu A",
+              "Reshetnyak YK",
+              "Andreev OA"
+            ],
+            "journal": "Scientific reports",
+            "year": "2013",
+            "doi": "10.1038/srep03560",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "treats",
+      "source": "GO:0031640",
+      "target": "MESH:D003234",
+      "evidence": [
+        {
+          "reference": "PMID:12429243",
+          "snippet": "Povidone-iodine 1.25% ophthalmic solution was as effective as neomycin-polymyxin B-gramicidin for treating bacterial conjunctivitis",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Gramicidin-containing ophthalmic solution treats bacterial conjunctivitis in a controlled clinical trial; the killing of bacteria by gramicidin underlies this therapeutic effect.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "A controlled trial of povidone-iodine to treat infectious conjunctivitis in children.",
+            "authors": [
+              "Isenberg SJ",
+              "Apt L",
+              "Valenton M",
+              "Del Signore M",
+              "Cubillan L",
+              "Labrador MA",
+              "Chan P",
+              "Berman NG"
+            ],
+            "journal": "American journal of ophthalmology",
+            "year": "2002",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:20084257",
+          "snippet": "Good choices include polymyxin/gramicidin, polymyxin/trimethoprim or sulfacetamide",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Clinical review identifies polymyxin/gramicidin as a recommended first-line agent for bacterial conjunctivitis in children.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Acute infectious conjunctivitis in childhood.",
+            "authors": [
+              "Chawla R",
+              "Kellner JD",
+              "Astle WF"
+            ],
+            "journal": "Paediatrics & child health",
+            "year": "2001",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://www.drugbank.ca/drugs/DB00027",
+      "type": "drugbank",
+      "label": "drugbank.ca — record source"
+    },
+    {
+      "url": "https://meshb.nlm.nih.gov/record/ui?ui=D006096",
+      "type": "other",
+      "label": "meshb.nlm.nih.gov — record source"
+    }
+  ],
+  "site": {
+    "id": "sonnet__P36",
+    "record_id": "P36_DB00027_MESH_D003234",
+    "run": "sonnet",
+    "run_label": "Sonnet (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/sonnet/outputs/P36.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/sonnet__P37.json b/web-revamp-mockup/data/records/sonnet__P37.json
new file mode 100644
index 0000000..2ffe9f1
--- /dev/null
+++ b/web-revamp-mockup/data/records/sonnet__P37.json
@@ -0,0 +1,172 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P37_DB00186_MESH_D001007",
+    "drug": "Lorazepam",
+    "drug_mesh": "MESH:D008140",
+    "drugbank": "DB:DB00186",
+    "disease": "Anxiety",
+    "disease_mesh": "MESH:D001007",
+    "summary": "Lorazepam → Gamma-aminobutyric acid receptor subunit alpha-1 → chloride channel activity → membrane hyperpolarization → Anxiety"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D008140",
+      "name": "Lorazepam",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P14867",
+      "name": "Gamma-aminobutyric acid receptor subunit alpha-1",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0005254",
+      "name": "chloride channel activity",
+      "label": "MolecularActivity"
+    },
+    {
+      "id": "GO:0060081",
+      "name": "membrane hyperpolarization",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D001007",
+      "name": "Anxiety",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "increased",
+      "source": "MESH:D008140",
+      "target": "UniProt:P14867",
+      "evidence": [
+        {
+          "reference": "PMID:12805666",
+          "snippet": "Benzodiazepines bind to a site on the GABA(A) receptor which is different from the GABA binding site, thus increasing the chloride current.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Lorazepam is a benzodiazepine that binds allosterically to the GABA-A receptor and increases its activity (chloride current).",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Identification of molecular substrate for the attenuation of anxiety: a step toward the development of better anti-anxiety drugs.",
+            "authors": [
+              "Rudolph U"
