Component

Human electron transfer flavoprotein dehydrogenase / ETFDH

Human ETF:ubiquinone oxidoreductase, ETF-QO; accepts electrons from ETF and links to ubiquinone.

5 recorded relationships. Experimental role, claim status and evidence remain attached to each record.

Read recorded mechanisms Open recursive mind map

How nutrients influence it

Every nutrient with a recorded effect on this component, credited to the nutrient that acted rather than the chapter that recorded it. Open a nutrient to see the findings and the conditions they were measured under.

How nutrients reach it in more than one step

Chains of two or more recorded steps that end here, grouped by the nutrient they start from. Each step is a separate finding, so a chain is a route a mechanism could take, not proof that it does.

Tracing routes…

What it does

Every recorded relationship this component is part of, grouped by its role. Plain wording comes first; the technical statement follows.

Recorded relationships

What it acts on

  1. 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

  2. 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

What acts on it

  1. 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

  2. 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

  3. Residual low thermal stability of the studied ETF-QO variants indicated that FAD availability did not fully correct their structural defects.

    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
    Riboflavin and temperature variation in cell-expression experiments.
    limitations
    Does not determine clinical outcomes during fever or response of an untested mutation.
    nutrient_topic
    Riboflavin research collection; topical membership is not evidence of a direct dietary effect. · Riboflavin (vitamin B2)
    organism
    Homo sapiens
    plain_language
    Cofactor support did not make the altered proteins structurally normal.
    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-derived variant ETF-QO assays
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Riboflavin: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 834–845

    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-thermal-rescue-limit Residual low thermal stability of the studied ETF-QO variants indicated that FAD availability did not fully correct their structural defects. Condition category: machinery_impairment nutrient_topic: Riboflavin research collection; topical membership is not evidence of a direct dietary effect. plain_language: Cofactor support did not make the altered proteins structurally normal. organism: Homo sapiens tissue_or_cell_type: HEK-293-derived variant ETF-QO assays experimental_model: Human HEK-293 cells expressing patient-associated ETF-QO variants under varied riboflavin and temperature. limitations: Does not determine clinical outcomes during fever or response of an untested mutation. exposure: Riboflavin and temperature variation in cell-expression experiments. 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

In the sources

Preserved passages that mention this component, quoted exactly. Open one to read it in context.

    This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.

    Evidence, AI assistance and curation standards