Component

Human pyruvate kinase PKM, splice isoform unresolved / PKM

Human pyruvate kinase PKM, splice isoform unresolved / PKM. Interpret through the linked study species, preparation, exposure and measured endpoint.

1 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 acts on it

  1. S-thioallylation was detected on Human pyruvate kinase PKM, splice isoform unresolved / PKM in allicin-exposed Jurkat cells.

    Experimental context and source evidence
    evidence_access
    Primary full text available; selected claim-relevant methods, results, tables/figures and limitations reviewed. Supplemental proteome and all secondary findings are not exhaustively extracted.
    experimental_model
    Human Jurkat cells, 100 uM allicin, ten minutes; main-text proteomic target identification.
    interpretation_status
    Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.
    limitations
    Protein modification detected; no blanket inhibition, protein depletion, necessity for phenotype, or oral target engagement is asserted. Isoform is retained as unresolved where appropriate.
    plain_language
    S-thioallylation was detected on Human pyruvate kinase PKM, splice isoform unresolved / PKM in allicin-exposed Jurkat cells.
    primary_references
    The human allicin-proteome: S-thioallylation of proteins by the garlic defence substance allicin and its biological effects. | 2019 | DOI 10.1016/j.freeradbiomed.2018.11.022 | PMID 30500420 | https://pubmed.ncbi.nlm.nih.gov/30500420/ | https://pmc.ncbi.nlm.nih.gov/articles/PMC6342545/ | https://doi.org/10.1016/j.freeradbiomed.2018.11.022
    source_locator
    Reviewed reference lines 43-43; exact primary location described in quoted passage where extracted.

    Allicin: detailed mechanisms of action (reviewed 5 October 2026) · lines 43–43

    Original AI-assisted review of primary studies and, where relevant, official regulatory records. Access level is retained per claim. Corrections, null results and unresolved questions remain explicit. Not publisher full text or independent replication. · supports · Human Jurkat cells, 100 uM allicin, ten minutes; main-text proteomic target identification. · source_derived_draft · unverified_draft

    **The human protein experiment.** Direct exposure of Jurkat cells to 100 µM allicin for ten minutes produced S-thioallylated peptides from 332 proteins, detected by an approximately +72-Da cysteine modification. Total free thiols fell by about half. Targets reported in the main text include ALDOA, GAPDH, PKM, ENO1, SOD1, PRDX1, CFL1, LCP1, FLNA, FLNB, HSPA4, EEF2, and HMGB1, alongside actin, tubulin, and HSP90 groups. These are adduct records; individual isoforms are not invented where unresolved. ENO1-associated lysate activity decreased, while the twenty-four-hour MTT readout was unchanged at up to 100 µM. MTT preservation does not mean every cellular function was unaffected. [Gruhlke 2019](https://pmc.ncbi.nlm.nih.gov/articles/PMC6342545/)
    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.