Nutrient chapter

Coenzyme Q10 / CoQ10 redox system

Coenzyme Q10 is an endogenously synthesized lipid redox carrier. Oxidized ubiquinone-10 and reduced ubiquinol-10 support electron transfer and membrane protection; their location, regeneration and availability matter.

100 recorded mechanisms · 16 availability situations · 6 preserved sources. Draft and verified records are labeled separately.

Read recorded mechanisms Open recursive mind map

The mechanisms

What the sources say this nutrient does, one relationship at a time. Plain wording comes first; the technical statement follows.

Complex I transferred electrons from NADH to ubiquinone-10 in reconstituted membranes.
Mitochondrial respiratory complex I → Ubiquinone-10 source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/29133414.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "139122e8a567596e6ec1b4bd361567d0e5cd4e3329fec72d47b949a86d29610d", "start_char": 0, "end_char": 1770, "text_sha256": "139122e8a567596e6ec1b4bd361567d0e5cd4e3329fec72d47b949a86d29610d"}
experimental_model
Proteoliposome enzyme kinetics
exposure
Ubiquinones with one to ten isoprenoid units
limitations
Purified enzyme system; short-chain analogues do not have identical binding and release kinetics to Q10.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
Mammalian complex I preparation
plain_language
CoQ receives electrons from the first respiratory complex.
primary_references
[coq10-p29133414] Correlating kinetic and structural data on ubiquinone binding and reduction by respiratory complex I. (2017). https://pubmed.ncbi.nlm.nih.gov/29133414/ DOI: 10.1073/pnas.1714074114
tissue_or_cell_type
Membrane quinone channel
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 385–396
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Proteoliposome enzyme kinetics · source_derived_draft · unverified_draft
### coq10-complex-i-q Complex I transferred electrons from NADH to ubiquinone-10 in reconstituted membranes. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: CoQ receives electrons from the first respiratory complex. organism: Mammalian complex I preparation tissue_or_cell_type: Membrane quinone channel experimental_model: Proteoliposome enzyme kinetics limitations: Purified enzyme system; short-chain analogues do not have identical binding and release kinetics to Q10. exposure: Ubiquinones with one to ten isoprenoid units evidence_span: {"source_cache": "artifacts/coq10-research/29133414.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "139122e8a567596e6ec1b4bd361567d0e5cd4e3329fec72d47b949a86d29610d", "start_char": 0, "end_char": 1770, "text_sha256": "139122e8a567596e6ec1b4bd361567d0e5cd4e3329fec72d47b949a86d29610d"} [coq10-p29133414] Correlating kinetic and structural data on ubiquinone binding and reduction by respiratory complex I. (2017). https://pubmed.ncbi.nlm.nih.gov/29133414/ DOI: 10.1073/pnas.1714074114
Complete structured claim and evidence
Complex III oxidizes reduced CoQ as part of respiratory electron flow examined in this study.
Mitochondrial respiratory complex III → Reduced CoQ10 source_derived_draftungraded
Experimental context and source evidence
evidence_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"}
experimental_model
Muscle-specific knockout and protein-complex analyses
exposure
Etfdh deletion and metabolon characterization
limitations
Skeletal-muscle context; does not establish identical complex organization in every human tissue.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
Mouse skeletal muscle and biochemical systems
plain_language
The carrier must release its electrons before it can accept more.
primary_references
[coq10-p38243131] An ETFDH-driven metabolon supports OXPHOS efficiency in skeletal muscle by regulating coenzyme Q homeostasis. (2024). https://pubmed.ncbi.nlm.nih.gov/38243131/ DOI: 10.1038/s42255-023-00956-y
tissue_or_cell_type
ETFDH-complex III-COQ2 assembly
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 424–435
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Muscle-specific knockout and protein-complex analyses · source_derived_draft · unverified_draft
### coq10-complex-iii-q Complex III oxidizes reduced CoQ as part of respiratory electron flow examined in this study. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: The carrier must release its electrons before it can accept more. organism: Mouse skeletal muscle and biochemical systems tissue_or_cell_type: ETFDH-complex III-COQ2 assembly experimental_model: Muscle-specific knockout and protein-complex analyses limitations: Skeletal-muscle context; does not establish identical complex organization in every human tissue. exposure: Etfdh deletion and metabolon characterization evidence_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"} [coq10-p38243131] An ETFDH-driven metabolon supports OXPHOS efficiency in skeletal muscle by regulating coenzyme Q homeostasis. (2024). https://pubmed.ncbi.nlm.nih.gov/38243131/ DOI: 10.1038/s42255-023-00956-y
Complete structured claim and evidence
COQ6 substrate conversion required the FDXR-FDX2 pair in the reconstructed assay.
Reconstructed ancestral tetrapod FDX2 → Reconstructed ancestral tetrapod COQ6 source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/38425362.fulltext.txt", "locator": "Primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "7d25af4ecd7340649536b8fea3b8a0a308a1611bbf8c57f6a79b362f443f1cba", "start_char": 9067, "end_char": 13813, "text_sha256": "49612ae4d3a59a75a02fe3fb132abd8aeb7ef8b7cae3b0f79b5557503c55ad51"}
experimental_model
Purified reconstructed COQ metabolon with short-chain substrates
exposure
Enzyme combinations, methyl donors, reductants and metal additions
limitations
Ancestral proteins and CoQ1 analogues; no clinical cofactor dose or proof of nutritional rate limitation. Reaction order need not be universal across species.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
Reconstructed ancestral tetrapod proteins
plain_language
The monooxygenase needed its electron-supplying partners.
primary_references
[coq10-p38425362] In vitro construction of the COQ metabolon unveils the molecular determinants of coenzyme Q biosynthesis. (2024). https://pubmed.ncbi.nlm.nih.gov/38425362/ DOI: 10.1038/s41929-023-01087-z
tissue_or_cell_type
Stepwise CoQ head-group assembly
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 632–643
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified reconstructed COQ metabolon with short-chain substrates · source_derived_draft · unverified_draft
### coq10-fdx2-coq6 COQ6 substrate conversion required the FDXR-FDX2 pair in the reconstructed assay. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: The monooxygenase needed its electron-supplying partners. organism: Reconstructed ancestral tetrapod proteins tissue_or_cell_type: Stepwise CoQ head-group assembly experimental_model: Purified reconstructed COQ metabolon with short-chain substrates limitations: Ancestral proteins and CoQ1 analogues; no clinical cofactor dose or proof of nutritional rate limitation. Reaction order need not be universal across species. exposure: Enzyme combinations, methyl donors, reductants and metal additions evidence_span: {"source_cache": "artifacts/coq10-research/38425362.fulltext.txt", "locator": "Primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "7d25af4ecd7340649536b8fea3b8a0a308a1611bbf8c57f6a79b362f443f1cba", "start_char": 9067, "end_char": 13813, "text_sha256": "49612ae4d3a59a75a02fe3fb132abd8aeb7ef8b7cae3b0f79b5557503c55ad51"} [coq10-p38425362] In vitro construction of the COQ metabolon unveils the molecular determinants of coenzyme Q biosynthesis. (2024). https://pubmed.ncbi.nlm.nih.gov/38425362/ DOI: 10.1038/s41929-023-01087-z
Complete structured claim and evidence
COQ3 methylated the tested precursor in the presence of SAM.
Reconstructed ancestral tetrapod COQ3 → S-Adenosyl-L-methionine source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/38425362.fulltext.txt", "locator": "Primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "7d25af4ecd7340649536b8fea3b8a0a308a1611bbf8c57f6a79b362f443f1cba", "start_char": 13814, "end_char": 15577, "text_sha256": "c43de1ac5dc6711fad8e37af3a52a8cd9784ed7eeaf77bd2981afe72abaf307f"}
experimental_model
Purified reconstructed COQ metabolon with short-chain substrates
exposure
Enzyme combinations, methyl donors, reductants and metal additions
limitations
Ancestral proteins and CoQ1 analogues; no clinical cofactor dose or proof of nutritional rate limitation. Reaction order need not be universal across species.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
Reconstructed ancestral tetrapod proteins
plain_language
CoQ synthesis shares the methyl-donor pool used by other pathways.
primary_references
[coq10-p38425362] In vitro construction of the COQ metabolon unveils the molecular determinants of coenzyme Q biosynthesis. (2024). https://pubmed.ncbi.nlm.nih.gov/38425362/ DOI: 10.1038/s41929-023-01087-z
tissue_or_cell_type
Stepwise CoQ head-group assembly
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 645–656
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified reconstructed COQ metabolon with short-chain substrates · source_derived_draft · unverified_draft
### coq10-coq3-sam COQ3 methylated the tested precursor in the presence of SAM. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: CoQ synthesis shares the methyl-donor pool used by other pathways. organism: Reconstructed ancestral tetrapod proteins tissue_or_cell_type: Stepwise CoQ head-group assembly experimental_model: Purified reconstructed COQ metabolon with short-chain substrates limitations: Ancestral proteins and CoQ1 analogues; no clinical cofactor dose or proof of nutritional rate limitation. Reaction order need not be universal across species. exposure: Enzyme combinations, methyl donors, reductants and metal additions evidence_span: {"source_cache": "artifacts/coq10-research/38425362.fulltext.txt", "locator": "Primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "7d25af4ecd7340649536b8fea3b8a0a308a1611bbf8c57f6a79b362f443f1cba", "start_char": 13814, "end_char": 15577, "text_sha256": "c43de1ac5dc6711fad8e37af3a52a8cd9784ed7eeaf77bd2981afe72abaf307f"} [coq10-p38425362] In vitro construction of the COQ metabolon unveils the molecular determinants of coenzyme Q biosynthesis. (2024). https://pubmed.ncbi.nlm.nih.gov/38425362/ DOI: 10.1038/s41929-023-01087-z
Complete structured claim and evidence
Added magnesium increased reconstructed COQ3 activity about fourfold and improved substrate binding; EDTA abolished turnover.
Mg2+ → Reconstructed ancestral tetrapod COQ3 source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/38425362.fulltext.txt", "locator": "Primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "7d25af4ecd7340649536b8fea3b8a0a308a1611bbf8c57f6a79b362f443f1cba", "start_char": 13814, "end_char": 15577, "text_sha256": "c43de1ac5dc6711fad8e37af3a52a8cd9784ed7eeaf77bd2981afe72abaf307f"}
experimental_model
Purified reconstructed COQ metabolon with short-chain substrates
exposure
Enzyme combinations, methyl donors, reductants and metal additions
limitations
Ancestral proteins and CoQ1 analogues; no clinical cofactor dose or proof of nutritional rate limitation. Reaction order need not be universal across species.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
Reconstructed ancestral tetrapod proteins
plain_language
Magnesium changed a specific methylation step in this biochemical system.
primary_references
[coq10-p38425362] In vitro construction of the COQ metabolon unveils the molecular determinants of coenzyme Q biosynthesis. (2024). https://pubmed.ncbi.nlm.nih.gov/38425362/ DOI: 10.1038/s41929-023-01087-z
tissue_or_cell_type
Stepwise CoQ head-group assembly
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 658–669
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified reconstructed COQ metabolon with short-chain substrates · source_derived_draft · unverified_draft
### coq10-coq3-magnesium Added magnesium increased reconstructed COQ3 activity about fourfold and improved substrate binding; EDTA abolished turnover. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: Magnesium changed a specific methylation step in this biochemical system. organism: Reconstructed ancestral tetrapod proteins tissue_or_cell_type: Stepwise CoQ head-group assembly experimental_model: Purified reconstructed COQ metabolon with short-chain substrates limitations: Ancestral proteins and CoQ1 analogues; no clinical cofactor dose or proof of nutritional rate limitation. Reaction order need not be universal across species. exposure: Enzyme combinations, methyl donors, reductants and metal additions evidence_span: {"source_cache": "artifacts/coq10-research/38425362.fulltext.txt", "locator": "Primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "7d25af4ecd7340649536b8fea3b8a0a308a1611bbf8c57f6a79b362f443f1cba", "start_char": 13814, "end_char": 15577, "text_sha256": "c43de1ac5dc6711fad8e37af3a52a8cd9784ed7eeaf77bd2981afe72abaf307f"} [coq10-p38425362] In vitro construction of the COQ metabolon unveils the molecular determinants of coenzyme Q biosynthesis. (2024). https://pubmed.ncbi.nlm.nih.gov/38425362/ DOI: 10.1038/s41929-023-01087-z
Complete structured claim and evidence
Zinc promoted COQ4 decarboxylase activity, whereas disruption of its metal-binding site eliminated detected product.
Zinc(II) ion → Reconstructed ancestral tetrapod COQ4 source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/38425362.fulltext.txt", "locator": "Primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "7d25af4ecd7340649536b8fea3b8a0a308a1611bbf8c57f6a79b362f443f1cba", "start_char": 19036, "end_char": 19993, "text_sha256": "b045e1167d6b11834b57a1d07ec6cfd4a9b4419ea9a0f482e9509488bd3b3178"}
experimental_model
Purified reconstructed COQ metabolon with short-chain substrates
exposure
Enzyme combinations, methyl donors, reductants and metal additions
limitations
Ancestral proteins and CoQ1 analogues; no clinical cofactor dose or proof of nutritional rate limitation. Reaction order need not be universal across species.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
Reconstructed ancestral tetrapod proteins
plain_language
A zinc-binding site helped a different head-group modification.
primary_references
[coq10-p38425362] In vitro construction of the COQ metabolon unveils the molecular determinants of coenzyme Q biosynthesis. (2024). https://pubmed.ncbi.nlm.nih.gov/38425362/ DOI: 10.1038/s41929-023-01087-z
tissue_or_cell_type
Stepwise CoQ head-group assembly
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 671–682
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified reconstructed COQ metabolon with short-chain substrates · source_derived_draft · unverified_draft
### coq10-coq4-zinc Zinc promoted COQ4 decarboxylase activity, whereas disruption of its metal-binding site eliminated detected product. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: A zinc-binding site helped a different head-group modification. organism: Reconstructed ancestral tetrapod proteins tissue_or_cell_type: Stepwise CoQ head-group assembly experimental_model: Purified reconstructed COQ metabolon with short-chain substrates limitations: Ancestral proteins and CoQ1 analogues; no clinical cofactor dose or proof of nutritional rate limitation. Reaction order need not be universal across species. exposure: Enzyme combinations, methyl donors, reductants and metal additions evidence_span: {"source_cache": "artifacts/coq10-research/38425362.fulltext.txt", "locator": "Primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "7d25af4ecd7340649536b8fea3b8a0a308a1611bbf8c57f6a79b362f443f1cba", "start_char": 19036, "end_char": 19993, "text_sha256": "b045e1167d6b11834b57a1d07ec6cfd4a9b4419ea9a0f482e9509488bd3b3178"} [coq10-p38425362] In vitro construction of the COQ metabolon unveils the molecular determinants of coenzyme Q biosynthesis. (2024). https://pubmed.ncbi.nlm.nih.gov/38425362/ DOI: 10.1038/s41929-023-01087-z
Complete structured claim and evidence
Mammalian TrxR1 reduced ubiquinone-10 to ubiquinol-10.
TXNRD1 → Ubiquinone-10 source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/12435734.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "929e8de2bc15ea62eb4a3814995fd289de759d721f16b848174ad65f95847c55", "start_char": 0, "end_char": 1340, "text_sha256": "929e8de2bc15ea62eb4a3814995fd289de759d721f16b848174ad65f95847c55"}
experimental_model
Enzyme kinetics, mutants and overexpressing-cell homogenates
exposure
NADPH or NADH; selenite and selenium-deprived enzyme variants
limitations
Biochemical selenium dependence; not proof that all CoQ recycling stops with low selenium or that combined supplements are synergistic clinically.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
Mammalian TrxR1 and human HEK293 cells
plain_language
A selenium-dependent enzyme can regenerate the antioxidant form of CoQ.
primary_references
[coq10-p12435734] The mammalian cytosolic selenoenzyme thioredoxin reductase reduces ubiquinone. A novel mechanism for defense against oxidative stress. (2003). https://pubmed.ncbi.nlm.nih.gov/12435734/ DOI: 10.1074/jbc.m210456200
tissue_or_cell_type
Ubiquinone reduction
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 762–773
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Enzyme kinetics, mutants and overexpressing-cell homogenates · source_derived_draft · unverified_draft
### coq10-txnrd1-coq Mammalian TrxR1 reduced ubiquinone-10 to ubiquinol-10. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: A selenium-dependent enzyme can regenerate the antioxidant form of CoQ. organism: Mammalian TrxR1 and human HEK293 cells tissue_or_cell_type: Ubiquinone reduction experimental_model: Enzyme kinetics, mutants and overexpressing-cell homogenates limitations: Biochemical selenium dependence; not proof that all CoQ recycling stops with low selenium or that combined supplements are synergistic clinically. exposure: NADPH or NADH; selenite and selenium-deprived enzyme variants evidence_span: {"source_cache": "artifacts/coq10-research/12435734.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "929e8de2bc15ea62eb4a3814995fd289de759d721f16b848174ad65f95847c55", "start_char": 0, "end_char": 1340, "text_sha256": "929e8de2bc15ea62eb4a3814995fd289de759d721f16b848174ad65f95847c55"} [coq10-p12435734] The mammalian cytosolic selenoenzyme thioredoxin reductase reduces ubiquinone. A novel mechanism for defense against oxidative stress. (2003). https://pubmed.ncbi.nlm.nih.gov/12435734/ DOI: 10.1074/jbc.m210456200
Complete structured claim and evidence
Cytosolic STARD7 was required for CoQ transport to the plasma membrane.
Human STARD7 lipid-transfer protein → Coenzyme Q delivery to the plasma membrane source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/36658222.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "8cd5c486ecb31ad03ea06a817eb5bc56e60abdfa8ae8d50a46502974be2898ce", "start_char": 0, "end_char": 1410, "text_sha256": "8cd5c486ecb31ad03ea06a817eb5bc56e60abdfa8ae8d50a46502974be2898ce"}
experimental_model
Protein processing, localization, transport and cell-growth experiments
exposure
PARL processing and compartment-specific STARD7 expression
limitations
Intracellular distribution mechanism; increasing oral dose does not prove delivery to a particular organelle.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
Mammalian cell models
plain_language
CoQ made in mitochondria needs a transport route to protect the cell surface.
primary_references
[coq10-p36658222] Mitochondria regulate intracellular coenzyme Q transport and ferroptotic resistance via STARD7. (2023). https://pubmed.ncbi.nlm.nih.gov/36658222/ DOI: 10.1038/s41556-022-01071-y
tissue_or_cell_type
Mitochondria and plasma membrane
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 476–487
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Protein processing, localization, transport and cell-growth experiments · source_derived_draft · unverified_draft
### coq10-stard7-export Cytosolic STARD7 was required for CoQ transport to the plasma membrane. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: CoQ made in mitochondria needs a transport route to protect the cell surface. organism: Mammalian cell models tissue_or_cell_type: Mitochondria and plasma membrane experimental_model: Protein processing, localization, transport and cell-growth experiments limitations: Intracellular distribution mechanism; increasing oral dose does not prove delivery to a particular organelle. exposure: PARL processing and compartment-specific STARD7 expression evidence_span: {"source_cache": "artifacts/coq10-research/36658222.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "8cd5c486ecb31ad03ea06a817eb5bc56e60abdfa8ae8d50a46502974be2898ce", "start_char": 0, "end_char": 1410, "text_sha256": "8cd5c486ecb31ad03ea06a817eb5bc56e60abdfa8ae8d50a46502974be2898ce"} [coq10-p36658222] Mitochondria regulate intracellular coenzyme Q transport and ferroptotic resistance via STARD7. (2023). https://pubmed.ncbi.nlm.nih.gov/36658222/ DOI: 10.1038/s41556-022-01071-y
Complete structured claim and evidence
CoQ-deficient human fibroblasts had impaired sulfide oxidation proportional to their residual CoQ.
Coenzyme Q10 / CoQ10 redox system → Mitochondrial hydrogen sulfide oxidation source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_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"}
experimental_model
Patient fibroblasts, biosynthesis inhibition and mouse genetics
exposure
Genetic or pharmacological CoQ depletion and in-vitro repletion
limitations
Tissue-specific disease models; mouse residual percentages are not diagnostic human thresholds.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
Human fibroblasts/HeLa cells and Pdss2 mutant mice
plain_language
A low CoQ pool can disrupt another pathway before considering ATP alone.
primary_references
[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
tissue_or_cell_type
Sulfide oxidation and tissue CoQ
trigger_kind
machinery_impairment Imported condition classification; unverified.
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 541–552
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Patient fibroblasts, biosynthesis inhibition and mouse genetics · source_derived_draft · unverified_draft
### coq10-coq-sulfide-loss CoQ-deficient human fibroblasts had impaired sulfide oxidation proportional to their residual CoQ. Condition category: machinery_impairment nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: A low CoQ pool can disrupt another pathway before considering ATP alone. organism: Human fibroblasts/HeLa cells and Pdss2 mutant mice tissue_or_cell_type: Sulfide oxidation and tissue CoQ experimental_model: Patient fibroblasts, biosynthesis inhibition and mouse genetics limitations: Tissue-specific disease models; mouse residual percentages are not diagnostic human thresholds. exposure: Genetic or pharmacological CoQ depletion and in-vitro repletion evidence_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"} [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
Complete structured claim and evidence
CoQ supplementation did not increase muscle CoQ or alter measured mitochondrial respiratory function, content or reactive-oxygen-species production.
Coenzyme Q10 / CoQ10 redox system → Muscle coenzyme Q10 concentration source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/36139772.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "07baaf957ba2b166fce6e23f157e7d2123c92bea20032628c332c0a40639b992", "start_char": 0, "end_char": 1370, "text_sha256": "07baaf957ba2b166fce6e23f157e7d2123c92bea20032628c332c0a40639b992"}
experimental_model
Randomized placebo-controlled muscle-biopsy supplementation trial
exposure
CoQ10 400 mg/day for eight weeks
limitations
One formulation/regimen and a small sample; a failed tissue or clinical response cannot establish universal nonresponse.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
37 simvastatin-treated adults with or without myalgia
plain_language
Taking more did not ensure delivery or functional change in the sampled muscle.
primary_references
[coq10-p36139772] Coenzyme Q10 Supplementation in Statin Treated Patients: A Double-Blinded Randomized Placebo-Controlled Trial. (2022). https://pubmed.ncbi.nlm.nih.gov/36139772/ DOI: 10.3390/antiox11091698
tissue_or_cell_type
Muscle CoQ, mitochondrial function and symptoms
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 983–994
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Randomized placebo-controlled muscle-biopsy supplementation trial · source_derived_draft · unverified_draft
### coq10-statin-muscle-repletion-null CoQ supplementation did not increase muscle CoQ or alter measured mitochondrial respiratory function, content or reactive-oxygen-species production. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: Taking more did not ensure delivery or functional change in the sampled muscle. organism: 37 simvastatin-treated adults with or without myalgia tissue_or_cell_type: Muscle CoQ, mitochondrial function and symptoms experimental_model: Randomized placebo-controlled muscle-biopsy supplementation trial limitations: One formulation/regimen and a small sample; a failed tissue or clinical response cannot establish universal nonresponse. exposure: CoQ10 400 mg/day for eight weeks evidence_span: {"source_cache": "artifacts/coq10-research/36139772.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "07baaf957ba2b166fce6e23f157e7d2123c92bea20032628c332c0a40639b992", "start_char": 0, "end_char": 1370, "text_sha256": "07baaf957ba2b166fce6e23f157e7d2123c92bea20032628c332c0a40639b992"} [coq10-p36139772] Coenzyme Q10 Supplementation in Statin Treated Patients: A Double-Blinded Randomized Placebo-Controlled Trial. (2022). https://pubmed.ncbi.nlm.nih.gov/36139772/ DOI: 10.3390/antiox11091698
Complete structured claim and evidence
The study reported DHODH-dependent ubiquinol generation as a mitochondrial ferroptosis-defense pathway.
Human dihydroorotate dehydrogenase / DHODH → Ubiquinone source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/33981038.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "b1af5a97412b5ebf797083a069385c4ed98258e68845692732448bfe061a453b", "start_char": 0, "end_char": 1716, "text_sha256": "b1af5a97412b5ebf797083a069385c4ed98258e68845692732448bfe061a453b"}
experimental_model
Genetic and pharmacological cancer-cell studies
exposure
DHODH loss or brequinar, with GPX4 inhibition
limitations
Pharmacological attribution and relative DHODH contribution were directly challenged in 2023; preserve the dispute rather than generalizing to dietary CoQ effects.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
Human cancer-cell and tumor models
plain_language
A pyrimidine-synthesis enzyme can also contribute reduced CoQ in the studied system.
primary_references
[coq10-p33981038] DHODH-mediated ferroptosis defence is a targetable vulnerability in cancer. (2021). https://pubmed.ncbi.nlm.nih.gov/33981038/ DOI: 10.1038/s41586-021-03539-7
tissue_or_cell_type
Mitochondrial ferroptosis defense
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 814–825
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Genetic and pharmacological cancer-cell studies · source_derived_draft · unverified_draft
### coq10-dhodh-quinol The study reported DHODH-dependent ubiquinol generation as a mitochondrial ferroptosis-defense pathway. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: A pyrimidine-synthesis enzyme can also contribute reduced CoQ in the studied system. organism: Human cancer-cell and tumor models tissue_or_cell_type: Mitochondrial ferroptosis defense experimental_model: Genetic and pharmacological cancer-cell studies limitations: Pharmacological attribution and relative DHODH contribution were directly challenged in 2023; preserve the dispute rather than generalizing to dietary CoQ effects. exposure: DHODH loss or brequinar, with GPX4 inhibition evidence_span: {"source_cache": "artifacts/coq10-research/33981038.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "b1af5a97412b5ebf797083a069385c4ed98258e68845692732448bfe061a453b", "start_char": 0, "end_char": 1716, "text_sha256": "b1af5a97412b5ebf797083a069385c4ed98258e68845692732448bfe061a453b"} [coq10-p33981038] DHODH-mediated ferroptosis defence is a targetable vulnerability in cancer. (2021). https://pubmed.ncbi.nlm.nih.gov/33981038/ DOI: 10.1038/s41586-021-03539-7
Complete structured claim and evidence
Median protein-to-creatinine ratio fell from 1.66 to 0.19 g/gCr at 12 months; six of seven patients with 12-month data had at least a 50% reduction.
Coenzyme Q10 / CoQ10 redox system → Urinary protein excretion / proteinuria source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/coq10-research/42435122.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "59862dedc0e8ce5d72cf95f5f04a1d16e447cc16e9f2310fac81d15fb1fa9aa4", "start_char": 0, "end_char": 1715, "text_sha256": "59862dedc0e8ce5d72cf95f5f04a1d16e447cc16e9f2310fac81d15fb1fa9aa4"}
experimental_model
Retrospective longitudinal clinical cohort
exposure
CoQ supplementation; median initial dose 10 mg/kg/day
limitations
2026 observational cohort without untreated randomization; incomplete 12-month data and genotype-specific context.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
12 Japanese patients: 11 COQ8B and one COQ6
plain_language
The treatment signal was in a genetically defined disease, not routine tiredness.
primary_references
[coq10-p42435122] Kidney outcomes of coenzyme Q10 supplementation in patients with genetically confirmed CoQ10 nephropathy in Japan. (2026). https://pubmed.ncbi.nlm.nih.gov/42435122/ DOI: 10.1007/s10157-026-02917-7
tissue_or_cell_type
Genetically confirmed CoQ nephropathy
trigger_kind
machinery_impairment Imported condition classification; unverified.
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 1048–1059
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Retrospective longitudinal clinical cohort · source_derived_draft · unverified_draft
### coq10-nephropathy-proteinuria Median protein-to-creatinine ratio fell from 1.66 to 0.19 g/gCr at 12 months; six of seven patients with 12-month data had at least a 50% reduction. Condition category: machinery_impairment nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: The treatment signal was in a genetically defined disease, not routine tiredness. organism: 12 Japanese patients: 11 COQ8B and one COQ6 tissue_or_cell_type: Genetically confirmed CoQ nephropathy experimental_model: Retrospective longitudinal clinical cohort limitations: 2026 observational cohort without untreated randomization; incomplete 12-month data and genotype-specific context. exposure: CoQ supplementation; median initial dose 10 mg/kg/day evidence_span: {"source_cache": "artifacts/coq10-research/42435122.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "59862dedc0e8ce5d72cf95f5f04a1d16e447cc16e9f2310fac81d15fb1fa9aa4", "start_char": 0, "end_char": 1715, "text_sha256": "59862dedc0e8ce5d72cf95f5f04a1d16e447cc16e9f2310fac81d15fb1fa9aa4"} [coq10-p42435122] Kidney outcomes of coenzyme Q10 supplementation in patients with genetically confirmed CoQ10 nephropathy in Japan. (2026). https://pubmed.ncbi.nlm.nih.gov/42435122/ DOI: 10.1007/s10157-026-02917-7
Complete structured claim and evidence
HPDL produced 4-hydroxymandelate in human cells.
Human hydroxyphenylpyruvate dioxygenase-like protein / HPDL → 4-Hydroxymandelate / 4-HMA source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/34471290.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "a3cbcc69203ace49d0451e55c2d4040109e16facb575f4d66a0396d375ba8956", "start_char": 0, "end_char": 1028, "text_sha256": "a3cbcc69203ace49d0451e55c2d4040109e16facb575f4d66a0396d375ba8956"}
experimental_model
Oxygen-isotope metabolomics and enzyme perturbation
exposure
18O2 labeling and HPDL activity
limitations
Cellular pathway; no evidence that additional tyrosine treats every CoQ deficiency.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
Human cell lines
plain_language
A separate enzyme helps make the head of the CoQ molecule.
primary_references
[coq10-p34471290] The polar oxy-metabolome reveals the 4-hydroxymandelate CoQ10 synthesis pathway. (2021). https://pubmed.ncbi.nlm.nih.gov/34471290/ DOI: 10.1038/s41586-021-03865-w
tissue_or_cell_type
Tyrosine-derived CoQ head-group precursor
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 164–175
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Oxygen-isotope metabolomics and enzyme perturbation · source_derived_draft · unverified_draft
### coq10-hpdl-hma HPDL produced 4-hydroxymandelate in human cells. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: A separate enzyme helps make the head of the CoQ molecule. organism: Human cell lines tissue_or_cell_type: Tyrosine-derived CoQ head-group precursor experimental_model: Oxygen-isotope metabolomics and enzyme perturbation limitations: Cellular pathway; no evidence that additional tyrosine treats every CoQ deficiency. exposure: 18O2 labeling and HPDL activity evidence_span: {"source_cache": "artifacts/coq10-research/34471290.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "a3cbcc69203ace49d0451e55c2d4040109e16facb575f4d66a0396d375ba8956", "start_char": 0, "end_char": 1028, "text_sha256": "a3cbcc69203ace49d0451e55c2d4040109e16facb575f4d66a0396d375ba8956"} [coq10-p34471290] The polar oxy-metabolome reveals the 4-hydroxymandelate CoQ10 synthesis pathway. (2021). https://pubmed.ncbi.nlm.nih.gov/34471290/ DOI: 10.1038/s41586-021-03865-w
Complete structured claim and evidence
Isotope tracing identified 4-hydroxymandelate as a CoQ10 head-group biosynthetic intermediate.
4-Hydroxymandelate / 4-HMA → Coenzyme Q aromatic head-group biosynthesis source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/34471290.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "a3cbcc69203ace49d0451e55c2d4040109e16facb575f4d66a0396d375ba8956", "start_char": 0, "end_char": 1028, "text_sha256": "a3cbcc69203ace49d0451e55c2d4040109e16facb575f4d66a0396d375ba8956"}
experimental_model
Oxygen-isotope metabolomics and enzyme perturbation
exposure
18O2 labeling and HPDL activity
limitations
Cellular pathway; no evidence that additional tyrosine treats every CoQ deficiency.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
Human cell lines
plain_language
The head group has its own supply route, separate from the lipid tail.
primary_references
[coq10-p34471290] The polar oxy-metabolome reveals the 4-hydroxymandelate CoQ10 synthesis pathway. (2021). https://pubmed.ncbi.nlm.nih.gov/34471290/ DOI: 10.1038/s41586-021-03865-w
tissue_or_cell_type
Tyrosine-derived CoQ head-group precursor
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 177–188
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Oxygen-isotope metabolomics and enzyme perturbation · source_derived_draft · unverified_draft
### coq10-hma-headgroup Isotope tracing identified 4-hydroxymandelate as a CoQ10 head-group biosynthetic intermediate. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: The head group has its own supply route, separate from the lipid tail. organism: Human cell lines tissue_or_cell_type: Tyrosine-derived CoQ head-group precursor experimental_model: Oxygen-isotope metabolomics and enzyme perturbation limitations: Cellular pathway; no evidence that additional tyrosine treats every CoQ deficiency. exposure: 18O2 labeling and HPDL activity evidence_span: {"source_cache": "artifacts/coq10-research/34471290.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "a3cbcc69203ace49d0451e55c2d4040109e16facb575f4d66a0396d375ba8956", "start_char": 0, "end_char": 1028, "text_sha256": "a3cbcc69203ace49d0451e55c2d4040109e16facb575f4d66a0396d375ba8956"} [coq10-p34471290] The polar oxy-metabolome reveals the 4-hydroxymandelate CoQ10 synthesis pathway. (2021). https://pubmed.ncbi.nlm.nih.gov/34471290/ DOI: 10.1038/s41586-021-03865-w
Complete structured claim and evidence
Patient fibroblasts with PDSS2 variants had severely impaired decaprenyl-diphosphate synthesis.
Human decaprenyl-diphosphate synthase subunit 2 / PDSS2 → Coenzyme Q isoprenoid side-chain biosynthesis source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/coq10-research/17186472.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e9c50c316029827591ba4c9e6cc96b6a1b7b890f5b8dadfd88ac686c73d83865", "start_char": 0, "end_char": 1039, "text_sha256": "e9c50c316029827591ba4c9e6cc96b6a1b7b890f5b8dadfd88ac686c73d83865"}
experimental_model
Human genetics and radiolabeled-substrate assays
exposure
Compound heterozygous PDSS2 variants
limitations
Rare genetic disease; dietary shortage and tissue-wide thresholds were not established.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
Human infant and patient fibroblasts
plain_language
The cell cannot finish CoQ normally if its tail-building machinery is impaired.
primary_references
[coq10-p17186472] Leigh syndrome with nephropathy and CoQ10 deficiency due to decaprenyl diphosphate synthase subunit 2 (PDSS2) mutations. (2006). https://pubmed.ncbi.nlm.nih.gov/17186472/ DOI: 10.1086/510023
tissue_or_cell_type
Muscle and fibroblast CoQ production
trigger_kind
machinery_impairment Imported condition classification; unverified.
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 190–201
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human genetics and radiolabeled-substrate assays · source_derived_draft · unverified_draft
