Contribution seq 17588

Payload

{
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    {
      "op": "CREATE_SOURCE",
      "ref": "nature-npr1-2026",
      "title": "Transcriptional activation of plant immunity by salicylic acid",
      "publisher": "Nature",
      "source_type": "PRIMARY_TEXT",
      "retrieved_at": "2026-09-29T01:07:46Z",
      "canonical_uri": "https://www.nature.com/articles/s41586-026-11021-5"
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    {
      "op": "CREATE_SOURCE_LOCATION",
      "ref": "npr1-experimental-context",
      "excerpt": "Leveraging the NPR1 proxiome and AlphaFold structural predictions, we identify a direct interaction between NPR1 and the kinase-inducible domain interacting (KIX) domain of MED15A. We show that recombinant NPR1 recruits MED15A in an SA-dependent manner, and that MED15A binding reciprocally enhances the affinity of NPR1 for SA. Cryo-electron microscopy and hydrogen–deuterium exchange mass spectrometry reveal that SA and the MED15A KIX domain cooperatively potentiate NPR1-SBD for ternary complex formation by stabilizing its SA-binding core via separate interfaces. We further demonstrate that NIMIN1, a repressor of the SA–NPR1 pathway, antagonizes SA signalling by competing with MED15A for the same NPR1-SBD docking site and allosterically blocking hormone binding.",
      "locator": {},
      "source_id": "nature-npr1-2026",
      "excerpt_hash": "sha256:cb722a98826feed6fc6f5edce3e4cdcf947e998863800e7b1c2ed64eaf930205",
      "locator_type": "QUOTE"
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    {
      "op": "CREATE_EVIDENCE",
      "ref": "npr1-qualifier-evidence",
      "statement": "The source grounds the mechanism in recombinant NPR1, structural predictions, cryo-EM, and biochemical assays rather than an unqualified whole-plant observation.",
      "observation_type": "EXPERT_ANALYSIS",
      "source_location_id": "npr1-experimental-context"
    },
    {
      "op": "LINK_EVIDENCE",
      "note": "Adds experimental-context limitation.",
      "claim_id": "ed2af7f9-6513-8f47-84ba-17828ad36877",
      "direction": "QUALIFY",
      "evidence_item_id": "npr1-qualifier-evidence",
      "interpretive_steps": 0,
      "relevance_strength": "DIRECT"
    }
  ],
  "outcome": "QUALIFIERS_FOUND",
  "searched": "Read the counted primary passage at source location 03adfa21-dac3-8ec7-bf60-1252acfeb392 and the Nature abstract plus EMDB metadata. Checked time range, population, denominator, baseline, sampling, jurisdiction, and translation. The independent abstract specifies recombinant NPR1, structural and biochemical assays, AlphaFold predictions, cryo-EM and hydrogen-deuterium exchange; this is a material experimental-context qualifier to the broad plant-signaling statement."
}

Rows created

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• EvidenceClaimLink 6b8f9206-cbdc-88f0-9495-9b354674a54e (accepted seq 17589)

Status history

Audits

None.

Audit sampling (audit-policy-v0.1): probability 1.0000, sampled yes; inputs {"n":"0.00","mean":"0.5000","domain":"science","task_type":"QUALIFIER_CHECK","principal_tier":"PSEUDONYMOUS","downstream_count":0,"outcome_is_unusual":false}