Allicin

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 fructose-bisphosphate aldolase A / ALDOA 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/)

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 cofilin 1 / CFL1 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/)

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 eukaryotic elongation factor 2 / EEF2 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/)

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/)

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 filamin A / FLNA 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/)

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 filamin B / FLNB 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/)

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 glyceraldehyde-3-phosphate dehydrogenase / GAPDH 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/)

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 high mobility group box 1 / HMGB1 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/)

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 heat shock protein family A member 4 / HSPA4 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/)

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 plastin 2 / LCP1 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/)

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/)

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 peroxiredoxin 1 / PRDX1 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/)

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 copper-zinc superoxide dismutase / SOD1 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/)

evidence_access

Primary indexed abstract reviewed; full methods, exact concentrations or species-specific attribution remain unextracted unless explicitly stated in the abstract or separately verified publisher text.

experimental_model

Cell-free chemical reaction; NMR characterization.

interpretation_status

Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.

limitations

Interpret only within the recorded preparation, exposure and comparator. The complete source passage retains qualifications; unspecified doses/timing have not been extracted here. No clinical efficacy, nutrient deficiency or unique molecular mediation is inferred.

plain_language

Allicin reacted with L-cysteine to form the identified mixed-disulfide product SAMC.

primary_references

The mode of action of allicin: trapping of radicals and interaction with thiol containing proteins. | 1998 | DOI 10.1016/s0304-4165(97)00104-9 | PMID 9528659 | https://pubmed.ncbi.nlm.nih.gov/9528659/ | https://doi.org/10.1016/s0304-4165(97)00104-9

source_locator

Reviewed reference lines 9-9; exact primary location described in quoted passage where extracted.

Allicin: detailed mechanisms of action (reviewed 5 October 2026) · lines 9–9

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 · Cell-free chemical reaction; NMR characterization. · source_derived_draft · unverified_draft

**Chemical identity.** Allicin is diallyl thiosulfinate, C6H10OS2, approximately 162.27 g/mol, with the structure CH2=CH–CH2–S(=O)–S–CH2–CH=CH2. The oxygen-containing thiosulfinate linkage matters: allicin is not diallyl disulfide, and the compounds cannot share target effects merely because both contain sulfur. Primary chemistry identified S-allylmercaptocysteine when allicin reacted with L-cysteine. [Rabinkov 1998](https://pubmed.ncbi.nlm.nih.gov/9528659/)

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/)

evidence_access

Primary indexed abstract reviewed; full methods, exact concentrations or species-specific attribution remain unextracted unless explicitly stated in the abstract or separately verified publisher text.

experimental_contrast

{"intervention": "Allicin incubation", "comparator": "Enzyme without allicin", "endpoint": "Allicin inhibited the tested purified horse-liver alcohol dehydrogenase.", "effect_direction": "decrease", "combination": "single", "conditions": []} Explicit extracted experimental comparison; source-derived draft.

experimental_model

Purified enzyme chemical-inhibition assay; species encoded in target.

interpretation_status

Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.

limitations

Exact dose/time unextracted from the accessible abstract; thiol-mediated reversal is target-dependent, not universal irreversibility.

plain_language

Allicin inhibited the tested purified horse-liver alcohol dehydrogenase.

primary_references

The mode of action of allicin: trapping of radicals and interaction with thiol containing proteins. | 1998 | DOI 10.1016/s0304-4165(97)00104-9 | PMID 9528659 | https://pubmed.ncbi.nlm.nih.gov/9528659/ | https://doi.org/10.1016/s0304-4165(97)00104-9

source_locator

Reviewed reference lines 41-41; exact primary location described in quoted passage where extracted.

Allicin: detailed mechanisms of action (reviewed 5 October 2026) · lines 41–41

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 · Purified enzyme chemical-inhibition assay; species encoded in target. · source_derived_draft · unverified_draft

**Enzyme inhibition and reversal differ by target.** The early purified-enzyme study observed inhibition of papain, bacterial NADP-dependent alcohol dehydrogenase, and horse-liver NAD-dependent alcohol dehydrogenase. Thiols could reactivate the enzymes, but not interchangeably: glutathione restored papain activity, whereas it did not restore the tested bacterial dehydrogenase under those conditions. Dithiothreitol or mercaptoethanol had different reversal profiles. Covalent inhibition is therefore not equivalent to unrecoverable injury, and a general glutathione rescue cannot be assumed for every enzyme. [Rabinkov 1998](https://pubmed.ncbi.nlm.nih.gov/9528659/)

evidence_access

Primary indexed abstract reviewed; full methods, exact concentrations or species-specific attribution remain unextracted unless explicitly stated in the abstract or separately verified publisher text.

experimental_contrast

{"intervention": "Allicin incubation", "comparator": "Enzyme without allicin", "endpoint": "Allicin inhibited the tested purified papain.", "effect_direction": "decrease", "combination": "single", "conditions": []} Explicit extracted experimental comparison; source-derived draft.

experimental_model

Purified enzyme chemical-inhibition assay; species encoded in target.

interpretation_status

Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.

limitations

Exact dose/time unextracted from the accessible abstract; thiol-mediated reversal is target-dependent, not universal irreversibility.

plain_language

Allicin inhibited the tested purified papain.

primary_references

The mode of action of allicin: trapping of radicals and interaction with thiol containing proteins. | 1998 | DOI 10.1016/s0304-4165(97)00104-9 | PMID 9528659 | https://pubmed.ncbi.nlm.nih.gov/9528659/ | https://doi.org/10.1016/s0304-4165(97)00104-9

source_locator

Reviewed reference lines 41-41; exact primary location described in quoted passage where extracted.

