{"id":"d951469b-f6ab-528d-b08f-153a8d50e01a","stable_key":"a8baf7e9-80e4-5d8c-adec-9a63e84d2f21:l-cysteine-ero1-regulatory-disulfides","predicate":"regulate","statement":"Regulatory cysteines in a flexible ERO1A loop change disulfide arrangements and electron transfer, restraining its oxidative activity.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"7fde4484-d5c6-53cf-9fc6-8816ef905b25","mechanism_event_label":"Cysteine bonds can regulate an enzyme as well as stabilize folded proteins.","subject":{"id":"c4027990-01c1-583a-9f2f-ce436cee5586","slug":"human-ero1a-regulatory-cysteines","display_name":"Regulatory cysteine residues in human ERO1A","entity_type_key":"cellular_process"},"object":{"id":"ff14ed5a-c990-5499-a789-a9d0c6450cff","slug":"ero1a","display_name":"Human endoplasmic reticulum oxidoreductin 1 alpha / ERO1A","entity_type_key":"protein"},"evidence_count":1,"mechanism_event":{"id":"7fde4484-d5c6-53cf-9fc6-8816ef905b25","stable_key":"a8baf7e9-80e4-5d8c-adec-9a63e84d2f21:l-cysteine-ero1-regulatory-disulfides-event","event_type":"observed_relationship","label":"Cysteine bonds can regulate an enzyme as well as stabilize folded proteins.","description":"Regulatory cysteines in a flexible ERO1A loop change disulfide arrangements and electron transfer, restraining its oxidative activity.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"c4027990-01c1-583a-9f2f-ce436cee5586","slug":"human-ero1a-regulatory-cysteines","display_name":"Regulatory cysteine residues in human ERO1A","entity_type_key":"cellular_process"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"ff14ed5a-c990-5499-a789-a9d0c6450cff","slug":"ero1a","display_name":"Human endoplasmic reticulum oxidoreductin 1 alpha / ERO1A","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":"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":"context_participant","stoichiometry":null,"state_label":"","sequence_order":3,"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":4,"notes":""}]},"contexts":[{"dimension":"evidence_access","value_text":"Primary abstract","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Human ERO1A hyperactive and inactive crystal structures.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"This is enzyme regulation, not proof that additional cysteine increases protein folding or antioxidant capacity.","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":"Cysteine bonds can regulate an enzyme as well as stabilize folded proteins.","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":"ab61b9ec-b3fd-558f-96b9-a28ecefbbb41","evidence_kind":"source_excerpt","locator":"Lines 492-498","start_line":492,"end_line":498,"excerpt":"## l-cysteine-ero1-regulatory-disulfides\nCysteine bonds can regulate an enzyme as well as stabilize folded proteins.\nRegulatory cysteines in a flexible ERO1A loop change disulfide arrangements and electron transfer, restraining its oxidative activity.\nModel: Human ERO1A hyperactive and inactive crystal structures.\nLimitations: This is enzyme regulation, not proof that additional cysteine increases protein folding or antioxidant capacity.\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 hyperactive and inactive crystal structures.","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}