+            ],
+            "journal": "TheScientificWorldJournal",
+            "year": "2001",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P14867",
+      "target": "GO:0005254",
+      "evidence": [
+        {
+          "reference": "PMID:12805666",
+          "snippet": "Synaptically released GABA binds to postsynaptic GABAA receptors, thus causing an influx of negatively charged chloride ions into the postsynaptic neuron.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "GABA-A receptor activation increases chloride ion influx through the receptor's integral chloride channel.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Identification of molecular substrate for the attenuation of anxiety: a step toward the development of better anti-anxiety drugs.",
+            "authors": [
+              "Rudolph U"
+            ],
+            "journal": "TheScientificWorldJournal",
+            "year": "2001",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "causes",
+      "source": "GO:0005254",
+      "target": "GO:0060081",
+      "evidence": [
+        {
+          "reference": "PMID:12805666",
+          "snippet": "This leads to a hyperpolarization and thus functional inhibition of the postsynaptic cell.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "explanation": "Chloride influx through the GABA-A channel causes membrane hyperpolarization of the postsynaptic neuron.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Identification of molecular substrate for the attenuation of anxiety: a step toward the development of better anti-anxiety drugs.",
+            "authors": [
+              "Rudolph U"
+            ],
+            "journal": "TheScientificWorldJournal",
+            "year": "2001",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "decreased",
+      "source": "GO:0060081",
+      "target": "MESH:D001007",
+      "evidence": [
+        {
+          "reference": "PMID:29628509",
+          "snippet": "Inhibitory neurotransmission plays a key role in anxiety disorders, as evidenced by the anxiolytic effect of the benzodiazepine class of γ-aminobutyric acid (GABA) receptor agonists",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Membrane hyperpolarization (inhibitory neurotransmission) via GABA-A receptor activation reduces anxiety.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Inhibition in the amygdala anxiety circuitry.",
+            "authors": [
+              "Babaev O",
+              "Piletti Chatain C",
+              "Krueger-Burg D"
+            ],
+            "journal": "Experimental & molecular medicine",
+            "year": "2018",
+            "doi": "10.1038/s12276-018-0063-8",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://www.drugbank.ca/drugs/DB00186",
+      "type": "drugbank",
+      "label": "drugbank.ca — record source"
+    }
+  ],
+  "site": {
+    "id": "sonnet__P37",
+    "record_id": "P37_DB00186_MESH_D001007",
+    "run": "sonnet",
+    "run_label": "Sonnet (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/sonnet/outputs/P37.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/sonnet__P38.json b/web-revamp-mockup/data/records/sonnet__P38.json
new file mode 100644
index 0000000..a344c4c
--- /dev/null
+++ b/web-revamp-mockup/data/records/sonnet__P38.json
@@ -0,0 +1,244 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P38_DB00175_MESH_D006937",
+    "drug": "Pravastatin",
+    "drug_mesh": "MESH:D017035",
+    "drugbank": "DB:DB00175",
+    "disease": "Hypercholesterolemia",
+    "disease_mesh": "MESH:D006937",
+    "summary": "Pravastatin → HMG-CoA reductase → cholesterol biosynthetic process → LDL receptor → Lipoproteins, LDL → Hypercholesterolemia"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D017035",
+      "name": "Pravastatin",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P04035",
+      "name": "HMG-CoA reductase",
+      "label": "Protein"
+    },
+    {
+      "id": "GO:0006695",
+      "name": "cholesterol biosynthetic process",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "UniProt:P01130",
+      "name": "LDL receptor",
+      "label": "Protein"
+    },
+    {
+      "id": "MESH:D008077",
+      "name": "Lipoproteins, LDL",
+      "label": "ChemicalSubstance"
+    },
+    {
+      "id": "MESH:D006937",
+      "name": "Hypercholesterolemia",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D017035",