Allicin: detailed mechanisms of action (reviewed 5 October 2026) · lines 41–41

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 · Purified enzyme chemical-inhibition assay; species encoded in target. · source_derived_draft · unverified_draft

**Enzyme inhibition and reversal differ by target.** The early purified-enzyme study observed inhibition of papain, bacterial NADP-dependent alcohol dehydrogenase, and horse-liver NAD-dependent alcohol dehydrogenase. Thiols could reactivate the enzymes, but not interchangeably: glutathione restored papain activity, whereas it did not restore the tested bacterial dehydrogenase under those conditions. Dithiothreitol or mercaptoethanol had different reversal profiles. Covalent inhibition is therefore not equivalent to unrecoverable injury, and a general glutathione rescue cannot be assumed for every enzyme. [Rabinkov 1998](https://pubmed.ncbi.nlm.nih.gov/9528659/)

evidence_access

Primary indexed abstract reviewed; full methods, exact concentrations or species-specific attribution remain unextracted unless explicitly stated in the abstract or separately verified publisher text.

experimental_contrast

{"intervention": "Allicin incubation", "comparator": "Enzyme without allicin", "endpoint": "Allicin inhibited the tested purified bacterial NADP-dependent alcohol dehydrogenase.", "effect_direction": "decrease", "combination": "single", "conditions": []} Explicit extracted experimental comparison; source-derived draft.

experimental_model

Purified enzyme chemical-inhibition assay; species encoded in target.

interpretation_status

Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.

limitations

Exact dose/time unextracted from the accessible abstract; thiol-mediated reversal is target-dependent, not universal irreversibility.

plain_language

Allicin inhibited the tested purified bacterial NADP-dependent alcohol dehydrogenase.

primary_references

The mode of action of allicin: trapping of radicals and interaction with thiol containing proteins. | 1998 | DOI 10.1016/s0304-4165(97)00104-9 | PMID 9528659 | https://pubmed.ncbi.nlm.nih.gov/9528659/ | https://doi.org/10.1016/s0304-4165(97)00104-9

source_locator

Reviewed reference lines 41-41; exact primary location described in quoted passage where extracted.

Allicin: detailed mechanisms of action (reviewed 5 October 2026) · lines 41–41

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 · Purified enzyme chemical-inhibition assay; species encoded in target. · source_derived_draft · unverified_draft

**Enzyme inhibition and reversal differ by target.** The early purified-enzyme study observed inhibition of papain, bacterial NADP-dependent alcohol dehydrogenase, and horse-liver NAD-dependent alcohol dehydrogenase. Thiols could reactivate the enzymes, but not interchangeably: glutathione restored papain activity, whereas it did not restore the tested bacterial dehydrogenase under those conditions. Dithiothreitol or mercaptoethanol had different reversal profiles. Covalent inhibition is therefore not equivalent to unrecoverable injury, and a general glutathione rescue cannot be assumed for every enzyme. [Rabinkov 1998](https://pubmed.ncbi.nlm.nih.gov/9528659/)

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": "Free cellular thiols fell approximately 50% after allicin treatment.", "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

Free cellular thiols fell approximately 50% after allicin treatment.

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/)

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

Cell-free product preparation and LC-MS characterization; not human oral metabolism.

interpretation_status

Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.

limitations

Interpret only within the recorded preparation, exposure and comparator. The complete source passage retains qualifications; unspecified doses/timing have not been extracted here. No clinical efficacy, nutrient deficiency or unique molecular mediation is inferred.

plain_language

Allicin reacts with glutathione to form GSSA, distinct from GSSG.

primary_references

<i>S</i>-allylmercaptoglutathione Is a Substrate for Glutathione Reductase (E.C. 1.8.1.7) from Yeast (<i>Saccharomyces cerevisiae</i>). | 2018 | DOI 10.3390/antiox7070086 | PMID 29986384 | https://pubmed.ncbi.nlm.nih.gov/29986384/ | https://pmc.ncbi.nlm.nih.gov/articles/PMC6070820/ | https://doi.org/10.3390/antiox7070086

source_locator

Reviewed reference lines 39-39; exact primary location described in quoted passage where extracted.

