{"id":"b0657f19-cd06-5000-aaae-95aeae043f15","stable_key":"a8baf7e9-80e4-5d8c-adec-9a63e84d2f21:l-cysteine-ero1-pdi-targeting","predicate":"selectively_oxidizes","statement":"Human ERO1A targets PDI through contacts with its b-prime substrate-binding domain, supporting the disulfide-forming pathway for protein folding.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"94bdacf0-421b-5bd4-a789-50800c0b40e7","mechanism_event_label":"Cysteines already incorporated into proteins are joined and rearranged during folding.","subject":{"id":"ff14ed5a-c990-5499-a789-a9d0c6450cff","slug":"ero1a","display_name":"Human endoplasmic reticulum oxidoreductin 1 alpha / ERO1A","entity_type_key":"protein"},"object":{"id":"193fbd7c-aa70-5078-bec5-acd1fd0fce11","slug":"p4h-beta-subunit","display_name":"The prolyl 4-hydroxylase beta subunit, identical to protein disulfide isomerase","entity_type_key":"protein"},"evidence_count":1,"mechanism_event":{"id":"94bdacf0-421b-5bd4-a789-50800c0b40e7","stable_key":"a8baf7e9-80e4-5d8c-adec-9a63e84d2f21:l-cysteine-ero1-pdi-targeting-event","event_type":"observed_relationship","label":"Cysteines already incorporated into proteins are joined and rearranged during folding.","description":"Human ERO1A targets PDI through contacts with its b-prime substrate-binding domain, supporting the disulfide-forming pathway for protein folding.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"ff14ed5a-c990-5499-a789-a9d0c6450cff","slug":"ero1a","display_name":"Human endoplasmic reticulum oxidoreductin 1 alpha / ERO1A","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"193fbd7c-aa70-5078-bec5-acd1fd0fce11","slug":"p4h-beta-subunit","display_name":"The prolyl 4-hydroxylase beta subunit, identical to protein disulfide isomerase","entity_type_key":"protein"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"ca899f13-50ad-55e5-ab99-329ae0038c74","slug":"l-cysteine","display_name":"L-Cysteine","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""},{"entity":{"id":"e2cd7179-f218-54e8-9ce9-7a836ae35fac","slug":"fad","display_name":"FAD","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""},{"entity":{"id":"da9d64bc-69d4-5d97-90a4-8f0ed03e0ac8","slug":"hydrogen-peroxide","display_name":"Hydrogen peroxide","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":4,"notes":""}]},"contexts":[{"dimension":"evidence_access","value_text":"Primary abstract","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Human ERO1A structural and biochemical study.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Protein-residue oxidation is separate from free cystine reduction; dietary cysteine effects were not tested.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"L-Cysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit.","comparator":null,"unit":null,"notes":"","entity":{"slug":"l-cysteine","display_name":"L-Cysteine","entity_type_key":"small_molecule"}},{"dimension":"plain_language","value_text":"Cysteines already incorporated into proteins are joined and rearranged during folding.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"Crystal structures of human Ero1α reveal the mechanisms of regulated and targeted oxidation of PDI. · 2010 · https://pubmed.ncbi.nlm.nih.gov/20834232/ · DOI 10.1038/emboj.2010.222","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"b6c74bf7-843b-55d9-9124-27710e687cb0","evidence_kind":"source_excerpt","locator":"Lines 484-490","start_line":484,"end_line":490,"excerpt":"## l-cysteine-ero1-pdi-targeting\nCysteines already incorporated into proteins are joined and rearranged during folding.\nHuman ERO1A targets PDI through contacts with its b-prime substrate-binding domain, supporting the disulfide-forming pathway for protein folding.\nModel: Human ERO1A structural and biochemical study.\nLimitations: Protein-residue oxidation is separate from free cystine reduction; dietary cysteine effects were not tested.\nEvidence access: Primary abstract\nCrystal structures of human Ero1α reveal the mechanisms of regulated and targeted oxidation of PDI. · 2010 · https://pubmed.ncbi.nlm.nih.gov/20834232/ · DOI 10.1038/emboj.2010.222","model_system":"Human ERO1A structural and biochemical study.","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":"654560f6-8d7f-596b-8722-48d94053cfe3","stable_key":"import-a8baf7e9-80e4-5d8c-adec-9a63e84d2f21","title":"L-Cysteine: sulfur allocation, redox supply 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":"f722669e54eab08ffe7289f9d79ddfc443014ed8c4bc5ba10ce2635470d22498","revision_id":"8ae25609-a031-5782-9c62-6cad8767ea46","review_status":"unverified_draft","notes":""}}],"relations":[],"conflicts":[],"corrections":[],"research":null}