+      "target": "UniProt:P04035",
+      "evidence": [
+        {
+          "reference": "PMID:14651445",
+          "snippet": "Pravastatin (Pravachol) is a competitive, reversible HMG-CoA reductase inhibitor that lowers serum cholesterol levels by inhibiting de novo cholesterol synthesis",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Pravastatin: a review of its use in elderly patients.",
+            "authors": [
+              "Bang LM",
+              "Goa KL"
+            ],
+            "journal": "Drugs & aging",
+            "year": "2003",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        },
+        {
+          "reference": "PMID:1298545",
+          "snippet": "Pravastatin is a new drug that inhibits 3-hydroxy-3-methylglutaryl-coenzyme A reductase, the key enzyme in cholesterol synthesis.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "[Evaluation of the therapeutic efficacy of pravastatin in monothereapy and in association with gemfibrozil in hypercholesterolemia associated with moderate hyperglyceridemia].",
+            "authors": [
+              "Napoli C",
+              "Lepore S",
+              "Ambrosio G",
+              "Chiariello M"
+            ],
+            "journal": "Cardiologia (Rome, Italy)",
+            "year": "1992",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "participates in",
+      "source": "UniProt:P04035",
+      "target": "GO:0006695",
+      "evidence": [
+        {
+          "reference": "PMID:34207840",
+          "snippet": "Statins have been widely used for the treatment of hypercholesterolemia due to their ability to inhibit HMG-CoA reductase, the rate-limiting enzyme of de novo cholesterol synthesis, via the so-called mevalonate pathway.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Comparison of Transcriptomic Profiles of MiaPaCa-2 Pancreatic Cancer Cells Treated with Different Statins.",
+            "authors": [
+              "Rimpelová S",
+              "Kolář M",
+              "Strnad H",
+              "Ruml T",
+              "Vítek L",
+              "Gbelcová H"
+            ],
+            "journal": "Molecules (Basel, Switzerland)",
+            "year": "2021",
+            "doi": "10.3390/molecules26123528",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "decreased",
+      "source": "GO:0006695",
+      "target": "UniProt:P01130",
+      "evidence": [
+        {
+          "reference": "PMID:1298545",
+          "snippet": "It prevents mevalonate synthesis, thus reducing cholesterol. Pravastatin also stimulates the expression of LDL receptors, leading to an activation of this specific pathway of LDL catabolism.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Inhibition of cholesterol biosynthesis (via reduced mevalonate synthesis) is linked to upregulation of LDL receptor expression, consistent with the negative feedback relationship between intracellular cholesterol levels and LDLR expression.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "[Evaluation of the therapeutic efficacy of pravastatin in monothereapy and in association with gemfibrozil in hypercholesterolemia associated with moderate hyperglyceridemia].",
+            "authors": [
+              "Napoli C",
+              "Lepore S",
+              "Ambrosio G",
+              "Chiariello M"
+            ],
+            "journal": "Cardiologia (Rome, Italy)",
+            "year": "1992",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "decreased",
+      "source": "UniProt:P01130",
+      "target": "MESH:D008077",
+      "evidence": [
+        {
+          "reference": "PMID:30953636",
+          "snippet": "LDL clearance involves binding to its receptor, LDLR, which enables the internalization of the LDL particle and drives its degradation in lysosomes.",
+          "supports": "SUPPORT",
+          "evidence_source": "OTHER",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Keep recycling going: New approaches to reduce LDL-C.",
+            "authors": [
+              "Klein-Szanto AJP",
+              "Bassi DE"
+            ],
+            "journal": "Biochemical pharmacology",
+            "year": "2019",
+            "doi": "10.1016/j.bcp.2019.04.003",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "causes",
+      "source": "MESH:D008077",
+      "target": "MESH:D006937",
+      "evidence": [
+        {