Allicin: detailed mechanisms of action (reviewed 5 October 2026) · lines 39–39

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 · Cell-free product preparation and LC-MS characterization; not human oral metabolism. · source_derived_draft · unverified_draft

**Thioallylation chemistry.** Allicin reacts with accessible cysteine thiols to form allyl-containing mixed disulfides. For a protein, the simplified first reaction is protein-SH + allicin → protein-S-S-allyl + allylsulfenic acid. Glutathione forms S-allylmercaptoglutathione (GSSA), which is chemically distinct from oxidized glutathione (GSSG). Accessibility, local environment, competing thiols, and exposure determine which targets are modified. An adduct alone does not demonstrate inhibition, phenotype mediation, or dietary target engagement. [Rabinkov 1998](https://pubmed.ncbi.nlm.nih.gov/9528659/) [Horn 2018](https://pmc.ncbi.nlm.nih.gov/articles/PMC6070820/)

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 concentration series", "comparator": "Matched untreated cells in each model", "endpoint": "Direct allicin exposure reduced mammalian-cell viability or proliferation in a concentration- and cell-type-dependent manner.", "effect_direction": "mixed", "combination": "single", "conditions": []} Explicit extracted experimental comparison; source-derived draft.

experimental_model

Human A549/HUVEC/HT29/MCF7 and mouse 3T3; separate viability, proliferation and apoptosis assays.

interpretation_status

Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.

limitations

Separate species and endpoints; no cancer-selective clinical efficacy or direct measurement of every GSH species.

plain_language

Direct allicin exposure reduced mammalian-cell viability or proliferation in a concentration- and cell-type-dependent manner.

primary_references

The Effects of Allicin, a Reactive Sulfur Species from Garlic, on a Selection of Mammalian Cell Lines. | 2016 | DOI 10.3390/antiox6010001 | PMID 28035949 | https://pubmed.ncbi.nlm.nih.gov/28035949/ | https://pmc.ncbi.nlm.nih.gov/articles/PMC5384165/ | https://doi.org/10.3390/antiox6010001

source_locator

Reviewed reference lines 53-53; exact primary location described in quoted passage where extracted.

Allicin: detailed mechanisms of action (reviewed 5 October 2026) · lines 53–53

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 A549/HUVEC/HT29/MCF7 and mouse 3T3; separate viability, proliferation and apoptosis assays. · source_derived_draft · unverified_draft

**Mammalian injury is context-dependent.** Allicin reduced viability or proliferation and altered thiol-associated fluorescence in a panel including human A549, HUVEC, HT29, and MCF7 cells and mouse 3T3 cells. Sensitivity and apoptotic responses differed. Fluorescence changes are not a complete measurement of every glutathione species. Thiol reactivity does not guarantee selective toxicity to microbes or cancer cells. [Gruhlke 2017](https://pmc.ncbi.nlm.nih.gov/articles/PMC5384165/)

evidence_access

Primary indexed abstract reviewed; full methods, exact concentrations or species-specific attribution remain unextracted unless explicitly stated in the abstract or separately verified publisher text.

experimental_model

Room-temperature preparation comparisons; aqueous/alcoholic extracts and vegetable oil.

interpretation_status

Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.

limitations

Not a universal body half-life. Full preparation-specific kinetic tables remain unextracted.

plain_language

Allicin stability depends on the medium; vegetable oil had a 3.1-hour chemical half-life and a separate 0.8-hour antibacterial-activity half-life.

primary_references

Biological and chemical stability of garlic-derived allicin. | 2008 | DOI 10.1021/jf8000907 | PMID 18489116 | https://pubmed.ncbi.nlm.nih.gov/18489116/ | https://doi.org/10.1021/jf8000907

source_locator

Reviewed reference lines 19-19; exact primary location described in quoted passage where extracted.

Allicin: detailed mechanisms of action (reviewed 5 October 2026) · lines 19–19

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 · Room-temperature preparation comparisons; aqueous/alcoholic extracts and vegetable oil. · source_derived_draft · unverified_draft

**Stability depends on medium.** Chemical allicin loss and loss of antibacterial activity were different measurements in aqueous, alcoholic, and oil preparations. A room-temperature study reported persistence over days in some aqueous/alcoholic conditions; vegetable oil gave a chemical half-life of 3.1 hours and an activity half-life of 0.8 hours. These are preparation-specific measurements, not a universal half-life in crushed garlic, blood, or the human body. Thiol consumption in biological material is also distinct from spontaneous decomposition. [Fujisawa 2008](https://pubmed.ncbi.nlm.nih.gov/18489116/)

evidence_access

Primary indexed abstract reviewed; full methods, exact concentrations or species-specific attribution remain unextracted unless explicitly stated in the abstract or separately verified publisher text.

experimental_contrast

{"intervention": "Allicin exposure", "comparator": "Corresponding membrane assay control", "endpoint": "Allicin did not produce detected leakage, fusion or aggregation in the tested membrane assays.", "effect_direction": "no_detected_change", "combination": "single", "conditions": []} Explicit extracted experimental comparison; source-derived draft.

experimental_model

Artificial membrane assays; primary abstract; exact exposure unextracted.

interpretation_status

Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.

limitations

Not proof of safety of all membranes, doses, or tissues.

plain_language

Allicin did not produce detected leakage, fusion or aggregation in the tested membrane assays.

primary_references

The mode of action of allicin: its ready permeability through phospholipid membranes may contribute to its biological activity. | 2000 | DOI 10.1016/s0005-2736(99)00174-1 | PMID 10631291 | https://pubmed.ncbi.nlm.nih.gov/10631291/ | https://doi.org/10.1016/s0005-2736(99)00174-1

source_locator

Reviewed reference lines 27-27; exact primary location described in quoted passage where extracted.