### coq10-pdss2 Patient fibroblasts with PDSS2 variants had severely impaired decaprenyl-diphosphate synthesis. Condition category: machinery_impairment nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: The cell cannot finish CoQ normally if its tail-building machinery is impaired. organism: Human infant and patient fibroblasts tissue_or_cell_type: Muscle and fibroblast CoQ production experimental_model: Human genetics and radiolabeled-substrate assays limitations: Rare genetic disease; dietary shortage and tissue-wide thresholds were not established. exposure: Compound heterozygous PDSS2 variants evidence_span: {"source_cache": "artifacts/coq10-research/17186472.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e9c50c316029827591ba4c9e6cc96b6a1b7b890f5b8dadfd88ac686c73d83865", "start_char": 0, "end_char": 1039, "text_sha256": "e9c50c316029827591ba4c9e6cc96b6a1b7b890f5b8dadfd88ac686c73d83865"} [coq10-p17186472] Leigh syndrome with nephropathy and CoQ10 deficiency due to decaprenyl diphosphate synthase subunit 2 (PDSS2) mutations. (2006). https://pubmed.ncbi.nlm.nih.gov/17186472/ DOI: 10.1086/510023
Complete structured claim and evidence
The PDSS1 D308E variant was associated with deficient CoQ-dependent respiratory activity and defective functional complementation.
Human decaprenyl-diphosphate synthase subunit 1 / PDSS1 → Coenzyme Q biosynthesis source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/coq10-research/17332895.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0a500ba6d7c7b5f32817074367d71993504fbd9c5a10cb76038faf718fb79b87", "start_char": 0, "end_char": 1416, "text_sha256": "0a500ba6d7c7b5f32817074367d71993504fbd9c5a10cb76038faf718fb79b87"}
experimental_model
Pedigrees, respiratory assays and yeast complementation
exposure
PDSS1 D308E or COQ2 frameshift variants
limitations
Distinct families and mutations; quinone rescue in an assay is not equivalent to proven oral treatment of every organ.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
Human families and yeast validation
plain_language
A second independent gene controls the same precursor supply route.
primary_references
[coq10-p17332895] Prenyldiphosphate synthase, subunit 1 (PDSS1) and OH-benzoate polyprenyltransferase (COQ2) mutations in ubiquinone deficiency and oxidative phosphorylation disorders. (2007). https://pubmed.ncbi.nlm.nih.gov/17332895/ DOI: 10.1172/jci29089
tissue_or_cell_type
CoQ-dependent respiratory function
trigger_kind
machinery_impairment Imported condition classification; unverified.
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 203–214
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Pedigrees, respiratory assays and yeast complementation · source_derived_draft · unverified_draft
### coq10-pdss1 The PDSS1 D308E variant was associated with deficient CoQ-dependent respiratory activity and defective functional complementation. Condition category: machinery_impairment nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: A second independent gene controls the same precursor supply route. organism: Human families and yeast validation tissue_or_cell_type: CoQ-dependent respiratory function experimental_model: Pedigrees, respiratory assays and yeast complementation limitations: Distinct families and mutations; quinone rescue in an assay is not equivalent to proven oral treatment of every organ. exposure: PDSS1 D308E or COQ2 frameshift variants evidence_span: {"source_cache": "artifacts/coq10-research/17332895.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0a500ba6d7c7b5f32817074367d71993504fbd9c5a10cb76038faf718fb79b87", "start_char": 0, "end_char": 1416, "text_sha256": "0a500ba6d7c7b5f32817074367d71993504fbd9c5a10cb76038faf718fb79b87"} [coq10-p17332895] Prenyldiphosphate synthase, subunit 1 (PDSS1) and OH-benzoate polyprenyltransferase (COQ2) mutations in ubiquinone deficiency and oxidative phosphorylation disorders. (2007). https://pubmed.ncbi.nlm.nih.gov/17332895/ DOI: 10.1172/jci29089
Complete structured claim and evidence
Adding quinone restored CoQ-dependent respiratory activities in the tested deficient preparations.
Ubiquinone → Mitochondrial respiratory electron transfer source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/17332895.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0a500ba6d7c7b5f32817074367d71993504fbd9c5a10cb76038faf718fb79b87", "start_char": 0, "end_char": 1416, "text_sha256": "0a500ba6d7c7b5f32817074367d71993504fbd9c5a10cb76038faf718fb79b87"}
experimental_model
Pedigrees, respiratory assays and yeast complementation
exposure
PDSS1 D308E or COQ2 frameshift variants
limitations
Distinct families and mutations; quinone rescue in an assay is not equivalent to proven oral treatment of every organ.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
Human families and yeast validation
plain_language
An intact respiratory enzyme can still fail when its mobile electron carrier is missing.
primary_references
[coq10-p17332895] Prenyldiphosphate synthase, subunit 1 (PDSS1) and OH-benzoate polyprenyltransferase (COQ2) mutations in ubiquinone deficiency and oxidative phosphorylation disorders. (2007). https://pubmed.ncbi.nlm.nih.gov/17332895/ DOI: 10.1172/jci29089
tissue_or_cell_type
CoQ-dependent respiratory function
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 216–227
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Pedigrees, respiratory assays and yeast complementation · source_derived_draft · unverified_draft
### coq10-quinone-rescue-assay Adding quinone restored CoQ-dependent respiratory activities in the tested deficient preparations. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: An intact respiratory enzyme can still fail when its mobile electron carrier is missing. organism: Human families and yeast validation tissue_or_cell_type: CoQ-dependent respiratory function experimental_model: Pedigrees, respiratory assays and yeast complementation limitations: Distinct families and mutations; quinone rescue in an assay is not equivalent to proven oral treatment of every organ. exposure: PDSS1 D308E or COQ2 frameshift variants evidence_span: {"source_cache": "artifacts/coq10-research/17332895.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0a500ba6d7c7b5f32817074367d71993504fbd9c5a10cb76038faf718fb79b87", "start_char": 0, "end_char": 1416, "text_sha256": "0a500ba6d7c7b5f32817074367d71993504fbd9c5a10cb76038faf718fb79b87"} [coq10-p17332895] Prenyldiphosphate synthase, subunit 1 (PDSS1) and OH-benzoate polyprenyltransferase (COQ2) mutations in ubiquinone deficiency and oxidative phosphorylation disorders. (2007). https://pubmed.ncbi.nlm.nih.gov/17332895/ DOI: 10.1172/jci29089
Complete structured claim and evidence
A homozygous COQ2 variant caused severe impairment of CoQ10 synthesis in patient fibroblasts.
Human 4-hydroxybenzoate polyprenyltransferase / COQ2 → Coenzyme Q biosynthesis source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/coq10-research/16400613.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "bd16a213ac563cf32b275cdee32ba3082e6c296cf9129e0930e2f96f0d2dc72a", "start_char": 0, "end_char": 1000, "text_sha256": "bd16a213ac563cf32b275cdee32ba3082e6c296cf9129e0930e2f96f0d2dc72a"}
experimental_model
Family sequencing and fibroblast tracer assays
exposure
Homozygous COQ2 missense variant
limitations
Rare primary deficiency; sequence numbering follows the original publication.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
Human siblings
plain_language
Having the building blocks does not help if the enzyme that joins them is defective.
primary_references
[coq10-p16400613] A mutation in para-hydroxybenzoate-polyprenyl transferase (COQ2) causes primary coenzyme Q10 deficiency. (2006). https://pubmed.ncbi.nlm.nih.gov/16400613/ DOI: 10.1086/500092
tissue_or_cell_type
CoQ synthesis
trigger_kind
machinery_impairment Imported condition classification; unverified.
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 229–240
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Family sequencing and fibroblast tracer assays · source_derived_draft · unverified_draft
### coq10-coq2-loss A homozygous COQ2 variant caused severe impairment of CoQ10 synthesis in patient fibroblasts. Condition category: machinery_impairment nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: Having the building blocks does not help if the enzyme that joins them is defective. organism: Human siblings tissue_or_cell_type: CoQ synthesis experimental_model: Family sequencing and fibroblast tracer assays limitations: Rare primary deficiency; sequence numbering follows the original publication. exposure: Homozygous COQ2 missense variant evidence_span: {"source_cache": "artifacts/coq10-research/16400613.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "bd16a213ac563cf32b275cdee32ba3082e6c296cf9129e0930e2f96f0d2dc72a", "start_char": 0, "end_char": 1000, "text_sha256": "bd16a213ac563cf32b275cdee32ba3082e6c296cf9129e0930e2f96f0d2dc72a"} [coq10-p16400613] A mutation in para-hydroxybenzoate-polyprenyl transferase (COQ2) causes primary coenzyme Q10 deficiency. (2006). https://pubmed.ncbi.nlm.nih.gov/16400613/ DOI: 10.1086/500092
Complete structured claim and evidence
Human COQ3 showed O-methyltransferase activity with early and final CoQ-intermediate analogues.
Human CoQ O-methyltransferase / COQ3 → Coenzyme Q precursor O-methylation source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/10777520.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0acc430af6b08f94dcbd0165e149ff76f9ba6fbfc47fcc934a0476182b4534bd", "start_char": 0, "end_char": 1345, "text_sha256": "0acc430af6b08f94dcbd0165e149ff76f9ba6fbfc47fcc934a0476182b4534bd"}
experimental_model
Human gene expression in yeast and methyltransferase assays
exposure
Farnesylated substrate analogues
limitations
Engineered complementation and analogue assays; not a human methyl-donor supplementation trial.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
Human COQ3 in yeast and cell-free assays
plain_language
The same enzyme performs methylation at two stages of CoQ assembly.
primary_references
[coq10-p10777520] Isolation and functional expression of human COQ3, a gene encoding a methyltransferase required for ubiquinone biosynthesis. (2000). https://pubmed.ncbi.nlm.nih.gov/10777520/ DOI: 10.1074/jbc.275.17.12381
tissue_or_cell_type
Early and final CoQ intermediates
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 242–253
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human gene expression in yeast and methyltransferase assays · source_derived_draft · unverified_draft
### coq10-coq3-methylation Human COQ3 showed O-methyltransferase activity with early and final CoQ-intermediate analogues. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: The same enzyme performs methylation at two stages of CoQ assembly. organism: Human COQ3 in yeast and cell-free assays tissue_or_cell_type: Early and final CoQ intermediates experimental_model: Human gene expression in yeast and methyltransferase assays limitations: Engineered complementation and analogue assays; not a human methyl-donor supplementation trial. exposure: Farnesylated substrate analogues evidence_span: {"source_cache": "artifacts/coq10-research/10777520.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0acc430af6b08f94dcbd0165e149ff76f9ba6fbfc47fcc934a0476182b4534bd", "start_char": 0, "end_char": 1345, "text_sha256": "0acc430af6b08f94dcbd0165e149ff76f9ba6fbfc47fcc934a0476182b4534bd"} [coq10-p10777520] Isolation and functional expression of human COQ3, a gene encoding a methyltransferase required for ubiquinone biosynthesis. (2000). https://pubmed.ncbi.nlm.nih.gov/10777520/ DOI: 10.1074/jbc.275.17.12381
Complete structured claim and evidence
Human COQ3 expression rescued respiratory growth and partially restored CoQ synthesis in coq3-null yeast.
Human CoQ O-methyltransferase / COQ3 → Coenzyme Q biosynthesis source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/10777520.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0acc430af6b08f94dcbd0165e149ff76f9ba6fbfc47fcc934a0476182b4534bd", "start_char": 0, "end_char": 1345, "text_sha256": "0acc430af6b08f94dcbd0165e149ff76f9ba6fbfc47fcc934a0476182b4534bd"}
experimental_model
Human gene expression in yeast and methyltransferase assays
exposure
Farnesylated substrate analogues
limitations
Engineered complementation and analogue assays; not a human methyl-donor supplementation trial.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
Human COQ3 in yeast and cell-free assays
plain_language
The human enzyme could replace part of the missing yeast machinery.
primary_references
[coq10-p10777520] Isolation and functional expression of human COQ3, a gene encoding a methyltransferase required for ubiquinone biosynthesis. (2000). https://pubmed.ncbi.nlm.nih.gov/10777520/ DOI: 10.1074/jbc.275.17.12381
tissue_or_cell_type
Early and final CoQ intermediates
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 255–266
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human gene expression in yeast and methyltransferase assays · source_derived_draft · unverified_draft
### coq10-coq3-rescue Human COQ3 expression rescued respiratory growth and partially restored CoQ synthesis in coq3-null yeast. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: The human enzyme could replace part of the missing yeast machinery. organism: Human COQ3 in yeast and cell-free assays tissue_or_cell_type: Early and final CoQ intermediates experimental_model: Human gene expression in yeast and methyltransferase assays limitations: Engineered complementation and analogue assays; not a human methyl-donor supplementation trial. exposure: Farnesylated substrate analogues evidence_span: {"source_cache": "artifacts/coq10-research/10777520.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0acc430af6b08f94dcbd0165e149ff76f9ba6fbfc47fcc934a0476182b4534bd", "start_char": 0, "end_char": 1345, "text_sha256": "0acc430af6b08f94dcbd0165e149ff76f9ba6fbfc47fcc934a0476182b4534bd"} [coq10-p10777520] Isolation and functional expression of human COQ3, a gene encoding a methyltransferase required for ubiquinone biosynthesis. (2000). https://pubmed.ncbi.nlm.nih.gov/10777520/ DOI: 10.1074/jbc.275.17.12381
Complete structured claim and evidence
Human COQ5 retained C-methyltransferase function and restored CoQ production when the yeast synthome was stabilized.
Human CoQ C-methyltransferase / COQ5 → Coenzyme Q precursor C-methylation source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/25152161.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "84482b69f7e6e575614f1cae122298d4328a881a5eda65eb7e96ed4f11db17fe", "start_char": 0, "end_char": 1655, "text_sha256": "84482b69f7e6e575614f1cae122298d4328a881a5eda65eb7e96ed4f11db17fe"}
experimental_model
Localization and yeast complementation
exposure
COQ5 complementation with or without synthome stabilization
limitations
Human protein in yeast; an assembled biosynthesis complex was important for rescue.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
Human COQ5 expressed in yeast
plain_language
A methylating enzyme also depends on the surrounding enzyme assembly.
primary_references
[coq10-p25152161] Molecular characterization of the human COQ5 C-methyltransferase in coenzyme Q10 biosynthesis. (2014). https://pubmed.ncbi.nlm.nih.gov/25152161/ DOI: 10.1016/j.bbalip.2014.08.007
tissue_or_cell_type
Mitochondrial matrix-facing biosynthetic complex
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 268–279
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Localization and yeast complementation · source_derived_draft · unverified_draft
### coq10-coq5-methylation Human COQ5 retained C-methyltransferase function and restored CoQ production when the yeast synthome was stabilized. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: A methylating enzyme also depends on the surrounding enzyme assembly. organism: Human COQ5 expressed in yeast tissue_or_cell_type: Mitochondrial matrix-facing biosynthetic complex experimental_model: Localization and yeast complementation limitations: Human protein in yeast; an assembled biosynthesis complex was important for rescue. exposure: COQ5 complementation with or without synthome stabilization evidence_span: {"source_cache": "artifacts/coq10-research/25152161.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "84482b69f7e6e575614f1cae122298d4328a881a5eda65eb7e96ed4f11db17fe", "start_char": 0, "end_char": 1655, "text_sha256": "84482b69f7e6e575614f1cae122298d4328a881a5eda65eb7e96ed4f11db17fe"} [coq10-p25152161] Molecular characterization of the human COQ5 C-methyltransferase in coenzyme Q10 biosynthesis. (2014). https://pubmed.ncbi.nlm.nih.gov/25152161/ DOI: 10.1016/j.bbalip.2014.08.007
Complete structured claim and evidence
COQ9 enhanced substrate binding in the hydrophobic channel of COQ7.
Human COQ9 lipid-binding protein → Human CoQ hydroxylase / COQ7 source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/36306796.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "adcddf90628bba3d14303fb8ec894bcece68fdf5b5591bbabb8f6bcef638d2e5", "start_char": 0, "end_char": 1049, "text_sha256": "adcddf90628bba3d14303fb8ec894bcece68fdf5b5591bbabb8f6bcef638d2e5"}
experimental_model
Structure, lipid binding and molecular dynamics
exposure
Lipid-, substrate- and NADH-bound complexes
limitations
Structural and simulation evidence; proposed membrane-deformation route is not directly measured dietary physiology.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
Human COQ7 and COQ9
plain_language
A lipid-binding helper presents a difficult-to-access substrate to a separate enzyme.
primary_references
[coq10-p36306796] Structure and functionality of a multimeric human COQ7:COQ9 complex. (2022). https://pubmed.ncbi.nlm.nih.gov/36306796/ DOI: 10.1016/j.molcel.2022.10.003
tissue_or_cell_type
Membrane-associated biosynthesis complex
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 281–292
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Structure, lipid binding and molecular dynamics · source_derived_draft · unverified_draft
### coq10-coq7-coq9 COQ9 enhanced substrate binding in the hydrophobic channel of COQ7. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: A lipid-binding helper presents a difficult-to-access substrate to a separate enzyme. organism: Human COQ7 and COQ9 tissue_or_cell_type: Membrane-associated biosynthesis complex experimental_model: Structure, lipid binding and molecular dynamics limitations: Structural and simulation evidence; proposed membrane-deformation route is not directly measured dietary physiology. exposure: Lipid-, substrate- and NADH-bound complexes evidence_span: {"source_cache": "artifacts/coq10-research/36306796.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "adcddf90628bba3d14303fb8ec894bcece68fdf5b5591bbabb8f6bcef638d2e5", "start_char": 0, "end_char": 1049, "text_sha256": "adcddf90628bba3d14303fb8ec894bcece68fdf5b5591bbabb8f6bcef638d2e5"} [coq10-p36306796] Structure and functionality of a multimeric human COQ7:COQ9 complex. (2022). https://pubmed.ncbi.nlm.nih.gov/36306796/ DOI: 10.1016/j.molcel.2022.10.003
Complete structured claim and evidence
COQ7:COQ9 assemblies deformed membranes in simulations, suggesting a route for hydrophobic precursor access.
Human CoQ hydroxylase / COQ7 → Delivery of CoQ biosynthetic intermediates to synthesis enzymes source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/36306796.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "adcddf90628bba3d14303fb8ec894bcece68fdf5b5591bbabb8f6bcef638d2e5", "start_char": 0, "end_char": 1049, "text_sha256": "adcddf90628bba3d14303fb8ec894bcece68fdf5b5591bbabb8f6bcef638d2e5"}
experimental_model
Structure, lipid binding and molecular dynamics
exposure
Lipid-, substrate- and NADH-bound complexes
limitations
Structural and simulation evidence; proposed membrane-deformation route is not directly measured dietary physiology.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
Human COQ7 and COQ9
plain_language
Getting the precursor out of the membrane may be part of how the enzyme pair works.
primary_references
[coq10-p36306796] Structure and functionality of a multimeric human COQ7:COQ9 complex. (2022). https://pubmed.ncbi.nlm.nih.gov/36306796/ DOI: 10.1016/j.molcel.2022.10.003
tissue_or_cell_type
Membrane-associated biosynthesis complex
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 294–305
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Structure, lipid binding and molecular dynamics · source_derived_draft · unverified_draft
### coq10-coq7-membrane-model COQ7:COQ9 assemblies deformed membranes in simulations, suggesting a route for hydrophobic precursor access. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: Getting the precursor out of the membrane may be part of how the enzyme pair works. organism: Human COQ7 and COQ9 tissue_or_cell_type: Membrane-associated biosynthesis complex experimental_model: Structure, lipid binding and molecular dynamics limitations: Structural and simulation evidence; proposed membrane-deformation route is not directly measured dietary physiology. exposure: Lipid-, substrate- and NADH-bound complexes evidence_span: {"source_cache": "artifacts/coq10-research/36306796.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "adcddf90628bba3d14303fb8ec894bcece68fdf5b5591bbabb8f6bcef638d2e5", "start_char": 0, "end_char": 1049, "text_sha256": "adcddf90628bba3d14303fb8ec894bcece68fdf5b5591bbabb8f6bcef638d2e5"} [coq10-p36306796] Structure and functionality of a multimeric human COQ7:COQ9 complex. (2022). https://pubmed.ncbi.nlm.nih.gov/36306796/ DOI: 10.1016/j.molcel.2022.10.003
Complete structured claim and evidence
Purified COQ9 associated with lipids including CoQ and used a conserved surface to interact with COQ7.
Human COQ9 lipid-binding protein → Ubiquinone source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/25339443.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "30231d534c146d800ac3035cced0e6ce0ba810d871b40967a5483a19ee90f1a5", "start_char": 0, "end_char": 1471, "text_sha256": "30231d534c146d800ac3035cced0e6ce0ba810d871b40967a5483a19ee90f1a5"}
experimental_model
Mouse disease model, protein structure and lipid-binding assays
exposure
COQ9 R239X disease model and purified COQ9
limitations
Protein loss is not dietary CoQ shortage; lipid-presentation details include mechanistic inference.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
Mouse Coq9 mutant and human COQ9 structure
plain_language
CoQ synthesis involves lipid handling as well as chemical reactions.
primary_references
[coq10-p25339443] Mitochondrial COQ9 is a lipid-binding protein that associates with COQ7 to enable coenzyme Q biosynthesis. (2014). https://pubmed.ncbi.nlm.nih.gov/25339443/ DOI: 10.1073/pnas.1413128111
tissue_or_cell_type
COQ9-COQ7 interaction
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 307–318
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Mouse disease model, protein structure and lipid-binding assays · source_derived_draft · unverified_draft
### coq10-coq9-binding Purified COQ9 associated with lipids including CoQ and used a conserved surface to interact with COQ7. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: CoQ synthesis involves lipid handling as well as chemical reactions. organism: Mouse Coq9 mutant and human COQ9 structure tissue_or_cell_type: COQ9-COQ7 interaction experimental_model: Mouse disease model, protein structure and lipid-binding assays limitations: Protein loss is not dietary CoQ shortage; lipid-presentation details include mechanistic inference. exposure: COQ9 R239X disease model and purified COQ9 evidence_span: {"source_cache": "artifacts/coq10-research/25339443.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "30231d534c146d800ac3035cced0e6ce0ba810d871b40967a5483a19ee90f1a5", "start_char": 0, "end_char": 1471, "text_sha256": "30231d534c146d800ac3035cced0e6ce0ba810d871b40967a5483a19ee90f1a5"} [coq10-p25339443] Mitochondrial COQ9 is a lipid-binding protein that associates with COQ7 to enable coenzyme Q biosynthesis. (2014). https://pubmed.ncbi.nlm.nih.gov/25339443/ DOI: 10.1073/pnas.1413128111
Complete structured claim and evidence
Human COQ8A showed ATPase activity as part of the conserved COQ8 biochemical function.
Human COQ8A / ADCK3 → ATP source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/29198567.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "4719b64857834d1a9b54316220f3d33aa529dce36938da0a063c74c5a5f30f67", "start_char": 0, "end_char": 1050, "text_sha256": "4719b64857834d1a9b54316220f3d33aa529dce36938da0a063c74c5a5f30f67"}
experimental_model
Biochemistry and chemical genetics
exposure
Cardiolipin-containing membranes and phenolic compounds
limitations
Human ATPase chemistry and yeast inhibition are distinct model components.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
Human COQ8A and yeast Coq8
plain_language
A protein once described mainly as kinase-like also uses ATP to support CoQ synthesis.
primary_references
[coq10-p29198567] Conserved Lipid and Small-Molecule Modulation of COQ8 Reveals Regulation of the Ancient Kinase-like UbiB Family. (2018). https://pubmed.ncbi.nlm.nih.gov/29198567/ DOI: 10.1016/j.chembiol.2017.11.001
tissue_or_cell_type
Membrane-regulated ATPase
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 320–331
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Biochemistry and chemical genetics · source_derived_draft · unverified_draft
### coq10-coq8a-atpase Human COQ8A showed ATPase activity as part of the conserved COQ8 biochemical function. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: A protein once described mainly as kinase-like also uses ATP to support CoQ synthesis. organism: Human COQ8A and yeast Coq8 tissue_or_cell_type: Membrane-regulated ATPase experimental_model: Biochemistry and chemical genetics limitations: Human ATPase chemistry and yeast inhibition are distinct model components. exposure: Cardiolipin-containing membranes and phenolic compounds evidence_span: {"source_cache": "artifacts/coq10-research/29198567.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "4719b64857834d1a9b54316220f3d33aa529dce36938da0a063c74c5a5f30f67", "start_char": 0, "end_char": 1050, "text_sha256": "4719b64857834d1a9b54316220f3d33aa529dce36938da0a063c74c5a5f30f67"} [coq10-p29198567] Conserved Lipid and Small-Molecule Modulation of COQ8 Reveals Regulation of the Ancient Kinase-like UbiB Family. (2018). https://pubmed.ncbi.nlm.nih.gov/29198567/ DOI: 10.1016/j.chembiol.2017.11.001
Complete structured claim and evidence
Binding to cardiolipin-containing membranes stimulated COQ8 ATPase activity.
Cardiolipin → COQ8 ATPase activity source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/29198567.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "4719b64857834d1a9b54316220f3d33aa529dce36938da0a063c74c5a5f30f67", "start_char": 0, "end_char": 1050, "text_sha256": "4719b64857834d1a9b54316220f3d33aa529dce36938da0a063c74c5a5f30f67"}
experimental_model
Biochemistry and chemical genetics
exposure
Cardiolipin-containing membranes and phenolic compounds
limitations
Human ATPase chemistry and yeast inhibition are distinct model components.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
Human COQ8A and yeast Coq8
plain_language
The surrounding membrane can change how this biosynthesis helper works.
primary_references
[coq10-p29198567] Conserved Lipid and Small-Molecule Modulation of COQ8 Reveals Regulation of the Ancient Kinase-like UbiB Family. (2018). https://pubmed.ncbi.nlm.nih.gov/29198567/ DOI: 10.1016/j.chembiol.2017.11.001
tissue_or_cell_type
Membrane-regulated ATPase
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 333–344
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Biochemistry and chemical genetics · source_derived_draft · unverified_draft
### coq10-coq8-cardiolipin Binding to cardiolipin-containing membranes stimulated COQ8 ATPase activity. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: The surrounding membrane can change how this biosynthesis helper works. organism: Human COQ8A and yeast Coq8 tissue_or_cell_type: Membrane-regulated ATPase experimental_model: Biochemistry and chemical genetics limitations: Human ATPase chemistry and yeast inhibition are distinct model components. exposure: Cardiolipin-containing membranes and phenolic compounds evidence_span: {"source_cache": "artifacts/coq10-research/29198567.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "4719b64857834d1a9b54316220f3d33aa529dce36938da0a063c74c5a5f30f67", "start_char": 0, "end_char": 1050, "text_sha256": "4719b64857834d1a9b54316220f3d33aa529dce36938da0a063c74c5a5f30f67"} [coq10-p29198567] Conserved Lipid and Small-Molecule Modulation of COQ8 Reveals Regulation of the Ancient Kinase-like UbiB Family. (2018). https://pubmed.ncbi.nlm.nih.gov/29198567/ DOI: 10.1016/j.chembiol.2017.11.001
Complete structured claim and evidence
Reconstructed COQ8A promoted CoQ production through ATPase-linked handling of insoluble pathway intermediates.
Reconstructed ancestral tetrapod COQ8A → Delivery of CoQ biosynthetic intermediates to synthesis enzymes source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/42525751.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "b7a49b25f09323a11c782afbdbff069e95429ed28e0ce2da5519abcbaa76c632", "start_char": 0, "end_char": 1058, "text_sha256": "b7a49b25f09323a11c782afbdbff069e95429ed28e0ce2da5519abcbaa76c632"}
experimental_model
Reconstructed-protein biochemistry, crystallography and mutagenesis
exposure
ATP-dependent pocket gating; excess final CoQ product
limitations
2026 reconstructed system using short-chain intermediates; do not assign all kinetics directly to intact human mitochondria.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
Ancestral tetrapod COQ8A/COQ8B and COQ metabolon
plain_language
The helper moves intermediates between synthesis enzymes rather than simply adding more raw material.
primary_references
[coq10-p42525751] COQ8 chaperones coenzyme Q lipid intermediates through ATP-driven structural gating. (2026). https://pubmed.ncbi.nlm.nih.gov/42525751/ DOI: 10.1126/sciadv.aeg1124
tissue_or_cell_type
Lipid-intermediate delivery
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 346–357
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Reconstructed-protein biochemistry, crystallography and mutagenesis · source_derived_draft · unverified_draft
### coq10-coq8a-chaperone Reconstructed COQ8A promoted CoQ production through ATPase-linked handling of insoluble pathway intermediates. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: The helper moves intermediates between synthesis enzymes rather than simply adding more raw material. organism: Ancestral tetrapod COQ8A/COQ8B and COQ metabolon tissue_or_cell_type: Lipid-intermediate delivery experimental_model: Reconstructed-protein biochemistry, crystallography and mutagenesis limitations: 2026 reconstructed system using short-chain intermediates; do not assign all kinetics directly to intact human mitochondria. exposure: ATP-dependent pocket gating; excess final CoQ product evidence_span: {"source_cache": "artifacts/coq10-research/42525751.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "b7a49b25f09323a11c782afbdbff069e95429ed28e0ce2da5519abcbaa76c632", "start_char": 0, "end_char": 1058, "text_sha256": "b7a49b25f09323a11c782afbdbff069e95429ed28e0ce2da5519abcbaa76c632"} [coq10-p42525751] COQ8 chaperones coenzyme Q lipid intermediates through ATP-driven structural gating. (2026). https://pubmed.ncbi.nlm.nih.gov/42525751/ DOI: 10.1126/sciadv.aeg1124
Complete structured claim and evidence
Reconstructed COQ8B promoted CoQ production through ATPase-linked handling of insoluble pathway intermediates.
Reconstructed ancestral tetrapod COQ8B → Delivery of CoQ biosynthetic intermediates to synthesis enzymes source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/42525751.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "b7a49b25f09323a11c782afbdbff069e95429ed28e0ce2da5519abcbaa76c632", "start_char": 0, "end_char": 1058, "text_sha256": "b7a49b25f09323a11c782afbdbff069e95429ed28e0ce2da5519abcbaa76c632"}
experimental_model
Reconstructed-protein biochemistry, crystallography and mutagenesis
exposure
ATP-dependent pocket gating; excess final CoQ product
limitations
2026 reconstructed system using short-chain intermediates; do not assign all kinetics directly to intact human mitochondria.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
Ancestral tetrapod COQ8A/COQ8B and COQ metabolon
plain_language
The helper moves intermediates between synthesis enzymes rather than simply adding more raw material.
primary_references
[coq10-p42525751] COQ8 chaperones coenzyme Q lipid intermediates through ATP-driven structural gating. (2026). https://pubmed.ncbi.nlm.nih.gov/42525751/ DOI: 10.1126/sciadv.aeg1124
tissue_or_cell_type
Lipid-intermediate delivery
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 359–370
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Reconstructed-protein biochemistry, crystallography and mutagenesis · source_derived_draft · unverified_draft
### coq10-coq8b-chaperone Reconstructed COQ8B promoted CoQ production through ATPase-linked handling of insoluble pathway intermediates. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: The helper moves intermediates between synthesis enzymes rather than simply adding more raw material. organism: Ancestral tetrapod COQ8A/COQ8B and COQ metabolon tissue_or_cell_type: Lipid-intermediate delivery experimental_model: Reconstructed-protein biochemistry, crystallography and mutagenesis limitations: 2026 reconstructed system using short-chain intermediates; do not assign all kinetics directly to intact human mitochondria. exposure: ATP-dependent pocket gating; excess final CoQ product evidence_span: {"source_cache": "artifacts/coq10-research/42525751.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "b7a49b25f09323a11c782afbdbff069e95429ed28e0ce2da5519abcbaa76c632", "start_char": 0, "end_char": 1058, "text_sha256": "b7a49b25f09323a11c782afbdbff069e95429ed28e0ce2da5519abcbaa76c632"} [coq10-p42525751] COQ8 chaperones coenzyme Q lipid intermediates through ATP-driven structural gating. (2026). https://pubmed.ncbi.nlm.nih.gov/42525751/ DOI: 10.1126/sciadv.aeg1124
Complete structured claim and evidence
Excess CoQ suppressed intermediate binding and the promoting effect of COQ8 in the reconstructed system.
Ubiquinone → Delivery of CoQ biosynthetic intermediates to synthesis enzymes source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/42525751.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "b7a49b25f09323a11c782afbdbff069e95429ed28e0ce2da5519abcbaa76c632", "start_char": 0, "end_char": 1058, "text_sha256": "b7a49b25f09323a11c782afbdbff069e95429ed28e0ce2da5519abcbaa76c632"}
experimental_model
Reconstructed-protein biochemistry, crystallography and mutagenesis
exposure
ATP-dependent pocket gating; excess final CoQ product
limitations
2026 reconstructed system using short-chain intermediates; do not assign all kinetics directly to intact human mitochondria.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
Ancestral tetrapod COQ8A/COQ8B and COQ metabolon
plain_language
The finished product can feed back on its own synthesis machinery.
primary_references
[coq10-p42525751] COQ8 chaperones coenzyme Q lipid intermediates through ATP-driven structural gating. (2026). https://pubmed.ncbi.nlm.nih.gov/42525751/ DOI: 10.1126/sciadv.aeg1124
tissue_or_cell_type
Lipid-intermediate delivery
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 372–383
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Reconstructed-protein biochemistry, crystallography and mutagenesis · source_derived_draft · unverified_draft
### coq10-coq-feedback Excess CoQ suppressed intermediate binding and the promoting effect of COQ8 in the reconstructed system. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: The finished product can feed back on its own synthesis machinery. organism: Ancestral tetrapod COQ8A/COQ8B and COQ metabolon tissue_or_cell_type: Lipid-intermediate delivery experimental_model: Reconstructed-protein biochemistry, crystallography and mutagenesis limitations: 2026 reconstructed system using short-chain intermediates; do not assign all kinetics directly to intact human mitochondria. exposure: ATP-dependent pocket gating; excess final CoQ product evidence_span: {"source_cache": "artifacts/coq10-research/42525751.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "b7a49b25f09323a11c782afbdbff069e95429ed28e0ce2da5519abcbaa76c632", "start_char": 0, "end_char": 1058, "text_sha256": "b7a49b25f09323a11c782afbdbff069e95429ed28e0ce2da5519abcbaa76c632"} [coq10-p42525751] COQ8 chaperones coenzyme Q lipid intermediates through ATP-driven structural gating. (2026). https://pubmed.ncbi.nlm.nih.gov/42525751/ DOI: 10.1126/sciadv.aeg1124
Complete structured claim and evidence
Ubiquinone-10 had the highest binding affinity and fastest binding rate among the tested chain lengths; ubiquinol-10 release was not rate limiting.
Ubiquinone-10 → Mitochondrial respiratory complex I source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/29133414.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "139122e8a567596e6ec1b4bd361567d0e5cd4e3329fec72d47b949a86d29610d", "start_char": 0, "end_char": 1770, "text_sha256": "139122e8a567596e6ec1b4bd361567d0e5cd4e3329fec72d47b949a86d29610d"}
experimental_model