+          "reference": "PMID:42034477",
+          "snippet": "Patients with severe hypercholesterolemia (SH), defined as low-density lipoprotein cholesterol (LDL-C) ≥190 mg/dL, have elevated cardiovascular risk",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "explanation": "Hypercholesterolemia is defined by elevated LDL-C levels; elevated LDL is both definitional and causative of hypercholesterolemia.",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Identifying severe hypercholesterolemia in participants of ASCVD trials: Implications for trial conduct and opportunistic screening.",
+            "authors": [
+              "Singh A",
+              "John JS",
+              "Laffin L",
+              "Knowles JW",
+              "Rodriguez F",
+              "Skoza W",
+              "Bruemmer D",
+              "Cho L",
+              "Nissen SE",
+              "Sarraju A"
+            ],
+            "journal": "Journal of clinical lipidology",
+            "year": "2026",
+            "doi": "10.1016/j.jacl.2026.03.018",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://go.drugbank.com/drugs/DB00175",
+      "type": "drugbank",
+      "label": "go.drugbank.com — record source"
+    },
+    {
+      "url": "https://meshb.nlm.nih.gov/record/ui?ui=D006937",
+      "type": "other",
+      "label": "meshb.nlm.nih.gov — record source"
+    }
+  ],
+  "site": {
+    "id": "sonnet__P38",
+    "record_id": "P38_DB00175_MESH_D006937",
+    "run": "sonnet",
+    "run_label": "Sonnet (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/sonnet/outputs/P38.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/data/records/sonnet__P40.json b/web-revamp-mockup/data/records/sonnet__P40.json
new file mode 100644
index 0000000..8520812
--- /dev/null
+++ b/web-revamp-mockup/data/records/sonnet__P40.json
@@ -0,0 +1,214 @@
+{
+  "directed": true,
+  "multigraph": true,
+  "graph": {
+    "_id": "P40_DB00043_MESH_D001249",
+    "drug": "Omalizumab",
+    "drug_mesh": "MESH:D000069444",
+    "drugbank": "DB:DB00043",
+    "disease": "Asthma",
+    "disease_mesh": "MESH:D001249",
+    "summary": "Omalizumab → Immunoglobulin E → High affinity immunoglobulin epsilon receptor subunit alpha → Mast cell degranulation → Mast cell"
+  },
+  "nodes": [
+    {
+      "id": "MESH:D000069444",
+      "name": "Omalizumab",
+      "label": "Drug"
+    },
+    {
+      "id": "UniProt:P01854",
+      "name": "Immunoglobulin E",
+      "label": "Protein"
+    },
+    {
+      "id": "UniProt:P12319",
+      "name": "High affinity immunoglobulin epsilon receptor subunit alpha",
+      "label": "Protein"
+    },
+    {
+      "id": "CL:0000097",
+      "name": "Mast cell",
+      "label": "Cell"
+    },
+    {
+      "id": "GO:0043303",
+      "name": "Mast cell degranulation",
+      "label": "BiologicalProcess"
+    },
+    {
+      "id": "MESH:D001249",
+      "name": "Asthma",
+      "label": "Disease"
+    }
+  ],
+  "links": [
+    {
+      "key": "affects",
+      "object_aspect_qualifier": "activity",
+      "object_direction_qualifier": "decreased",
+      "source": "MESH:D000069444",
+      "target": "UniProt:P01854",
+      "evidence": [
+        {
+          "reference": "PMID:16464445",
+          "snippet": "This non-anaphylactogenic anti-IgE monoclonal antibody (omalizumab) binds IgE at the same site as these antibodies bind FcepsilonRI and FcepsilonRII. Consequently, omalizumab inhibits IgE effector functions by blocking IgE binding to high-affinity receptors on IgE effector cells.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Role of anti-IgE monoclonal antibody (omalizumab) in the treatment of bronchial asthma and allergic respiratory diseases.",
+            "authors": [
+              "D'Amato G"
+            ],
+            "journal": "European journal of pharmacology",
+            "year": "2006",
+            "doi": null,
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P01854",
+      "target": "UniProt:P12319",
+      "evidence": [
+        {
+          "reference": "PMID:30069035",
+          "snippet": "interaction with FcεRI on mast cells and basophils leads to immediate hypersensitivity reactions upon allergen challenge",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Structural basis for selective inhibition of immunoglobulin E-receptor interactions by an anti-IgE antibody.",
+            "authors": [
+              "Chen JB",
