{"id":"dc2c0851-6baa-5fb4-a2cb-720e9ce00bc8","stable_key":"182336c6-ed36-5ec6-8a09-25c31096262e:dim-ondansetron-cyp2d6","predicate":"contributes_to_metabolism_of","statement":"CYP2D6 contributed to ondansetron metabolism in the studied human systems.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"68fd32a8-6494-5999-aa9e-16349de0c9b4","mechanism_event_label":"A substrate list alone omits other routes that can limit a single-enzyme interaction.","subject":{"id":"10f7a103-d63d-5bf4-8384-c5e1308ce126","slug":"cyp2d6","display_name":"Human cytochrome P450 2D6","entity_type_key":"protein"},"object":{"id":"c2321d52-b985-5d4f-901f-394d306b8ae3","slug":"ondansetron","display_name":"Ondansetron","entity_type_key":"small_molecule"},"evidence_count":1,"mechanism_event":{"id":"68fd32a8-6494-5999-aa9e-16349de0c9b4","stable_key":"182336c6-ed36-5ec6-8a09-25c31096262e:dim-ondansetron-cyp2d6-event","event_type":"biochemical_relationship","label":"A substrate list alone omits other routes that can limit a single-enzyme interaction.","description":"CYP2D6 contributed to ondansetron metabolism in the studied human systems.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"10f7a103-d63d-5bf4-8384-c5e1308ce126","slug":"cyp2d6","display_name":"Human cytochrome P450 2D6","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"c2321d52-b985-5d4f-901f-394d306b8ae3","slug":"ondansetron","display_name":"Ondansetron","entity_type_key":"small_molecule"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""}]},"contexts":[{"dimension":"evidence_span","value_text":"{\"source_cache\": \"artifacts/dim-research/8591723.abstract.txt\", \"locator\": \"Primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"04a615c551d95089eb1a966d88d8be011687d658f383e81af5b651845427b66e\", \"start_char\": 0, \"end_char\": 1460, \"text_sha256\": \"04a615c551d95089eb1a966d88d8be011687d658f383e81af5b651845427b66e\"}","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Human microsomes and individually expressed enzymes","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"exposure","value_text":"Enzyme-specific inhibitors and radiolabeled substrate","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"CYP3A is identified at subfamily level, without an exclusive isoform assignment. Multiple CYP pathways contribute; no DIM coadministration or clinically measured DIM effect.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"Diindolylmethane (DIM) research collection; topical membership is not evidence of a direct dietary effect.","comparator":null,"unit":null,"notes":"","entity":{"slug":"dim","display_name":"3,3'-Diindolylmethane / DIM","entity_type_key":"small_molecule"}},{"dimension":"organism","value_text":"Human CYP systems","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"A substrate list alone omits other routes that can limit a single-enzyme interaction.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[dim-p8591723] Multiple forms of cytochrome P450 are involved in the metabolism of ondansetron in humans. (1995). https://pubmed.ncbi.nlm.nih.gov/8591723/ DOI: 10.1016/s0090-9556(25)06820-5","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Ondansetron oxidation","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"fb6f6070-958c-5e0a-9251-f32d40857764","evidence_kind":"source_excerpt","locator":"Lines 961-972","start_line":961,"end_line":972,"excerpt":"### dim-ondansetron-cyp2d6\nCYP2D6 contributed to ondansetron metabolism in the studied human systems.\nCondition category: normal\nnutrient_topic: Diindolylmethane (DIM) research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: A substrate list alone omits other routes that can limit a single-enzyme interaction.\norganism: Human CYP systems\ntissue_or_cell_type: Ondansetron oxidation\nexperimental_model: Human microsomes and individually expressed enzymes\nlimitations: CYP3A is identified at subfamily level, without an exclusive isoform assignment. Multiple CYP pathways contribute; no DIM coadministration or clinically measured DIM effect.\nexposure: Enzyme-specific inhibitors and radiolabeled substrate\nevidence_span: {\"source_cache\": \"artifacts/dim-research/8591723.abstract.txt\", \"locator\": \"Primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"04a615c551d95089eb1a966d88d8be011687d658f383e81af5b651845427b66e\", \"start_char\": 0, \"end_char\": 1460, \"text_sha256\": \"04a615c551d95089eb1a966d88d8be011687d658f383e81af5b651845427b66e\"}\n[dim-p8591723] Multiple forms of cytochrome P450 are involved in the metabolism of ondansetron in humans. (1995). https://pubmed.ncbi.nlm.nih.gov/8591723/ DOI: 10.1016/s0090-9556(25)06820-5","model_system":"Human microsomes and individually expressed enzymes","directness":"author_interpretation","verification_status":"source_derived_draft","notes":"Exact curation-document quotation, not publisher quotation. Study references: [dim-p8591723] Multiple forms of cytochrome P450 are involved in the metabolism of ondansetron in humans. (1995). https://pubmed.ncbi.nlm.nih.gov/8591723/ DOI: 10.1016/s0090-9556(25)06820-5","relationship":"supports","weight":1.0,"link_notes":"","source":{"id":"b6d70682-97f9-5893-a03c-f9f88836033c","stable_key":"import-182336c6-ed36-5ec6-8a09-25c31096262e","title":"Diindolylmethane (DIM): formation, receptor signaling, metabolism and drug interactions (2026-09-17)","document_type":"imported_text","citation_label":"AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text.","file_path":"","sha256":"31e14060de904976d2f5d439f2bc9c8a99a72d34626c562c78429025e050d404","revision_id":"611094c1-a9cf-5b9b-b255-ac70b571696a","review_status":"unverified_draft","notes":""}}],"relations":[],"conflicts":[],"corrections":[],"research":null}