Proteoliposome enzyme kinetics
exposure
Ubiquinones with one to ten isoprenoid units
limitations
Purified enzyme system; short-chain analogues do not have identical binding and release kinetics to Q10.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
Mammalian complex I preparation
plain_language
The ten-unit tail is part of the working molecule, not an inert label.
primary_references
[coq10-p29133414] Correlating kinetic and structural data on ubiquinone binding and reduction by respiratory complex I. (2017). https://pubmed.ncbi.nlm.nih.gov/29133414/ DOI: 10.1073/pnas.1714074114
tissue_or_cell_type
Membrane quinone channel
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 398–409
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Proteoliposome enzyme kinetics · source_derived_draft · unverified_draft
### coq10-complex-i-tail Ubiquinone-10 had the highest binding affinity and fastest binding rate among the tested chain lengths; ubiquinol-10 release was not rate limiting. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: The ten-unit tail is part of the working molecule, not an inert label. organism: Mammalian complex I preparation tissue_or_cell_type: Membrane quinone channel experimental_model: Proteoliposome enzyme kinetics limitations: Purified enzyme system; short-chain analogues do not have identical binding and release kinetics to Q10. exposure: Ubiquinones with one to ten isoprenoid units evidence_span: {"source_cache": "artifacts/coq10-research/29133414.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "139122e8a567596e6ec1b4bd361567d0e5cd4e3329fec72d47b949a86d29610d", "start_char": 0, "end_char": 1770, "text_sha256": "139122e8a567596e6ec1b4bd361567d0e5cd4e3329fec72d47b949a86d29610d"} [coq10-p29133414] Correlating kinetic and structural data on ubiquinone binding and reduction by respiratory complex I. (2017). https://pubmed.ncbi.nlm.nih.gov/29133414/ DOI: 10.1073/pnas.1714074114
Complete structured claim and evidence
The study identified an ETFDH-complex III-COQ2 assembly directing lipid-derived electrons to the respiratory chain in skeletal muscle.
Mouse electron transfer flavoprotein dehydrogenase / Etfdh → Mitochondrial respiratory complex III source_derived_draftungraded
Experimental context and source evidence
evidence_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"}
experimental_model
Muscle-specific knockout and protein-complex analyses
exposure
Etfdh deletion and metabolon characterization
limitations
Skeletal-muscle context; does not establish identical complex organization in every human tissue.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
Mouse skeletal muscle and biochemical systems
plain_language
Fat oxidation and CoQ synthesis connect to the complex that reoxidizes reduced CoQ.
primary_references
[coq10-p38243131] An ETFDH-driven metabolon supports OXPHOS efficiency in skeletal muscle by regulating coenzyme Q homeostasis. (2024). https://pubmed.ncbi.nlm.nih.gov/38243131/ DOI: 10.1038/s42255-023-00956-y
tissue_or_cell_type
ETFDH-complex III-COQ2 assembly
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 411–422
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Muscle-specific knockout and protein-complex analyses · source_derived_draft · unverified_draft
### coq10-etfdh-metabolon The study identified an ETFDH-complex III-COQ2 assembly directing lipid-derived electrons to the respiratory chain in skeletal muscle. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: Fat oxidation and CoQ synthesis connect to the complex that reoxidizes reduced CoQ. organism: Mouse skeletal muscle and biochemical systems tissue_or_cell_type: ETFDH-complex III-COQ2 assembly experimental_model: Muscle-specific knockout and protein-complex analyses limitations: Skeletal-muscle context; does not establish identical complex organization in every human tissue. exposure: Etfdh deletion and metabolon characterization evidence_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"} [coq10-p38243131] An ETFDH-driven metabolon supports OXPHOS efficiency in skeletal muscle by regulating coenzyme Q homeostasis. (2024). https://pubmed.ncbi.nlm.nih.gov/38243131/ DOI: 10.1038/s42255-023-00956-y
Complete structured claim and evidence
Muscle-specific Etfdh deletion caused complex III dysfunction and myopathy in mice.
Mouse electron transfer flavoprotein dehydrogenase / Etfdh → Mitochondrial respiratory complex III source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_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"}
experimental_model
Muscle-specific knockout and protein-complex analyses
exposure
Etfdh deletion and metabolon characterization
limitations
Skeletal-muscle context; does not establish identical complex organization in every human tissue.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
Mouse skeletal muscle and biochemical systems
plain_language
A defect upstream can disturb the system that recycles the shared electron carrier.
primary_references
[coq10-p38243131] An ETFDH-driven metabolon supports OXPHOS efficiency in skeletal muscle by regulating coenzyme Q homeostasis. (2024). https://pubmed.ncbi.nlm.nih.gov/38243131/ DOI: 10.1038/s42255-023-00956-y
tissue_or_cell_type
ETFDH-complex III-COQ2 assembly
trigger_kind
machinery_impairment Imported condition classification; unverified.
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 437–448
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Muscle-specific knockout and protein-complex analyses · source_derived_draft · unverified_draft
### coq10-etfdh-muscle-loss Muscle-specific Etfdh deletion caused complex III dysfunction and myopathy in mice. Condition category: machinery_impairment nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: A defect upstream can disturb the system that recycles the shared electron carrier. organism: Mouse skeletal muscle and biochemical systems tissue_or_cell_type: ETFDH-complex III-COQ2 assembly experimental_model: Muscle-specific knockout and protein-complex analyses limitations: Skeletal-muscle context; does not establish identical complex organization in every human tissue. exposure: Etfdh deletion and metabolon characterization evidence_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"} [coq10-p38243131] An ETFDH-driven metabolon supports OXPHOS efficiency in skeletal muscle by regulating coenzyme Q homeostasis. (2024). https://pubmed.ncbi.nlm.nih.gov/38243131/ DOI: 10.1038/s42255-023-00956-y
Complete structured claim and evidence
Truncated human DHODH penetrated the outer lipid leaflet toward membrane-embedded Q10.
Human dihydroorotate dehydrogenase / DHODH → Ubiquinone-10 source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/35269583.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "bf7a62576c30f509f5b4fbcf701cdf1cb6058de5c75d71e4a5f000394254e29a", "start_char": 0, "end_char": 1389, "text_sha256": "bf7a62576c30f509f5b4fbcf701cdf1cb6058de5c75d71e4a5f000394254e29a"}
experimental_model
Neutron reflectometry in supported lipid membranes
exposure
Membrane composition and Q10 placement
limitations
Truncated human enzyme and synthetic bilayers, not complete mitochondrial nucleotide flux.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
Truncated human DHODH and E. coli DHODH
plain_language
The enzyme that helps make pyrimidines must reach its electron acceptor in the membrane.
primary_references
[coq10-p35269583] New Insights into the Interaction of Class II Dihydroorotate Dehydrogenases with Ubiquinone in Lipid Bilayers as a Function of Lipid Composition. (2022). https://pubmed.ncbi.nlm.nih.gov/35269583/ DOI: 10.3390/ijms23052437
tissue_or_cell_type
Ubiquinone-containing bilayers
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 450–461
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Neutron reflectometry in supported lipid membranes · source_derived_draft · unverified_draft
### coq10-dhodh-q-access Truncated human DHODH penetrated the outer lipid leaflet toward membrane-embedded Q10. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: The enzyme that helps make pyrimidines must reach its electron acceptor in the membrane. organism: Truncated human DHODH and E. coli DHODH tissue_or_cell_type: Ubiquinone-containing bilayers experimental_model: Neutron reflectometry in supported lipid membranes limitations: Truncated human enzyme and synthetic bilayers, not complete mitochondrial nucleotide flux. exposure: Membrane composition and Q10 placement evidence_span: {"source_cache": "artifacts/coq10-research/35269583.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "bf7a62576c30f509f5b4fbcf701cdf1cb6058de5c75d71e4a5f000394254e29a", "start_char": 0, "end_char": 1389, "text_sha256": "bf7a62576c30f509f5b4fbcf701cdf1cb6058de5c75d71e4a5f000394254e29a"} [coq10-p35269583] New Insights into the Interaction of Class II Dihydroorotate Dehydrogenases with Ubiquinone in Lipid Bilayers as a Function of Lipid Composition. (2022). https://pubmed.ncbi.nlm.nih.gov/35269583/ DOI: 10.3390/ijms23052437
Complete structured claim and evidence
PARL cleavage supported the dual mitochondrial and cytosolic localization of STARD7.
Human mitochondrial rhomboid protease / PARL → Human STARD7 lipid-transfer protein source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/36658222.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "8cd5c486ecb31ad03ea06a817eb5bc56e60abdfa8ae8d50a46502974be2898ce", "start_char": 0, "end_char": 1410, "text_sha256": "8cd5c486ecb31ad03ea06a817eb5bc56e60abdfa8ae8d50a46502974be2898ce"}
experimental_model
Protein processing, localization, transport and cell-growth experiments
exposure
PARL processing and compartment-specific STARD7 expression
limitations
Intracellular distribution mechanism; increasing oral dose does not prove delivery to a particular organelle.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
Mammalian cell models
plain_language
Processing one transport protein helps decide where CoQ can go.
primary_references
[coq10-p36658222] Mitochondria regulate intracellular coenzyme Q transport and ferroptotic resistance via STARD7. (2023). https://pubmed.ncbi.nlm.nih.gov/36658222/ DOI: 10.1038/s41556-022-01071-y
tissue_or_cell_type
Mitochondria and plasma membrane
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 463–474
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Protein processing, localization, transport and cell-growth experiments · source_derived_draft · unverified_draft
### coq10-parl-stard7 PARL cleavage supported the dual mitochondrial and cytosolic localization of STARD7. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: Processing one transport protein helps decide where CoQ can go. organism: Mammalian cell models tissue_or_cell_type: Mitochondria and plasma membrane experimental_model: Protein processing, localization, transport and cell-growth experiments limitations: Intracellular distribution mechanism; increasing oral dose does not prove delivery to a particular organelle. exposure: PARL processing and compartment-specific STARD7 expression evidence_span: {"source_cache": "artifacts/coq10-research/36658222.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "8cd5c486ecb31ad03ea06a817eb5bc56e60abdfa8ae8d50a46502974be2898ce", "start_char": 0, "end_char": 1410, "text_sha256": "8cd5c486ecb31ad03ea06a817eb5bc56e60abdfa8ae8d50a46502974be2898ce"} [coq10-p36658222] Mitochondria regulate intracellular coenzyme Q transport and ferroptotic resistance via STARD7. (2023). https://pubmed.ncbi.nlm.nih.gov/36658222/ DOI: 10.1038/s41556-022-01071-y
Complete structured claim and evidence
Mitochondrial STARD7 preserved CoQ synthesis, oxidative phosphorylation and cristae organization.
Human STARD7 lipid-transfer protein → Coenzyme Q biosynthesis source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/36658222.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "8cd5c486ecb31ad03ea06a817eb5bc56e60abdfa8ae8d50a46502974be2898ce", "start_char": 0, "end_char": 1410, "text_sha256": "8cd5c486ecb31ad03ea06a817eb5bc56e60abdfa8ae8d50a46502974be2898ce"}
experimental_model
Protein processing, localization, transport and cell-growth experiments
exposure
PARL processing and compartment-specific STARD7 expression
limitations
Intracellular distribution mechanism; increasing oral dose does not prove delivery to a particular organelle.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
Mammalian cell models
plain_language
The same protein has a different job when retained inside mitochondria.
primary_references
[coq10-p36658222] Mitochondria regulate intracellular coenzyme Q transport and ferroptotic resistance via STARD7. (2023). https://pubmed.ncbi.nlm.nih.gov/36658222/ DOI: 10.1038/s41556-022-01071-y
tissue_or_cell_type
Mitochondria and plasma membrane
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 489–500
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Protein processing, localization, transport and cell-growth experiments · source_derived_draft · unverified_draft
### coq10-stard7-mito Mitochondrial STARD7 preserved CoQ synthesis, oxidative phosphorylation and cristae organization. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: The same protein has a different job when retained inside mitochondria. organism: Mammalian cell models tissue_or_cell_type: Mitochondria and plasma membrane experimental_model: Protein processing, localization, transport and cell-growth experiments limitations: Intracellular distribution mechanism; increasing oral dose does not prove delivery to a particular organelle. exposure: PARL processing and compartment-specific STARD7 expression evidence_span: {"source_cache": "artifacts/coq10-research/36658222.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "8cd5c486ecb31ad03ea06a817eb5bc56e60abdfa8ae8d50a46502974be2898ce", "start_char": 0, "end_char": 1410, "text_sha256": "8cd5c486ecb31ad03ea06a817eb5bc56e60abdfa8ae8d50a46502974be2898ce"} [coq10-p36658222] Mitochondria regulate intracellular coenzyme Q transport and ferroptotic resistance via STARD7. (2023). https://pubmed.ncbi.nlm.nih.gov/36658222/ DOI: 10.1038/s41556-022-01071-y
Complete structured claim and evidence
A CoQ variant competed with phosphatidylcholine for binding to purified STARD7.
Phosphatidylcholine → Ubiquinone source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/36658222.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "8cd5c486ecb31ad03ea06a817eb5bc56e60abdfa8ae8d50a46502974be2898ce", "start_char": 0, "end_char": 1410, "text_sha256": "8cd5c486ecb31ad03ea06a817eb5bc56e60abdfa8ae8d50a46502974be2898ce"}
experimental_model
Protein processing, localization, transport and cell-growth experiments
exposure
PARL processing and compartment-specific STARD7 expression
limitations
Purified-protein binding with a CoQ variant; not demonstrated dietary choline competition with CoQ10 absorption.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
Mammalian cell models
plain_language
Choline-containing membrane lipid and a CoQ analogue shared access to a transport protein.
primary_references
[coq10-p36658222] Mitochondria regulate intracellular coenzyme Q transport and ferroptotic resistance via STARD7. (2023). https://pubmed.ncbi.nlm.nih.gov/36658222/ DOI: 10.1038/s41556-022-01071-y
tissue_or_cell_type
Mitochondria and plasma membrane
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 502–513
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Protein processing, localization, transport and cell-growth experiments · source_derived_draft · unverified_draft
### coq10-stard7-pc A CoQ variant competed with phosphatidylcholine for binding to purified STARD7. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: Choline-containing membrane lipid and a CoQ analogue shared access to a transport protein. organism: Mammalian cell models tissue_or_cell_type: Mitochondria and plasma membrane experimental_model: Protein processing, localization, transport and cell-growth experiments limitations: Purified-protein binding with a CoQ variant; not demonstrated dietary choline competition with CoQ10 absorption. exposure: PARL processing and compartment-specific STARD7 expression evidence_span: {"source_cache": "artifacts/coq10-research/36658222.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "8cd5c486ecb31ad03ea06a817eb5bc56e60abdfa8ae8d50a46502974be2898ce", "start_char": 0, "end_char": 1410, "text_sha256": "8cd5c486ecb31ad03ea06a817eb5bc56e60abdfa8ae8d50a46502974be2898ce"} [coq10-p36658222] Mitochondria regulate intracellular coenzyme Q transport and ferroptotic resistance via STARD7. (2023). https://pubmed.ncbi.nlm.nih.gov/36658222/ DOI: 10.1038/s41556-022-01071-y
Complete structured claim and evidence
Cytosolic STARD7 overexpression increased ferroptosis resistance while reducing mitochondrial CoQ abundance and respiratory growth.
Human STARD7 lipid-transfer protein → Mitochondrial coenzyme Q pool source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/coq10-research/36658222.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "8cd5c486ecb31ad03ea06a817eb5bc56e60abdfa8ae8d50a46502974be2898ce", "start_char": 0, "end_char": 1410, "text_sha256": "8cd5c486ecb31ad03ea06a817eb5bc56e60abdfa8ae8d50a46502974be2898ce"}
experimental_model
Protein processing, localization, transport and cell-growth experiments
exposure
PARL processing and compartment-specific STARD7 expression
limitations
Intracellular distribution mechanism; increasing oral dose does not prove delivery to a particular organelle.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
Mammalian cell models
plain_language
Total supply and the location of that supply are different questions.
primary_references
[coq10-p36658222] Mitochondria regulate intracellular coenzyme Q transport and ferroptotic resistance via STARD7. (2023). https://pubmed.ncbi.nlm.nih.gov/36658222/ DOI: 10.1038/s41556-022-01071-y
tissue_or_cell_type
Mitochondria and plasma membrane
trigger_kind
machinery_impairment Imported condition classification; unverified.
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 515–526
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Protein processing, localization, transport and cell-growth experiments · source_derived_draft · unverified_draft
### coq10-stard7-tradeoff Cytosolic STARD7 overexpression increased ferroptosis resistance while reducing mitochondrial CoQ abundance and respiratory growth. Condition category: machinery_impairment nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: Total supply and the location of that supply are different questions. organism: Mammalian cell models tissue_or_cell_type: Mitochondria and plasma membrane experimental_model: Protein processing, localization, transport and cell-growth experiments limitations: Intracellular distribution mechanism; increasing oral dose does not prove delivery to a particular organelle. exposure: PARL processing and compartment-specific STARD7 expression evidence_span: {"source_cache": "artifacts/coq10-research/36658222.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "8cd5c486ecb31ad03ea06a817eb5bc56e60abdfa8ae8d50a46502974be2898ce", "start_char": 0, "end_char": 1410, "text_sha256": "8cd5c486ecb31ad03ea06a817eb5bc56e60abdfa8ae8d50a46502974be2898ce"} [coq10-p36658222] Mitochondria regulate intracellular coenzyme Q transport and ferroptotic resistance via STARD7. (2023). https://pubmed.ncbi.nlm.nih.gov/36658222/ DOI: 10.1038/s41556-022-01071-y
Complete structured claim and evidence
CoQ serves as electron acceptor for SQOR at the start of mitochondrial sulfide oxidation.
Human sulfide:quinone oxidoreductase / SQOR → Ubiquinone source_derived_draftungraded
Experimental context and source evidence
evidence_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"}
experimental_model
Patient fibroblasts, biosynthesis inhibition and mouse genetics
exposure
Genetic or pharmacological CoQ depletion and in-vitro repletion
limitations
Tissue-specific disease models; mouse residual percentages are not diagnostic human thresholds.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
Human fibroblasts/HeLa cells and Pdss2 mutant mice
plain_language
CoQ connects energy metabolism to sulfur disposal.
primary_references
[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
tissue_or_cell_type
Sulfide oxidation and tissue CoQ
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 528–539
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Patient fibroblasts, biosynthesis inhibition and mouse genetics · source_derived_draft · unverified_draft
### coq10-sqor-electron-acceptor CoQ serves as electron acceptor for SQOR at the start of mitochondrial sulfide oxidation. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: CoQ connects energy metabolism to sulfur disposal. organism: Human fibroblasts/HeLa cells and Pdss2 mutant mice tissue_or_cell_type: Sulfide oxidation and tissue CoQ experimental_model: Patient fibroblasts, biosynthesis inhibition and mouse genetics limitations: Tissue-specific disease models; mouse residual percentages are not diagnostic human thresholds. exposure: Genetic or pharmacological CoQ depletion and in-vitro repletion evidence_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"} [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
Complete structured claim and evidence
CoQ supplementation rescued sulfide-pathway biochemical abnormalities in deficient fibroblasts.
Coenzyme Q10 / CoQ10 redox system → Mitochondrial hydrogen sulfide oxidation source_derived_draftungraded
Experimental context and source evidence
evidence_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"}
experimental_model
Patient fibroblasts, biosynthesis inhibition and mouse genetics
exposure
Genetic or pharmacological CoQ depletion and in-vitro repletion
limitations
Tissue-specific disease models; mouse residual percentages are not diagnostic human thresholds.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
Human fibroblasts/HeLa cells and Pdss2 mutant mice
plain_language
Supplying the missing carrier improved the tested disposal pathway in cells.
primary_references
[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
tissue_or_cell_type
Sulfide oxidation and tissue CoQ
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 554–565
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Patient fibroblasts, biosynthesis inhibition and mouse genetics · source_derived_draft · unverified_draft
### coq10-coq-sulfide-rescue CoQ supplementation rescued sulfide-pathway biochemical abnormalities in deficient fibroblasts. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: Supplying the missing carrier improved the tested disposal pathway in cells. organism: Human fibroblasts/HeLa cells and Pdss2 mutant mice tissue_or_cell_type: Sulfide oxidation and tissue CoQ experimental_model: Patient fibroblasts, biosynthesis inhibition and mouse genetics limitations: Tissue-specific disease models; mouse residual percentages are not diagnostic human thresholds. exposure: Genetic or pharmacological CoQ depletion and in-vitro repletion evidence_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"} [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
Complete structured claim and evidence
Affected Pdss2-mutant kidneys accumulated sulfide and had reduced sulfide-oxidation pathway proteins.
Mouse Pdss2 → Renal hydrogen sulfide accumulation source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_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"}
experimental_model
Patient fibroblasts, biosynthesis inhibition and mouse genetics
exposure
Genetic or pharmacological CoQ depletion and in-vitro repletion
limitations
Tissue-specific disease models; mouse residual percentages are not diagnostic human thresholds.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
Human fibroblasts/HeLa cells and Pdss2 mutant mice
plain_language
The same mutation had different biochemical consequences in different tissues.
primary_references
[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
tissue_or_cell_type
Sulfide oxidation and tissue CoQ
trigger_kind
machinery_impairment Imported condition classification; unverified.
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 567–578
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Patient fibroblasts, biosynthesis inhibition and mouse genetics · source_derived_draft · unverified_draft
### coq10-kidney-sulfide Affected Pdss2-mutant kidneys accumulated sulfide and had reduced sulfide-oxidation pathway proteins. Condition category: machinery_impairment nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: The same mutation had different biochemical consequences in different tissues. organism: Human fibroblasts/HeLa cells and Pdss2 mutant mice tissue_or_cell_type: Sulfide oxidation and tissue CoQ experimental_model: Patient fibroblasts, biosynthesis inhibition and mouse genetics limitations: Tissue-specific disease models; mouse residual percentages are not diagnostic human thresholds. exposure: Genetic or pharmacological CoQ depletion and in-vitro repletion evidence_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"} [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
Complete structured claim and evidence
Pdss2-mutant kidneys had glutathione depletion, whereas the less CoQ-depleted brain lacked these abnormalities.
Mouse Pdss2 → GSH source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_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"}
experimental_model
Patient fibroblasts, biosynthesis inhibition and mouse genetics
exposure
Genetic or pharmacological CoQ depletion and in-vitro repletion
limitations
Tissue-specific disease models; mouse residual percentages are not diagnostic human thresholds.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
Human fibroblasts/HeLa cells and Pdss2 mutant mice
plain_language
The CoQ defect connected to another antioxidant pool in this kidney model.
primary_references
[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
tissue_or_cell_type
Sulfide oxidation and tissue CoQ
trigger_kind
machinery_impairment Imported condition classification; unverified.
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 580–591
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Patient fibroblasts, biosynthesis inhibition and mouse genetics · source_derived_draft · unverified_draft
### coq10-kidney-glutathione Pdss2-mutant kidneys had glutathione depletion, whereas the less CoQ-depleted brain lacked these abnormalities. Condition category: machinery_impairment nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: The CoQ defect connected to another antioxidant pool in this kidney model. organism: Human fibroblasts/HeLa cells and Pdss2 mutant mice tissue_or_cell_type: Sulfide oxidation and tissue CoQ experimental_model: Patient fibroblasts, biosynthesis inhibition and mouse genetics limitations: Tissue-specific disease models; mouse residual percentages are not diagnostic human thresholds. exposure: Genetic or pharmacological CoQ depletion and in-vitro repletion evidence_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"} [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
Complete structured claim and evidence
Purified reconstructed FDXR retained FAD.
Reconstructed ancestral tetrapod FDXR → FAD source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/38425362.fulltext.txt", "locator": "Primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "7d25af4ecd7340649536b8fea3b8a0a308a1611bbf8c57f6a79b362f443f1cba", "start_char": 9067, "end_char": 13813, "text_sha256": "49612ae4d3a59a75a02fe3fb132abd8aeb7ef8b7cae3b0f79b5557503c55ad51"}
experimental_model
Purified reconstructed COQ metabolon with short-chain substrates
exposure
Enzyme combinations, methyl donors, reductants and metal additions
limitations
Ancestral proteins and CoQ1 analogues; no clinical cofactor dose or proof of nutritional rate limitation. Reaction order need not be universal across species.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
Reconstructed ancestral tetrapod proteins
plain_language
A riboflavin-derived cofactor is part of the electron-supply machinery for synthesis.
primary_references
[coq10-p38425362] In vitro construction of the COQ metabolon unveils the molecular determinants of coenzyme Q biosynthesis. (2024). https://pubmed.ncbi.nlm.nih.gov/38425362/ DOI: 10.1038/s41929-023-01087-z
tissue_or_cell_type
Stepwise CoQ head-group assembly
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 593–604
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified reconstructed COQ metabolon with short-chain substrates · source_derived_draft · unverified_draft
### coq10-fdxr-fad Purified reconstructed FDXR retained FAD. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: A riboflavin-derived cofactor is part of the electron-supply machinery for synthesis. organism: Reconstructed ancestral tetrapod proteins tissue_or_cell_type: Stepwise CoQ head-group assembly experimental_model: Purified reconstructed COQ metabolon with short-chain substrates limitations: Ancestral proteins and CoQ1 analogues; no clinical cofactor dose or proof of nutritional rate limitation. Reaction order need not be universal across species. exposure: Enzyme combinations, methyl donors, reductants and metal additions evidence_span: {"source_cache": "artifacts/coq10-research/38425362.fulltext.txt", "locator": "Primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "7d25af4ecd7340649536b8fea3b8a0a308a1611bbf8c57f6a79b362f443f1cba", "start_char": 9067, "end_char": 13813, "text_sha256": "49612ae4d3a59a75a02fe3fb132abd8aeb7ef8b7cae3b0f79b5557503c55ad51"} [coq10-p38425362] In vitro construction of the COQ metabolon unveils the molecular determinants of coenzyme Q biosynthesis. (2024). https://pubmed.ncbi.nlm.nih.gov/38425362/ DOI: 10.1038/s41929-023-01087-z
Complete structured claim and evidence
Purified reconstructed FDX2 retained a two-iron, two-sulfur cluster.
Reconstructed ancestral tetrapod FDX2 → [2Fe-2S] iron-sulfur cluster source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/38425362.fulltext.txt", "locator": "Primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "7d25af4ecd7340649536b8fea3b8a0a308a1611bbf8c57f6a79b362f443f1cba", "start_char": 9067, "end_char": 13813, "text_sha256": "49612ae4d3a59a75a02fe3fb132abd8aeb7ef8b7cae3b0f79b5557503c55ad51"}
experimental_model
Purified reconstructed COQ metabolon with short-chain substrates
exposure
Enzyme combinations, methyl donors, reductants and metal additions
limitations
Ancestral proteins and CoQ1 analogues; no clinical cofactor dose or proof of nutritional rate limitation. Reaction order need not be universal across species.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
Reconstructed ancestral tetrapod proteins
plain_language
Iron participates in an electron-transfer component, not as a substitute for CoQ.
primary_references
[coq10-p38425362] In vitro construction of the COQ metabolon unveils the molecular determinants of coenzyme Q biosynthesis. (2024). https://pubmed.ncbi.nlm.nih.gov/38425362/ DOI: 10.1038/s41929-023-01087-z
tissue_or_cell_type
Stepwise CoQ head-group assembly
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 606–617
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified reconstructed COQ metabolon with short-chain substrates · source_derived_draft · unverified_draft
### coq10-fdx2-iron Purified reconstructed FDX2 retained a two-iron, two-sulfur cluster. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: Iron participates in an electron-transfer component, not as a substitute for CoQ. organism: Reconstructed ancestral tetrapod proteins tissue_or_cell_type: Stepwise CoQ head-group assembly experimental_model: Purified reconstructed COQ metabolon with short-chain substrates limitations: Ancestral proteins and CoQ1 analogues; no clinical cofactor dose or proof of nutritional rate limitation. Reaction order need not be universal across species. exposure: Enzyme combinations, methyl donors, reductants and metal additions evidence_span: {"source_cache": "artifacts/coq10-research/38425362.fulltext.txt", "locator": "Primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "7d25af4ecd7340649536b8fea3b8a0a308a1611bbf8c57f6a79b362f443f1cba", "start_char": 9067, "end_char": 13813, "text_sha256": "49612ae4d3a59a75a02fe3fb132abd8aeb7ef8b7cae3b0f79b5557503c55ad51"} [coq10-p38425362] In vitro construction of the COQ metabolon unveils the molecular determinants of coenzyme Q biosynthesis. (2024). https://pubmed.ncbi.nlm.nih.gov/38425362/ DOI: 10.1038/s41929-023-01087-z
Complete structured claim and evidence
FDX2 accepted electrons from reduced FDXR in the reconstructed system.
Reconstructed ancestral tetrapod FDXR → Reconstructed ancestral tetrapod FDX2 source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/38425362.fulltext.txt", "locator": "Primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "7d25af4ecd7340649536b8fea3b8a0a308a1611bbf8c57f6a79b362f443f1cba", "start_char": 9067, "end_char": 13813, "text_sha256": "49612ae4d3a59a75a02fe3fb132abd8aeb7ef8b7cae3b0f79b5557503c55ad51"}
experimental_model
Purified reconstructed COQ metabolon with short-chain substrates
exposure
Enzyme combinations, methyl donors, reductants and metal additions
limitations
Ancestral proteins and CoQ1 analogues; no clinical cofactor dose or proof of nutritional rate limitation. Reaction order need not be universal across species.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
Reconstructed ancestral tetrapod proteins
plain_language
The synthesis pathway has a separate relay supplying reducing power.
primary_references
[coq10-p38425362] In vitro construction of the COQ metabolon unveils the molecular determinants of coenzyme Q biosynthesis. (2024). https://pubmed.ncbi.nlm.nih.gov/38425362/ DOI: 10.1038/s41929-023-01087-z
tissue_or_cell_type
Stepwise CoQ head-group assembly
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 619–630
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified reconstructed COQ metabolon with short-chain substrates · source_derived_draft · unverified_draft
### coq10-fdxr-fdx2 FDX2 accepted electrons from reduced FDXR in the reconstructed system. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: The synthesis pathway has a separate relay supplying reducing power. organism: Reconstructed ancestral tetrapod proteins tissue_or_cell_type: Stepwise CoQ head-group assembly experimental_model: Purified reconstructed COQ metabolon with short-chain substrates limitations: Ancestral proteins and CoQ1 analogues; no clinical cofactor dose or proof of nutritional rate limitation. Reaction order need not be universal across species. exposure: Enzyme combinations, methyl donors, reductants and metal additions evidence_span: {"source_cache": "artifacts/coq10-research/38425362.fulltext.txt", "locator": "Primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "7d25af4ecd7340649536b8fea3b8a0a308a1611bbf8c57f6a79b362f443f1cba", "start_char": 9067, "end_char": 13813, "text_sha256": "49612ae4d3a59a75a02fe3fb132abd8aeb7ef8b7cae3b0f79b5557503c55ad51"} [coq10-p38425362] In vitro construction of the COQ metabolon unveils the molecular determinants of coenzyme Q biosynthesis. (2024). https://pubmed.ncbi.nlm.nih.gov/38425362/ DOI: 10.1038/s41929-023-01087-z
Complete structured claim and evidence
Reconstructed COQ4 catalyzed C1 decarboxylation without the C1 hydroxylation product in this assay.
Reconstructed ancestral tetrapod COQ4 → Coenzyme Q precursor C1 decarboxylation source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/38425362.fulltext.txt", "locator": "Primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "7d25af4ecd7340649536b8fea3b8a0a308a1611bbf8c57f6a79b362f443f1cba", "start_char": 17236, "end_char": 17638, "text_sha256": "a33802f50b3854ca1f866d40a31707302fc79c4ecfe2d9e4abdc73e1efe18152"}
experimental_model
Purified reconstructed COQ metabolon with short-chain substrates
exposure
Enzyme combinations, methyl donors, reductants and metal additions
limitations
Ancestral proteins and CoQ1 analogues; no clinical cofactor dose or proof of nutritional rate limitation. Reaction order need not be universal across species.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
Reconstructed ancestral tetrapod proteins
plain_language
Removing a carbon group and adding oxygen were separable in this reconstruction.
primary_references
[coq10-p38425362] In vitro construction of the COQ metabolon unveils the molecular determinants of coenzyme Q biosynthesis. (2024). https://pubmed.ncbi.nlm.nih.gov/38425362/ DOI: 10.1038/s41929-023-01087-z
tissue_or_cell_type
Stepwise CoQ head-group assembly
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 684–695
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified reconstructed COQ metabolon with short-chain substrates · source_derived_draft · unverified_draft
### coq10-coq4-decarboxylation Reconstructed COQ4 catalyzed C1 decarboxylation without the C1 hydroxylation product in this assay. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: Removing a carbon group and adding oxygen were separable in this reconstruction. organism: Reconstructed ancestral tetrapod proteins tissue_or_cell_type: Stepwise CoQ head-group assembly experimental_model: Purified reconstructed COQ metabolon with short-chain substrates limitations: Ancestral proteins and CoQ1 analogues; no clinical cofactor dose or proof of nutritional rate limitation. Reaction order need not be universal across species. exposure: Enzyme combinations, methyl donors, reductants and metal additions evidence_span: {"source_cache": "artifacts/coq10-research/38425362.fulltext.txt", "locator": "Primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "7d25af4ecd7340649536b8fea3b8a0a308a1611bbf8c57f6a79b362f443f1cba", "start_char": 17236, "end_char": 17638, "text_sha256": "a33802f50b3854ca1f866d40a31707302fc79c4ecfe2d9e4abdc73e1efe18152"} [coq10-p38425362] In vitro construction of the COQ metabolon unveils the molecular determinants of coenzyme Q biosynthesis. (2024). https://pubmed.ncbi.nlm.nih.gov/38425362/ DOI: 10.1038/s41929-023-01087-z
Complete structured claim and evidence