+              "Ramadani F",
+              "Pang MOY",
+              "Beavil RL",
+              "Holdom MD",
+              "Mitropoulou AN",
+              "Beavil AJ",
+              "Gould HJ",
+              "Chang TW",
+              "Sutton BJ",
+              "McDonnell JM",
+              "Davies AM"
+            ],
+            "journal": "Scientific reports",
+            "year": "2018",
+            "doi": "10.1038/s41598-018-29664-4",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "regulates",
+      "object_direction_qualifier": "increased",
+      "source": "UniProt:P12319",
+      "target": "GO:0043303",
+      "evidence": [
+        {
+          "reference": "PMID:26206871",
+          "snippet": "IgE on mast cells is cross-linked by an allergen, causing degranulation and the release of histamine, neutral proteases and chemotactic factors, and the production of newly formed mediators, such as cysteinyl leukotrienes and prostaglandin D2.",
+          "supports": "SUPPORT",
+          "evidence_source": "HUMAN_CLINICAL",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Allergen-induced airway responses.",
+            "authors": [
+              "Gauvreau GM",
+              "El-Gammal AI",
+              "O'Byrne PM"
+            ],
+            "journal": "The European respiratory journal",
+            "year": "2015",
+            "doi": "10.1183/13993003.00536-2015",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "occurs in",
+      "source": "GO:0043303",
+      "target": "CL:0000097",
+      "evidence": [
+        {
+          "reference": "PMID:39051334",
+          "snippet": "These cells display IgE on their surface, bound to the high-affinity IgE receptor FcεRI. A cross-linking antigen then triggers degranulation and the release of inflammatory mediators from the cells.",
+          "supports": "SUPPORT",
+          "evidence_source": "IN_VITRO",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "A Comparison of Natural and Therapeutic Anti-IgE Antibodies.",
+            "authors": [
+              "Vogel M",
+              "Engeroff P"
+            ],
+            "journal": "Antibodies (Basel, Switzerland)",
+            "year": "2024",
+            "doi": "10.3390/antib13030058",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    },
+    {
+      "key": "contributes to",
+      "source": "GO:0043303",
+      "target": "MESH:D001249",
+      "evidence": [
+        {
+          "reference": "PMID:38790633",
+          "snippet": "Mast cell activation influences the pathogenesis and exacerbation of allergic asthma.",
+          "supports": "SUPPORT",
+          "evidence_source": "MODEL_ORGANISM",
+          "source_type": "pubmed",
+          "paper": {
+            "title": "Hispidulin Alleviates Mast Cell-Mediated Allergic Airway Inflammation through FcεR1 and Nrf2/HO-1 Signaling Pathway.",
+            "authors": [
+              "Jeong S",
+              "Kim YY",
+              "Lee D",
+              "Kim SH",
+              "Lee S"
+            ],
+            "journal": "Antioxidants (Basel, Switzerland)",
+            "year": "2024",
+            "doi": "10.3390/antiox13050528",
+            "pmcid": null,
+            "license": null
+          },
+          "source_tier": "ABSTRACT"
+        }
+      ]
+    }
+  ],
+  "references": [
+    {
+      "url": "https://www.drugbank.ca/drugs/DB00043",
+      "type": "drugbank",
+      "label": "drugbank.ca — record source"
+    }
+  ],
+  "site": {
+    "id": "sonnet__P40",
+    "record_id": "P40_DB00043_MESH_D001249",
+    "run": "sonnet",
+    "run_label": "Sonnet (model eval)",
+    "source_file": "experiments/opus_vs_sonnet/sonnet/outputs/P40.yaml",
+    "summary_generated": true
+  }
+}
diff --git a/web-revamp-mockup/dmdb-data.js b/web-revamp-mockup/dmdb-data.js
index 96277a7..2437082 100644
--- a/web-revamp-mockup/dmdb-data.js
+++ b/web-revamp-mockup/dmdb-data.js
@@ -27,7 +27,9 @@
   "use strict";
 
   // ── THE SWAP POINT ──────────────────────────────────────────────────────────
-  const SOURCE = "sample";               // "sample" (bundled data.js) | "live" (fetch JSON)
+  const SOURCE = "live";                 // "sample" (bundled data.js) | "live" (fetch JSON)
+  // LIVE: data/ is built from the agentic curation runs by
+  // scripts/build_site_data.py (135 records across 4 runs). Re-run it after a curation.