Allicin: detailed mechanisms of action (reviewed 5 October 2026) · lines 27–27

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 · Artificial membrane assays; primary abstract; exact exposure unextracted. · source_derived_draft · unverified_draft

**Membrane entry.** Allicin crossed phospholipid vesicles and human erythrocyte membranes and reacted with enclosed thiols. The investigators did not find membrane leakage, fusion, or aggregation in those assays. Permeation supports intracellular target access during direct exposure; it does not establish oral delivery to a distant tissue or make transport and resistance irrelevant in every organism. [Miron 2000](https://pubmed.ncbi.nlm.nih.gov/10631291/)

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", "comparator": "Matched bacterial assay control", "endpoint": "Allicin inhibited growth of tested bacterial isolates with substantial strain and assay variation.", "effect_direction": "decrease", "combination": "single", "conditions": []} Explicit extracted experimental comparison; source-derived draft.

experimental_model

In vitro clinical-isolate panel; liquid/vapor observations; primary full-text results.

interpretation_status

Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.

limitations

Not an organism-independent MIC, clinical infection therapy, or safe inhaled exposure.

plain_language

Allicin inhibited growth of tested bacterial isolates with substantial strain and assay variation.

primary_references

Diallylthiosulfinate (Allicin), a Volatile Antimicrobial from Garlic (Allium sativum), Kills Human Lung Pathogenic Bacteria, Including MDR Strains, as a Vapor. | 2017 | DOI 10.3390/molecules22101711 | PMID 29023413 | https://pubmed.ncbi.nlm.nih.gov/29023413/ | https://pmc.ncbi.nlm.nih.gov/articles/PMC6151386/ | https://doi.org/10.3390/molecules22101711

source_locator

Reviewed reference lines 65-65; exact primary location described in quoted passage where extracted.

Allicin: detailed mechanisms of action (reviewed 5 October 2026) · lines 65–65

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 · In vitro clinical-isolate panel; liquid/vapor observations; primary full-text results. · source_derived_draft · unverified_draft

**Laboratory antimicrobial activity.** Purified allicin inhibited multiple tested respiratory bacterial isolates, including some resistant to clinical antibiotics; susceptibility varied by organism and assay. The same investigation measured mammalian-cell and rat-lung-slice toxicity. Added glutathione reduced toxicity in those models. The experimental 1-mM glutathione condition must not be presented as a validated normal plasma concentration or a safe inhalation regimen. Luminal or surface accessibility is a hypothesis about delivery, not a calculation proving efficacy from nominal dose divided by fluid volume. [Reiter 2017](https://pmc.ncbi.nlm.nih.gov/articles/PMC6151386/)

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", "comparator": "Untreated mouse fibroblasts", "endpoint": "Allicin disrupted filamentous-actin organization in mouse L929 fibroblasts.", "effect_direction": "decrease", "combination": "single", "conditions": []} Explicit extracted experimental comparison; source-derived draft.

experimental_model

Mouse L929, 25-100 uM, ten minutes; rhodamine-phalloidin imaging.

interpretation_status

Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.

limitations

Exact individual protein mediation was not established; not a human Jurkat functional result.

plain_language

Allicin disrupted filamentous-actin organization in mouse L929 fibroblasts.

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 45-45; exact primary location described in quoted passage where extracted.

Allicin: detailed mechanisms of action (reviewed 5 October 2026) · lines 45–45

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 · Mouse L929, 25-100 uM, ten minutes; rhodamine-phalloidin imaging. · source_derived_draft · unverified_draft

**Cytoskeleton and zinc.** In separate mouse-cell experiments in the same paper, 25–100 µM allicin disrupted L929 fibroblast actin organization after ten minutes. In EL-4 cells, 25 µM increased labile zinc at thirty minutes. For the IL-2 experiment, cells received 25 µM allicin for thirty minutes, were washed and supplied fresh medium, then received 0.5 ng/mL IL-1β for twenty-four hours; allicin pretreatment enhanced the stimulated IL-2 response. Detecting SOD1 modification in human Jurkat cells does not prove that SOD1 supplied the released zinc in mouse EL-4 cells. These outcomes do not establish improved human zinc nutrition or immune protection. [Gruhlke 2019](https://pmc.ncbi.nlm.nih.gov/articles/PMC6342545/)

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_condition

IL-1beta stimulation without allicin pretreatment pretreatment followed by wash · Allicin Condition belongs to the full experimental contrast; do not separate a joint intervention.

experimental_condition

IL-1beta stimulation without allicin pretreatment subsequent stimulation · Interleukin-1 beta / IL1B Condition belongs to the full experimental contrast; do not separate a joint intervention.

