{"id":"392fec5f-bb35-5ac7-ac91-c51262061a94","stable_key":"3b5aff9b-4086-5574-bfb4-3ea49ba520d7:coq10-coq-sulfide-loss","predicate":"low_cellular_supply_impairs","statement":"CoQ-deficient human fibroblasts had impaired sulfide oxidation proportional to their residual CoQ.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"9b305382-40e6-5700-b942-62bbb4447c8c","mechanism_event_label":"A low CoQ pool can disrupt another pathway before considering ATP alone.","subject":{"id":"f1bcf0ac-3578-5afa-97d7-ef3551b657c5","slug":"coq10","display_name":"Coenzyme Q10 / CoQ10 redox system","entity_type_key":"chemical_species"},"object":{"id":"a6245bb3-d772-56bf-8bcd-b96725f620f3","slug":"sulfide-oxidation","display_name":"Mitochondrial hydrogen sulfide oxidation","entity_type_key":"cellular_process"},"evidence_count":1,"mechanism_event":{"id":"9b305382-40e6-5700-b942-62bbb4447c8c","stable_key":"3b5aff9b-4086-5574-bfb4-3ea49ba520d7:coq10-coq-sulfide-loss-event","event_type":"biochemical_relationship","label":"A low CoQ pool can disrupt another pathway before considering ATP alone.","description":"CoQ-deficient human fibroblasts had impaired sulfide oxidation proportional to their residual CoQ.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"6ddb0a1d-9690-5a4b-a837-052d69c7b88b","slug":"sqor","display_name":"Human sulfide:quinone oxidoreductase / SQOR","entity_type_key":"protein"},"role":"affected_enzyme","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"f1bcf0ac-3578-5afa-97d7-ef3551b657c5","slug":"coq10","display_name":"Coenzyme Q10 / CoQ10 redox system","entity_type_key":"chemical_species"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"a6245bb3-d772-56bf-8bcd-b96725f620f3","slug":"sulfide-oxidation","display_name":"Mitochondrial hydrogen sulfide oxidation","entity_type_key":"cellular_process"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""}]},"contexts":[{"dimension":"availability_state","value_text":"machinery_impairment","comparator":null,"unit":null,"notes":"Imported condition classification; unverified.","entity":null},{"dimension":"evidence_span","value_text":"{\"source_cache\": \"artifacts/coq10-research/27856618.abstract.txt\", \"locator\": \"Primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"a8b98767d3bed9661c05c7b82b55817b6d9912abd8bfc9dd9d59ca9763025485\", \"start_char\": 0, \"end_char\": 1261, \"text_sha256\": \"a8b98767d3bed9661c05c7b82b55817b6d9912abd8bfc9dd9d59ca9763025485\"}","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Patient fibroblasts, biosynthesis inhibition and mouse genetics","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"exposure","value_text":"Genetic or pharmacological CoQ depletion and in-vitro repletion","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Tissue-specific disease models; mouse residual percentages are not diagnostic human thresholds.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect.","comparator":null,"unit":null,"notes":"","entity":{"slug":"coq10","display_name":"Coenzyme Q10 / CoQ10 redox system","entity_type_key":"chemical_species"}},{"dimension":"organism","value_text":"Human fibroblasts/HeLa cells and Pdss2 mutant mice","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"A low CoQ pool can disrupt another pathway before considering ATP alone.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[coq10-p27856618] Coenzyme Q deficiency causes impairment of the sulfide oxidation pathway. (2017). https://pubmed.ncbi.nlm.nih.gov/27856618/ DOI: 10.15252/emmm.201606356","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Sulfide oxidation and tissue CoQ","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"trigger_kind","value_text":"machinery_impairment","comparator":null,"unit":null,"notes":"Imported condition classification; unverified.","entity":null}],"evidence":[{"id":"6437a979-8eb3-548c-810c-65863852b48d","evidence_kind":"source_excerpt","locator":"Lines 541-552","start_line":541,"end_line":552,"excerpt":"### coq10-coq-sulfide-loss\nCoQ-deficient human fibroblasts had impaired sulfide oxidation proportional to their residual CoQ.\nCondition category: machinery_impairment\nnutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: A low CoQ pool can disrupt another pathway before considering ATP alone.\norganism: Human fibroblasts/HeLa cells and Pdss2 mutant mice\ntissue_or_cell_type: Sulfide oxidation and tissue CoQ\nexperimental_model: Patient fibroblasts, biosynthesis inhibition and mouse genetics\nlimitations: Tissue-specific disease models; mouse residual percentages are not diagnostic human thresholds.\nexposure: Genetic or pharmacological CoQ depletion and in-vitro repletion\nevidence_span: {\"source_cache\": \"artifacts/coq10-research/27856618.abstract.txt\", \"locator\": \"Primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"a8b98767d3bed9661c05c7b82b55817b6d9912abd8bfc9dd9d59ca9763025485\", \"start_char\": 0, \"end_char\": 1261, \"text_sha256\": \"a8b98767d3bed9661c05c7b82b55817b6d9912abd8bfc9dd9d59ca9763025485\"}\n[coq10-p27856618] Coenzyme Q deficiency causes impairment of the sulfide oxidation pathway. 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