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(2024). https://pubmed.ncbi.nlm.nih.gov/38243131/ DOI: 10.1038/s42255-023-00956-y","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"ETFDH-complex III-COQ2 assembly","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"8cc1d6e1-eb6d-50c0-b7a9-2f38d4b0728e","evidence_kind":"source_excerpt","locator":"Lines 411-422","start_line":411,"end_line":422,"excerpt":"### coq10-etfdh-metabolon\nThe study identified an ETFDH-complex III-COQ2 assembly directing lipid-derived electrons to the respiratory chain in skeletal muscle.\nCondition category: normal\nnutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: Fat oxidation and CoQ synthesis connect to the complex that reoxidizes reduced CoQ.\norganism: Mouse skeletal muscle and biochemical systems\ntissue_or_cell_type: ETFDH-complex III-COQ2 assembly\nexperimental_model: Muscle-specific knockout and protein-complex analyses\nlimitations: Skeletal-muscle context; does not establish identical complex organization in every human tissue.\nexposure: Etfdh deletion and metabolon characterization\nevidence_span: {\"source_cache\": \"artifacts/coq10-research/38243131.abstract.txt\", \"locator\": \"Primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"de9afaeca8a144d79c9f0d0d3b3faafaa4560af2292b8624d1a04ed45ee5d136\", \"start_char\": 0, \"end_char\": 1039, \"text_sha256\": \"de9afaeca8a144d79c9f0d0d3b3faafaa4560af2292b8624d1a04ed45ee5d136\"}\n[coq10-p38243131] An ETFDH-driven metabolon supports OXPHOS efficiency in skeletal muscle by regulating coenzyme Q homeostasis. 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