experimental_contrast

{"intervention": "Allicin pretreatment, wash, then IL-1beta stimulation", "comparator": "IL-1beta stimulation without allicin pretreatment", "endpoint": "Allicin pretreatment followed by washing enhanced subsequent IL-1beta-stimulated IL-2 production in mouse EL-4 cells.", "effect_direction": "increase", "combination": "joint", "conditions": [{"entity_slug": "allicin", "state": "pretreatment followed by wash"}, {"entity_slug": "il1b", "state": "subsequent stimulation"}]} Explicit extracted experimental comparison; source-derived draft.

experimental_model

Mouse EL-4: allicin 25 uM for 30 minutes, wash and fresh medium, then IL-1beta 0.5 ng/mL for 24 hours.

interpretation_status

Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.

limitations

Sequential joint condition; not simultaneous exposure, basal IL-2 enhancement or human immune protection.

plain_language

Allicin pretreatment followed by washing enhanced subsequent IL-1beta-stimulated IL-2 production in mouse EL-4 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 45-45; exact primary location described in quoted passage where extracted.

Allicin: detailed mechanisms of action (reviewed 5 October 2026) · lines 45–45

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 · Mouse EL-4: allicin 25 uM for 30 minutes, wash and fresh medium, then IL-1beta 0.5 ng/mL for 24 hours. · source_derived_draft · unverified_draft

**Cytoskeleton and zinc.** In separate mouse-cell experiments in the same paper, 25–100 µM allicin disrupted L929 fibroblast actin organization after ten minutes. In EL-4 cells, 25 µM increased labile zinc at thirty minutes. For the IL-2 experiment, cells received 25 µM allicin for thirty minutes, were washed and supplied fresh medium, then received 0.5 ng/mL IL-1β for twenty-four hours; allicin pretreatment enhanced the stimulated IL-2 response. Detecting SOD1 modification in human Jurkat cells does not prove that SOD1 supplied the released zinc in mouse EL-4 cells. These outcomes do not establish improved human zinc nutrition or immune protection. [Gruhlke 2019](https://pmc.ncbi.nlm.nih.gov/articles/PMC6342545/)

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 25 uM", "comparator": "Untreated cells", "endpoint": "Allicin increased labile zinc in mouse EL-4 cells.", "effect_direction": "increase", "combination": "single", "conditions": []} Explicit extracted experimental comparison; source-derived draft.

experimental_model

Mouse EL-4, 25 uM, 30 minutes.

interpretation_status

Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.

limitations

Not additional total zinc or identification of SOD1 as the donor. Mouse functional assay and human proteomic adducts are separate.

plain_language

Allicin increased labile zinc in mouse EL-4 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 45-45; exact primary location described in quoted passage where extracted.

Allicin: detailed mechanisms of action (reviewed 5 October 2026) · lines 45–45

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 · Mouse EL-4, 25 uM, 30 minutes. · source_derived_draft · unverified_draft

**Cytoskeleton and zinc.** In separate mouse-cell experiments in the same paper, 25–100 µM allicin disrupted L929 fibroblast actin organization after ten minutes. In EL-4 cells, 25 µM increased labile zinc at thirty minutes. For the IL-2 experiment, cells received 25 µM allicin for thirty minutes, were washed and supplied fresh medium, then received 0.5 ng/mL IL-1β for twenty-four hours; allicin pretreatment enhanced the stimulated IL-2 response. Detecting SOD1 modification in human Jurkat cells does not prove that SOD1 supplied the released zinc in mouse EL-4 cells. These outcomes do not establish improved human zinc nutrition or immune protection. [Gruhlke 2019](https://pmc.ncbi.nlm.nih.gov/articles/PMC6342545/)

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": "MTT metabolic-activity readout did not significantly decrease after exposure up to 100 uM in the tested Jurkat system.", "effect_direction": "no_detected_change", "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

MTT metabolic-activity readout did not significantly decrease after exposure up to 100 uM in the tested Jurkat system.

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/)

evidence_access

Primary indexed abstract reviewed; full methods, exact concentrations or species-specific attribution remain unextracted unless explicitly stated in the abstract or separately verified publisher text.

experimental_model

Phospholipid vesicles loaded with hydrophilic thiols

interpretation_status

Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.

limitations

Interpret only within the recorded preparation, exposure and comparator. The complete source passage retains qualifications; unspecified doses/timing have not been extracted here. No clinical efficacy, nutrient deficiency or unique molecular mediation is inferred.

plain_language

Allicin permeated the tested membrane and reached thiols on the other side.

primary_references

The mode of action of allicin: its ready permeability through phospholipid membranes may contribute to its biological activity. | 2000 | DOI 10.1016/s0005-2736(99)00174-1 | PMID 10631291 | https://pubmed.ncbi.nlm.nih.gov/10631291/ | https://doi.org/10.1016/s0005-2736(99)00174-1

source_locator

Reviewed reference lines 27-27; exact primary location described in quoted passage where extracted.