Reconstructed COQ6 supported C1 hydroxylation after the COQ4 decarboxylation step.
Reconstructed ancestral tetrapod COQ6 → Coenzyme Q precursor C1 hydroxylation source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/38425362.fulltext.txt", "locator": "Primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "7d25af4ecd7340649536b8fea3b8a0a308a1611bbf8c57f6a79b362f443f1cba", "start_char": 20281, "end_char": 22240, "text_sha256": "3fcbd5b3b192d3f28670b7d8b637f2d09e169f51fbdfe73fac36963e95ba973f"}
experimental_model
Purified reconstructed COQ metabolon with short-chain substrates
exposure
Enzyme combinations, methyl donors, reductants and metal additions
limitations
Ancestral proteins and CoQ1 analogues; no clinical cofactor dose or proof of nutritional rate limitation. Reaction order need not be universal across species.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
Reconstructed ancestral tetrapod proteins
plain_language
The next enzyme completed the other part of that transformation.
primary_references
[coq10-p38425362] In vitro construction of the COQ metabolon unveils the molecular determinants of coenzyme Q biosynthesis. (2024). https://pubmed.ncbi.nlm.nih.gov/38425362/ DOI: 10.1038/s41929-023-01087-z
tissue_or_cell_type
Stepwise CoQ head-group assembly
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 697–708
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified reconstructed COQ metabolon with short-chain substrates · source_derived_draft · unverified_draft
### coq10-coq6-c1 Reconstructed COQ6 supported C1 hydroxylation after the COQ4 decarboxylation step. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: The next enzyme completed the other part of that transformation. organism: Reconstructed ancestral tetrapod proteins tissue_or_cell_type: Stepwise CoQ head-group assembly experimental_model: Purified reconstructed COQ metabolon with short-chain substrates limitations: Ancestral proteins and CoQ1 analogues; no clinical cofactor dose or proof of nutritional rate limitation. Reaction order need not be universal across species. exposure: Enzyme combinations, methyl donors, reductants and metal additions evidence_span: {"source_cache": "artifacts/coq10-research/38425362.fulltext.txt", "locator": "Primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "7d25af4ecd7340649536b8fea3b8a0a308a1611bbf8c57f6a79b362f443f1cba", "start_char": 20281, "end_char": 22240, "text_sha256": "3fcbd5b3b192d3f28670b7d8b637f2d09e169f51fbdfe73fac36963e95ba973f"} [coq10-p38425362] In vitro construction of the COQ metabolon unveils the molecular determinants of coenzyme Q biosynthesis. (2024). https://pubmed.ncbi.nlm.nih.gov/38425362/ DOI: 10.1038/s41929-023-01087-z
Complete structured claim and evidence
Reconstructed COQ5 catalyzed C-methylation with SAM.
Reconstructed ancestral tetrapod COQ5 → S-Adenosyl-L-methionine source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/38425362.fulltext.txt", "locator": "Primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "7d25af4ecd7340649536b8fea3b8a0a308a1611bbf8c57f6a79b362f443f1cba", "start_char": 23488, "end_char": 27391, "text_sha256": "7147c9d517477cd7bbec4a155e5f13bc733d294380975977eba11b64517047f3"}
experimental_model
Purified reconstructed COQ metabolon with short-chain substrates
exposure
Enzyme combinations, methyl donors, reductants and metal additions
limitations
Ancestral proteins and CoQ1 analogues; no clinical cofactor dose or proof of nutritional rate limitation. Reaction order need not be universal across species.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
Reconstructed ancestral tetrapod proteins
plain_language
A second methylating enzyme links CoQ assembly to methyl-donor availability.
primary_references
[coq10-p38425362] In vitro construction of the COQ metabolon unveils the molecular determinants of coenzyme Q biosynthesis. (2024). https://pubmed.ncbi.nlm.nih.gov/38425362/ DOI: 10.1038/s41929-023-01087-z
tissue_or_cell_type
Stepwise CoQ head-group assembly
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 710–721
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified reconstructed COQ metabolon with short-chain substrates · source_derived_draft · unverified_draft
### coq10-coq5-sam Reconstructed COQ5 catalyzed C-methylation with SAM. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: A second methylating enzyme links CoQ assembly to methyl-donor availability. organism: Reconstructed ancestral tetrapod proteins tissue_or_cell_type: Stepwise CoQ head-group assembly experimental_model: Purified reconstructed COQ metabolon with short-chain substrates limitations: Ancestral proteins and CoQ1 analogues; no clinical cofactor dose or proof of nutritional rate limitation. Reaction order need not be universal across species. exposure: Enzyme combinations, methyl donors, reductants and metal additions evidence_span: {"source_cache": "artifacts/coq10-research/38425362.fulltext.txt", "locator": "Primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "7d25af4ecd7340649536b8fea3b8a0a308a1611bbf8c57f6a79b362f443f1cba", "start_char": 23488, "end_char": 27391, "text_sha256": "7147c9d517477cd7bbec4a155e5f13bc733d294380975977eba11b64517047f3"} [coq10-p38425362] In vitro construction of the COQ metabolon unveils the molecular determinants of coenzyme Q biosynthesis. (2024). https://pubmed.ncbi.nlm.nih.gov/38425362/ DOI: 10.1038/s41929-023-01087-z
Complete structured claim and evidence
COQ7 hydroxylation assays consumed NADH in a substrate-dependent manner.
Reconstructed ancestral tetrapod COQ7 → NADH source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/38425362.fulltext.txt", "locator": "Primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "7d25af4ecd7340649536b8fea3b8a0a308a1611bbf8c57f6a79b362f443f1cba", "start_char": 23488, "end_char": 27391, "text_sha256": "7147c9d517477cd7bbec4a155e5f13bc733d294380975977eba11b64517047f3"}
experimental_model
Purified reconstructed COQ metabolon with short-chain substrates
exposure
Enzyme combinations, methyl donors, reductants and metal additions
limitations
Ancestral proteins and CoQ1 analogues; no clinical cofactor dose or proof of nutritional rate limitation. Reaction order need not be universal across species.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
Reconstructed ancestral tetrapod proteins
plain_language
Niacin-derived reducing power also feeds a later synthesis step.
primary_references
[coq10-p38425362] In vitro construction of the COQ metabolon unveils the molecular determinants of coenzyme Q biosynthesis. (2024). https://pubmed.ncbi.nlm.nih.gov/38425362/ DOI: 10.1038/s41929-023-01087-z
tissue_or_cell_type
Stepwise CoQ head-group assembly
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 723–734
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified reconstructed COQ metabolon with short-chain substrates · source_derived_draft · unverified_draft
### coq10-coq7-nadh COQ7 hydroxylation assays consumed NADH in a substrate-dependent manner. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: Niacin-derived reducing power also feeds a later synthesis step. organism: Reconstructed ancestral tetrapod proteins tissue_or_cell_type: Stepwise CoQ head-group assembly experimental_model: Purified reconstructed COQ metabolon with short-chain substrates limitations: Ancestral proteins and CoQ1 analogues; no clinical cofactor dose or proof of nutritional rate limitation. Reaction order need not be universal across species. exposure: Enzyme combinations, methyl donors, reductants and metal additions evidence_span: {"source_cache": "artifacts/coq10-research/38425362.fulltext.txt", "locator": "Primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "7d25af4ecd7340649536b8fea3b8a0a308a1611bbf8c57f6a79b362f443f1cba", "start_char": 23488, "end_char": 27391, "text_sha256": "7147c9d517477cd7bbec4a155e5f13bc733d294380975977eba11b64517047f3"} [coq10-p38425362] In vitro construction of the COQ metabolon unveils the molecular determinants of coenzyme Q biosynthesis. (2024). https://pubmed.ncbi.nlm.nih.gov/38425362/ DOI: 10.1038/s41929-023-01087-z
Complete structured claim and evidence
Adding COQ9 increased COQ7 catalytic efficiency about 1.5-fold in the reconstructed system.
Reconstructed ancestral tetrapod COQ9 → Reconstructed ancestral tetrapod COQ7 source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/38425362.fulltext.txt", "locator": "Primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "7d25af4ecd7340649536b8fea3b8a0a308a1611bbf8c57f6a79b362f443f1cba", "start_char": 23488, "end_char": 27391, "text_sha256": "7147c9d517477cd7bbec4a155e5f13bc733d294380975977eba11b64517047f3"}
experimental_model
Purified reconstructed COQ metabolon with short-chain substrates
exposure
Enzyme combinations, methyl donors, reductants and metal additions
limitations
Ancestral proteins and CoQ1 analogues; no clinical cofactor dose or proof of nutritional rate limitation. Reaction order need not be universal across species.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
Reconstructed ancestral tetrapod proteins
plain_language
A helper protein improved the neighboring enzyme reaction.
primary_references
[coq10-p38425362] In vitro construction of the COQ metabolon unveils the molecular determinants of coenzyme Q biosynthesis. (2024). https://pubmed.ncbi.nlm.nih.gov/38425362/ DOI: 10.1038/s41929-023-01087-z
tissue_or_cell_type
Stepwise CoQ head-group assembly
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 736–747
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified reconstructed COQ metabolon with short-chain substrates · source_derived_draft · unverified_draft
### coq10-coq9-assistance Adding COQ9 increased COQ7 catalytic efficiency about 1.5-fold in the reconstructed system. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: A helper protein improved the neighboring enzyme reaction. organism: Reconstructed ancestral tetrapod proteins tissue_or_cell_type: Stepwise CoQ head-group assembly experimental_model: Purified reconstructed COQ metabolon with short-chain substrates limitations: Ancestral proteins and CoQ1 analogues; no clinical cofactor dose or proof of nutritional rate limitation. Reaction order need not be universal across species. exposure: Enzyme combinations, methyl donors, reductants and metal additions evidence_span: {"source_cache": "artifacts/coq10-research/38425362.fulltext.txt", "locator": "Primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "7d25af4ecd7340649536b8fea3b8a0a308a1611bbf8c57f6a79b362f443f1cba", "start_char": 23488, "end_char": 27391, "text_sha256": "7147c9d517477cd7bbec4a155e5f13bc733d294380975977eba11b64517047f3"} [coq10-p38425362] In vitro construction of the COQ metabolon unveils the molecular determinants of coenzyme Q biosynthesis. (2024). https://pubmed.ncbi.nlm.nih.gov/38425362/ DOI: 10.1038/s41929-023-01087-z
Complete structured claim and evidence
COQ4 expression supported an oxidative-decarboxylation route combining C1 carbon removal with hydroxylation.
Human COQ4 biosynthesis protein → Coenzyme Q precursor C1 hydroxylation source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/38295803.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "82bbf9ebf67bcf7d7d22a428dc8d13f75a6210d75abea0e0fb40064d368a3dfb", "start_char": 0, "end_char": 1019, "text_sha256": "82bbf9ebf67bcf7d7d22a428dc8d13f75a6210d75abea0e0fb40064d368a3dfb"}
experimental_model
Genetic complementation and heterologous product analysis
exposure
COQ4 expression in deficient E. coli and non-CoQ-producing Corynebacterium
limitations
Supports oxidative decarboxylation in these systems. Compare with the separate steps in ancestral reconstruction; model and substrate differences remain unresolved.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
Eukaryotic COQ4 expressed in bacterial systems
plain_language
This cellular reconstruction assigned both parts to COQ4.
primary_references
[coq10-p38295803] COQ4 is required for the oxidative decarboxylation of the C1 carbon of coenzyme Q in eukaryotic cells. (2024). https://pubmed.ncbi.nlm.nih.gov/38295803/ DOI: 10.1016/j.molcel.2024.01.003
tissue_or_cell_type
CoQ head-group C1 modification
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 749–760
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Genetic complementation and heterologous product analysis · source_derived_draft · unverified_draft
### coq10-coq4-oxidative COQ4 expression supported an oxidative-decarboxylation route combining C1 carbon removal with hydroxylation. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: This cellular reconstruction assigned both parts to COQ4. organism: Eukaryotic COQ4 expressed in bacterial systems tissue_or_cell_type: CoQ head-group C1 modification experimental_model: Genetic complementation and heterologous product analysis limitations: Supports oxidative decarboxylation in these systems. Compare with the separate steps in ancestral reconstruction; model and substrate differences remain unresolved. exposure: COQ4 expression in deficient E. coli and non-CoQ-producing Corynebacterium evidence_span: {"source_cache": "artifacts/coq10-research/38295803.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "82bbf9ebf67bcf7d7d22a428dc8d13f75a6210d75abea0e0fb40064d368a3dfb", "start_char": 0, "end_char": 1019, "text_sha256": "82bbf9ebf67bcf7d7d22a428dc8d13f75a6210d75abea0e0fb40064d368a3dfb"} [coq10-p38295803] COQ4 is required for the oxidative decarboxylation of the C1 carbon of coenzyme Q in eukaryotic cells. (2024). https://pubmed.ncbi.nlm.nih.gov/38295803/ DOI: 10.1016/j.molcel.2024.01.003
Complete structured claim and evidence
Comparison with selenium-deprived and truncated mammalian TrxR forms showed selenium-dependent ubiquinone reduction.
TXNRD1 → Ubiquinone-10 source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/coq10-research/12435734.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "929e8de2bc15ea62eb4a3814995fd289de759d721f16b848174ad65f95847c55", "start_char": 0, "end_char": 1340, "text_sha256": "929e8de2bc15ea62eb4a3814995fd289de759d721f16b848174ad65f95847c55"}
experimental_model
Enzyme kinetics, mutants and overexpressing-cell homogenates
exposure
NADPH or NADH; selenite and selenium-deprived enzyme variants
limitations
Biochemical selenium dependence; not proof that all CoQ recycling stops with low selenium or that combined supplements are synergistic clinically.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
Mammalian TrxR1 and human HEK293 cells
plain_language
The chemistry depends on the enzyme being assembled correctly.
primary_references
[coq10-p12435734] The mammalian cytosolic selenoenzyme thioredoxin reductase reduces ubiquinone. A novel mechanism for defense against oxidative stress. (2003). https://pubmed.ncbi.nlm.nih.gov/12435734/ DOI: 10.1074/jbc.m210456200
tissue_or_cell_type
Ubiquinone reduction
trigger_kind
machinery_impairment Imported condition classification; unverified.
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 775–786
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Enzyme kinetics, mutants and overexpressing-cell homogenates · source_derived_draft · unverified_draft
### coq10-txnrd-selenium Comparison with selenium-deprived and truncated mammalian TrxR forms showed selenium-dependent ubiquinone reduction. Condition category: machinery_impairment nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: The chemistry depends on the enzyme being assembled correctly. organism: Mammalian TrxR1 and human HEK293 cells tissue_or_cell_type: Ubiquinone reduction experimental_model: Enzyme kinetics, mutants and overexpressing-cell homogenates limitations: Biochemical selenium dependence; not proof that all CoQ recycling stops with low selenium or that combined supplements are synergistic clinically. exposure: NADPH or NADH; selenite and selenium-deprived enzyme variants evidence_span: {"source_cache": "artifacts/coq10-research/12435734.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "929e8de2bc15ea62eb4a3814995fd289de759d721f16b848174ad65f95847c55", "start_char": 0, "end_char": 1340, "text_sha256": "929e8de2bc15ea62eb4a3814995fd289de759d721f16b848174ad65f95847c55"} [coq10-p12435734] The mammalian cytosolic selenoenzyme thioredoxin reductase reduces ubiquinone. A novel mechanism for defense against oxidative stress. (2003). https://pubmed.ncbi.nlm.nih.gov/12435734/ DOI: 10.1074/jbc.m210456200
Complete structured claim and evidence
Selenite treatment increased cytosolic TrxR activity together with ubiquinone reduction in the tested cell homogenates.
Selenite ion → TrxR1-associated ubiquinone reductase activity source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/12435734.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "929e8de2bc15ea62eb4a3814995fd289de759d721f16b848174ad65f95847c55", "start_char": 0, "end_char": 1340, "text_sha256": "929e8de2bc15ea62eb4a3814995fd289de759d721f16b848174ad65f95847c55"}
experimental_model
Enzyme kinetics, mutants and overexpressing-cell homogenates
exposure
NADPH or NADH; selenite and selenium-deprived enzyme variants
limitations
Cell-culture exposure; no clinical supplement ratio or systemic outcome was tested.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
Mammalian TrxR1 and human HEK293 cells
plain_language
A cell experiment connected selenium supply with CoQ recycling capacity.
primary_references
[coq10-p12435734] The mammalian cytosolic selenoenzyme thioredoxin reductase reduces ubiquinone. A novel mechanism for defense against oxidative stress. (2003). https://pubmed.ncbi.nlm.nih.gov/12435734/ DOI: 10.1074/jbc.m210456200
tissue_or_cell_type
Ubiquinone reduction
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 788–799
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Enzyme kinetics, mutants and overexpressing-cell homogenates · source_derived_draft · unverified_draft
### coq10-selenite-cell-recycling Selenite treatment increased cytosolic TrxR activity together with ubiquinone reduction in the tested cell homogenates. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: A cell experiment connected selenium supply with CoQ recycling capacity. organism: Mammalian TrxR1 and human HEK293 cells tissue_or_cell_type: Ubiquinone reduction experimental_model: Enzyme kinetics, mutants and overexpressing-cell homogenates limitations: Cell-culture exposure; no clinical supplement ratio or systemic outcome was tested. exposure: NADPH or NADH; selenite and selenium-deprived enzyme variants evidence_span: {"source_cache": "artifacts/coq10-research/12435734.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "929e8de2bc15ea62eb4a3814995fd289de759d721f16b848174ad65f95847c55", "start_char": 0, "end_char": 1340, "text_sha256": "929e8de2bc15ea62eb4a3814995fd289de759d721f16b848174ad65f95847c55"} [coq10-p12435734] The mammalian cytosolic selenoenzyme thioredoxin reductase reduces ubiquinone. A novel mechanism for defense against oxidative stress. (2003). https://pubmed.ncbi.nlm.nih.gov/12435734/ DOI: 10.1074/jbc.m210456200
Complete structured claim and evidence
FSP1 used NAD(P)H to regenerate the reduced CoQ pool that traps lipid peroxyl radicals.
NADPH → FSP1 / AIFM2 source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/31634899.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1e96f6d5aed6def29533d907cd9ae90bc287d3f7beb6b9447aec3308d57a0dfe", "start_char": 0, "end_char": 1818, "text_sha256": "1e96f6d5aed6def29533d907cd9ae90bc287d3f7beb6b9447aec3308d57a0dfe"}
experimental_model
Expression cloning and cell-death experiments
exposure
GPX4 deletion or inhibitors and FSP1 manipulation
limitations
Cancer-cell defense mechanism; preventing ferroptosis is not always a desirable disease outcome and oral CoQ benefit is not tested.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
Human cancer-cell models
plain_language
The antioxidant form must be regenerated using reducing power.
primary_references
[coq10-p31634899] FSP1 is a glutathione-independent ferroptosis suppressor. (2019). https://pubmed.ncbi.nlm.nih.gov/31634899/ DOI: 10.1038/s41586-019-1707-0
tissue_or_cell_type
FSP1-CoQ antioxidant pathway
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 801–812
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Expression cloning and cell-death experiments · source_derived_draft · unverified_draft
### coq10-fsp1-nadph FSP1 used NAD(P)H to regenerate the reduced CoQ pool that traps lipid peroxyl radicals. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: The antioxidant form must be regenerated using reducing power. organism: Human cancer-cell models tissue_or_cell_type: FSP1-CoQ antioxidant pathway experimental_model: Expression cloning and cell-death experiments limitations: Cancer-cell defense mechanism; preventing ferroptosis is not always a desirable disease outcome and oral CoQ benefit is not tested. exposure: GPX4 deletion or inhibitors and FSP1 manipulation evidence_span: {"source_cache": "artifacts/coq10-research/31634899.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1e96f6d5aed6def29533d907cd9ae90bc287d3f7beb6b9447aec3308d57a0dfe", "start_char": 0, "end_char": 1818, "text_sha256": "1e96f6d5aed6def29533d907cd9ae90bc287d3f7beb6b9447aec3308d57a0dfe"} [coq10-p31634899] FSP1 is a glutathione-independent ferroptosis suppressor. (2019). https://pubmed.ncbi.nlm.nih.gov/31634899/ DOI: 10.1038/s41586-019-1707-0
Complete structured claim and evidence
DHODH inactivation increased mitochondrial lipid peroxidation and ferroptosis in the reported GPX4-dependent experimental contexts.
Human dihydroorotate dehydrogenase / DHODH → Mitochondrial membrane lipid peroxidation source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/coq10-research/33981038.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "b1af5a97412b5ebf797083a069385c4ed98258e68845692732448bfe061a453b", "start_char": 0, "end_char": 1716, "text_sha256": "b1af5a97412b5ebf797083a069385c4ed98258e68845692732448bfe061a453b"}
experimental_model
Genetic and pharmacological cancer-cell studies
exposure
DHODH loss or brequinar, with GPX4 inhibition
limitations
Pharmacological attribution and relative DHODH contribution were directly challenged in 2023; preserve the dispute rather than generalizing to dietary CoQ effects.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
Human cancer-cell and tumor models
plain_language
The effect depended on which other defense route remained available.
primary_references
[coq10-p33981038] DHODH-mediated ferroptosis defence is a targetable vulnerability in cancer. (2021). https://pubmed.ncbi.nlm.nih.gov/33981038/ DOI: 10.1038/s41586-021-03539-7
tissue_or_cell_type
Mitochondrial ferroptosis defense
trigger_kind
machinery_impairment Imported condition classification; unverified.
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 827–838
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Genetic and pharmacological cancer-cell studies · source_derived_draft · unverified_draft
### coq10-dhodh-loss DHODH inactivation increased mitochondrial lipid peroxidation and ferroptosis in the reported GPX4-dependent experimental contexts. Condition category: machinery_impairment nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: The effect depended on which other defense route remained available. organism: Human cancer-cell and tumor models tissue_or_cell_type: Mitochondrial ferroptosis defense experimental_model: Genetic and pharmacological cancer-cell studies limitations: Pharmacological attribution and relative DHODH contribution were directly challenged in 2023; preserve the dispute rather than generalizing to dietary CoQ effects. exposure: DHODH loss or brequinar, with GPX4 inhibition evidence_span: {"source_cache": "artifacts/coq10-research/33981038.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "b1af5a97412b5ebf797083a069385c4ed98258e68845692732448bfe061a453b", "start_char": 0, "end_char": 1716, "text_sha256": "b1af5a97412b5ebf797083a069385c4ed98258e68845692732448bfe061a453b"} [coq10-p33981038] DHODH-mediated ferroptosis defence is a targetable vulnerability in cancer. (2021). https://pubmed.ncbi.nlm.nih.gov/33981038/ DOI: 10.1038/s41586-021-03539-7
Complete structured claim and evidence
The 2023 study attributed strong ferroptosis sensitization by high concentrations of DHODH inhibitors to concurrent FSP1 inhibition.
Brequinar → FSP1 / AIFM2 source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/37407687.publisher-preview.txt", "locator": "Primary public publisher preview, reference superscripts removed; zero-based, end-exclusive Unicode character offsets", "file_sha256": "dd04682c5ac5215eff4a195cf2fcff7c5f6cf59eb659cc5710e6a2ecd09b0529", "start_char": 0, "end_char": 477, "text_sha256": "dd04682c5ac5215eff4a195cf2fcff7c5f6cf59eb659cc5710e6a2ecd09b0529"}
experimental_model
Primary experimental Matters Arising; public publisher preview
exposure
DHODH inhibitors at different concentrations
limitations
Public preview only; exact dose-response tables not extracted. Do not deny all DHODH effects or invent a universal concentration cutoff.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
Cancer-cell inhibitor and genetic comparisons
plain_language
A drug can affect a second enzyme, changing the explanation of its result.
primary_references
[coq10-p37407687] DHODH inhibitors sensitize to ferroptosis by FSP1 inhibition. (2023). https://pubmed.ncbi.nlm.nih.gov/37407687/ DOI: 10.1038/s41586-023-06269-0
tissue_or_cell_type
DHODH versus FSP1 attribution
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 840–851
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Primary experimental Matters Arising; public publisher preview · source_derived_draft · unverified_draft
### coq10-dhodh-offtarget The 2023 study attributed strong ferroptosis sensitization by high concentrations of DHODH inhibitors to concurrent FSP1 inhibition. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: A drug can affect a second enzyme, changing the explanation of its result. organism: Cancer-cell inhibitor and genetic comparisons tissue_or_cell_type: DHODH versus FSP1 attribution experimental_model: Primary experimental Matters Arising; public publisher preview limitations: Public preview only; exact dose-response tables not extracted. Do not deny all DHODH effects or invent a universal concentration cutoff. exposure: DHODH inhibitors at different concentrations evidence_span: {"source_cache": "artifacts/coq10-research/37407687.publisher-preview.txt", "locator": "Primary public publisher preview, reference superscripts removed; zero-based, end-exclusive Unicode character offsets", "file_sha256": "dd04682c5ac5215eff4a195cf2fcff7c5f6cf59eb659cc5710e6a2ecd09b0529", "start_char": 0, "end_char": 477, "text_sha256": "dd04682c5ac5215eff4a195cf2fcff7c5f6cf59eb659cc5710e6a2ecd09b0529"} [coq10-p37407687] DHODH inhibitors sensitize to ferroptosis by FSP1 inhibition. (2023). https://pubmed.ncbi.nlm.nih.gov/37407687/ DOI: 10.1038/s41586-023-06269-0
Complete structured claim and evidence
GPD2 coupled glycerol-3-phosphate oxidation to ubiquinol formation.
Human mitochondrial glycerol-3-phosphate dehydrogenase / GPD2 → Ubiquinone source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/35749365.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "8d8219ff3cd63697715c88c25a9e558315bcd95c25bbc38f76987544bfee7581", "start_char": 0, "end_char": 1142, "text_sha256": "8d8219ff3cd63697715c88c25a9e558315bcd95c25bbc38f76987544bfee7581"}
experimental_model
Metabolomics, genetic deletion and tumor experiments
exposure
G3P supply and GPD2/GPX4 loss
limitations
Preclinical mechanism; no evidence that glycerol or CoQ supplements treat cancer.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
Cancer-cell and tumor models
plain_language
Another metabolic input feeds the same reduced CoQ pool.
primary_references
[coq10-p35749365] A ferroptosis defense mechanism mediated by glycerol-3-phosphate dehydrogenase 2 in mitochondria. (2022). https://pubmed.ncbi.nlm.nih.gov/35749365/ DOI: 10.1073/pnas.2121987119
tissue_or_cell_type
Mitochondrial glycerol-phosphate oxidation
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 853–864
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Metabolomics, genetic deletion and tumor experiments · source_derived_draft · unverified_draft
### coq10-gpd2-quinol GPD2 coupled glycerol-3-phosphate oxidation to ubiquinol formation. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: Another metabolic input feeds the same reduced CoQ pool. organism: Cancer-cell and tumor models tissue_or_cell_type: Mitochondrial glycerol-phosphate oxidation experimental_model: Metabolomics, genetic deletion and tumor experiments limitations: Preclinical mechanism; no evidence that glycerol or CoQ supplements treat cancer. exposure: G3P supply and GPD2/GPX4 loss evidence_span: {"source_cache": "artifacts/coq10-research/35749365.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "8d8219ff3cd63697715c88c25a9e558315bcd95c25bbc38f76987544bfee7581", "start_char": 0, "end_char": 1142, "text_sha256": "8d8219ff3cd63697715c88c25a9e558315bcd95c25bbc38f76987544bfee7581"} [coq10-p35749365] A ferroptosis defense mechanism mediated by glycerol-3-phosphate dehydrogenase 2 in mitochondria. (2022). https://pubmed.ncbi.nlm.nih.gov/35749365/ DOI: 10.1073/pnas.2121987119
Complete structured claim and evidence
GPD2 deletion sensitized cancer cells to GPX4-inhibition-induced mitochondrial lipid peroxidation and ferroptosis.
Human mitochondrial glycerol-3-phosphate dehydrogenase / GPD2 → Mitochondrial membrane lipid peroxidation source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/coq10-research/35749365.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "8d8219ff3cd63697715c88c25a9e558315bcd95c25bbc38f76987544bfee7581", "start_char": 0, "end_char": 1142, "text_sha256": "8d8219ff3cd63697715c88c25a9e558315bcd95c25bbc38f76987544bfee7581"}
experimental_model
Metabolomics, genetic deletion and tumor experiments
exposure
G3P supply and GPD2/GPX4 loss
limitations
Preclinical mechanism; no evidence that glycerol or CoQ supplements treat cancer.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
Cancer-cell and tumor models
plain_language
Dependence on one pathway changed when the parallel defense was blocked.
primary_references
[coq10-p35749365] A ferroptosis defense mechanism mediated by glycerol-3-phosphate dehydrogenase 2 in mitochondria. (2022). https://pubmed.ncbi.nlm.nih.gov/35749365/ DOI: 10.1073/pnas.2121987119
tissue_or_cell_type
Mitochondrial glycerol-phosphate oxidation
trigger_kind
machinery_impairment Imported condition classification; unverified.
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 866–877
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Metabolomics, genetic deletion and tumor experiments · source_derived_draft · unverified_draft
### coq10-gpd2-loss GPD2 deletion sensitized cancer cells to GPX4-inhibition-induced mitochondrial lipid peroxidation and ferroptosis. Condition category: machinery_impairment nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: Dependence on one pathway changed when the parallel defense was blocked. organism: Cancer-cell and tumor models tissue_or_cell_type: Mitochondrial glycerol-phosphate oxidation experimental_model: Metabolomics, genetic deletion and tumor experiments limitations: Preclinical mechanism; no evidence that glycerol or CoQ supplements treat cancer. exposure: G3P supply and GPD2/GPX4 loss evidence_span: {"source_cache": "artifacts/coq10-research/35749365.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "8d8219ff3cd63697715c88c25a9e558315bcd95c25bbc38f76987544bfee7581", "start_char": 0, "end_char": 1142, "text_sha256": "8d8219ff3cd63697715c88c25a9e558315bcd95c25bbc38f76987544bfee7581"} [coq10-p35749365] A ferroptosis defense mechanism mediated by glycerol-3-phosphate dehydrogenase 2 in mitochondria. (2022). https://pubmed.ncbi.nlm.nih.gov/35749365/ DOI: 10.1073/pnas.2121987119
Complete structured claim and evidence
The tested water-soluble formulation had 2.4-fold higher baseline-corrected exposure than standard ubiquinone capsules; the ubiquinol-capsule comparison was not statistically significant.
Coenzyme Q10 / CoQ10 redox system → Plasma coenzyme Q10 concentration source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/32188111.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "651570863e9a81a09c85040d74da26366d5b9f94145d97cac6aad48378597ce6", "start_char": 0, "end_char": 1662, "text_sha256": "651570863e9a81a09c85040d74da26366d5b9f94145d97cac6aad48378597ce6"}
experimental_model
Randomized three-period crossover pharmacokinetic study
exposure
Single equivalent 100-mg doses in three formulations
limitations
Small single-dose formulation comparison; plasma exposure is not tissue delivery or clinical efficacy. Product-specific findings cannot rank every ubiquinone or ubiquinol product.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
21 healthy adults aged 65-74
plain_language
The formulation mattered; the redox-form label alone did not establish superiority.
primary_references
[coq10-p32188111] Comparative Bioavailability of Different Coenzyme Q10 Formulations in Healthy Elderly Individuals. (2020). https://pubmed.ncbi.nlm.nih.gov/32188111/ DOI: 10.3390/nu12030784
tissue_or_cell_type
Plasma total CoQ and redox state over 48 hours
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 879–890
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Randomized three-period crossover pharmacokinetic study · source_derived_draft · unverified_draft
### coq10-formulation-exposure The tested water-soluble formulation had 2.4-fold higher baseline-corrected exposure than standard ubiquinone capsules; the ubiquinol-capsule comparison was not statistically significant. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: The formulation mattered; the redox-form label alone did not establish superiority. organism: 21 healthy adults aged 65-74 tissue_or_cell_type: Plasma total CoQ and redox state over 48 hours experimental_model: Randomized three-period crossover pharmacokinetic study limitations: Small single-dose formulation comparison; plasma exposure is not tissue delivery or clinical efficacy. Product-specific findings cannot rank every ubiquinone or ubiquinol product. exposure: Single equivalent 100-mg doses in three formulations evidence_span: {"source_cache": "artifacts/coq10-research/32188111.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "651570863e9a81a09c85040d74da26366d5b9f94145d97cac6aad48378597ce6", "start_char": 0, "end_char": 1662, "text_sha256": "651570863e9a81a09c85040d74da26366d5b9f94145d97cac6aad48378597ce6"} [coq10-p32188111] Comparative Bioavailability of Different Coenzyme Q10 Formulations in Healthy Elderly Individuals. (2020). https://pubmed.ncbi.nlm.nih.gov/32188111/ DOI: 10.3390/nu12030784
Complete structured claim and evidence
CoQ appeared in blood predominantly as ubiquinol regardless of which of the tested redox forms was consumed.
Ubiquinone-10 → Reduced CoQ10 source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/32188111.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "651570863e9a81a09c85040d74da26366d5b9f94145d97cac6aad48378597ce6", "start_char": 0, "end_char": 1662, "text_sha256": "651570863e9a81a09c85040d74da26366d5b9f94145d97cac6aad48378597ce6"}
experimental_model
Randomized three-period crossover pharmacokinetic study
exposure
Single equivalent 100-mg doses in three formulations
limitations
Small single-dose formulation comparison; plasma exposure is not tissue delivery or clinical efficacy. Product-specific findings cannot rank every ubiquinone or ubiquinol product.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
21 healthy adults aged 65-74
plain_language
The form swallowed and the form circulating are not necessarily the same.
primary_references
[coq10-p32188111] Comparative Bioavailability of Different Coenzyme Q10 Formulations in Healthy Elderly Individuals. (2020). https://pubmed.ncbi.nlm.nih.gov/32188111/ DOI: 10.3390/nu12030784
tissue_or_cell_type
Plasma total CoQ and redox state over 48 hours
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 892–903
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Randomized three-period crossover pharmacokinetic study · source_derived_draft · unverified_draft
