Component
Human alpha-enolase / ENO1
Human alpha-enolase / ENO1. Interpret through the linked study species, preparation, exposure and measured endpoint.
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.
Other things that act on it
Enzymes, hormones, genes, and other components with a recorded effect. These are not nutrients, so they do not count toward the arrows above. Each finding names the chapter that recorded it.
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.
What acts on it
S-thioallylation was detected on Human alpha-enolase / ENO1 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 alpha-enolase / ENO1 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
Where it participates (unsigned role)
Enolase activity decreased in lysates from 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_contrast
- {"intervention": "Allicin exposure at the specified assay dose/time", "comparator": "Untreated matched cells", "endpoint": "Enolase activity decreased in lysates from allicin-exposed Jurkat cells.", "effect_direction": "decrease", "combination": "single", "conditions": []} Explicit extracted experimental comparison; source-derived draft.
- experimental_model
- Human Jurkat cells; ten-minute 100 uM exposure for thiols/enolase, 24-hour MTT observation.
- interpretation_status
- Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.
- limitations
- MTT, free thiols and specific enzyme activity measure different quantities. The lysate assay does not isolate every possible contribution to inhibition.
- plain_language
- Enolase activity decreased in lysates from 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; ten-minute 100 uM exposure for thiols/enolase, 24-hour MTT observation. · 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
The events it takes part in
A mechanism often involves more than two components. These are the full events, with every participant and its role.
Situations it appears in
Low-supply and faulty-machinery situations recorded in the chapters where this component plays a part.
In the sources
Preserved passages that mention this component, quoted exactly. Open one to read it in context.
Open hypotheses
Proposed ideas that involve this component. They are labeled as hypotheses and do not change any recorded statement.
This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.