Allicin: detailed mechanisms of action (reviewed 5 October 2026) · lines 27–27

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 · Phospholipid vesicles loaded with hydrophilic thiols · source_derived_draft · unverified_draft

**Membrane entry.** Allicin crossed phospholipid vesicles and human erythrocyte membranes and reacted with enclosed thiols. The investigators did not find membrane leakage, fusion, or aggregation in those assays. Permeation supports intracellular target access during direct exposure; it does not establish oral delivery to a distant tissue or make transport and resistance irrelevant in every organism. [Miron 2000](https://pubmed.ncbi.nlm.nih.gov/10631291/)

evidence_access

Primary indexed abstract reviewed; full methods, exact concentrations or species-specific attribution remain unextracted unless explicitly stated in the abstract or separately verified publisher text.

experimental_model

Isolated human red blood cells

interpretation_status

Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.

limitations

Interpret only within the recorded preparation, exposure and comparator. The complete source passage retains qualifications; unspecified doses/timing have not been extracted here. No clinical efficacy, nutrient deficiency or unique molecular mediation is inferred.

plain_language

Allicin permeated the tested membrane and reached thiols on the other side.

primary_references

The mode of action of allicin: its ready permeability through phospholipid membranes may contribute to its biological activity. | 2000 | DOI 10.1016/s0005-2736(99)00174-1 | PMID 10631291 | https://pubmed.ncbi.nlm.nih.gov/10631291/ | https://doi.org/10.1016/s0005-2736(99)00174-1

source_locator

Reviewed reference lines 27-27; exact primary location described in quoted passage where extracted.

Allicin: detailed mechanisms of action (reviewed 5 October 2026) · lines 27–27

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 · Isolated human red blood cells · source_derived_draft · unverified_draft

**Membrane entry.** Allicin crossed phospholipid vesicles and human erythrocyte membranes and reacted with enclosed thiols. The investigators did not find membrane leakage, fusion, or aggregation in those assays. Permeation supports intracellular target access during direct exposure; it does not establish oral delivery to a distant tissue or make transport and resistance irrelevant in every organism. [Miron 2000](https://pubmed.ncbi.nlm.nih.gov/10631291/)

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 for ten minutes, LC-MS/MS.

interpretation_status

Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.

limitations

The full supplemental list is not independently resolved into 332 canonical proteins here. Adduct detection is separate from function or human dietary target engagement.

plain_language

S-thioallylated peptides were detected from 332 proteins after direct allicin exposure.

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 for ten minutes, LC-MS/MS. · 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/)

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", "comparator": "Patch before allicin", "endpoint": "Allicin activated rat TRPV1 expressed in HEK293 membrane patches.", "effect_direction": "increase", "combination": "single", "conditions": []} Explicit extracted experimental comparison; source-derived draft.

experimental_model

Rat TRPV1 construct in human HEK293 host cells; inside-out patch recordings.

interpretation_status

Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.

limitations

Interpret only within the recorded preparation, exposure and comparator. The complete source passage retains qualifications; unspecified doses/timing have not been extracted here. No clinical efficacy, nutrient deficiency or unique molecular mediation is inferred.

plain_language

Allicin activated rat TRPV1 expressed in HEK293 membrane patches.

primary_references

A single N-terminal cysteine in TRPV1 determines activation by pungent compounds from onion and garlic. | 2008 | DOI 10.1038/nn2056 | PMID 18297068 | https://pubmed.ncbi.nlm.nih.gov/18297068/ | https://pmc.ncbi.nlm.nih.gov/articles/PMC4370189/ | https://doi.org/10.1038/nn2056

source_locator

Reviewed reference lines 73-73; exact primary location described in quoted passage where extracted.

Allicin: detailed mechanisms of action (reviewed 5 October 2026) · lines 73–73

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 · Rat TRPV1 construct in human HEK293 host cells; inside-out patch recordings. · source_derived_draft · unverified_draft

**A tested TRPV1 cysteine.** In rat TRPV1 expressed in HEK293 cells, the C157A substitution eliminated allicin responsiveness; reinserting C157 into a cysteine-less construct restored it. Capsaicin responsiveness persisted in the relevant mutant controls. A reducing agent reversed activation. This is direct functional evidence for a cysteine-dependent activation mechanism in that construct, not proof that every electrophile makes the same adduct or that the cell line makes the protein human. [Salazar 2008](https://pmc.ncbi.nlm.nih.gov/articles/PMC4370189/)

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

Naturally isolated bacteria and laboratory characterization; no clinical resistance prevalence estimate.

interpretation_status

Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.

limitations

Broad targeting does not make resistance impossible. This is an observed resistance limitation, not an increase in resistance caused by oral garlic.

plain_language

Naturally adapted Pseudomonas isolates demonstrated resistance to allicin associated with multicomponent redox defenses.

primary_references

Genetic and molecular characterization of multicomponent resistance of <i>Pseudomonas</i> against allicin. | 2020 | DOI 10.26508/lsa.202000670 | PMID 32234751 | https://pubmed.ncbi.nlm.nih.gov/32234751/ | https://pmc.ncbi.nlm.nih.gov/articles/PMC7119367/ | https://doi.org/10.26508/lsa.202000670

source_locator

Reviewed reference lines 67-67; exact primary location described in quoted passage where extracted.