### coq10-oral-redox CoQ appeared in blood predominantly as ubiquinol regardless of which of the tested redox forms was consumed. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: The form swallowed and the form circulating are not necessarily the same. organism: 21 healthy adults aged 65-74 tissue_or_cell_type: Plasma total CoQ and redox state over 48 hours experimental_model: Randomized three-period crossover pharmacokinetic study limitations: Small single-dose formulation comparison; plasma exposure is not tissue delivery or clinical efficacy. Product-specific findings cannot rank every ubiquinone or ubiquinol product. exposure: Single equivalent 100-mg doses in three formulations evidence_span: {"source_cache": "artifacts/coq10-research/32188111.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "651570863e9a81a09c85040d74da26366d5b9f94145d97cac6aad48378597ce6", "start_char": 0, "end_char": 1662, "text_sha256": "651570863e9a81a09c85040d74da26366d5b9f94145d97cac6aad48378597ce6"} [coq10-p32188111] Comparative Bioavailability of Different Coenzyme Q10 Formulations in Healthy Elderly Individuals. (2020). https://pubmed.ncbi.nlm.nih.gov/32188111/ DOI: 10.3390/nu12030784
Complete structured claim and evidence
Simvastatin inhibits HMG-CoA reductase, an upstream enzyme in the mevalonate pathway shared by sterol and CoQ precursor production.
Simvastatin → HMG-CoA reductase (HMGCR) source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/7828383.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e6aac0f5f784ab8a43755c6c878ea010b8673acc19bfa41f7a1272880c745197", "start_char": 0, "end_char": 800, "text_sha256": "e6aac0f5f784ab8a43755c6c878ea010b8673acc19bfa41f7a1272880c745197"}
experimental_model
Short-term treatment with serum and muscle sampling
exposure
Four weeks of simvastatin
limitations
Established biochemical background described in this primary report; enzyme target engagement was not the independent endpoint of this serum/muscle study.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
Humans with hypercholesterolemia
plain_language
A cholesterol-lowering drug acts upstream of more than cholesterol.
primary_references
[coq10-p7828383] Decreases in serum ubiquinone concentrations do not result in reduced levels in muscle tissue during short-term simvastatin treatment in humans. (1995). https://pubmed.ncbi.nlm.nih.gov/7828383/ DOI: 10.1016/0009-9236(95)90266-x
tissue_or_cell_type
Serum versus skeletal-muscle CoQ
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 905–916
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Short-term treatment with serum and muscle sampling · source_derived_draft · unverified_draft
### coq10-statin-target Simvastatin inhibits HMG-CoA reductase, an upstream enzyme in the mevalonate pathway shared by sterol and CoQ precursor production. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: A cholesterol-lowering drug acts upstream of more than cholesterol. organism: Humans with hypercholesterolemia tissue_or_cell_type: Serum versus skeletal-muscle CoQ experimental_model: Short-term treatment with serum and muscle sampling limitations: Established biochemical background described in this primary report; enzyme target engagement was not the independent endpoint of this serum/muscle study. exposure: Four weeks of simvastatin evidence_span: {"source_cache": "artifacts/coq10-research/7828383.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e6aac0f5f784ab8a43755c6c878ea010b8673acc19bfa41f7a1272880c745197", "start_char": 0, "end_char": 800, "text_sha256": "e6aac0f5f784ab8a43755c6c878ea010b8673acc19bfa41f7a1272880c745197"} [coq10-p7828383] Decreases in serum ubiquinone concentrations do not result in reduced levels in muscle tissue during short-term simvastatin treatment in humans. (1995). https://pubmed.ncbi.nlm.nih.gov/7828383/ DOI: 10.1016/0009-9236(95)90266-x
Complete structured claim and evidence
After four weeks, serum ubiquinone decreased while muscle ubiquinone increased; no participant developed myopathy.
Simvastatin → Muscle coenzyme Q10 concentration source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/7828383.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e6aac0f5f784ab8a43755c6c878ea010b8673acc19bfa41f7a1272880c745197", "start_char": 0, "end_char": 800, "text_sha256": "e6aac0f5f784ab8a43755c6c878ea010b8673acc19bfa41f7a1272880c745197"}
experimental_model
Short-term treatment with serum and muscle sampling
exposure
Four weeks of simvastatin
limitations
Small short-term study; serum and muscle moved differently. No participants developed myopathy; this does not exclude other regimens or vulnerable patients.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
Humans with hypercholesterolemia
plain_language
A falling blood result did not mean falling muscle supply in this study.
primary_references
[coq10-p7828383] Decreases in serum ubiquinone concentrations do not result in reduced levels in muscle tissue during short-term simvastatin treatment in humans. (1995). https://pubmed.ncbi.nlm.nih.gov/7828383/ DOI: 10.1016/0009-9236(95)90266-x
tissue_or_cell_type
Serum versus skeletal-muscle CoQ
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 918–929
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Short-term treatment with serum and muscle sampling · source_derived_draft · unverified_draft
### coq10-statin-serum-muscle After four weeks, serum ubiquinone decreased while muscle ubiquinone increased; no participant developed myopathy. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: A falling blood result did not mean falling muscle supply in this study. organism: Humans with hypercholesterolemia tissue_or_cell_type: Serum versus skeletal-muscle CoQ experimental_model: Short-term treatment with serum and muscle sampling limitations: Small short-term study; serum and muscle moved differently. No participants developed myopathy; this does not exclude other regimens or vulnerable patients. exposure: Four weeks of simvastatin evidence_span: {"source_cache": "artifacts/coq10-research/7828383.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e6aac0f5f784ab8a43755c6c878ea010b8673acc19bfa41f7a1272880c745197", "start_char": 0, "end_char": 800, "text_sha256": "e6aac0f5f784ab8a43755c6c878ea010b8673acc19bfa41f7a1272880c745197"} [coq10-p7828383] Decreases in serum ubiquinone concentrations do not result in reduced levels in muscle tissue during short-term simvastatin treatment in humans. (1995). https://pubmed.ncbi.nlm.nih.gov/7828383/ DOI: 10.1016/0009-9236(95)90266-x
Complete structured claim and evidence
Simvastatin, alone or with ezetimibe, lowered plasma CoQ; CoQ change correlated with LDL-cholesterol change and the CoQ-to-LDL ratio increased.
Simvastatin → Plasma coenzyme Q10 concentration source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/16872244.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "65abd11b5f58ce1125f554d52ed5203575d7a3ba0d20b789abce16148f3b5e27", "start_char": 0, "end_char": 2245, "text_sha256": "65abd11b5f58ce1125f554d52ed5203575d7a3ba0d20b789abce16148f3b5e27"}
experimental_model
Randomized three-arm parallel study
exposure
Simvastatin 40 mg/day, ezetimibe 10 mg/day or both for 14 days
limitations
Plasma measurements and correlation; neither tissue CoQ nor mitochondrial dysfunction was demonstrated.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
72 healthy men
plain_language
The blood concentration also depends on the particles carrying CoQ.
primary_references
[coq10-p16872244] Effect of ezetimibe and/or simvastatin on coenzyme Q10 levels in plasma: a randomised trial. (2006). https://pubmed.ncbi.nlm.nih.gov/16872244/ DOI: 10.2165/00002018-200629080-00007
tissue_or_cell_type
Plasma CoQ and lipoprotein concentrations
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 931–942
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Randomized three-arm parallel study · source_derived_draft · unverified_draft
### coq10-statin-plasma-carriers Simvastatin, alone or with ezetimibe, lowered plasma CoQ; CoQ change correlated with LDL-cholesterol change and the CoQ-to-LDL ratio increased. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: The blood concentration also depends on the particles carrying CoQ. organism: 72 healthy men tissue_or_cell_type: Plasma CoQ and lipoprotein concentrations experimental_model: Randomized three-arm parallel study limitations: Plasma measurements and correlation; neither tissue CoQ nor mitochondrial dysfunction was demonstrated. exposure: Simvastatin 40 mg/day, ezetimibe 10 mg/day or both for 14 days evidence_span: {"source_cache": "artifacts/coq10-research/16872244.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "65abd11b5f58ce1125f554d52ed5203575d7a3ba0d20b789abce16148f3b5e27", "start_char": 0, "end_char": 2245, "text_sha256": "65abd11b5f58ce1125f554d52ed5203575d7a3ba0d20b789abce16148f3b5e27"} [coq10-p16872244] Effect of ezetimibe and/or simvastatin on coenzyme Q10 levels in plasma: a randomised trial. (2006). https://pubmed.ncbi.nlm.nih.gov/16872244/ DOI: 10.2165/00002018-200629080-00007
Complete structured claim and evidence
The authors proposed that lower plasma CoQ could reflect loss of lipoprotein carriers rather than a statin-specific depletion mechanism.
Plasma coenzyme Q10 concentration → Cellular coenzyme Q concentration source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/16872244.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "65abd11b5f58ce1125f554d52ed5203575d7a3ba0d20b789abce16148f3b5e27", "start_char": 0, "end_char": 2245, "text_sha256": "65abd11b5f58ce1125f554d52ed5203575d7a3ba0d20b789abce16148f3b5e27"}
experimental_model
Randomized three-arm parallel study
exposure
Simvastatin 40 mg/day, ezetimibe 10 mg/day or both for 14 days
limitations
Plasma measurements and correlation; neither tissue CoQ nor mitochondrial dysfunction was demonstrated.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
72 healthy men
plain_language
Blood transport and intracellular deficiency are different explanations to test.
primary_references
[coq10-p16872244] Effect of ezetimibe and/or simvastatin on coenzyme Q10 levels in plasma: a randomised trial. (2006). https://pubmed.ncbi.nlm.nih.gov/16872244/ DOI: 10.2165/00002018-200629080-00007
tissue_or_cell_type
Plasma CoQ and lipoprotein concentrations
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 944–955
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Randomized three-arm parallel study · source_derived_draft · unverified_draft
### coq10-statin-carrier-interpretation The authors proposed that lower plasma CoQ could reflect loss of lipoprotein carriers rather than a statin-specific depletion mechanism. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: Blood transport and intracellular deficiency are different explanations to test. organism: 72 healthy men tissue_or_cell_type: Plasma CoQ and lipoprotein concentrations experimental_model: Randomized three-arm parallel study limitations: Plasma measurements and correlation; neither tissue CoQ nor mitochondrial dysfunction was demonstrated. exposure: Simvastatin 40 mg/day, ezetimibe 10 mg/day or both for 14 days evidence_span: {"source_cache": "artifacts/coq10-research/16872244.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "65abd11b5f58ce1125f554d52ed5203575d7a3ba0d20b789abce16148f3b5e27", "start_char": 0, "end_char": 2245, "text_sha256": "65abd11b5f58ce1125f554d52ed5203575d7a3ba0d20b789abce16148f3b5e27"} [coq10-p16872244] Effect of ezetimibe and/or simvastatin on coenzyme Q10 levels in plasma: a randomised trial. (2006). https://pubmed.ncbi.nlm.nih.gov/16872244/ DOI: 10.2165/00002018-200629080-00007
Complete structured claim and evidence
Muscle CoQ fell from 39.7 to 26.4 nmol/g with simvastatin 80 mg/day; it did not fall with atorvastatin 40 mg/day or placebo.
Simvastatin → Muscle coenzyme Q10 concentration source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/coq10-research/16003294.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "6293a60171af6eb5cc8dc58449792c024ee282cdbcb80f777dc9156f4c44250b", "start_char": 0, "end_char": 1774, "text_sha256": "6293a60171af6eb5cc8dc58449792c024ee282cdbcb80f777dc9156f4c44250b"}
experimental_model
Randomized double-blind placebo-controlled trial with muscle biopsies
exposure
Simvastatin 80 mg/day, atorvastatin 40 mg/day or placebo for eight weeks
limitations
Different statin/dose regimens. Respiratory-enzyme comparison selected six simvastatin participants with marked CoQ decline and matched participants; not an unbiased whole-arm estimate.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
48 hypercholesterolemic adults in three groups
plain_language
Some regimens lowered the muscle pool, but the finding did not apply equally to every statin arm.
primary_references
[coq10-p16003294] High-dose statins and skeletal muscle metabolism in humans: a randomized, controlled trial. (2005). https://pubmed.ncbi.nlm.nih.gov/16003294/ DOI: 10.1016/j.clpt.2005.03.006
tissue_or_cell_type
Muscle CoQ and respiratory enzymes
trigger_kind
machinery_impairment Imported condition classification; unverified.
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 957–968
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Randomized double-blind placebo-controlled trial with muscle biopsies · source_derived_draft · unverified_draft
### coq10-statin-muscle-low Muscle CoQ fell from 39.7 to 26.4 nmol/g with simvastatin 80 mg/day; it did not fall with atorvastatin 40 mg/day or placebo. Condition category: machinery_impairment nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: Some regimens lowered the muscle pool, but the finding did not apply equally to every statin arm. organism: 48 hypercholesterolemic adults in three groups tissue_or_cell_type: Muscle CoQ and respiratory enzymes experimental_model: Randomized double-blind placebo-controlled trial with muscle biopsies limitations: Different statin/dose regimens. Respiratory-enzyme comparison selected six simvastatin participants with marked CoQ decline and matched participants; not an unbiased whole-arm estimate. exposure: Simvastatin 80 mg/day, atorvastatin 40 mg/day or placebo for eight weeks evidence_span: {"source_cache": "artifacts/coq10-research/16003294.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "6293a60171af6eb5cc8dc58449792c024ee282cdbcb80f777dc9156f4c44250b", "start_char": 0, "end_char": 1774, "text_sha256": "6293a60171af6eb5cc8dc58449792c024ee282cdbcb80f777dc9156f4c44250b"} [coq10-p16003294] High-dose statins and skeletal muscle metabolism in humans: a randomized, controlled trial. (2005). https://pubmed.ncbi.nlm.nih.gov/16003294/ DOI: 10.1016/j.clpt.2005.03.006
Complete structured claim and evidence
Respiratory-chain enzyme and citrate-synthase activities were lower in the selected simvastatin subgroup with marked muscle CoQ decline.
Simvastatin → Mitochondrial respiratory electron transfer source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/coq10-research/16003294.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "6293a60171af6eb5cc8dc58449792c024ee282cdbcb80f777dc9156f4c44250b", "start_char": 0, "end_char": 1774, "text_sha256": "6293a60171af6eb5cc8dc58449792c024ee282cdbcb80f777dc9156f4c44250b"}
experimental_model
Randomized double-blind placebo-controlled trial with muscle biopsies
exposure
Simvastatin 80 mg/day, atorvastatin 40 mg/day or placebo for eight weeks
limitations
Six selected simvastatin participants were compared with matched participants from other arms. Selection and mitochondrial-content changes prevent assigning the entire effect specifically to CoQ depletion.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
48 hypercholesterolemic adults in three groups
plain_language
Both respiratory capacity and a mitochondrial-content marker changed in a selected subgroup.
primary_references
[coq10-p16003294] High-dose statins and skeletal muscle metabolism in humans: a randomized, controlled trial. (2005). https://pubmed.ncbi.nlm.nih.gov/16003294/ DOI: 10.1016/j.clpt.2005.03.006
tissue_or_cell_type
Muscle CoQ and respiratory enzymes
trigger_kind
machinery_impairment Imported condition classification; unverified.
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 970–981
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Randomized double-blind placebo-controlled trial with muscle biopsies · source_derived_draft · unverified_draft
### coq10-statin-respiratory-subset Respiratory-chain enzyme and citrate-synthase activities were lower in the selected simvastatin subgroup with marked muscle CoQ decline. Condition category: machinery_impairment nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: Both respiratory capacity and a mitochondrial-content marker changed in a selected subgroup. organism: 48 hypercholesterolemic adults in three groups tissue_or_cell_type: Muscle CoQ and respiratory enzymes experimental_model: Randomized double-blind placebo-controlled trial with muscle biopsies limitations: Six selected simvastatin participants were compared with matched participants from other arms. Selection and mitochondrial-content changes prevent assigning the entire effect specifically to CoQ depletion. exposure: Simvastatin 80 mg/day, atorvastatin 40 mg/day or placebo for eight weeks evidence_span: {"source_cache": "artifacts/coq10-research/16003294.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "6293a60171af6eb5cc8dc58449792c024ee282cdbcb80f777dc9156f4c44250b", "start_char": 0, "end_char": 1774, "text_sha256": "6293a60171af6eb5cc8dc58449792c024ee282cdbcb80f777dc9156f4c44250b"} [coq10-p16003294] High-dose statins and skeletal muscle metabolism in humans: a randomized, controlled trial. (2005). https://pubmed.ncbi.nlm.nih.gov/16003294/ DOI: 10.1016/j.clpt.2005.03.006
Complete structured claim and evidence
The 2022 trial found no effect on myalgia; individual changes in muscle CoQ did not correlate with changes in symptom intensity.
Coenzyme Q10 / CoQ10 redox system → Statin-associated muscle pain source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/36139772.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "07baaf957ba2b166fce6e23f157e7d2123c92bea20032628c332c0a40639b992", "start_char": 0, "end_char": 1370, "text_sha256": "07baaf957ba2b166fce6e23f157e7d2123c92bea20032628c332c0a40639b992"}
experimental_model
Randomized placebo-controlled muscle-biopsy supplementation trial
exposure
CoQ10 400 mg/day for eight weeks
limitations
One formulation/regimen and a small sample; a failed tissue or clinical response cannot establish universal nonresponse.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
37 simvastatin-treated adults with or without myalgia
plain_language
A measured muscle pool and the pain outcome must be assessed separately.
primary_references
[coq10-p36139772] Coenzyme Q10 Supplementation in Statin Treated Patients: A Double-Blinded Randomized Placebo-Controlled Trial. (2022). https://pubmed.ncbi.nlm.nih.gov/36139772/ DOI: 10.3390/antiox11091698
tissue_or_cell_type
Muscle CoQ, mitochondrial function and symptoms
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 996–1007
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Randomized placebo-controlled muscle-biopsy supplementation trial · source_derived_draft · unverified_draft
### coq10-statin-2022-pain-null The 2022 trial found no effect on myalgia; individual changes in muscle CoQ did not correlate with changes in symptom intensity. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: A measured muscle pool and the pain outcome must be assessed separately. organism: 37 simvastatin-treated adults with or without myalgia tissue_or_cell_type: Muscle CoQ, mitochondrial function and symptoms experimental_model: Randomized placebo-controlled muscle-biopsy supplementation trial limitations: One formulation/regimen and a small sample; a failed tissue or clinical response cannot establish universal nonresponse. exposure: CoQ10 400 mg/day for eight weeks evidence_span: {"source_cache": "artifacts/coq10-research/36139772.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "07baaf957ba2b166fce6e23f157e7d2123c92bea20032628c332c0a40639b992", "start_char": 0, "end_char": 1370, "text_sha256": "07baaf957ba2b166fce6e23f157e7d2123c92bea20032628c332c0a40639b992"} [coq10-p36139772] Coenzyme Q10 Supplementation in Statin Treated Patients: A Double-Blinded Randomized Placebo-Controlled Trial. (2022). https://pubmed.ncbi.nlm.nih.gov/36139772/ DOI: 10.3390/antiox11091698
Complete structured claim and evidence
Six COQ6 mutations in 13 individuals were linked to early nephrotic syndrome and sensorineural deafness.
Human CoQ monooxygenase / COQ6 → Nephrotic syndrome source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/coq10-research/21540551.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "3f01d7d237328376c3eb1ed5a3c2c1ee7561d78fb3890101ab5e8eb678c64def", "start_char": 0, "end_char": 1142, "text_sha256": "3f01d7d237328376c3eb1ed5a3c2c1ee7561d78fb3890101ab5e8eb678c64def"}
experimental_model
Human pedigrees, yeast validation, podocyte and zebrafish knockdown
exposure
COQ6 variants; cell/embryo knockdown and CoQ treatment
limitations
Human disease association and model rescue are different evidence layers; not proof that every nephrotic syndrome responds to CoQ.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
13 humans from seven families plus model systems
plain_language
A renal presentation can arise from a CoQ synthesis gene.
primary_references
[coq10-p21540551] COQ6 mutations in human patients produce nephrotic syndrome with sensorineural deafness. (2011). https://pubmed.ncbi.nlm.nih.gov/21540551/ DOI: 10.1172/jci45693
tissue_or_cell_type
Renal podocytes and inner-ear disease
trigger_kind
machinery_impairment Imported condition classification; unverified.
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 1009–1020
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human pedigrees, yeast validation, podocyte and zebrafish knockdown · source_derived_draft · unverified_draft
### coq10-coq6-nephropathy Six COQ6 mutations in 13 individuals were linked to early nephrotic syndrome and sensorineural deafness. Condition category: machinery_impairment nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: A renal presentation can arise from a CoQ synthesis gene. organism: 13 humans from seven families plus model systems tissue_or_cell_type: Renal podocytes and inner-ear disease experimental_model: Human pedigrees, yeast validation, podocyte and zebrafish knockdown limitations: Human disease association and model rescue are different evidence layers; not proof that every nephrotic syndrome responds to CoQ. exposure: COQ6 variants; cell/embryo knockdown and CoQ treatment evidence_span: {"source_cache": "artifacts/coq10-research/21540551.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "3f01d7d237328376c3eb1ed5a3c2c1ee7561d78fb3890101ab5e8eb678c64def", "start_char": 0, "end_char": 1142, "text_sha256": "3f01d7d237328376c3eb1ed5a3c2c1ee7561d78fb3890101ab5e8eb678c64def"} [coq10-p21540551] COQ6 mutations in human patients produce nephrotic syndrome with sensorineural deafness. (2011). https://pubmed.ncbi.nlm.nih.gov/21540551/ DOI: 10.1172/jci45693
Complete structured claim and evidence
CoQ treatment partly reversed apoptosis after Coq6 knockdown in podocyte and zebrafish models.
Coenzyme Q10 / CoQ10 redox system → Podocyte apoptosis source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/21540551.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "3f01d7d237328376c3eb1ed5a3c2c1ee7561d78fb3890101ab5e8eb678c64def", "start_char": 0, "end_char": 1142, "text_sha256": "3f01d7d237328376c3eb1ed5a3c2c1ee7561d78fb3890101ab5e8eb678c64def"}
experimental_model
Human pedigrees, yeast validation, podocyte and zebrafish knockdown
exposure
COQ6 variants; cell/embryo knockdown and CoQ treatment
limitations
The canonical podocyte process is the cell endpoint; zebrafish apoptosis was also studied. Partial model rescue is not universal clinical reversal.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
13 humans from seven families plus model systems
plain_language
Replacing the carrier helped in models of a specific synthesis defect.
primary_references
[coq10-p21540551] COQ6 mutations in human patients produce nephrotic syndrome with sensorineural deafness. (2011). https://pubmed.ncbi.nlm.nih.gov/21540551/ DOI: 10.1172/jci45693
tissue_or_cell_type
Renal podocytes and inner-ear disease
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 1022–1033
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human pedigrees, yeast validation, podocyte and zebrafish knockdown · source_derived_draft · unverified_draft
### coq10-coq6-model-rescue CoQ treatment partly reversed apoptosis after Coq6 knockdown in podocyte and zebrafish models. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: Replacing the carrier helped in models of a specific synthesis defect. organism: 13 humans from seven families plus model systems tissue_or_cell_type: Renal podocytes and inner-ear disease experimental_model: Human pedigrees, yeast validation, podocyte and zebrafish knockdown limitations: The canonical podocyte process is the cell endpoint; zebrafish apoptosis was also studied. Partial model rescue is not universal clinical reversal. exposure: COQ6 variants; cell/embryo knockdown and CoQ treatment evidence_span: {"source_cache": "artifacts/coq10-research/21540551.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "3f01d7d237328376c3eb1ed5a3c2c1ee7561d78fb3890101ab5e8eb678c64def", "start_char": 0, "end_char": 1142, "text_sha256": "3f01d7d237328376c3eb1ed5a3c2c1ee7561d78fb3890101ab5e8eb678c64def"} [coq10-p21540551] COQ6 mutations in human patients produce nephrotic syndrome with sensorineural deafness. (2011). https://pubmed.ncbi.nlm.nih.gov/21540551/ DOI: 10.1172/jci45693
Complete structured claim and evidence
Affected siblings with COQ5 duplications had low white-cell CoQ; the available muscle sample was also depleted.
Human CoQ C-methyltransferase / COQ5 → Cellular coenzyme Q concentration source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/coq10-research/29044765.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "704d515eb76ce1074ae021346c10abee852de623057b33d287e4fad0b69d23b4", "start_char": 0, "end_char": 1271, "text_sha256": "704d515eb76ce1074ae021346c10abee852de623057b33d287e4fad0b69d23b4"}
experimental_model
Family sequencing and biochemical measurements
exposure
Biallelic COQ5 duplications; supplementation follow-up
limitations
Small uncontrolled genetic case series; clinical improvement cannot yield a general efficacy estimate.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
Three human siblings
plain_language
A low circulating-cell pool was linked to a defined synthesis defect.
primary_references
[coq10-p29044765] A novel inborn error of the coenzyme Q10 biosynthesis pathway: cerebellar ataxia and static encephalomyopathy due to COQ5 C-methyltransferase deficiency. (2018). https://pubmed.ncbi.nlm.nih.gov/29044765/ DOI: 10.1002/humu.23345
tissue_or_cell_type
Neurologic disease and CoQ measurements
trigger_kind
machinery_impairment Imported condition classification; unverified.
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 1035–1046
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Family sequencing and biochemical measurements · source_derived_draft · unverified_draft
### coq10-coq5-deficiency Affected siblings with COQ5 duplications had low white-cell CoQ; the available muscle sample was also depleted. Condition category: machinery_impairment nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: A low circulating-cell pool was linked to a defined synthesis defect. organism: Three human siblings tissue_or_cell_type: Neurologic disease and CoQ measurements experimental_model: Family sequencing and biochemical measurements limitations: Small uncontrolled genetic case series; clinical improvement cannot yield a general efficacy estimate. exposure: Biallelic COQ5 duplications; supplementation follow-up evidence_span: {"source_cache": "artifacts/coq10-research/29044765.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "704d515eb76ce1074ae021346c10abee852de623057b33d287e4fad0b69d23b4", "start_char": 0, "end_char": 1271, "text_sha256": "704d515eb76ce1074ae021346c10abee852de623057b33d287e4fad0b69d23b4"} [coq10-p29044765] A novel inborn error of the coenzyme Q10 biosynthesis pathway: cerebellar ataxia and static encephalomyopathy due to COQ5 C-methyltransferase deficiency. (2018). https://pubmed.ncbi.nlm.nih.gov/29044765/ DOI: 10.1002/humu.23345
Complete structured claim and evidence
All seven patients in the 2007 ETFDH-associated myopathy series had significantly reduced muscle CoQ10.
Human electron transfer flavoprotein dehydrogenase / ETFDH → Muscle coenzyme Q10 concentration source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/coq10-research/17412732.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "38627f0140b8d1f861ce0e836bc8ac1edc9684314e8d664f3040e1c3fff42494", "start_char": 0, "end_char": 1533, "text_sha256": "38627f0140b8d1f861ce0e836bc8ac1edc9684314e8d664f3040e1c3fff42494"}
experimental_model
Genetic case series and muscle biochemistry
exposure
Biallelic ETFDH variants
limitations
Secondary CoQ depletion reported in this cohort; later cohorts did not reproduce universal muscle depletion.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
Seven patients from five families
plain_language
A defect outside the core COQ synthesis genes accompanied low muscle CoQ in this group.
primary_references
[coq10-p17412732] The myopathic form of coenzyme Q10 deficiency is caused by mutations in the electron-transferring-flavoprotein dehydrogenase (ETFDH) gene. (2007). https://pubmed.ncbi.nlm.nih.gov/17412732/ DOI: 10.1093/brain/awm054
tissue_or_cell_type
ETFDH-associated myopathy
trigger_kind
machinery_impairment Imported condition classification; unverified.
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 1061–1072
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Genetic case series and muscle biochemistry · source_derived_draft · unverified_draft
### coq10-etfdh-coq-low All seven patients in the 2007 ETFDH-associated myopathy series had significantly reduced muscle CoQ10. Condition category: machinery_impairment nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: A defect outside the core COQ synthesis genes accompanied low muscle CoQ in this group. organism: Seven patients from five families tissue_or_cell_type: ETFDH-associated myopathy experimental_model: Genetic case series and muscle biochemistry limitations: Secondary CoQ depletion reported in this cohort; later cohorts did not reproduce universal muscle depletion. exposure: Biallelic ETFDH variants evidence_span: {"source_cache": "artifacts/coq10-research/17412732.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "38627f0140b8d1f861ce0e836bc8ac1edc9684314e8d664f3040e1c3fff42494", "start_char": 0, "end_char": 1533, "text_sha256": "38627f0140b8d1f861ce0e836bc8ac1edc9684314e8d664f3040e1c3fff42494"} [coq10-p17412732] The myopathic form of coenzyme Q10 deficiency is caused by mutations in the electron-transferring-flavoprotein dehydrogenase (ETFDH) gene. (2007). https://pubmed.ncbi.nlm.nih.gov/17412732/ DOI: 10.1093/brain/awm054
Complete structured claim and evidence
Muscle CoQ was elevated in the 34-patient cohort but not significantly different from controls after normalization to citrate synthase.
Human electron transfer flavoprotein dehydrogenase / ETFDH → Muscle coenzyme Q10 concentration source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/coq10-research/23628458.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "4395652f36b9a39c5de72db7abb11b7f42b7e3124b1dfd3c8cd2a0212a9f7de6", "start_char": 0, "end_char": 1706, "text_sha256": "4395652f36b9a39c5de72db7abb11b7f42b7e3124b1dfd3c8cd2a0212a9f7de6"}
experimental_model
Muscle HPLC, citrate-synthase normalization and mtDNA measurements
exposure
Genetically defined MADD cohort
limitations
Different variants/cohort from the earlier report; bulk concentration and concentration per mitochondrial mass are different measurements.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
34 riboflavin-responsive ETFDH-MADD patients
plain_language
More mitochondria can change a bulk tissue measurement without increasing CoQ per mitochondrial mass.
primary_references
[coq10-p23628458] Increased muscle coenzyme Q10 in riboflavin responsive MADD with ETFDH gene mutations due to secondary mitochondrial proliferation. (2013). https://pubmed.ncbi.nlm.nih.gov/23628458/ DOI: 10.1016/j.ymgme.2013.04.007
tissue_or_cell_type
Muscle CoQ and mitochondrial mass
trigger_kind
machinery_impairment Imported condition classification; unverified.
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 1074–1085
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Muscle HPLC, citrate-synthase normalization and mtDNA measurements · source_derived_draft · unverified_draft
### coq10-etfdh-coq-normalized Muscle CoQ was elevated in the 34-patient cohort but not significantly different from controls after normalization to citrate synthase. Condition category: machinery_impairment nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: More mitochondria can change a bulk tissue measurement without increasing CoQ per mitochondrial mass. organism: 34 riboflavin-responsive ETFDH-MADD patients tissue_or_cell_type: Muscle CoQ and mitochondrial mass experimental_model: Muscle HPLC, citrate-synthase normalization and mtDNA measurements limitations: Different variants/cohort from the earlier report; bulk concentration and concentration per mitochondrial mass are different measurements. exposure: Genetically defined MADD cohort evidence_span: {"source_cache": "artifacts/coq10-research/23628458.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "4395652f36b9a39c5de72db7abb11b7f42b7e3124b1dfd3c8cd2a0212a9f7de6", "start_char": 0, "end_char": 1706, "text_sha256": "4395652f36b9a39c5de72db7abb11b7f42b7e3124b1dfd3c8cd2a0212a9f7de6"} [coq10-p23628458] Increased muscle coenzyme Q10 in riboflavin responsive MADD with ETFDH gene mutations due to secondary mitochondrial proliferation. (2013). https://pubmed.ncbi.nlm.nih.gov/23628458/ DOI: 10.1016/j.ymgme.2013.04.007
Complete structured claim and evidence
Two-year major adverse events occurred in 15% on CoQ versus 26% on placebo, hazard ratio 0.50 (95% CI 0.32-0.80).
Coenzyme Q10 / CoQ10 redox system → Major adverse cardiovascular events in heart failure source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/25282031.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "20ff9f86de1fab16a33ecadfb2c4e09e9017860f01854cfecf490d473fb8fb65", "start_char": 0, "end_char": 2024, "text_sha256": "20ff9f86de1fab16a33ecadfb2c4e09e9017860f01854cfecf490d473fb8fb65"}
experimental_model
Q-SYMBIO randomized double-blind multicenter trial
exposure
100 mg CoQ10 three times daily added to standard therapy
limitations
One adjunctive-treatment trial; recruitment preceded current heart-failure regimens. Does not show universal benefit or replacement of standard treatment.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
420 patients with moderate-to-severe chronic heart failure
plain_language
This trial found a benefit on clinical events when CoQ was added to usual care.
primary_references
[coq10-p25282031] The effect of coenzyme Q10 on morbidity and mortality in chronic heart failure: results from Q-SYMBIO: a randomized double-blind trial. (2014). https://pubmed.ncbi.nlm.nih.gov/25282031/ DOI: 10.1016/j.jchf.2014.06.008
tissue_or_cell_type
Short-term function and two-year clinical events
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 1087–1098
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Q-SYMBIO randomized double-blind multicenter trial · source_derived_draft · unverified_draft
### coq10-heart-failure-events Two-year major adverse events occurred in 15% on CoQ versus 26% on placebo, hazard ratio 0.50 (95% CI 0.32-0.80). Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: This trial found a benefit on clinical events when CoQ was added to usual care. organism: 420 patients with moderate-to-severe chronic heart failure tissue_or_cell_type: Short-term function and two-year clinical events experimental_model: Q-SYMBIO randomized double-blind multicenter trial limitations: One adjunctive-treatment trial; recruitment preceded current heart-failure regimens. Does not show universal benefit or replacement of standard treatment. exposure: 100 mg CoQ10 three times daily added to standard therapy evidence_span: {"source_cache": "artifacts/coq10-research/25282031.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "20ff9f86de1fab16a33ecadfb2c4e09e9017860f01854cfecf490d473fb8fb65", "start_char": 0, "end_char": 2024, "text_sha256": "20ff9f86de1fab16a33ecadfb2c4e09e9017860f01854cfecf490d473fb8fb65"} [coq10-p25282031] The effect of coenzyme Q10 on morbidity and mortality in chronic heart failure: results from Q-SYMBIO: a randomized double-blind trial. (2014). https://pubmed.ncbi.nlm.nih.gov/25282031/ DOI: 10.1016/j.jchf.2014.06.008
Complete structured claim and evidence
All-cause mortality was 10% versus 18%, and cardiovascular mortality was 9% versus 16%, favoring CoQ in Q-SYMBIO.
Coenzyme Q10 / CoQ10 redox system → All-cause mortality source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/25282031.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "20ff9f86de1fab16a33ecadfb2c4e09e9017860f01854cfecf490d473fb8fb65", "start_char": 0, "end_char": 2024, "text_sha256": "20ff9f86de1fab16a33ecadfb2c4e09e9017860f01854cfecf490d473fb8fb65"}
experimental_model
Q-SYMBIO randomized double-blind multicenter trial
exposure
100 mg CoQ10 three times daily added to standard therapy
limitations
One adjunctive-treatment trial; recruitment preceded current heart-failure regimens. Does not show universal benefit or replacement of standard treatment.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
420 patients with moderate-to-severe chronic heart failure
plain_language
Mortality was a reported secondary outcome, separate from symptom markers.
