Component

Protein cysteine CoAlation

Protein cysteine CoAlation. Identity is distinct from its gene and experimentally modified states; see each claim for organism and scope.

3 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 acts on it

  1. After removal of hydrogen peroxide from HEK293/Pank1beta cultures, induced protein CoAlation declined within 5 minutes and returned to baseline within 90 minutes.

    Protein cysteine–CoA mixed disulfides → Protein cysteine CoAlation source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    false
    evidence_location
    Full text line 115; Fig. 2C
    experimental_model
    Oxidant washout in HEK293 cells stably overexpressing Pank1beta
    exposure
    500 micromolar H2O2 for 60 minutes, then recovery in complete growth medium.
    limitations
    The removal mechanism was not identified; engineered high-CoA cells are not ordinary circulating blood cells. This experiment does not establish a dietary pantothenate threshold or benefit from B5 supplementation.
    nutrient_topic
    Pantothenic acid (vitamin B5) research collection; topical membership is not evidence of a direct dietary effect. · Pantothenate (vitamin B5)
    organism
    Homo sapiens
    plain_language
    The CoA modification receded when the oxidative exposure ended.
    primary_references
    [b5-met-coalation2017] Protein CoAlation: a redox-regulated protein modification by coenzyme A in mammalian cells. (2017). https://pubmed.ncbi.nlm.nih.gov/28341808/ DOI: 10.1042/bcj20170129
    tissue_or_cell_type
    Engineered HEK293 cultures

    Pantothenic acid (vitamin B5): coenzyme A, deficiency and nutrient interactions (2026-09-17) · lines 1061–1073

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Oxidant washout in HEK293 cells stably overexpressing Pank1beta · source_derived_draft · unverified_draft

    ### b5-met-coalation-reversal After removal of hydrogen peroxide from HEK293/Pank1beta cultures, induced protein CoAlation declined within 5 minutes and returned to baseline within 90 minutes. Condition category: normal nutrient_topic: Pantothenic acid (vitamin B5) research collection; topical membership is not evidence of a direct dietary effect. plain_language: The CoA modification receded when the oxidative exposure ended. organism: Homo sapiens tissue_or_cell_type: Engineered HEK293 cultures experimental_model: Oxidant washout in HEK293 cells stably overexpressing Pank1beta limitations: The removal mechanism was not identified; engineered high-CoA cells are not ordinary circulating blood cells. This experiment does not establish a dietary pantothenate threshold or benefit from B5 supplementation. exposure: 500 micromolar H2O2 for 60 minutes, then recovery in complete growth medium. cross_nutrient: false evidence_location: Full text line 115; Fig. 2C [b5-met-coalation2017] Protein CoAlation: a redox-regulated protein modification by coenzyme A in mammalian cells. (2017). https://pubmed.ncbi.nlm.nih.gov/28341808/ DOI: 10.1042/bcj20170129
    Complete structured claim and evidence

  2. Hydrogen peroxide exposure induced DTT-sensitive protein CoAlation in isolated rat cardiomyocytes and perfused rat hearts.

    Hydrogen peroxide → Protein cysteine CoAlation source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    false
    evidence_location
    Full text lines 105–107; Fig. 1B–D
    experimental_model
    Primary cardiomyocyte exposure and Langendorff-perfused rat hearts
    exposure
    Cardiomyocytes: 1–100 micromolar H2O2, 30 minutes; perfused hearts: 100 micromolar H2O2, 20 minutes.
    limitations
    DTT sensitivity supports mixed disulfides. Antioxidant protection or improved organ function was not established by this endpoint. This experiment does not establish a dietary pantothenate threshold or benefit from B5 supplementation.
    nutrient_topic
    Pantothenic acid (vitamin B5) research collection; topical membership is not evidence of a direct dietary effect. · Pantothenate (vitamin B5)
    organism
    Rattus norvegicus
    plain_language
    Oxidative stress caused CoA to form reversible bonds with protein cysteines.
    primary_references
    [b5-met-coalation2017] Protein CoAlation: a redox-regulated protein modification by coenzyme A in mammalian cells. (2017). https://pubmed.ncbi.nlm.nih.gov/28341808/ DOI: 10.1042/bcj20170129
    tissue_or_cell_type
    Adult cardiomyocytes and isolated heart