Allicin: detailed mechanisms of action (reviewed 5 October 2026) · lines 67–67

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 · Naturally isolated bacteria and laboratory characterization; no clinical resistance prevalence estimate. · source_derived_draft · unverified_draft

**Resistance exists.** Naturally allicin-resistant Pseudomonas isolates and multicomponent redox defenses were characterized. Broad thiol targeting does not require an organism to replace every susceptible cysteine before resistance can occur. Resistance and variation between strains limit generalization from susceptibility assays. Laboratory findings also do not establish allicin as a clinical treatment for H. pylori, parasites, or an altered microbiome. [Borlinghaus 2020](https://pmc.ncbi.nlm.nih.gov/articles/PMC7119367/)

evidence_access

Primary indexed abstract reviewed; full methods, exact concentrations or species-specific attribution remain unextracted unless explicitly stated in the abstract or separately verified publisher text.

experimental_contrast

{"intervention": "Allicin stress", "comparator": "Matched unstressed bacterial cells", "endpoint": "Allicin shifted the bacillithiol redox potential toward a more oxidized state in Staphylococcus aureus.", "effect_direction": "increase", "combination": "single", "conditions": []} Explicit extracted experimental comparison; source-derived draft.

experimental_model

Bacterial redox-biosensor study; primary abstract; exact dose/time unextracted.

interpretation_status

Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.

limitations

Redox potential is not total bacillithiol depletion; no equivalence to human GSH physiology.

plain_language

Allicin shifted the bacillithiol redox potential toward a more oxidized state in Staphylococcus aureus.

primary_references

Staphylococcus aureus responds to allicin by global S-thioallylation - Role of the Brx/BSH/YpdA pathway and the disulfide reductase MerA to overcome allicin stress. | 2019 | DOI 10.1016/j.freeradbiomed.2019.05.018 | PMID 31121222 | https://pubmed.ncbi.nlm.nih.gov/31121222/ | https://doi.org/10.1016/j.freeradbiomed.2019.05.018

source_locator

Reviewed reference lines 51-51; exact primary location described in quoted passage where extracted.

Allicin: detailed mechanisms of action (reviewed 5 October 2026) · lines 51–51

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 · Bacterial redox-biosensor study; primary abstract; exact dose/time unextracted. · source_derived_draft · unverified_draft

**Bacterial thiol systems differ.** Staphylococcus aureus uses bacillithiol rather than treating glutathione as its universal buffer. The 2019 study reported a bacillithiol redox shift, protein S-thioallylation, and reversal through bacilliredoxin/bacillithiol/YpdA chemistry; YpdA could use the allyl-bacillithiol adduct to regenerate bacillithiol. These are organism-specific repair findings, not evidence for the same proteins in humans. [Loi 2019](https://pubmed.ncbi.nlm.nih.gov/31121222/)

evidence_access

Primary indexed abstract reviewed; full methods, exact concentrations or species-specific attribution remain unextracted unless explicitly stated in the abstract or separately verified publisher text.

experimental_model

Editorial study-scope relationship, not experimental causation or chemical composition.

interpretation_status

Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.

limitations

Unsigned navigation only. Does not assert allicin content, metabolic conversion, causation or intervention equivalence.

plain_language

The aged-garlic-gardner-2007 study is a preparation-specific translation comparison; its outcomes are not assigned to purified allicin.

primary_references

Effect of raw garlic vs commercial garlic supplements on plasma lipid concentrations in adults with moderate hypercholesterolemia: a randomized clinical trial. | 2007 | DOI 10.1001/archinte.167.4.346 | PMID 17325296 | https://pubmed.ncbi.nlm.nih.gov/17325296/ | https://doi.org/10.1001/archinte.167.4.346

source_locator

Reviewed reference lines 91-91; exact primary location described in quoted passage where extracted.

Allicin: detailed mechanisms of action (reviewed 5 October 2026) · lines 91–91

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 · Editorial study-scope relationship, not experimental causation or chemical composition. · source_derived_draft · unverified_draft

**Cholesterol null.** Gardner randomized 192 adults with moderately elevated LDL cholesterol to raw garlic, garlic powder, aged garlic extract, or placebo for six months. Products equivalent to roughly a four-gram clove were used six days per week and chemically monitored. None significantly improved LDL, HDL, triglycerides, or the total-cholesterol/HDL ratio. This substantial null result should remain visible beside biochemical enzyme findings. It neither disproves every possible formulation nor proves that all positive trials were publication bias. [Gardner 2007](https://pubmed.ncbi.nlm.nih.gov/17325296/)

evidence_access

Primary indexed abstract reviewed; full methods, exact concentrations or species-specific attribution remain unextracted unless explicitly stated in the abstract or separately verified publisher text.

experimental_model

Editorial study-scope relationship, not experimental causation or chemical composition.

interpretation_status

Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.

limitations

Unsigned navigation only. Does not assert allicin content, metabolic conversion, causation or intervention equivalence.

plain_language

The aged-garlic-nantz-2012 study is a preparation-specific translation comparison; its outcomes are not assigned to purified allicin.

primary_references

Supplementation with aged garlic extract improves both NK and γδ-T cell function and reduces the severity of cold and flu symptoms: a randomized, double-blind, placebo-controlled nutrition intervention. | 2012 | DOI 10.1016/j.clnu.2011.11.019 | PMID 22280901 | https://pubmed.ncbi.nlm.nih.gov/22280901/ | https://doi.org/10.1016/j.clnu.2011.11.019

source_locator

Reviewed reference lines 95-95; exact primary location described in quoted passage where extracted.