primary_references
[coq10-p25282031] The effect of coenzyme Q10 on morbidity and mortality in chronic heart failure: results from Q-SYMBIO: a randomized double-blind trial. (2014). https://pubmed.ncbi.nlm.nih.gov/25282031/ DOI: 10.1016/j.jchf.2014.06.008
tissue_or_cell_type
Short-term function and two-year clinical events
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 1100–1111
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Q-SYMBIO randomized double-blind multicenter trial · source_derived_draft · unverified_draft
### coq10-heart-failure-mortality All-cause mortality was 10% versus 18%, and cardiovascular mortality was 9% versus 16%, favoring CoQ in Q-SYMBIO. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: Mortality was a reported secondary outcome, separate from symptom markers. organism: 420 patients with moderate-to-severe chronic heart failure tissue_or_cell_type: Short-term function and two-year clinical events experimental_model: Q-SYMBIO randomized double-blind multicenter trial limitations: One adjunctive-treatment trial; recruitment preceded current heart-failure regimens. Does not show universal benefit or replacement of standard treatment. exposure: 100 mg CoQ10 three times daily added to standard therapy evidence_span: {"source_cache": "artifacts/coq10-research/25282031.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "20ff9f86de1fab16a33ecadfb2c4e09e9017860f01854cfecf490d473fb8fb65", "start_char": 0, "end_char": 2024, "text_sha256": "20ff9f86de1fab16a33ecadfb2c4e09e9017860f01854cfecf490d473fb8fb65"} [coq10-p25282031] The effect of coenzyme Q10 on morbidity and mortality in chronic heart failure: results from Q-SYMBIO: a randomized double-blind trial. (2014). https://pubmed.ncbi.nlm.nih.gov/25282031/ DOI: 10.1016/j.jchf.2014.06.008
Complete structured claim and evidence
The 16-week NT-proBNP, NYHA-class and six-minute-walk endpoints did not significantly change between trial groups.
Coenzyme Q10 / CoQ10 redox system → Circulating NT-proBNP source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/25282031.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "20ff9f86de1fab16a33ecadfb2c4e09e9017860f01854cfecf490d473fb8fb65", "start_char": 0, "end_char": 2024, "text_sha256": "20ff9f86de1fab16a33ecadfb2c4e09e9017860f01854cfecf490d473fb8fb65"}
experimental_model
Q-SYMBIO randomized double-blind multicenter trial
exposure
100 mg CoQ10 three times daily added to standard therapy
limitations
One adjunctive-treatment trial; recruitment preceded current heart-failure regimens. Does not show universal benefit or replacement of standard treatment.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
420 patients with moderate-to-severe chronic heart failure
plain_language
The early markers did not mirror the later event finding.
primary_references
[coq10-p25282031] The effect of coenzyme Q10 on morbidity and mortality in chronic heart failure: results from Q-SYMBIO: a randomized double-blind trial. (2014). https://pubmed.ncbi.nlm.nih.gov/25282031/ DOI: 10.1016/j.jchf.2014.06.008
tissue_or_cell_type
Short-term function and two-year clinical events
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 1113–1124
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Q-SYMBIO randomized double-blind multicenter trial · source_derived_draft · unverified_draft
### coq10-heart-failure-short The 16-week NT-proBNP, NYHA-class and six-minute-walk endpoints did not significantly change between trial groups. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: The early markers did not mirror the later event finding. organism: 420 patients with moderate-to-severe chronic heart failure tissue_or_cell_type: Short-term function and two-year clinical events experimental_model: Q-SYMBIO randomized double-blind multicenter trial limitations: One adjunctive-treatment trial; recruitment preceded current heart-failure regimens. Does not show universal benefit or replacement of standard treatment. exposure: 100 mg CoQ10 three times daily added to standard therapy evidence_span: {"source_cache": "artifacts/coq10-research/25282031.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "20ff9f86de1fab16a33ecadfb2c4e09e9017860f01854cfecf490d473fb8fb65", "start_char": 0, "end_char": 2024, "text_sha256": "20ff9f86de1fab16a33ecadfb2c4e09e9017860f01854cfecf490d473fb8fb65"} [coq10-p25282031] The effect of coenzyme Q10 on morbidity and mortality in chronic heart failure: results from Q-SYMBIO: a randomized double-blind trial. (2014). https://pubmed.ncbi.nlm.nih.gov/25282031/ DOI: 10.1016/j.jchf.2014.06.008
Complete structured claim and evidence
Cardiovascular mortality was 5.9% with combined selenium/CoQ versus 12.6% with placebo in the Swedish trial.
Coenzyme Q10 / CoQ10 redox system → Cardiovascular mortality source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/22626835.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "68f71b162945240d48d14b42d132856ad242c2cc57640eae3a60a3aaa2706587", "start_char": 0, "end_char": 1797, "text_sha256": "68f71b162945240d48d14b42d132856ad242c2cc57640eae3a60a3aaa2706587"}
experimental_model
Randomized double-blind combined-supplement trial
exposure
Selenium plus CoQ10 versus placebo; 5.2-year follow-up
limitations
Combined intervention without selenium-only and CoQ-only arms; no independent CoQ effect or statistical nutrient synergy can be identified.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
443 Swedish adults aged 70-88
plain_language
The combination had a favorable result, but the design cannot tell how much came from each component.
primary_references
[coq10-p22626835] Cardiovascular mortality and N-terminal-proBNP reduced after combined selenium and coenzyme Q10 supplementation: a 5-year prospective randomized double-blind placebo-controlled trial among elderly Swedish citizens. (2013). https://pubmed.ncbi.nlm.nih.gov/22626835/ DOI: 10.1016/j.ijcard.2012.04.156
tissue_or_cell_type
Cardiovascular mortality and cardiac measurements
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 1126–1137
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Randomized double-blind combined-supplement trial · source_derived_draft · unverified_draft
### coq10-selenium-combination-mortality Cardiovascular mortality was 5.9% with combined selenium/CoQ versus 12.6% with placebo in the Swedish trial. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: The combination had a favorable result, but the design cannot tell how much came from each component. organism: 443 Swedish adults aged 70-88 tissue_or_cell_type: Cardiovascular mortality and cardiac measurements experimental_model: Randomized double-blind combined-supplement trial limitations: Combined intervention without selenium-only and CoQ-only arms; no independent CoQ effect or statistical nutrient synergy can be identified. exposure: Selenium plus CoQ10 versus placebo; 5.2-year follow-up evidence_span: {"source_cache": "artifacts/coq10-research/22626835.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "68f71b162945240d48d14b42d132856ad242c2cc57640eae3a60a3aaa2706587", "start_char": 0, "end_char": 1797, "text_sha256": "68f71b162945240d48d14b42d132856ad242c2cc57640eae3a60a3aaa2706587"} [coq10-p22626835] Cardiovascular mortality and N-terminal-proBNP reduced after combined selenium and coenzyme Q10 supplementation: a 5-year prospective randomized double-blind placebo-controlled trial among elderly Swedish citizens. (2013). https://pubmed.ncbi.nlm.nih.gov/22626835/ DOI: 10.1016/j.ijcard.2012.04.156
Complete structured claim and evidence
Mean NT-proBNP at 48 months was 214 ng/L in the combined-treatment group versus 302 ng/L with placebo.
Coenzyme Q10 / CoQ10 redox system → Circulating NT-proBNP source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/22626835.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "68f71b162945240d48d14b42d132856ad242c2cc57640eae3a60a3aaa2706587", "start_char": 0, "end_char": 1797, "text_sha256": "68f71b162945240d48d14b42d132856ad242c2cc57640eae3a60a3aaa2706587"}
experimental_model
Randomized double-blind combined-supplement trial
exposure
Selenium plus CoQ10 versus placebo; 5.2-year follow-up
limitations
Combined intervention without selenium-only and CoQ-only arms; no independent CoQ effect or statistical nutrient synergy can be identified.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
443 Swedish adults aged 70-88
plain_language
A heart-stress marker also differed; this was the same trial, not an independent replication.
primary_references
[coq10-p22626835] Cardiovascular mortality and N-terminal-proBNP reduced after combined selenium and coenzyme Q10 supplementation: a 5-year prospective randomized double-blind placebo-controlled trial among elderly Swedish citizens. (2013). https://pubmed.ncbi.nlm.nih.gov/22626835/ DOI: 10.1016/j.ijcard.2012.04.156
tissue_or_cell_type
Cardiovascular mortality and cardiac measurements
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 1139–1150
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Randomized double-blind combined-supplement trial · source_derived_draft · unverified_draft
### coq10-selenium-combination-marker Mean NT-proBNP at 48 months was 214 ng/L in the combined-treatment group versus 302 ng/L with placebo. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: A heart-stress marker also differed; this was the same trial, not an independent replication. organism: 443 Swedish adults aged 70-88 tissue_or_cell_type: Cardiovascular mortality and cardiac measurements experimental_model: Randomized double-blind combined-supplement trial limitations: Combined intervention without selenium-only and CoQ-only arms; no independent CoQ effect or statistical nutrient synergy can be identified. exposure: Selenium plus CoQ10 versus placebo; 5.2-year follow-up evidence_span: {"source_cache": "artifacts/coq10-research/22626835.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "68f71b162945240d48d14b42d132856ad242c2cc57640eae3a60a3aaa2706587", "start_char": 0, "end_char": 1797, "text_sha256": "68f71b162945240d48d14b42d132856ad242c2cc57640eae3a60a3aaa2706587"} [coq10-p22626835] Cardiovascular mortality and N-terminal-proBNP reduced after combined selenium and coenzyme Q10 supplementation: a 5-year prospective randomized double-blind placebo-controlled trial among elderly Swedish citizens. (2013). https://pubmed.ncbi.nlm.nih.gov/22626835/ DOI: 10.1016/j.ijcard.2012.04.156
Complete structured claim and evidence
Pain severity and interference improved relative to placebo after 30 days of CoQ in the 50-patient study.
Coenzyme Q10 / CoQ10 redox system → Statin-associated muscle pain source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/25375075.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "c1b3bae22ef80093dd226d2bebbc1791ac08e3952c694f801a72f308fd7258e4", "start_char": 0, "end_char": 1622, "text_sha256": "c1b3bae22ef80093dd226d2bebbc1791ac08e3952c694f801a72f308fd7258e4"}
experimental_model
Randomized placebo-controlled study
exposure
CoQ10 50 mg twice daily for 30 days
limitations
Small short study; symptoms were not confirmed by a blinded statin-placebo lead-in as in the later trial.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
50 statin-treated patients reporting mild-to-moderate muscle symptoms
plain_language
One trial found less muscle pain with added CoQ.
primary_references
[coq10-p25375075] Coenzyme Q10 supplementation decreases statin-related mild-to-moderate muscle symptoms: a randomized clinical study. (2014). https://pubmed.ncbi.nlm.nih.gov/25375075/ DOI: 10.12659/msm.890777
tissue_or_cell_type
Brief Pain Inventory scores
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 1152–1163
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Randomized placebo-controlled study · source_derived_draft · unverified_draft
### coq10-statin-pain-positive Pain severity and interference improved relative to placebo after 30 days of CoQ in the 50-patient study. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: One trial found less muscle pain with added CoQ. organism: 50 statin-treated patients reporting mild-to-moderate muscle symptoms tissue_or_cell_type: Brief Pain Inventory scores experimental_model: Randomized placebo-controlled study limitations: Small short study; symptoms were not confirmed by a blinded statin-placebo lead-in as in the later trial. exposure: CoQ10 50 mg twice daily for 30 days evidence_span: {"source_cache": "artifacts/coq10-research/25375075.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "c1b3bae22ef80093dd226d2bebbc1791ac08e3952c694f801a72f308fd7258e4", "start_char": 0, "end_char": 1622, "text_sha256": "c1b3bae22ef80093dd226d2bebbc1791ac08e3952c694f801a72f308fd7258e4"} [coq10-p25375075] Coenzyme Q10 supplementation decreases statin-related mild-to-moderate muscle symptoms: a randomized clinical study. (2014). https://pubmed.ncbi.nlm.nih.gov/25375075/ DOI: 10.12659/msm.890777
Complete structured claim and evidence
Ubiquinol did not reduce pain severity or interference versus placebo in confirmed simvastatin myalgia.
Reduced CoQ10 → Statin-associated muscle pain source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/25545331.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "2aad217d0053cae8ea41f5be8ee7e0be0fa83f83d779f34e30fabe2a0b29c837", "start_char": 0, "end_char": 1976, "text_sha256": "2aad217d0053cae8ea41f5be8ee7e0be0fa83f83d779f34e30fabe2a0b29c837"}
experimental_model
Randomized double-blind trial after blinded symptom confirmation
exposure
600 mg/day ubiquinol with simvastatin 20 mg/day for eight weeks
limitations
Small confirmed-myalgia sample; null outcome is not proof that every other regimen is ineffective.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
41 subjects with confirmed simvastatin myalgia
plain_language
A more strictly selected trial did not reproduce the pain benefit.
primary_references
[coq10-p25545331] A randomized trial of coenzyme Q10 in patients with confirmed statin myopathy. (2015). https://pubmed.ncbi.nlm.nih.gov/25545331/ DOI: 10.1016/j.atherosclerosis.2014.12.016
tissue_or_cell_type
Pain, muscle performance and serum CoQ
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 1165–1176
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Randomized double-blind trial after blinded symptom confirmation · source_derived_draft · unverified_draft
### coq10-statin-pain-null Ubiquinol did not reduce pain severity or interference versus placebo in confirmed simvastatin myalgia. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: A more strictly selected trial did not reproduce the pain benefit. organism: 41 subjects with confirmed simvastatin myalgia tissue_or_cell_type: Pain, muscle performance and serum CoQ experimental_model: Randomized double-blind trial after blinded symptom confirmation limitations: Small confirmed-myalgia sample; null outcome is not proof that every other regimen is ineffective. exposure: 600 mg/day ubiquinol with simvastatin 20 mg/day for eight weeks evidence_span: {"source_cache": "artifacts/coq10-research/25545331.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "2aad217d0053cae8ea41f5be8ee7e0be0fa83f83d779f34e30fabe2a0b29c837", "start_char": 0, "end_char": 1976, "text_sha256": "2aad217d0053cae8ea41f5be8ee7e0be0fa83f83d779f34e30fabe2a0b29c837"} [coq10-p25545331] A randomized trial of coenzyme Q10 in patients with confirmed statin myopathy. (2015). https://pubmed.ncbi.nlm.nih.gov/25545331/ DOI: 10.1016/j.atherosclerosis.2014.12.016
Complete structured claim and evidence
Serum CoQ increased from 1.3 to 5.2 micrograms/mL with ubiquinol, without improved muscle strength or aerobic performance.
Reduced CoQ10 → Plasma coenzyme Q10 concentration source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/25545331.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "2aad217d0053cae8ea41f5be8ee7e0be0fa83f83d779f34e30fabe2a0b29c837", "start_char": 0, "end_char": 1976, "text_sha256": "2aad217d0053cae8ea41f5be8ee7e0be0fa83f83d779f34e30fabe2a0b29c837"}
experimental_model
Randomized double-blind trial after blinded symptom confirmation
exposure
600 mg/day ubiquinol with simvastatin 20 mg/day for eight weeks
limitations
Small confirmed-myalgia sample; null outcome is not proof that every other regimen is ineffective.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
41 subjects with confirmed simvastatin myalgia
plain_language
A larger blood pool did not guarantee a functional response.
primary_references
[coq10-p25545331] A randomized trial of coenzyme Q10 in patients with confirmed statin myopathy. (2015). https://pubmed.ncbi.nlm.nih.gov/25545331/ DOI: 10.1016/j.atherosclerosis.2014.12.016
tissue_or_cell_type
Pain, muscle performance and serum CoQ
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 1178–1189
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Randomized double-blind trial after blinded symptom confirmation · source_derived_draft · unverified_draft
### coq10-statin-plasma-not-function Serum CoQ increased from 1.3 to 5.2 micrograms/mL with ubiquinol, without improved muscle strength or aerobic performance. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: A larger blood pool did not guarantee a functional response. organism: 41 subjects with confirmed simvastatin myalgia tissue_or_cell_type: Pain, muscle performance and serum CoQ experimental_model: Randomized double-blind trial after blinded symptom confirmation limitations: Small confirmed-myalgia sample; null outcome is not proof that every other regimen is ineffective. exposure: 600 mg/day ubiquinol with simvastatin 20 mg/day for eight weeks evidence_span: {"source_cache": "artifacts/coq10-research/25545331.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "2aad217d0053cae8ea41f5be8ee7e0be0fa83f83d779f34e30fabe2a0b29c837", "start_char": 0, "end_char": 1976, "text_sha256": "2aad217d0053cae8ea41f5be8ee7e0be0fa83f83d779f34e30fabe2a0b29c837"} [coq10-p25545331] A randomized trial of coenzyme Q10 in patients with confirmed statin myopathy. (2015). https://pubmed.ncbi.nlm.nih.gov/25545331/ DOI: 10.1016/j.atherosclerosis.2014.12.016
Complete structured claim and evidence
The 50% responder rate for attack frequency was 47.6% with CoQ versus 14.4% with placebo in the third treatment month.
Coenzyme Q10 / CoQ10 redox system → Migraine attack frequency source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/15728298.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "efc7a89a0f36fb7248716b6a3e951d719b4e7f2c1051cd8ea50b61a1f4e4941f", "start_char": 0, "end_char": 533, "text_sha256": "efc7a89a0f36fb7248716b6a3e951d719b4e7f2c1051cd8ea50b61a1f4e4941f"}
experimental_model
Double-blind randomized placebo-controlled trial
exposure
CoQ10 100 mg three times daily
limitations
Small preventive trial; third-month endpoint, not proof of correction of a diagnosed CoQ deficiency.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
42 migraine patients
plain_language
A small migraine trial reported fewer attacks.
primary_references
[coq10-p15728298] Efficacy of coenzyme Q10 in migraine prophylaxis: a randomized controlled trial. (2005). https://pubmed.ncbi.nlm.nih.gov/15728298/ DOI: 10.1212/01.wnl.0000151975.03598.ed
tissue_or_cell_type
Attack frequency and headache days
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 1191–1202
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Double-blind randomized placebo-controlled trial · source_derived_draft · unverified_draft
### coq10-migraine-adult The 50% responder rate for attack frequency was 47.6% with CoQ versus 14.4% with placebo in the third treatment month. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: A small migraine trial reported fewer attacks. organism: 42 migraine patients tissue_or_cell_type: Attack frequency and headache days experimental_model: Double-blind randomized placebo-controlled trial limitations: Small preventive trial; third-month endpoint, not proof of correction of a diagnosed CoQ deficiency. exposure: CoQ10 100 mg three times daily evidence_span: {"source_cache": "artifacts/coq10-research/15728298.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "efc7a89a0f36fb7248716b6a3e951d719b4e7f2c1051cd8ea50b61a1f4e4941f", "start_char": 0, "end_char": 533, "text_sha256": "efc7a89a0f36fb7248716b6a3e951d719b4e7f2c1051cd8ea50b61a1f4e4941f"} [coq10-p15728298] Efficacy of coenzyme Q10 in migraine prophylaxis: a randomized controlled trial. (2005). https://pubmed.ncbi.nlm.nih.gov/15728298/ DOI: 10.1212/01.wnl.0000151975.03598.ed
Complete structured claim and evidence
At day 224, headache outcomes did not differ between CoQ and placebo; both groups improved over time.
Coenzyme Q10 / CoQ10 redox system → Migraine attack frequency source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/21586650.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "f3500b1c0ad9329d8b4f4c4cc7bdadb07c8cae55e8d336dccf0265620aa25292", "start_char": 0, "end_char": 2235, "text_sha256": "f3500b1c0ad9329d8b4f4c4cc7bdadb07c8cae55e8d336dccf0265620aa25292"}
experimental_model
Randomized double-blind crossover add-on trial
exposure
CoQ10 100 mg with standardized multidisciplinary care
limitations
Substantial attrition; early improvement and final between-group outcome are different analyses.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
120 children/adolescents randomized; 50 analyzed at final endpoint
plain_language
A pediatric study did not establish a lasting added benefit beyond the background care.
primary_references
[coq10-p21586650] A randomized, double-blinded, placebo-controlled, crossover, add-on study of CoEnzyme Q10 in the prevention of pediatric and adolescent migraine. (2011). https://pubmed.ncbi.nlm.nih.gov/21586650/ DOI: 10.1177/0333102411406755
tissue_or_cell_type
Migraine outcomes
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 1204–1215
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Randomized double-blind crossover add-on trial · source_derived_draft · unverified_draft
### coq10-migraine-child At day 224, headache outcomes did not differ between CoQ and placebo; both groups improved over time. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: A pediatric study did not establish a lasting added benefit beyond the background care. organism: 120 children/adolescents randomized; 50 analyzed at final endpoint tissue_or_cell_type: Migraine outcomes experimental_model: Randomized double-blind crossover add-on trial limitations: Substantial attrition; early improvement and final between-group outcome are different analyses. exposure: CoQ10 100 mg with standardized multidisciplinary care evidence_span: {"source_cache": "artifacts/coq10-research/21586650.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "f3500b1c0ad9329d8b4f4c4cc7bdadb07c8cae55e8d336dccf0265620aa25292", "start_char": 0, "end_char": 2235, "text_sha256": "f3500b1c0ad9329d8b4f4c4cc7bdadb07c8cae55e8d336dccf0265620aa25292"} [coq10-p21586650] A randomized, double-blinded, placebo-controlled, crossover, add-on study of CoEnzyme Q10 in the prevention of pediatric and adolescent migraine. (2011). https://pubmed.ncbi.nlm.nih.gov/21586650/ DOI: 10.1177/0333102411406755
Complete structured claim and evidence
Neither CoQ dose slowed UPDRS worsening versus placebo; the trial stopped for futility.
Coenzyme Q10 / CoQ10 redox system → Parkinson disease UPDRS progression source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/24664227.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "b1f301e82d4650432dab586db0be51f96e131f3c6084af9aebde932e8072676b", "start_char": 0, "end_char": 3023, "text_sha256": "b1f301e82d4650432dab586db0be51f96e131f3c6084af9aebde932e8072676b"}
experimental_model
Randomized double-blind phase III trial
exposure
CoQ10 1200 or 2400 mg/day; all groups received 1200 IU/day vitamin E
limitations
Vitamin E was a common background intervention; this comparison cannot identify its independent effect.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
600 early-Parkinson patients
plain_language
A plausible mitochondrial mechanism did not translate into slower Parkinson progression in this trial.
primary_references
[coq10-p24664227] A randomized clinical trial of high-dosage coenzyme Q10 in early Parkinson disease: no evidence of benefit. (2014). https://pubmed.ncbi.nlm.nih.gov/24664227/ DOI: 10.1001/jamaneurol.2014.131
tissue_or_cell_type
UPDRS progression
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 1217–1228
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Randomized double-blind phase III trial · source_derived_draft · unverified_draft
### coq10-parkinson-null Neither CoQ dose slowed UPDRS worsening versus placebo; the trial stopped for futility. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: A plausible mitochondrial mechanism did not translate into slower Parkinson progression in this trial. organism: 600 early-Parkinson patients tissue_or_cell_type: UPDRS progression experimental_model: Randomized double-blind phase III trial limitations: Vitamin E was a common background intervention; this comparison cannot identify its independent effect. exposure: CoQ10 1200 or 2400 mg/day; all groups received 1200 IU/day vitamin E evidence_span: {"source_cache": "artifacts/coq10-research/24664227.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "b1f301e82d4650432dab586db0be51f96e131f3c6084af9aebde932e8072676b", "start_char": 0, "end_char": 3023, "text_sha256": "b1f301e82d4650432dab586db0be51f96e131f3c6084af9aebde932e8072676b"} [coq10-p24664227] A randomized clinical trial of high-dosage coenzyme Q10 in early Parkinson disease: no evidence of benefit. (2014). https://pubmed.ncbi.nlm.nih.gov/24664227/ DOI: 10.1001/jamaneurol.2014.131
Complete structured claim and evidence
CoQ modestly attenuated exercise-related lactate rise and improved one cycling oxygen-consumption measure.
Coenzyme Q10 / CoQ10 redox system → Rise in blood lactate after exercise source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/20886510.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "7df48f2e8cf3da738d09c37cb1e96cb62a3eceae213ff722b49855ea174f863e", "start_char": 0, "end_char": 1053, "text_sha256": "7df48f2e8cf3da738d09c37cb1e96cb62a3eceae213ff722b49855ea174f863e"}
experimental_model
Randomized double-blind crossover trial
exposure
CoQ10 1200 mg/day for 60 days
limitations
Heterogeneous mitochondrial disease, not exclusively genetically proven primary CoQ deficiency; small short study.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
30 mitochondrial-cytopathy patients
plain_language
Some exercise measurements changed in this heterogeneous group.
primary_references
[coq10-p20886510] A randomized trial of coenzyme Q10 in mitochondrial disorders. (2010). https://pubmed.ncbi.nlm.nih.gov/20886510/ DOI: 10.1002/mus.21758
tissue_or_cell_type
Exercise and clinical function
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 1230–1241
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Randomized double-blind crossover trial · source_derived_draft · unverified_draft
### coq10-mitochondrial-exercise CoQ modestly attenuated exercise-related lactate rise and improved one cycling oxygen-consumption measure. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: Some exercise measurements changed in this heterogeneous group. organism: 30 mitochondrial-cytopathy patients tissue_or_cell_type: Exercise and clinical function experimental_model: Randomized double-blind crossover trial limitations: Heterogeneous mitochondrial disease, not exclusively genetically proven primary CoQ deficiency; small short study. exposure: CoQ10 1200 mg/day for 60 days evidence_span: {"source_cache": "artifacts/coq10-research/20886510.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "7df48f2e8cf3da738d09c37cb1e96cb62a3eceae213ff722b49855ea174f863e", "start_char": 0, "end_char": 1053, "text_sha256": "7df48f2e8cf3da738d09c37cb1e96cb62a3eceae213ff722b49855ea174f863e"} [coq10-p20886510] A randomized trial of coenzyme Q10 in mitochondrial disorders. (2010). https://pubmed.ncbi.nlm.nih.gov/20886510/ DOI: 10.1002/mus.21758
Complete structured claim and evidence
The trial found no improvement in strength or other major clinical variables despite minor exercise effects.
Coenzyme Q10 / CoQ10 redox system → Skeletal muscle strength source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/20886510.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "7df48f2e8cf3da738d09c37cb1e96cb62a3eceae213ff722b49855ea174f863e", "start_char": 0, "end_char": 1053, "text_sha256": "7df48f2e8cf3da738d09c37cb1e96cb62a3eceae213ff722b49855ea174f863e"}
experimental_model
Randomized double-blind crossover trial
exposure
CoQ10 1200 mg/day for 60 days
limitations
Heterogeneous mitochondrial disease, not exclusively genetically proven primary CoQ deficiency; small short study.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
30 mitochondrial-cytopathy patients
plain_language
Mitochondrial disease does not automatically imply a broad response to CoQ.
primary_references
[coq10-p20886510] A randomized trial of coenzyme Q10 in mitochondrial disorders. (2010). https://pubmed.ncbi.nlm.nih.gov/20886510/ DOI: 10.1002/mus.21758
tissue_or_cell_type
Exercise and clinical function
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 1243–1254
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Randomized double-blind crossover trial · source_derived_draft · unverified_draft
### coq10-mitochondrial-strength-null The trial found no improvement in strength or other major clinical variables despite minor exercise effects. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: Mitochondrial disease does not automatically imply a broad response to CoQ. organism: 30 mitochondrial-cytopathy patients tissue_or_cell_type: Exercise and clinical function experimental_model: Randomized double-blind crossover trial limitations: Heterogeneous mitochondrial disease, not exclusively genetically proven primary CoQ deficiency; small short study. exposure: CoQ10 1200 mg/day for 60 days evidence_span: {"source_cache": "artifacts/coq10-research/20886510.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "7df48f2e8cf3da738d09c37cb1e96cb62a3eceae213ff722b49855ea174f863e", "start_char": 0, "end_char": 1053, "text_sha256": "7df48f2e8cf3da738d09c37cb1e96cb62a3eceae213ff722b49855ea174f863e"} [coq10-p20886510] A randomized trial of coenzyme Q10 in mitochondrial disorders. (2010). https://pubmed.ncbi.nlm.nih.gov/20886510/ DOI: 10.1002/mus.21758
Complete structured claim and evidence
The case report described reduced warfarin responsiveness during CoQ use and recovery after withdrawal.
Coenzyme Q10 / CoQ10 redox system → Anticoagulant response to warfarin source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/9621803.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "510d412753fc2f3ff7e974beda97125c6112e530d6379145495e56fa01adb498", "start_char": 0, "end_char": 752, "text_sha256": "510d412753fc2f3ff7e974beda97125c6112e530d6379145495e56fa01adb498"}
experimental_model
Case report with supplement withdrawal
exposure
CoQ10 exposure then discontinuation
limitations
Single case; temporal association is not proof of mechanism or interaction frequency. Chemical similarity does not establish vitamin K activity.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
72-year-old woman taking warfarin
plain_language
A possible drug interaction was reported, but one case cannot determine how often it occurs.
primary_references
[coq10-p9621803] [Interaction between warfarin and coenzyme Q10]. (1998). https://pubmed.ncbi.nlm.nih.gov/9621803/
tissue_or_cell_type
Anticoagulant response
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 1256–1267
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Case report with supplement withdrawal · source_derived_draft · unverified_draft
### coq10-warfarin-case The case report described reduced warfarin responsiveness during CoQ use and recovery after withdrawal. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: A possible drug interaction was reported, but one case cannot determine how often it occurs. organism: 72-year-old woman taking warfarin tissue_or_cell_type: Anticoagulant response experimental_model: Case report with supplement withdrawal limitations: Single case; temporal association is not proof of mechanism or interaction frequency. Chemical similarity does not establish vitamin K activity. exposure: CoQ10 exposure then discontinuation evidence_span: {"source_cache": "artifacts/coq10-research/9621803.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "510d412753fc2f3ff7e974beda97125c6112e530d6379145495e56fa01adb498", "start_char": 0, "end_char": 752, "text_sha256": "510d412753fc2f3ff7e974beda97125c6112e530d6379145495e56fa01adb498"} [coq10-p9621803] [Interaction between warfarin and coenzyme Q10]. (1998). https://pubmed.ncbi.nlm.nih.gov/9621803/
Complete structured claim and evidence
INR remained stable and mean warfarin dose did not change significantly during CoQ versus placebo periods.
Coenzyme Q10 / CoQ10 redox system → Warfarin dose required to maintain anticoagulation source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/12772396.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0c668036863182db6c07a131179cd78f773088609808e320fdee5fe34d2d9d14", "start_char": 0, "end_char": 1260, "text_sha256": "0c668036863182db6c07a131179cd78f773088609808e320fdee5fe34d2d9d14"}
experimental_model
Randomized double-blind placebo-controlled crossover trial
exposure
CoQ10 100 mg/day for four weeks; separate ginkgo and placebo periods
limitations
Small short trial with dose adjustment to maintain INR. Same trial was reported in a 2002 letter; not independent replication.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
24 stable warfarin-treated outpatients; three withdrawals
plain_language
A small controlled study did not demonstrate the interaction reported in cases.
primary_references
[coq10-p12772396] [Effect of Coenzyme Q10 and Ginkgo biloba on warfarin dosage in patients on long-term warfarin treatment. A randomized, double-blind, placebo-controlled cross-over trial]. (2003). https://pubmed.ncbi.nlm.nih.gov/12772396/
tissue_or_cell_type
INR and adjusted weekly warfarin dose
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 1269–1280
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Randomized double-blind placebo-controlled crossover trial · source_derived_draft · unverified_draft
### coq10-warfarin-trial INR remained stable and mean warfarin dose did not change significantly during CoQ versus placebo periods. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: A small controlled study did not demonstrate the interaction reported in cases. organism: 24 stable warfarin-treated outpatients; three withdrawals tissue_or_cell_type: INR and adjusted weekly warfarin dose experimental_model: Randomized double-blind placebo-controlled crossover trial limitations: Small short trial with dose adjustment to maintain INR. Same trial was reported in a 2002 letter; not independent replication. exposure: CoQ10 100 mg/day for four weeks; separate ginkgo and placebo periods evidence_span: {"source_cache": "artifacts/coq10-research/12772396.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0c668036863182db6c07a131179cd78f773088609808e320fdee5fe34d2d9d14", "start_char": 0, "end_char": 1260, "text_sha256": "0c668036863182db6c07a131179cd78f773088609808e320fdee5fe34d2d9d14"} [coq10-p12772396] [Effect of Coenzyme Q10 and Ginkgo biloba on warfarin dosage in patients on long-term warfarin treatment. A randomized, double-blind, placebo-controlled cross-over trial]. (2003). https://pubmed.ncbi.nlm.nih.gov/12772396/
Complete structured claim and evidence
FMN restored rotenone-sensitive NADH:quinone reductase activity after alkaline reductive inactivation of bovine membrane-bound complex I.
Flavin mononucleotide → Mitochondrial respiratory complex I source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_spans
[{"source_bundle": "artifacts/riboflavin_metabolism_sources.json", "source_key": "PMC2440658", "locator": "HTML article p", "paragraph_index": 19, "char_start": 0, "char_end": 1242, "evidence_access": "full-text"}]
experimental_model
Bovine heart submitochondrial particles; alkaline reductive inactivation and cofactor reconstitution.
exposure
10 micromolar FMN after NADH/respiratory blockade at pH 10.
limitations
pH 10 treatment; not a test of dietary deficiency or oral supplementation.
nutrient_topic
Riboflavin research collection; topical membership is not evidence of a direct dietary effect. · Riboflavin (vitamin B2)
organism
Bos taurus
plain_language
Putting the correct flavin back restored this experimentally inactivated respiratory enzyme.
primary_references
[gostimskaya-2007-complex-i-fmn] Reversible dissociation of flavin mononucleotide from the mammalian membrane-bound NADH: ubiquinone oxidoreductase (complex I) (2007). https://pubmed.ncbi.nlm.nih.gov/18037377/ DOI: 10.1016/j.febslet.2007.11.048
tissue_or_cell_type
Heart submitochondrial particles
trigger_kind
machinery_impairment Imported condition classification; unverified.
Riboflavin: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 570–581
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Bovine heart submitochondrial particles; alkaline reductive inactivation and cofactor reconstitution. · source_derived_draft · unverified_draft