   const ENDPOINTS = {
     index:     "data/index.json",
     record:    (id) => `data/records/${encodeURIComponent(id)}.json`,
@@ -112,7 +114,14 @@
       return SOURCE === "live" ? fetchJSON(ENDPOINTS.index) : (window.DMDB_INDEX || []);
     },
     async getRecord(id) {
-      if (SOURCE === "live") return fetchJSON(ENDPOINTS.record(id));
+      if (SOURCE === "live") {
+        if (!id) {                                     // no ?id= -> first index row
+          const idx = await fetchJSON(ENDPOINTS.index);
+          if (!idx.length) throw new Error("DMDB: index.json is empty");
+          id = idx[0].id;
+        }
+        return fetchJSON(ENDPOINTS.record(id));
+      }
       const r = window.DMDB_RECORD || null;                 // sample ships a single record
       return (r && id && r.graph && r.graph._id !== id) ? r : r;
     },
diff --git a/web-revamp-mockup/pathograph.js b/web-revamp-mockup/pathograph.js
index c8df951..935e620 100644
--- a/web-revamp-mockup/pathograph.js
+++ b/web-revamp-mockup/pathograph.js
@@ -19,12 +19,27 @@ function el(tag, attrs={}) {
   for (const k in attrs) e.setAttribute(k, attrs[k]);
   return e;
 }
-function edgeDir(key) {
-  const k = key.toLowerCase();
+/* Biolink 4.4.4 carries an edge's polarity in object_direction_qualifier rather than in
+   the predicate name (`affects`/`regulates` are neutral words), so read the qualifier
+   first and fall back to the name for legacy-vocabulary edges. */
+const EDGE_DIR_SIGN = {increased: "pos", upregulated: "pos", decreased: "neg", downregulated: "neg"};
+function edgeDir(edge) {
+  if (edge && typeof edge === "object") {
+    const q = EDGE_DIR_SIGN[edge.object_direction_qualifier];
+    if (q) return q;
+  }
+  const k = String(edge && typeof edge === "object" ? edge.key : edge).toLowerCase();
   if (/(decrease|inhibit|negativ|down|block|disrupt|suppress|antagon)/.test(k)) return "neg";
   if (/(increase|positiv|activat|\bup\b|stimulat|induc|agonist|correlated)/.test(k)) return "pos";
   return "neutral";
 }
+/* Predicate with its qualifiers: `affects` -> `affects activity (decreased)`. */
+function edgeLabel(edge) {
+  const bits = [edge.key];
+  if (edge.object_aspect_qualifier) bits.push(edge.object_aspect_qualifier.replace(/_/g, " "));
+  if (edge.object_direction_qualifier) bits.push(`(${edge.object_direction_qualifier})`);
+  return bits.join(" ");
+}
 function wrap(name, max) {
   const words = name.split(" "); const lines = []; let cur = "";
   for (const w of words) {
@@ -100,18 +115,18 @@ function renderPathograph(containerId, record, onNodeClick) {
     const s = layout[l.source], t = layout[l.target];
     if (!s || !t) return;
     const x1 = s.x + s.w, y1 = s.y + s.h / 2, x2 = t.x, y2 = t.y + t.h / 2, dx = (x2 - x1) * 0.5;
-    const dir = edgeDir(l.key);
+    const dir = edgeDir(l);
     const p = el("path", {
       d: `M${x1},${y1} C${x1 + dx},${y1} ${x2 - dx},${y2} ${x2},${y2}`,
       class: "gedge " + dir, "marker-end": `url(#arw-${dir})`
     });
-    p.addEventListener("mouseenter", e => showTip(e, `<div class="tt-name">${byId[l.source].name}</div><div>${l.key}</div><div class="tt-name" style="margin-top:4px">${byId[l.target].name}</div>`));
+    p.addEventListener("mouseenter", e => showTip(e, `<div class="tt-name">${byId[l.source].name}</div><div>${edgeLabel(l)}</div><div class="tt-name" style="margin-top:4px">${byId[l.target].name}</div>`));
     p.addEventListener("mousemove", moveTip);
     p.addEventListener("mouseleave", hideTip);
     edgeLayer.appendChild(p);
     edgeEls.push({ p, s: l.source, t: l.target });
 
-    const key = rank[l.source] + ">" + rank[l.target] + "::" + l.key;
+    const key = rank[l.source] + ">" + rank[l.target] + "::" + edgeLabel(l);
     const g = groups[key] || (groups[key] = { key: l.key, dir, mx: [], my: [], ids: new Set() });
     g.mx.push((x1 + x2) / 2); g.my.push((y1 + y2) / 2); g.ids.add(l.source); g.ids.add(l.target);
   });
diff --git a/web-revamp-mockup/record.html b/web-revamp-mockup/record.html
index 23283ae..832c3e1 100644
--- a/web-revamp-mockup/record.html
+++ b/web-revamp-mockup/record.html
@@ -7,7 +7,7 @@
 <link rel="stylesheet" href="styles.css?v=6">
 </head>
 <body>
-<div class="mock-banner">MOCKUP · DrugMechDB website revamp · sample data, not final — for design review</div>
+<div class="mock-banner">LIVE · AI-curated record from an agentic curation run · site design still a mockup</div>
 
 <nav class="nav"><div class="container nav-inner">
   <a class="brand" href="index.html"><span class="mark">D</span>DrugMech<span class="tail">DB</span></a>
@@ -111,13 +111,29 @@
 /* Read through the DMDB data adapter — the single swap-point for real data.
