Component

Cardiolipin

Cardiolipin. Species, exposure and limitations are retained in each linked claim.

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

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. 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

Where it participates (unsigned role)

  1. Mitochondrial creatine kinase selectively recruited cardiolipin and promoted lipid clustering in the tested reconstituted membranes.

    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/creatine-research/19289067.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "3880cefa5c138a1e112b50ad2d734e8f38c70da3a545aff80969e7aa1e9a5666", "start_char": 0, "end_char": 1484, "text_sha256": "3880cefa5c138a1e112b50ad2d734e8f38c70da3a545aff80969e7aa1e9a5666"}
    experimental_model
    Protein–lipid monolayer and mixed-membrane experiments
    exposure
    Creatine kinase added to cardiolipin or mixed phospholipid films
    limitations
    Mitochondrial CK family record; the specific human isoform is not assigned from this abstract. Reconstituted membrane experiment; no human outcome.
    nutrient_topic
    Creatine research collection; topical membership is not evidence of a direct dietary effect. · Creatine
    organism
    Mitochondrial creatine kinase in reconstituted lipid systems
    plain_language
    The enzyme can help organize the membrane lipids around it.
    primary_references
    [creatine-p19289067] Mitochondrial creatine kinase binding to phospholipid monolayers induces cardiolipin segregation. (2009). https://pubmed.ncbi.nlm.nih.gov/19289067/ DOI: 10.1016/j.bpj.2008.12.3911
    tissue_or_cell_type
    Synthetic cardiolipin-containing membranes

    Creatine: synthesis, transport, phosphocreatine energetics and nutrient interactions (2026-09-17) · lines 373–384

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Protein–lipid monolayer and mixed-membrane experiments · source_derived_draft · unverified_draft

    ### creatine-mtck-cardiolipin Mitochondrial creatine kinase selectively recruited cardiolipin and promoted lipid clustering in the tested reconstituted membranes. Condition category: normal nutrient_topic: Creatine research collection; topical membership is not evidence of a direct dietary effect. plain_language: The enzyme can help organize the membrane lipids around it. organism: Mitochondrial creatine kinase in reconstituted lipid systems tissue_or_cell_type: Synthetic cardiolipin-containing membranes experimental_model: Protein–lipid monolayer and mixed-membrane experiments limitations: Mitochondrial CK family record; the specific human isoform is not assigned from this abstract. Reconstituted membrane experiment; no human outcome. exposure: Creatine kinase added to cardiolipin or mixed phospholipid films evidence_span: {"source_cache": "artifacts/creatine-research/19289067.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "3880cefa5c138a1e112b50ad2d734e8f38c70da3a545aff80969e7aa1e9a5666", "start_char": 0, "end_char": 1484, "text_sha256": "3880cefa5c138a1e112b50ad2d734e8f38c70da3a545aff80969e7aa1e9a5666"} [creatine-p19289067] Mitochondrial creatine kinase binding to phospholipid monolayers induces cardiolipin segregation. (2009). https://pubmed.ncbi.nlm.nih.gov/19289067/ DOI: 10.1016/j.bpj.2008.12.3911
    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