### b2-met-complex-i-fmn-reconstitution FMN restored rotenone-sensitive NADH:quinone reductase activity after alkaline reductive inactivation of bovine membrane-bound complex I. Condition category: machinery_impairment nutrient_topic: Riboflavin research collection; topical membership is not evidence of a direct dietary effect. plain_language: Putting the correct flavin back restored this experimentally inactivated respiratory enzyme. organism: Bos taurus tissue_or_cell_type: Heart submitochondrial particles experimental_model: Bovine heart submitochondrial particles; alkaline reductive inactivation and cofactor reconstitution. limitations: pH 10 treatment; not a test of dietary deficiency or oral supplementation. exposure: 10 micromolar FMN after NADH/respiratory blockade at pH 10. evidence_spans: [{"source_bundle": "artifacts/riboflavin_metabolism_sources.json", "source_key": "PMC2440658", "locator": "HTML article p", "paragraph_index": 19, "char_start": 0, "char_end": 1242, "evidence_access": "full-text"}] [gostimskaya-2007-complex-i-fmn] Reversible dissociation of flavin mononucleotide from the mammalian membrane-bound NADH: ubiquinone oxidoreductase (complex I) (2007). https://pubmed.ncbi.nlm.nih.gov/18037377/ DOI: 10.1016/j.febslet.2007.11.048
Complete structured claim and evidence
Riboflavin-free culture reduced complex I abundance; human 143B proteomics identified particularly strong loss of its NADH-oxidizing N-module subunits.
Riboflavin (vitamin B2) → Mitochondrial respiratory complex I source_derived_draftungraded
Experimental context and source evidence
availability_state
nutrient_deficiency Imported condition classification; unverified.
evidence_spans
[{"source_bundle": "artifacts/riboflavin_metabolism_sources.json", "source_key": "PMC10767280", "locator": "XML .//body//p", "paragraph_index": 58, "char_start": 0, "char_end": 905, "evidence_access": "full-text"}]
experimental_model
Human 143B cells and mouse adult fibroblasts, riboflavin-free medium and separate DPI interventions.
exposure
Riboflavin-free medium; matched control contained 1 micromolar riboflavin.
limitations
Cell-culture withdrawal; proteomic abundance does not establish a human blood threshold.
nutrient_topic
Riboflavin research collection; topical membership is not evidence of a direct dietary effect. · Riboflavin (vitamin B2)
organism
Homo sapiens; Mus musculus
plain_language
Removing B2 reduced parts needed to build the respiratory enzyme.
primary_references
[curtabbi-2024-fmn-assembly] Regulation of respiratory complex I assembly by FMN cofactor targeting (2024). https://pubmed.ncbi.nlm.nih.gov/38145589/ DOI: 10.1016/j.redox.2023.103001
tissue_or_cell_type
143B cells and mouse adult fibroblasts
trigger_kind
nutrient_deficiency Imported condition classification; unverified.
Riboflavin: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 609–620
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human 143B cells and mouse adult fibroblasts, riboflavin-free medium and separate DPI interventions. · source_derived_draft · unverified_draft
### b2-met-depletion-complex-i Riboflavin-free culture reduced complex I abundance; human 143B proteomics identified particularly strong loss of its NADH-oxidizing N-module subunits. Condition category: nutrient_deficiency nutrient_topic: Riboflavin research collection; topical membership is not evidence of a direct dietary effect. plain_language: Removing B2 reduced parts needed to build the respiratory enzyme. organism: Homo sapiens; Mus musculus tissue_or_cell_type: 143B cells and mouse adult fibroblasts experimental_model: Human 143B cells and mouse adult fibroblasts, riboflavin-free medium and separate DPI interventions. limitations: Cell-culture withdrawal; proteomic abundance does not establish a human blood threshold. exposure: Riboflavin-free medium; matched control contained 1 micromolar riboflavin. evidence_spans: [{"source_bundle": "artifacts/riboflavin_metabolism_sources.json", "source_key": "PMC10767280", "locator": "XML .//body//p", "paragraph_index": 58, "char_start": 0, "char_end": 905, "evidence_access": "full-text"}] [curtabbi-2024-fmn-assembly] Regulation of respiratory complex I assembly by FMN cofactor targeting (2024). https://pubmed.ncbi.nlm.nih.gov/38145589/ DOI: 10.1016/j.redox.2023.103001
Complete structured claim and evidence
Purified human complex II coupled succinate oxidation to ubiquinone reduction in a UQ1/DCIP assay, with reported kcat 0.67 +/- 0.02 per second.
Respiratory complex II → Ubiquinone-1 source_derived_draftungraded
Experimental context and source evidence
evidence_spans
[{"source_bundle": "artifacts/riboflavin_metabolism_sources.json", "source_key": "PMC10161127", "locator": "XML .//body//p", "paragraph_index": 2, "char_start": 0, "char_end": 1105, "evidence_access": "full-text"}]
experimental_model
Human complex II purified from HEK293F cells, cryo-EM, EPR and succinate-quinone activity assays.
exposure
No nutrient intervention; structural or biochemical characterization.
limitations
UQ1/DCIP are assay reagents; the isolated turnover value is not whole-cell ATP production.
nutrient_topic
Riboflavin research collection; topical membership is not evidence of a direct dietary effect. · Riboflavin (vitamin B2)
organism
Homo sapiens
plain_language
The intact complex moves electrons from succinate into a quinone carrier.
primary_references
[du-2023-human-complex-ii] Structure of the human respiratory complex II (2023). https://pubmed.ncbi.nlm.nih.gov/37098072/ DOI: 10.1073/pnas.2216713120
tissue_or_cell_type
HEK293F-derived purified complex II
Riboflavin: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 663–674
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human complex II purified from HEK293F cells, cryo-EM, EPR and succinate-quinone activity assays. · source_derived_draft · unverified_draft
### b2-met-human-complex-ii-succinate-quinone Purified human complex II coupled succinate oxidation to ubiquinone reduction in a UQ1/DCIP assay, with reported kcat 0.67 +/- 0.02 per second. Condition category: normal nutrient_topic: Riboflavin research collection; topical membership is not evidence of a direct dietary effect. plain_language: The intact complex moves electrons from succinate into a quinone carrier. organism: Homo sapiens tissue_or_cell_type: HEK293F-derived purified complex II experimental_model: Human complex II purified from HEK293F cells, cryo-EM, EPR and succinate-quinone activity assays. limitations: UQ1/DCIP are assay reagents; the isolated turnover value is not whole-cell ATP production. exposure: No nutrient intervention; structural or biochemical characterization. evidence_spans: [{"source_bundle": "artifacts/riboflavin_metabolism_sources.json", "source_key": "PMC10161127", "locator": "XML .//body//p", "paragraph_index": 2, "char_start": 0, "char_end": 1105, "evidence_access": "full-text"}] [du-2023-human-complex-ii] Structure of the human respiratory complex II (2023). https://pubmed.ncbi.nlm.nih.gov/37098072/ DOI: 10.1073/pnas.2216713120
Complete structured claim and evidence
Porcine ETF-QO crystal structures resolved one FAD and one [4Fe-4S] cluster per protein, together with a separate ubiquinone-binding region.
Porcine electron transfer flavoprotein dehydrogenase → FAD source_derived_draftungraded
Experimental context and source evidence
cross_nutrient
B2-derived FAD and iron-containing cluster are distinct required molecular components; this does not establish supplement interactions.
evidence_spans
[{"source_bundle": "artifacts/riboflavin_metabolism_sources.json", "source_key": "PMC1637562", "locator": "HTML article p", "paragraph_index": 10, "char_start": 0, "char_end": 3701, "evidence_access": "full-text"}]
experimental_model
Purified porcine ETF-QO crystal structures with and without bound ubiquinone.
exposure
No nutrient intervention; structural or biochemical characterization.
limitations
Static structure; the exact electron-entry sequence required additional functional experiments.
nutrient_topic
Riboflavin research collection; topical membership is not evidence of a direct dietary effect. · Riboflavin (vitamin B2)
organism
Sus scrofa
plain_language
ETF-QO combines flavin and iron-sulfur chemistry in one protein downstream of ETF.
primary_references
[zhang-2006-etf-qo] Structure of electron transfer flavoprotein-ubiquinone oxidoreductase and electron transfer to the mitochondrial ubiquinone pool (2006). https://pubmed.ncbi.nlm.nih.gov/17050691/ DOI: 10.1073/pnas.0604567103
tissue_or_cell_type
Purified porcine mitochondrial ETF-QO
Riboflavin: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 767–779
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified porcine ETF-QO crystal structures with and without bound ubiquinone. · source_derived_draft · unverified_draft
### b2-met-porcine-etfdh-cofactors Porcine ETF-QO crystal structures resolved one FAD and one [4Fe-4S] cluster per protein, together with a separate ubiquinone-binding region. Condition category: normal nutrient_topic: Riboflavin research collection; topical membership is not evidence of a direct dietary effect. plain_language: ETF-QO combines flavin and iron-sulfur chemistry in one protein downstream of ETF. organism: Sus scrofa tissue_or_cell_type: Purified porcine mitochondrial ETF-QO experimental_model: Purified porcine ETF-QO crystal structures with and without bound ubiquinone. limitations: Static structure; the exact electron-entry sequence required additional functional experiments. exposure: No nutrient intervention; structural or biochemical characterization. cross_nutrient: B2-derived FAD and iron-containing cluster are distinct required molecular components; this does not establish supplement interactions. evidence_spans: [{"source_bundle": "artifacts/riboflavin_metabolism_sources.json", "source_key": "PMC1637562", "locator": "HTML article p", "paragraph_index": 10, "char_start": 0, "char_end": 3701, "evidence_access": "full-text"}] [zhang-2006-etf-qo] Structure of electron transfer flavoprotein-ubiquinone oxidoreductase and electron transfer to the mitochondrial ubiquinone pool (2006). https://pubmed.ncbi.nlm.nih.gov/17050691/ DOI: 10.1073/pnas.0604567103
Complete structured claim and evidence
Selective effects of ETF-QO FAD-site mutations supported electron entry from ETF through the [4Fe-4S] center, followed by flavin-mediated transfer to ubiquinone.
Rhodobacter sphaeroides ETF-QO → [4Fe-4S] iron-sulfur cluster source_derived_draftungraded
Experimental context and source evidence
cross_nutrient
Direct mechanistic integration of an iron-containing center with B2-derived FAD.
evidence_spans
[{"source_bundle": "artifacts/riboflavin_metabolism_sources.json", "source_key": "PMC3106343", "locator": "HTML article p", "paragraph_index": 51, "char_start": 0, "char_end": 1197, "evidence_access": "full-text"}]
experimental_model
Recombinant Rhodobacter sphaeroides ETF-QO; human ETF and MCAD in mixed-species reconstitution; mutagenesis and EPR.
exposure
No nutrient intervention; structural or biochemical characterization.
limitations
Mechanistic inference from mutagenesis/EPR and activity; no dietary iron or B2 intervention.
nutrient_topic
Riboflavin research collection; topical membership is not evidence of a direct dietary effect. · Riboflavin (vitamin B2)
organism
Rhodobacter sphaeroides; human ETF/MCAD reagents
plain_language
ETF-QO uses its iron-sulfur center and flavin for different stages of the electron relay.
primary_references
[swanson-2008-etf-qo] The iron-sulfur cluster of electron transfer flavoprotein-ubiquinone oxidoreductase is the electron acceptor for electron transfer flavoprotein (2008). https://pubmed.ncbi.nlm.nih.gov/18672901/ DOI: 10.1021/bi800507p
tissue_or_cell_type
Purified proteins
Riboflavin: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 794–806
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant Rhodobacter sphaeroides ETF-QO; human ETF and MCAD in mixed-species reconstitution; mutagenesis and EPR. · source_derived_draft · unverified_draft
### b2-met-etf-qo-iron-sulfur-entry Selective effects of ETF-QO FAD-site mutations supported electron entry from ETF through the [4Fe-4S] center, followed by flavin-mediated transfer to ubiquinone. Condition category: normal nutrient_topic: Riboflavin research collection; topical membership is not evidence of a direct dietary effect. plain_language: ETF-QO uses its iron-sulfur center and flavin for different stages of the electron relay. organism: Rhodobacter sphaeroides; human ETF/MCAD reagents tissue_or_cell_type: Purified proteins experimental_model: Recombinant Rhodobacter sphaeroides ETF-QO; human ETF and MCAD in mixed-species reconstitution; mutagenesis and EPR. limitations: Mechanistic inference from mutagenesis/EPR and activity; no dietary iron or B2 intervention. exposure: No nutrient intervention; structural or biochemical characterization. cross_nutrient: Direct mechanistic integration of an iron-containing center with B2-derived FAD. evidence_spans: [{"source_bundle": "artifacts/riboflavin_metabolism_sources.json", "source_key": "PMC3106343", "locator": "HTML article p", "paragraph_index": 51, "char_start": 0, "char_end": 1197, "evidence_access": "full-text"}] [swanson-2008-etf-qo] The iron-sulfur cluster of electron transfer flavoprotein-ubiquinone oxidoreductase is the electron acceptor for electron transfer flavoprotein (2008). https://pubmed.ncbi.nlm.nih.gov/18672901/ DOI: 10.1021/bi800507p
Complete structured claim and evidence
Under the same supplemented culture conditions, ETF-QO variants linked to riboflavin-responsive MADD exhibited milder folding defects than the nonresponsive or partly responsive variants.
Human ETF-QO variants studied by Cornelius 2012 → Human electron transfer flavoprotein dehydrogenase / ETFDH source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_spans
[{"source_bundle": "artifacts/riboflavin_metabolism_sources.json", "source_key": "PMID22611163", "locator": "metadata.abstractText", "paragraph_index": 0, "char_start": 0, "char_end": 1899, "evidence_access": "primary-abstract"}]
experimental_model
Human HEK-293 cells expressing patient-associated ETF-QO variants under varied riboflavin and temperature.
exposure
Variant expression with supplemented riboflavin, comparing clinical response groups.
limitations
Response-associated molecular comparison; no dose recommendation and no claim that all missense variants respond.
nutrient_topic
Riboflavin research collection; topical membership is not evidence of a direct dietary effect. · Riboflavin (vitamin B2)
organism
Homo sapiens
plain_language
Different inherited changes left different amounts of rescuable protein function.
primary_references
[cornelius-2012-etfdh-rescue] Molecular mechanisms of riboflavin responsiveness in patients with ETF-QO variations and multiple acyl-CoA dehydrogenation deficiency (2012). https://pubmed.ncbi.nlm.nih.gov/22611163/ DOI: 10.1093/hmg/dds175
tissue_or_cell_type
HEK-293 expression system
trigger_kind
machinery_impairment Imported condition classification; unverified.
Riboflavin: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 821–832
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human HEK-293 cells expressing patient-associated ETF-QO variants under varied riboflavin and temperature. · source_derived_draft · unverified_draft
### b2-met-etfdh-responsive-milder-folding Under the same supplemented culture conditions, ETF-QO variants linked to riboflavin-responsive MADD exhibited milder folding defects than the nonresponsive or partly responsive variants. Condition category: machinery_impairment nutrient_topic: Riboflavin research collection; topical membership is not evidence of a direct dietary effect. plain_language: Different inherited changes left different amounts of rescuable protein function. organism: Homo sapiens tissue_or_cell_type: HEK-293 expression system experimental_model: Human HEK-293 cells expressing patient-associated ETF-QO variants under varied riboflavin and temperature. limitations: Response-associated molecular comparison; no dose recommendation and no claim that all missense variants respond. exposure: Variant expression with supplemented riboflavin, comparing clinical response groups. evidence_spans: [{"source_bundle": "artifacts/riboflavin_metabolism_sources.json", "source_key": "PMID22611163", "locator": "metadata.abstractText", "paragraph_index": 0, "char_start": 0, "char_end": 1899, "evidence_access": "primary-abstract"}] [cornelius-2012-etfdh-rescue] Molecular mechanisms of riboflavin responsiveness in patients with ETF-QO variations and multiple acyl-CoA dehydrogenation deficiency (2012). https://pubmed.ncbi.nlm.nih.gov/22611163/ DOI: 10.1093/hmg/dds175
Complete structured claim and evidence
ETFDH variants associated with nonresponsive or partially responsive MADD showed severe misfolding in HEK-293 cells even in riboflavin-supplemented medium.
Human ETF-QO variants studied by Cornelius 2012 → Human electron transfer flavoprotein dehydrogenase / ETFDH source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_spans
[{"source_bundle": "artifacts/riboflavin_metabolism_sources.json", "source_key": "PMID22611163", "locator": "metadata.abstractText", "paragraph_index": 0, "char_start": 0, "char_end": 1899, "evidence_access": "primary-abstract"}]
experimental_model
Human HEK-293 cells expressing patient-associated ETF-QO variants under varied riboflavin and temperature.
exposure
Clinical-response-defined ETFDH variants; supplemented culture riboflavin.
limitations
Primary abstract-level claim; variants are grouped by this study, not a universal response classifier.
nutrient_topic
Riboflavin research collection; topical membership is not evidence of a direct dietary effect. · Riboflavin (vitamin B2)
organism
Homo sapiens
plain_language
Some inherited ETF-QO defects remained severe despite greater B2 supply.
primary_references
[cornelius-2012-etfdh-rescue] Molecular mechanisms of riboflavin responsiveness in patients with ETF-QO variations and multiple acyl-CoA dehydrogenation deficiency (2012). https://pubmed.ncbi.nlm.nih.gov/22611163/ DOI: 10.1093/hmg/dds175
tissue_or_cell_type
HEK-293 expression system
trigger_kind
machinery_impairment Imported condition classification; unverified.
Riboflavin: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 808–819
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human HEK-293 cells expressing patient-associated ETF-QO variants under varied riboflavin and temperature. · source_derived_draft · unverified_draft
### b2-met-etfdh-severe-rescue-boundary ETFDH variants associated with nonresponsive or partially responsive MADD showed severe misfolding in HEK-293 cells even in riboflavin-supplemented medium. Condition category: machinery_impairment nutrient_topic: Riboflavin research collection; topical membership is not evidence of a direct dietary effect. plain_language: Some inherited ETF-QO defects remained severe despite greater B2 supply. organism: Homo sapiens tissue_or_cell_type: HEK-293 expression system experimental_model: Human HEK-293 cells expressing patient-associated ETF-QO variants under varied riboflavin and temperature. limitations: Primary abstract-level claim; variants are grouped by this study, not a universal response classifier. exposure: Clinical-response-defined ETFDH variants; supplemented culture riboflavin. evidence_spans: [{"source_bundle": "artifacts/riboflavin_metabolism_sources.json", "source_key": "PMID22611163", "locator": "metadata.abstractText", "paragraph_index": 0, "char_start": 0, "char_end": 1899, "evidence_access": "primary-abstract"}] [cornelius-2012-etfdh-rescue] Molecular mechanisms of riboflavin responsiveness in patients with ETF-QO variations and multiple acyl-CoA dehydrogenation deficiency (2012). https://pubmed.ncbi.nlm.nih.gov/22611163/ DOI: 10.1093/hmg/dds175
Complete structured claim and evidence
The sodium-linked membrane change reduced free ubiquinone mobility between complexes II and III, while transport within supercomplexes was spared.
Sodium ion → Mobility of free ubiquinone between respiratory complexes II and III source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sodium-research/32728214.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "2780431aa362c99c816f986e923fd65ed0c0324e8c8674af8ff2a2f9367762c1", "start_char": 0, "end_char": 1533, "text_sha256": "2780431aa362c99c816f986e923fd65ed0c0324e8c8674af8ff2a2f9367762c1"}
experimental_model
Acute-hypoxia cellular and mitochondrial experiments with ion imaging and respiratory/membrane assays
exposure
Acute hypoxia and inhibition of mitochondrial sodium/calcium exchange
limitations
Mechanistic research under hypoxia, including multiple preparations. Do not infer that dietary salt drives this chain, that every tissue responds identically, or that ROS here proves disease.
nutrient_topic
Sodium research collection; topical membership is not evidence of a direct dietary effect. · Sodium
organism
Human and mouse cells; additional rat vascular experiments in the paper
plain_language
The effect depended on how the respiratory machinery was organized.
primary_references
[sodium-p32728214] Na+ controls hypoxic signalling by the mitochondrial respiratory chain. (2020). https://pubmed.ncbi.nlm.nih.gov/32728214/ DOI: 10.1038/s41586-020-2551-y
tissue_or_cell_type
Mitochondrial matrix and inner membrane
Sodium: gradients, nutrient transport, fluid regulation and loss states (2026-09-17) · lines 798–809
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Acute-hypoxia cellular and mitochondrial experiments with ion imaging and respiratory/membrane assays · source_derived_draft · unverified_draft
### sodium-quinone-mobility The sodium-linked membrane change reduced free ubiquinone mobility between complexes II and III, while transport within supercomplexes was spared. Condition category: normal nutrient_topic: Sodium research collection; topical membership is not evidence of a direct dietary effect. plain_language: The effect depended on how the respiratory machinery was organized. organism: Human and mouse cells; additional rat vascular experiments in the paper tissue_or_cell_type: Mitochondrial matrix and inner membrane experimental_model: Acute-hypoxia cellular and mitochondrial experiments with ion imaging and respiratory/membrane assays limitations: Mechanistic research under hypoxia, including multiple preparations. Do not infer that dietary salt drives this chain, that every tissue responds identically, or that ROS here proves disease. exposure: Acute hypoxia and inhibition of mitochondrial sodium/calcium exchange evidence_span: {"source_cache": "artifacts/sodium-research/32728214.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "2780431aa362c99c816f986e923fd65ed0c0324e8c8674af8ff2a2f9367762c1", "start_char": 0, "end_char": 1533, "text_sha256": "2780431aa362c99c816f986e923fd65ed0c0324e8c8674af8ff2a2f9367762c1"} [sodium-p32728214] Na+ controls hypoxic signalling by the mitochondrial respiratory chain. (2020). https://pubmed.ncbi.nlm.nih.gov/32728214/ DOI: 10.1038/s41586-020-2551-y
Complete structured claim and evidence
Ubiquinol-10 reduced alpha-tocopheroxyl to alpha-tocopherol in stopped-flow solution experiments, with second-order rate constants of 3.74 × 10^5 M^-1 s^-1 in benzene and 2.15 × 10^5 M^-1 s^-1 in ethanol at 25 °C.
Reduced CoQ10 → Alpha-tocopherol source_derived_draftungraded
Experimental context and source evidence
cross_nutrient
true
evidence_location
Primary abstract
experimental_model
Stopped-flow spectrophotometry
exposure
25 °C; reduced CoQ10.
limitations
No direct tissue flux or oral CoQ10 effect was measured.
nutrient_topic
Vitamin E research collection; topical membership is not evidence of a direct dietary effect. · Vitamin E
organism
Cell-free
plain_language
Reduced CoQ10 recycled the vitamin E radical in these chemical assays.
primary_references
[ver-mukai1990] Stopped-flow kinetic study of the regeneration reaction of tocopheroxyl radical by reduced ubiquinone-10 in solution. (1990). https://pubmed.ncbi.nlm.nih.gov/2383582/ DOI: 10.1016/0304-4165(90)90176-w
tissue_or_cell_type
Benzene or ethanol solution
Vitamin E: transport, membrane protection and nutrient interactions (2026-09-17) · lines 508–520
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Stopped-flow spectrophotometry · source_derived_draft · unverified_draft
### ver-ubiquinol-regeneration Ubiquinol-10 reduced alpha-tocopheroxyl to alpha-tocopherol in stopped-flow solution experiments, with second-order rate constants of 3.74 × 10^5 M^-1 s^-1 in benzene and 2.15 × 10^5 M^-1 s^-1 in ethanol at 25 °C. Condition category: normal nutrient_topic: Vitamin E research collection; topical membership is not evidence of a direct dietary effect. plain_language: Reduced CoQ10 recycled the vitamin E radical in these chemical assays. organism: Cell-free tissue_or_cell_type: Benzene or ethanol solution experimental_model: Stopped-flow spectrophotometry limitations: No direct tissue flux or oral CoQ10 effect was measured. exposure: 25 °C; reduced CoQ10. cross_nutrient: true evidence_location: Primary abstract [ver-mukai1990] Stopped-flow kinetic study of the regeneration reaction of tocopheroxyl radical by reduced ubiquinone-10 in solution. (1990). https://pubmed.ncbi.nlm.nih.gov/2383582/ DOI: 10.1016/0304-4165(90)90176-w
Complete structured claim and evidence
The same solution study detected no reaction of oxidized ubiquinone-10 with tocopheroxyl radicals, distinguishing it from the active reduced ubiquinol-10 form.
Ubiquinone-10 → Alpha-tocopherol source_derived_draftungraded
Experimental context and source evidence
cross_nutrient
true
evidence_location
Primary abstract
experimental_model
Stopped-flow comparison of CoQ10 redox states
exposure
Oxidized ubiquinone-10 comparator.
limitations
A non-detected reaction under these assay conditions is not an assertion that cellular CoQ cannot first be reduced.
nutrient_topic
Vitamin E research collection; topical membership is not evidence of a direct dietary effect. · Vitamin E
organism
Cell-free
plain_language
CoQ10 needed to be in its reduced state for the measured recycling reaction.
primary_references
[ver-mukai1990] Stopped-flow kinetic study of the regeneration reaction of tocopheroxyl radical by reduced ubiquinone-10 in solution. (1990). https://pubmed.ncbi.nlm.nih.gov/2383582/ DOI: 10.1016/0304-4165(90)90176-w
tissue_or_cell_type
Chemical solution
Vitamin E: transport, membrane protection and nutrient interactions (2026-09-17) · lines 522–534
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Stopped-flow comparison of CoQ10 redox states · source_derived_draft · unverified_draft
### ver-oxidized-coq-no-regeneration The same solution study detected no reaction of oxidized ubiquinone-10 with tocopheroxyl radicals, distinguishing it from the active reduced ubiquinol-10 form. Condition category: normal nutrient_topic: Vitamin E research collection; topical membership is not evidence of a direct dietary effect. plain_language: CoQ10 needed to be in its reduced state for the measured recycling reaction. organism: Cell-free tissue_or_cell_type: Chemical solution experimental_model: Stopped-flow comparison of CoQ10 redox states limitations: A non-detected reaction under these assay conditions is not an assertion that cellular CoQ cannot first be reduced. exposure: Oxidized ubiquinone-10 comparator. cross_nutrient: true evidence_location: Primary abstract [ver-mukai1990] Stopped-flow kinetic study of the regeneration reaction of tocopheroxyl radical by reduced ubiquinone-10 in solution. (1990). https://pubmed.ncbi.nlm.nih.gov/2383582/ DOI: 10.1016/0304-4165(90)90176-w
Complete structured claim and evidence
Another defense changes how vulnerable cells are to GPX4 loss.
FSP1 reduces CoQ and supplies a lipid-radical defense operating in parallel with GPX4.
FSP1 → Reduced CoQ10 source_derived_draftliterature_reviewed:direct_experimental
Experimental context and source evidence
cell_type
Experimental cultured cells
experimental_model
Cell genetics and biochemical experiments
limitations
Capacity and dependence vary by cell; not a universal dietary threshold.
organism
Human cell models
Selenium: literature corrections and mechanism additions · lines 1492–1502
Metabolic Ledger literature curation, 17 September 2026; primary papers linked individually · supports · Cell genetics and biochemical experiments · secondary_verified · secondary_verified
## fsp1-parallel Another defense changes how vulnerable cells are to GPX4 loss. FSP1 reduces CoQ and supplies a lipid-radical defense operating in parallel with GPX4. Organism: Human cell models Cell type: Experimental cultured cells Experimental model: Cell genetics and biochemical experiments Limitations: Capacity and dependence vary by cell; not a universal dietary threshold. Primary reference: [The CoQ oxidoreductase FSP1 acts parallel to GPX4 to inhibit ferroptosis](https://www.nature.com/articles/s41586-019-1705-2)
Complete structured claim and evidence
FSP1 reduced vitamin K quinones to radical-trapping hydroquinones using NAD(P)H.
FSP1 / AIFM2 → Reduced vitamin K hydroquinone family source_derived_draftungraded
Experimental context and source evidence
evidence_span
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experimental_model
Enzyme/liposome chemistry, knockout cells and warfarin-exposed mice
exposure
MK-4/K1, NAD(P)H, FSP1 loss and inhibitors
limitations
Preclinical experiments; not a demonstrated oral MK-7 treatment for ferroptosis-related disease or a self-treatment regimen for anticoagulant poisoning.
nutrient_topic
Vitamin K2 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin K2 / menaquinone family
organism
Human recombinant FSP1, mammalian cells and mice
plain_language
A niacin-derived electron donor helps regenerate the reduced antioxidant form.
primary_references
[k2-p35922516] A non-canonical vitamin K cycle is a potent ferroptosis suppressor. (2022). https://pubmed.ncbi.nlm.nih.gov/35922516/ DOI: 10.1038/s41586-022-05022-3
tissue_or_cell_type
Lipid peroxidation and vitamin K reduction
Vitamin K2: menaquinone forms, carboxylation, recycling and nutrient interactions (2026-09-17) · lines 773–784
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Enzyme/liposome chemistry, knockout cells and warfarin-exposed mice · source_derived_draft · unverified_draft
### k2-fsp1-k-reduction FSP1 reduced vitamin K quinones to radical-trapping hydroquinones using NAD(P)H. Condition category: normal nutrient_topic: Vitamin K2 research collection; topical membership is not evidence of a direct dietary effect. plain_language: A niacin-derived electron donor helps regenerate the reduced antioxidant form. organism: Human recombinant FSP1, mammalian cells and mice tissue_or_cell_type: Lipid peroxidation and vitamin K reduction experimental_model: Enzyme/liposome chemistry, knockout cells and warfarin-exposed mice limitations: Preclinical experiments; not a demonstrated oral MK-7 treatment for ferroptosis-related disease or a self-treatment regimen for anticoagulant poisoning. exposure: MK-4/K1, NAD(P)H, FSP1 loss and inhibitors evidence_span: {"source_cache": "artifacts/k2-research/35922516.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "3bd5750fd2d12a754ad4237018851391c6b5b80bac6ad58307321fb7c3042c5a", "start_char": 0, "end_char": 1403, "text_sha256": "3bd5750fd2d12a754ad4237018851391c6b5b80bac6ad58307321fb7c3042c5a"} [k2-p35922516] A non-canonical vitamin K cycle is a potent ferroptosis suppressor. (2022). https://pubmed.ncbi.nlm.nih.gov/35922516/ DOI: 10.1038/s41586-022-05022-3
Complete structured claim and evidence
Vitamin K2 entered mitochondria but restored neither respiratory electron flow nor ATP synthesis in CoQ-deficient human cells and yeast; CoQ4 did restore function.
Menaquinone-4 / MK-4 / menatetrenone → Mitochondrial respiratory electron transfer source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/k2-research/31024065.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "23cca3c157b598de639355c855be4221ce916ee9a338e2b59923fc980614281e", "start_char": 0, "end_char": 943, "text_sha256": "23cca3c157b598de639355c855be4221ce916ee9a338e2b59923fc980614281e"}
experimental_model
Cellular uptake and respiratory rescue comparisons
exposure
MK-4 versus CoQ4
limitations
Different organism and deficiency model from the fly study; failure here is a boundary to extrapolation, not a clerical error in either experiment.
nutrient_topic
Vitamin K2 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin K2 / menaquinone family
organism
Human CoQ10-deficient cell lines and CoQ6-deficient yeast
plain_language
Getting into the organelle did not make MK-4 a functional substitute for CoQ.
primary_references
[k2-p31024065] Vitamin K2 cannot substitute Coenzyme Q10 as electron carrier in the mitochondrial respiratory chain of mammalian cells. (2019). https://pubmed.ncbi.nlm.nih.gov/31024065/ DOI: 10.1038/s41598-019-43014-y
tissue_or_cell_type
Mitochondrial respiratory chain
trigger_kind
machinery_impairment Imported condition classification; unverified.
Vitamin K2: menaquinone forms, carboxylation, recycling and nutrient interactions (2026-09-17) · lines 877–888
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Cellular uptake and respiratory rescue comparisons · source_derived_draft · unverified_draft
### k2-mk4-not-coq Vitamin K2 entered mitochondria but restored neither respiratory electron flow nor ATP synthesis in CoQ-deficient human cells and yeast; CoQ4 did restore function. Condition category: machinery_impairment nutrient_topic: Vitamin K2 research collection; topical membership is not evidence of a direct dietary effect. plain_language: Getting into the organelle did not make MK-4 a functional substitute for CoQ. organism: Human CoQ10-deficient cell lines and CoQ6-deficient yeast tissue_or_cell_type: Mitochondrial respiratory chain experimental_model: Cellular uptake and respiratory rescue comparisons limitations: Different organism and deficiency model from the fly study; failure here is a boundary to extrapolation, not a clerical error in either experiment. exposure: MK-4 versus CoQ4 evidence_span: {"source_cache": "artifacts/k2-research/31024065.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "23cca3c157b598de639355c855be4221ce916ee9a338e2b59923fc980614281e", "start_char": 0, "end_char": 943, "text_sha256": "23cca3c157b598de639355c855be4221ce916ee9a338e2b59923fc980614281e"} [k2-p31024065] Vitamin K2 cannot substitute Coenzyme Q10 as electron carrier in the mitochondrial respiratory chain of mammalian cells. (2019). https://pubmed.ncbi.nlm.nih.gov/31024065/ DOI: 10.1038/s41598-019-43014-y
Complete structured claim and evidence
DHODH did not support vitamin K-dependent carboxylation in the tested reporter system despite its separate ubiquinone-associated ferroptosis role.
Human dihydroorotate dehydrogenase / DHODH → Vitamin K-dependent protein gamma-carboxylation source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/k2-research/36788244.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "5fda09197d386351a1b1d261c9b385db36e02eab0c238bf18599d7086b501f93", "start_char": 0, "end_char": 1359, "text_sha256": "5fda09197d386351a1b1d261c9b385db36e02eab0c238bf18599d7086b501f93"}
experimental_model
Genome-wide CRISPR screen and reporter biochemistry
exposure
FSP1 knockout/inhibition and DHODH comparison
limitations
Supports cycle biochemistry; a different ferroptosis defense enzyme need not share the same vitamin K function.
nutrient_topic
Vitamin K2 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin K2 / menaquinone family
organism
Human vitamin K-dependent reporter cells
plain_language
Similar antioxidant roles do not make two enzymes interchangeable.
primary_references
[k2-p36788244] A genome-wide CRISPR-Cas9 knockout screen identifies FSP1 as the warfarin-resistant vitamin K reductase. (2023). https://pubmed.ncbi.nlm.nih.gov/36788244/ DOI: 10.1038/s41467-023-36446-8
tissue_or_cell_type
Warfarin-resistant quinone reduction
Vitamin K2: menaquinone forms, carboxylation, recycling and nutrient interactions (2026-09-17) · lines 838–849
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Genome-wide CRISPR screen and reporter biochemistry · source_derived_draft · unverified_draft
### k2-dhodh-not-k-reductase DHODH did not support vitamin K-dependent carboxylation in the tested reporter system despite its separate ubiquinone-associated ferroptosis role. Condition category: normal nutrient_topic: Vitamin K2 research collection; topical membership is not evidence of a direct dietary effect. plain_language: Similar antioxidant roles do not make two enzymes interchangeable. organism: Human vitamin K-dependent reporter cells tissue_or_cell_type: Warfarin-resistant quinone reduction experimental_model: Genome-wide CRISPR screen and reporter biochemistry limitations: Supports cycle biochemistry; a different ferroptosis defense enzyme need not share the same vitamin K function. exposure: FSP1 knockout/inhibition and DHODH comparison evidence_span: {"source_cache": "artifacts/k2-research/36788244.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "5fda09197d386351a1b1d261c9b385db36e02eab0c238bf18599d7086b501f93", "start_char": 0, "end_char": 1359, "text_sha256": "5fda09197d386351a1b1d261c9b385db36e02eab0c238bf18599d7086b501f93"} [k2-p36788244] A genome-wide CRISPR-Cas9 knockout screen identifies FSP1 as the warfarin-resistant vitamin K reductase. (2023). https://pubmed.ncbi.nlm.nih.gov/36788244/ DOI: 10.1038/s41467-023-36446-8
Complete structured claim and evidence

