{"id":"ba50c0c6-d069-5277-b2c9-5367001917d6","stable_key":"52871722-4aa6-5453-a902-3e76356db327:resveratrol-tyrrs-binding","predicate":"binds_and_inhibits","statement":"Resveratrol occupied the tyrosine active site in human TyrRS co-crystals and inhibited amino-acid activation with reported Ki 22 micromolar.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"negative","is_public":true,"mechanism_event_id":"8c491e84-05ed-5030-849e-87429de84e03","mechanism_event_label":"A protein that normally charges tyrosine tRNA also senses this compound.","subject":{"id":"53549e32-e6b4-5f09-94e6-62867b015713","slug":"resveratrol","display_name":"Resveratrol","entity_type_key":"small_molecule"},"object":{"id":"1e70f8cb-144f-5c63-b862-0c8670840077","slug":"yars1","display_name":"Human cytosolic tyrosyl-tRNA synthetase / YARS1","entity_type_key":"protein"},"evidence_count":1,"mechanism_event":{"id":"8c491e84-05ed-5030-849e-87429de84e03","stable_key":"52871722-4aa6-5453-a902-3e76356db327:resveratrol-tyrrs-binding-event","event_type":"observed_relationship","label":"A protein that normally charges tyrosine tRNA also senses this compound.","description":"Resveratrol occupied the tyrosine active site in human TyrRS co-crystals and inhibited amino-acid activation with reported Ki 22 micromolar.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"53549e32-e6b4-5f09-94e6-62867b015713","slug":"resveratrol","display_name":"Resveratrol","entity_type_key":"small_molecule"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"1e70f8cb-144f-5c63-b862-0c8670840077","slug":"yars1","display_name":"Human cytosolic tyrosyl-tRNA synthetase / YARS1","entity_type_key":"protein"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"61e08499-3296-56f9-9656-e7263b876637","slug":"trans-resveratrol","display_name":"trans-Resveratrol","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""},{"entity":{"id":"ae625c84-0823-5f4a-bdfd-54b7a99cf8fd","slug":"cis-resveratrol","display_name":"cis-Resveratrol","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""},{"entity":{"id":"bcfef85f-831d-5439-ba51-1aef4b090441","slug":"l-tyrosine","display_name":"L-Tyrosine","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":4,"notes":""}]},"contexts":[{"dimension":"evidence_access","value_text":"Primary full text","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Purified human enzyme and structure.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"The bound ligand adopts a cis conformation; the authors propose conformational accommodation from predominantly trans solution. This is not proof of physiological bulk photoisomerization.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"Resveratrol collection; molecular form, preparation, species, exposure and manipulation remain explicit.","comparator":null,"unit":null,"notes":"","entity":{"slug":"resveratrol","display_name":"Resveratrol","entity_type_key":"small_molecule"}},{"dimension":"plain_language","value_text":"A protein that normally charges tyrosine tRNA also senses this compound.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"A human tRNA synthetase is a potent PARP1-activating effector target for resveratrol. · 2015 · https://pubmed.ncbi.nlm.nih.gov/25533949/ · DOI 10.1038/nature14028","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"0b12dabc-7222-53c7-8c68-8d7431a19eb0","evidence_kind":"source_excerpt","locator":"Lines 286-292","start_line":286,"end_line":292,"excerpt":"## resveratrol-tyrrs-binding\nA protein that normally charges tyrosine tRNA also senses this compound.\nResveratrol occupied the tyrosine active site in human TyrRS co-crystals and inhibited amino-acid activation with reported Ki 22 micromolar.\nModel: Purified human enzyme and structure.\nLimitations: The bound ligand adopts a cis conformation; the authors propose conformational accommodation from predominantly trans solution. This is not proof of physiological bulk photoisomerization.\nEvidence access: Primary full text\nA human tRNA synthetase is a potent PARP1-activating effector target for resveratrol. · 2015 · https://pubmed.ncbi.nlm.nih.gov/25533949/ · DOI 10.1038/nature14028","model_system":"Purified human enzyme and structure.","directness":"reported_statement","verification_status":"source_derived_draft","notes":"Original curation paraphrase; evidence access and experimental limitations specified.","relationship":"supports","weight":1.0,"link_notes":"","source":{"id":"2844eda9-a122-5357-ae47-cd58227c5994","stable_key":"import-52871722-4aa6-5453-a902-3e76356db327","title":"Resveratrol: metabolites, target selectivity and cross-nutrient mechanisms (2026-09-19)","document_type":"imported_text","citation_label":"AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text.","file_path":"","sha256":"04885b4bee72f912a7f3f618f1b2bf79c944dbcb20500398c2729fc8228dcd9a","revision_id":"99504ff2-f1d3-5f4c-bc31-e1030d27a918","review_status":"unverified_draft","notes":""}}],"relations":[],"conflicts":[],"corrections":[],"research":null}