    Wrapped in an async IIFE so live mode (fetch) works with no page changes. */
 (async () => {
-const R = await window.DMDB.getRecord();
+const R = await window.DMDB.getRecord(new URLSearchParams(location.search).get("id"));
 const byId = {};
 R.nodes.forEach(n => byId[n.id] = n);
 
-function dir(key){const k=key.toLowerCase();
+/* Since Biolink 4.4.4 an edge's polarity lives in object_direction_qualifier, not in the
+   predicate name — `affects` and `regulates` are neutral words. Read the qualifier first
+   and fall back to the name for legacy-vocabulary edges. */
+const DIR_SIGN = {increased:"pos", upregulated:"pos", decreased:"neg", downregulated:"neg"};
+function dir(edge){
+  if(typeof edge === "object" && edge){
+    const q = DIR_SIGN[edge.object_direction_qualifier];
+    if(q) return q;
+  }
+  const k = String(typeof edge === "object" && edge ? edge.key : edge).toLowerCase();
   if(/(decrease|inhibit|negativ|block|disrupt|suppress|antagon)/.test(k))return"neg";
   if(/(increase|positiv|stimulat|induc|agonist|correlated|activat)/.test(k))return"pos";return"";}
+/* Render the predicate with its qualifiers: `affects` -> `affects activity (decreased)`. */
+function predLabel(edge){
+  const bits = [edge.key];
+  if(edge.object_aspect_qualifier) bits.push(edge.object_aspect_qualifier.replace(/_/g," "));
+  if(edge.object_direction_qualifier) bits.push(`(${edge.object_direction_qualifier})`);
+  return bits.join(" ");
+}
 function curieUrl(id){return "https://identifiers.org/"+id;}
 
 // header
@@ -125,8 +141,9 @@
 $("t-disease").textContent = R.graph.disease;
 $("summary").textContent = R.graph.summary;
 $("ids").innerHTML = [
-  ["DrugBank", R.graph.drugbank],["Drug MeSH", R.graph.drug_mesh],["Disease MeSH", R.graph.disease_mesh],["Path ID", R.graph._id]
-].map(([k,v])=>`<span class="badge">${k} <span class="mono">${v}</span></span>`).join("");
+  ["DrugBank", R.graph.drugbank],["Drug MeSH", R.graph.drug_mesh],["Disease MeSH", R.graph.disease_mesh],["Path ID", R.graph._id],
+  ...(R.site ? [["Curation run", R.site.run_label]] : [])
+].filter(([,v]) => v).map(([k,v])=>`<span class="badge">${k} <span class="mono">${v}</span></span>`).join("");
 
 // stats
 function longestPath(R){
@@ -167,9 +184,9 @@
 // relationships
 $("rcount").textContent = R.links.length;
 $("rels").innerHTML = R.links.map(l=>{
-  const d = dir(l.key);
+  const d = dir(l);
   return `<div class="rel"><span class="subj">${byId[l.source].name}</span>
-    <span class="pred ${d}">${l.key}</span>
+    <span class="pred ${d}">${predLabel(l)}</span>
     <span class="obj">${byId[l.target].name}</span></div>`;
 }).join("");
 
@@ -223,7 +240,7 @@
   const items = l.evidence;
   const flagged = items.some(it => it.supports && it.supports!=="SUPPORT");
   return `<details class="ev"${flagged?' data-flag="1"':''}><summary><span class="caret">▸</span>
-    <span class="ev-edge">${byId[l.source].name} <span class="pred ${dir(l.key)}">${l.key}</span> ${byId[l.target].name}</span>
+    <span class="ev-edge">${byId[l.source].name} <span class="pred ${dir(l)}">${predLabel(l)}</span> ${byId[l.target].name}</span>
     <span class="ev-count">${items.length} ref${items.length>1?"s":""}${flagged?" · ⚑ flagged":""}</span></summary>
     <div class="ev-body">${items.map(evItem).join("")}</div></details>`;
 }).join("") : `<p style="padding:0;color:var(--muted)">This legacy record carries record-level sources (below). Per-edge evidence is added during AI re-curation.</p>`;