Availability and dependencies

Each situation shows the normal role first, then what the sources report under a specific condition. A shortfall in the diet, a fault in the machinery, and a low blood reading are kept separate because they are not the same thing.

A defective tail-building enzyme limits CoQ production

Condition: machinery_impairment · Pathogenic PDSS2 variants

Normal role: PDSS2 supports production of the CoQ isoprenoid tail.

Recorded consequence: Low muscle/fibroblast CoQ and impaired decaprenyl-diphosphate synthesis.

Scope: Human infant with Leigh syndrome and nephrotic syndrome

Measured CoQ reduction after high-dose mouse exposure

Condition: biomarker_context · Acute red yeast rice gavage.

Normal role: CoQ participates in mitochondrial redox function.

Recorded consequence: Lower liver and heart CoQ10 were reported.

Scope: Male ICR mice.

Another subunit of the tail-building machinery can fail

Condition: machinery_impairment · PDSS1 D308E

Normal role: PDSS1 participates in CoQ side-chain synthesis.

Recorded consequence: CoQ-dependent OXPHOS impairment with deficient functional complementation.

Scope: Human genetics with yeast validation

Attaching the tail to the head group is a separate failure point

Condition: machinery_impairment · Biallelic pathogenic COQ2 variant

Normal role: COQ2 is the 4-hydroxybenzoate polyprenyltransferase.

Recorded consequence: Severely reduced CoQ10 biosynthesis in patient fibroblasts.

Scope: Human primary CoQ deficiency

Electron input and CoQ recycling can fail together

Condition: machinery_impairment · Muscle-specific Etfdh deletion

Normal role: ETFDH links lipid-derived electrons with complex III and CoQ homeostasis.

Recorded consequence: Complex III dysfunction and myopathy.

Scope: Mouse skeletal muscle

More protection in one membrane can mean less CoQ in another

Condition: machinery_impairment · Cytosolic STARD7 overexpression

Normal role: STARD7 coordinates intracellular CoQ distribution.

Recorded consequence: Greater ferroptosis resistance but lower mitochondrial CoQ and respiratory growth.

Scope: Engineered mammalian cells

CoQ shortage can interfere with sulfide disposal

Condition: machinery_impairment · Low cellular CoQ caused by biosynthesis impairment

Normal role: SQOR uses CoQ as electron acceptor in the first sulfide oxidation step.

Recorded consequence: Reduced sulfide oxidation, rescued by CoQ in cultured cells.

Scope: Human deficient fibroblasts and pharmacological/ADCK3-depletion models

A synthesis defect can disturb kidney sulfur and glutathione handling

Condition: machinery_impairment · Pdss2 mutant kidney with severe residual CoQ depletion

Normal role: CoQ supports sulfide oxidation.

Recorded consequence: Sulfide accumulation, lower pathway-protein levels and depleted glutathione.

Scope: Pdss2 mutant mouse kidney; brain was less depleted and unaffected in these measurements

Removing selenium from a recycling enzyme limits its CoQ reaction

Condition: machinery_impairment · Selenium-deprived, mutant or truncated enzyme forms

Normal role: TrxR1 can reduce ubiquinone to ubiquinol.

Recorded consequence: Lower ubiquinone reduction relative to the tested intact mammalian enzyme.

Scope: Purified-enzyme comparison; not a dietary selenium threshold

Blocking one CoQ-reducing route can expose mitochondrial lipids

Condition: machinery_impairment · DHODH inactivation, especially with low or inhibited GPX4

Normal role: DHODH was reported to support mitochondrial ubiquinol-dependent defense.

Recorded consequence: More mitochondrial lipid peroxidation and ferroptosis in the reported cancer models.

Scope: 2021 cancer-cell study; magnitude and inhibitor specificity disputed in 2023

A second mitochondrial CoQ-reducing route affects vulnerability

Condition: machinery_impairment · GPD2 deletion with GPX4 inhibition

Normal role: GPD2 generates reduced CoQ during glycerol-phosphate oxidation.

Recorded consequence: More mitochondrial lipid peroxidation and ferroptosis.

Scope: Cancer-cell genetic experiments

Drug-related precursor inhibition can affect muscle CoQ under some conditions

Condition: machinery_impairment · High-dose simvastatin in the studied eight-week regimen

Normal role: Endogenous synthesis maintains the muscle CoQ pool.

Recorded consequence: Muscle CoQ fell, unlike the tested atorvastatin regimen; serum values alone cannot identify this response.

Scope: Randomized human muscle-biopsy study

CoQ synthesis failure can damage kidney and hearing function

Condition: machinery_impairment · Pathogenic COQ6 variants

Normal role: COQ6 supports CoQ ring hydroxylation.

Recorded consequence: Early steroid-resistant nephrotic syndrome with sensorineural deafness in the studied families.

Scope: Human genetics with yeast validation

A methylating enzyme defect can cause primary CoQ deficiency

Condition: machinery_impairment · Biallelic COQ5 disruption

Normal role: COQ5 performs a CoQ precursor C-methylation step.

Recorded consequence: Low white-cell and available muscle CoQ with neurologic disease.

Scope: Three-sibling genetic report

Some genetic CoQ kidney disease can respond to replacement

Condition: machinery_impairment · Genetically confirmed COQ8B- or COQ6-related nephropathy

Normal role: CoQ biosynthetic proteins support kidney-cell mitochondrial function.

Recorded consequence: Proteinuria fell during CoQ treatment in this observational series.

Scope: Japanese genetic kidney-disease cohort

An electron-transfer defect can coexist with altered muscle CoQ

Condition: machinery_impairment · Biallelic ETFDH-related myopathy

Normal role: ETFDH feeds electrons into the quinone pool.

Recorded consequence: Low muscle CoQ in one series; another series found different values after accounting for mitochondrial mass.

Scope: Human MADD cohorts; actual tissue measurements matter

The sources

Every document behind this chapter is preserved word for word. Open one to read it in full with its recorded conflicts marked in place.

Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17)AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · unverified_draftRead preserved source
Riboflavin: mechanisms, deficiency and nutrient interactions (2026-09-17)AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · unverified_draftRead preserved source
Selenium: literature corrections and mechanism additionsMetabolic Ledger literature curation, 17 September 2026; primary papers linked individually · secondary_verifiedRead preserved source
Sodium: gradients, nutrient transport, fluid regulation and loss states (2026-09-17)AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · unverified_draftRead preserved source
Vitamin E: transport, membrane protection and nutrient interactions (2026-09-17)AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · unverified_draftRead preserved source
Vitamin K2: menaquinone forms, carboxylation, recycling and nutrient interactions (2026-09-17)AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · unverified_draftRead preserved source

Recorded disagreements

Where two sources say different things, both are kept and the difference is explained. You can discuss a disagreement or propose a mechanism that might account for it.

DHODH ferroptosis protection: mitochondrial pathway versus inhibitor off-target effectsThe 2021 study assigned substantial mitochondrial defense to DHODH. The 2023 experimental challenge argued that genetic effects were small and context-dependent and that strong inhibitor sensitization involved FSP1 inhibition. The original authors replied with counterarguments. This is a published mechanistic dispute, not an editorial correction.Read the recorded disagreement
ETFDH-related myopathy: depleted muscle CoQ versus no deficit after mitochondrial normalizationThe 2007 series reported low muscle CoQ in every patient; the 2013 study explicitly revisited that conclusion and found an elevated bulk pool with no deficit after citrate-synthase normalization. This challenges a universal secondary-CoQ-deficiency interpretation of ETFDH disease.Read the recorded disagreement
Statin-associated muscle pain: improvement in one trial, absent in othersThe 2014 study found pain relief, whereas the 2015 trial found no benefit after symptoms were confirmed with blinded simvastatin/placebo exposure. A 2022 trial also found no pain benefit or increase in muscle CoQ. These challenge a general claim of CoQ efficacy for statin-associated muscle pain; selection, formulation, dose and duration differed.Read the recorded disagreement

Open questions in this collection

Questions the curators could not answer from the sources in front of them, kept here with the reason each one is still open. These are gaps in this collection, not findings or proof that no one has studied them.

How fully do reconstructed ancestral enzyme kinetics and reaction order describe the intact human CoQ synthome?Short-chain substrates, protein ancestry, lipid environment and enzyme coupling differ. These are explicit experimental boundaries, not automatic scientific contradictions.
What predicts CoQ treatment response across primary deficiency, secondary depletion and common chronic diseases?A disease label, serum level or genetic association does not substitute for tissue measurements and an appropriate clinical comparison.
How frequent and mechanistically specific is the proposed CoQ-warfarin interaction?Case reports and a small short controlled trial provide different evidence strengths; this is not established vitamin K-like activity or a basis to alter anticoagulant dosing.
Do low methyl-donor, flavin, iron, magnesium or zinc pools actually limit CoQ synthesis in a given person?Cofactor use and reconstructed-enzyme dependence do not establish a clinical nutrient deficiency, optimal ratio or benefit from adding the cofactor.
What predicts whether oral CoQ reaches the affected membrane and restores its function?Plasma exposure, whole-tissue abundance, mitochondrial content and plasma-membrane antioxidant capacity are distinct quantities.

Chapters are assembled from supplied drafts and curated literature summaries. Statements remain unverified against the primary studies, and the ledger is not medical advice.

Evidence, AI assistance and curation standards

Coenzyme Q10 / CoQ10 redox system

The mechanisms

Complex I transferred electrons from NADH to ubiquinone-10 in reconstituted membranes.

Complex III oxidizes reduced CoQ as part of respiratory electron flow examined in this study.

COQ6 substrate conversion required the FDXR-FDX2 pair in the reconstructed assay.

COQ3 methylated the tested precursor in the presence of SAM.

Added magnesium increased reconstructed COQ3 activity about fourfold and improved substrate binding; EDTA abolished turnover.

Zinc promoted COQ4 decarboxylase activity, whereas disruption of its metal-binding site eliminated detected product.

Mammalian TrxR1 reduced ubiquinone-10 to ubiquinol-10.

Cytosolic STARD7 was required for CoQ transport to the plasma membrane.

CoQ-deficient human fibroblasts had impaired sulfide oxidation proportional to their residual CoQ.

CoQ supplementation did not increase muscle CoQ or alter measured mitochondrial respiratory function, content or reactive-oxygen-species production.

The study reported DHODH-dependent ubiquinol generation as a mitochondrial ferroptosis-defense pathway.

Median protein-to-creatinine ratio fell from 1.66 to 0.19 g/gCr at 12 months; six of seven patients with 12-month data had at least a 50% reduction.

HPDL produced 4-hydroxymandelate in human cells.

Isotope tracing identified 4-hydroxymandelate as a CoQ10 head-group biosynthetic intermediate.

Patient fibroblasts with PDSS2 variants had severely impaired decaprenyl-diphosphate synthesis.

The PDSS1 D308E variant was associated with deficient CoQ-dependent respiratory activity and defective functional complementation.

Adding quinone restored CoQ-dependent respiratory activities in the tested deficient preparations.

A homozygous COQ2 variant caused severe impairment of CoQ10 synthesis in patient fibroblasts.

Human COQ3 showed O-methyltransferase activity with early and final CoQ-intermediate analogues.

Human COQ3 expression rescued respiratory growth and partially restored CoQ synthesis in coq3-null yeast.

Human COQ5 retained C-methyltransferase function and restored CoQ production when the yeast synthome was stabilized.

COQ9 enhanced substrate binding in the hydrophobic channel of COQ7.

COQ7:COQ9 assemblies deformed membranes in simulations, suggesting a route for hydrophobic precursor access.

Purified COQ9 associated with lipids including CoQ and used a conserved surface to interact with COQ7.

Human COQ8A showed ATPase activity as part of the conserved COQ8 biochemical function.

Binding to cardiolipin-containing membranes stimulated COQ8 ATPase activity.

Reconstructed COQ8A promoted CoQ production through ATPase-linked handling of insoluble pathway intermediates.

Reconstructed COQ8B promoted CoQ production through ATPase-linked handling of insoluble pathway intermediates.

Excess CoQ suppressed intermediate binding and the promoting effect of COQ8 in the reconstructed system.

Ubiquinone-10 had the highest binding affinity and fastest binding rate among the tested chain lengths; ubiquinol-10 release was not rate limiting.

The study identified an ETFDH-complex III-COQ2 assembly directing lipid-derived electrons to the respiratory chain in skeletal muscle.

Muscle-specific Etfdh deletion caused complex III dysfunction and myopathy in mice.

Truncated human DHODH penetrated the outer lipid leaflet toward membrane-embedded Q10.

PARL cleavage supported the dual mitochondrial and cytosolic localization of STARD7.

Mitochondrial STARD7 preserved CoQ synthesis, oxidative phosphorylation and cristae organization.

A CoQ variant competed with phosphatidylcholine for binding to purified STARD7.

Cytosolic STARD7 overexpression increased ferroptosis resistance while reducing mitochondrial CoQ abundance and respiratory growth.

CoQ serves as electron acceptor for SQOR at the start of mitochondrial sulfide oxidation.

CoQ supplementation rescued sulfide-pathway biochemical abnormalities in deficient fibroblasts.

Affected Pdss2-mutant kidneys accumulated sulfide and had reduced sulfide-oxidation pathway proteins.

Pdss2-mutant kidneys had glutathione depletion, whereas the less CoQ-depleted brain lacked these abnormalities.

Purified reconstructed FDXR retained FAD.

Purified reconstructed FDX2 retained a two-iron, two-sulfur cluster.

FDX2 accepted electrons from reduced FDXR in the reconstructed system.

Reconstructed COQ4 catalyzed C1 decarboxylation without the C1 hydroxylation product in this assay.

Reconstructed COQ6 supported C1 hydroxylation after the COQ4 decarboxylation step.

Reconstructed COQ5 catalyzed C-methylation with SAM.

COQ7 hydroxylation assays consumed NADH in a substrate-dependent manner.

Adding COQ9 increased COQ7 catalytic efficiency about 1.5-fold in the reconstructed system.

COQ4 expression supported an oxidative-decarboxylation route combining C1 carbon removal with hydroxylation.

Comparison with selenium-deprived and truncated mammalian TrxR forms showed selenium-dependent ubiquinone reduction.

Selenite treatment increased cytosolic TrxR activity together with ubiquinone reduction in the tested cell homogenates.

FSP1 used NAD(P)H to regenerate the reduced CoQ pool that traps lipid peroxyl radicals.

DHODH inactivation increased mitochondrial lipid peroxidation and ferroptosis in the reported GPX4-dependent experimental contexts.

The 2023 study attributed strong ferroptosis sensitization by high concentrations of DHODH inhibitors to concurrent FSP1 inhibition.

GPD2 coupled glycerol-3-phosphate oxidation to ubiquinol formation.

GPD2 deletion sensitized cancer cells to GPX4-inhibition-induced mitochondrial lipid peroxidation and ferroptosis.

The tested water-soluble formulation had 2.4-fold higher baseline-corrected exposure than standard ubiquinone capsules; the ubiquinol-capsule comparison was not statistically significant.

CoQ appeared in blood predominantly as ubiquinol regardless of which of the tested redox forms was consumed.

Simvastatin inhibits HMG-CoA reductase, an upstream enzyme in the mevalonate pathway shared by sterol and CoQ precursor production.

After four weeks, serum ubiquinone decreased while muscle ubiquinone increased; no participant developed myopathy.

Simvastatin, alone or with ezetimibe, lowered plasma CoQ; CoQ change correlated with LDL-cholesterol change and the CoQ-to-LDL ratio increased.

The authors proposed that lower plasma CoQ could reflect loss of lipoprotein carriers rather than a statin-specific depletion mechanism.

Muscle CoQ fell from 39.7 to 26.4 nmol/g with simvastatin 80 mg/day; it did not fall with atorvastatin 40 mg/day or placebo.

Respiratory-chain enzyme and citrate-synthase activities were lower in the selected simvastatin subgroup with marked muscle CoQ decline.

The 2022 trial found no effect on myalgia; individual changes in muscle CoQ did not correlate with changes in symptom intensity.

Six COQ6 mutations in 13 individuals were linked to early nephrotic syndrome and sensorineural deafness.

CoQ treatment partly reversed apoptosis after Coq6 knockdown in podocyte and zebrafish models.

Affected siblings with COQ5 duplications had low white-cell CoQ; the available muscle sample was also depleted.

All seven patients in the 2007 ETFDH-associated myopathy series had significantly reduced muscle CoQ10.

Muscle CoQ was elevated in the 34-patient cohort but not significantly different from controls after normalization to citrate synthase.

Two-year major adverse events occurred in 15% on CoQ versus 26% on placebo, hazard ratio 0.50 (95% CI 0.32-0.80).

All-cause mortality was 10% versus 18%, and cardiovascular mortality was 9% versus 16%, favoring CoQ in Q-SYMBIO.

The 16-week NT-proBNP, NYHA-class and six-minute-walk endpoints did not significantly change between trial groups.

Cardiovascular mortality was 5.9% with combined selenium/CoQ versus 12.6% with placebo in the Swedish trial.

Mean NT-proBNP at 48 months was 214 ng/L in the combined-treatment group versus 302 ng/L with placebo.

Pain severity and interference improved relative to placebo after 30 days of CoQ in the 50-patient study.

Ubiquinol did not reduce pain severity or interference versus placebo in confirmed simvastatin myalgia.