    Pantothenic acid (vitamin B5): coenzyme A, deficiency and nutrient interactions (2026-09-17) · lines 1047–1059

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Primary cardiomyocyte exposure and Langendorff-perfused rat hearts · source_derived_draft · unverified_draft

    ### b5-met-oxidant-coalation Hydrogen peroxide exposure induced DTT-sensitive protein CoAlation in isolated rat cardiomyocytes and perfused rat hearts. Condition category: normal nutrient_topic: Pantothenic acid (vitamin B5) research collection; topical membership is not evidence of a direct dietary effect. plain_language: Oxidative stress caused CoA to form reversible bonds with protein cysteines. organism: Rattus norvegicus tissue_or_cell_type: Adult cardiomyocytes and isolated heart experimental_model: Primary cardiomyocyte exposure and Langendorff-perfused rat hearts limitations: DTT sensitivity supports mixed disulfides. Antioxidant protection or improved organ function was not established by this endpoint. This experiment does not establish a dietary pantothenate threshold or benefit from B5 supplementation. exposure: Cardiomyocytes: 1–100 micromolar H2O2, 30 minutes; perfused hearts: 100 micromolar H2O2, 20 minutes. cross_nutrient: false evidence_location: Full text lines 105–107; Fig. 1B–D [b5-met-coalation2017] Protein CoAlation: a redox-regulated protein modification by coenzyme A in mammalian cells. (2017). https://pubmed.ncbi.nlm.nih.gov/28341808/ DOI: 10.1042/bcj20170129
    Complete structured claim and evidence

  3. Vitamin C pretreatment reduced diamide-induced anti-CoA protein immunoreactivity by approximately 50% in HEK293/Pank1beta cells.

    L-Ascorbic acid → Protein cysteine CoAlation source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    true
    evidence_location
    Full text lines 29 and 117; Fig. 2E
    experimental_model
    Antioxidant pretreatment of engineered HEK293/Pank1beta cells
    exposure
    1 mM vitamin C for 2 hours before 0.5 mM diamide for 30 minutes.
    limitations
    The endpoint is protein anti-CoA immunoreactivity, not clinical benefit; lower CoAlation is not assumed universally beneficial. This experiment does not establish a dietary pantothenate threshold or benefit from B5 supplementation.
    nutrient_topic
    Pantothenic acid (vitamin B5) research collection; topical membership is not evidence of a direct dietary effect. · Pantothenate (vitamin B5)
    organism
    Homo sapiens
    plain_language
    Vitamin C exposure blunted the measured CoA protein modification during this experimental oxidative challenge.
    primary_references
    [b5-met-coalation2017] Protein CoAlation: a redox-regulated protein modification by coenzyme A in mammalian cells. (2017). https://pubmed.ncbi.nlm.nih.gov/28341808/ DOI: 10.1042/bcj20170129
    tissue_or_cell_type
    Engineered HEK293 cultures

    Pantothenic acid (vitamin B5): coenzyme A, deficiency and nutrient interactions (2026-09-17) · lines 1075–1087

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Antioxidant pretreatment of engineered HEK293/Pank1beta cells · source_derived_draft · unverified_draft

    ### b5-met-vitc-coalation Vitamin C pretreatment reduced diamide-induced anti-CoA protein immunoreactivity by approximately 50% in HEK293/Pank1beta cells. Condition category: normal nutrient_topic: Pantothenic acid (vitamin B5) research collection; topical membership is not evidence of a direct dietary effect. plain_language: Vitamin C exposure blunted the measured CoA protein modification during this experimental oxidative challenge. organism: Homo sapiens tissue_or_cell_type: Engineered HEK293 cultures experimental_model: Antioxidant pretreatment of engineered HEK293/Pank1beta cells limitations: The endpoint is protein anti-CoA immunoreactivity, not clinical benefit; lower CoAlation is not assumed universally beneficial. This experiment does not establish a dietary pantothenate threshold or benefit from B5 supplementation. exposure: 1 mM vitamin C for 2 hours before 0.5 mM diamide for 30 minutes. cross_nutrient: true evidence_location: Full text lines 29 and 117; Fig. 2E [b5-met-coalation2017] Protein CoAlation: a redox-regulated protein modification by coenzyme A in mammalian cells. (2017). https://pubmed.ncbi.nlm.nih.gov/28341808/ DOI: 10.1042/bcj20170129
    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