Allicin: detailed mechanisms of action (reviewed 5 October 2026) · lines 95–95

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 · Editorial study-scope relationship, not experimental causation or chemical composition. · source_derived_draft · unverified_draft

**Cold outcomes differ by preparation.** Josling's trial randomized 146 volunteers for twelve weeks and reported fewer diary-recorded colds with an allicin-containing supplement (24 versus 65 episodes). Nantz tested 2.56 g/day aged garlic extract in 120 participants: the ninety-day cold/flu incidence difference was not significant, although some symptom and activity-impact measures improved. At forty-five days, ex vivo γδ-T-cell and NK-cell proliferation also increased. These are different interventions and endpoints, not a replication of purified allicin efficacy. Neither proves that one specific compound caused the clinical effect. [Josling 2001](https://pubmed.ncbi.nlm.nih.gov/11697022/) [Nantz 2012](https://pubmed.ncbi.nlm.nih.gov/22280901/)

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

Editorial study-scope relationship, not experimental causation or chemical composition.

interpretation_status

Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.

limitations

Unsigned navigation only. Does not assert allicin content, metabolic conversion, causation or intervention equivalence.

plain_language

The aged-garlic-ried-2016 study is a preparation-specific translation comparison; its outcomes are not assigned to purified allicin.

primary_references

The effect of aged garlic extract on blood pressure and other cardiovascular risk factors in uncontrolled hypertensives: the AGE at Heart trial. | 2016 | DOI 10.2147/ibpc.s93335 | PMID 26869811 | https://pubmed.ncbi.nlm.nih.gov/26869811/ | https://pmc.ncbi.nlm.nih.gov/articles/PMC4734812/ | https://doi.org/10.2147/ibpc.s93335

source_locator

Reviewed reference lines 89-89; exact primary location described in quoted passage where extracted.

Allicin: detailed mechanisms of action (reviewed 5 October 2026) · lines 89–89

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 · Editorial study-scope relationship, not experimental causation or chemical composition. · source_derived_draft · unverified_draft

**Blood pressure.** AGE at Heart tested 1.2 g/day aged garlic extract containing 1.2 mg SAC for twelve weeks. Ninety-five participants completed the trial; seven were excluded for protocol deviations, leaving eighty-eight in the full analysis. Mean placebo-adjusted systolic change was about −5.0 ± 2.1 mmHg. The overall diastolic difference was not significant (−1.9 ± 1.2 mmHg, P=0.12). Larger reductions in retrospectively defined responders do not replace the overall comparison. This was an extract trial, not purified allicin or proof of sulfide mediation. Manufacturer involvement and the analysis exclusions limit interpretation. [Ried 2016](https://pmc.ncbi.nlm.nih.gov/articles/PMC4734812/)

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

Editorial study-scope relationship, not experimental causation or chemical composition.

interpretation_status

Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.

limitations

Unsigned navigation only. Does not assert allicin content, metabolic conversion, causation or intervention equivalence.

plain_language

The aged-garlic-wlosinska-2020 study is a preparation-specific translation comparison; its outcomes are not assigned to purified allicin.

primary_references

The effect of aged garlic extract on the atherosclerotic process - a randomized double-blind placebo-controlled trial. | 2020 | DOI 10.1186/s12906-020-02932-5 | PMID 32349742 | https://pubmed.ncbi.nlm.nih.gov/32349742/ | https://pmc.ncbi.nlm.nih.gov/articles/PMC7191741/ | https://doi.org/10.1186/s12906-020-02932-5

source_locator

Reviewed reference lines 93-93; exact primary location described in quoted passage where extracted.

Allicin: detailed mechanisms of action (reviewed 5 October 2026) · lines 93–93

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 · Editorial study-scope relationship, not experimental causation or chemical composition. · source_derived_draft · unverified_draft

**Coronary imaging.** A European trial randomized 104 participants to 2.4 g/day aged garlic extract or placebo for one year; ninety-three were analyzed. It reported lower coronary-calcium progression with the extract. It was retrospectively registered and received manufacturer funding and product support alongside other funding. Coronary calcium progression is an imaging outcome, not proof of plaque reversal, fewer infarctions, or allicin target engagement. It must remain distinct from low-attenuation plaque and total plaque-volume measurements. [Wlosinska 2020](https://pmc.ncbi.nlm.nih.gov/articles/PMC7191741/)

evidence_access

Primary indexed abstract reviewed; full methods, exact concentrations or species-specific attribution remain unextracted unless explicitly stated in the abstract or separately verified publisher text.

experimental_model

Editorial study-scope relationship, not experimental causation or chemical composition.

interpretation_status

Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.

limitations

Unsigned navigation only. Does not assert allicin content, metabolic conversion, causation or intervention equivalence.

plain_language

The garlic-caplets-piscitelli-2002 study is a preparation-specific translation comparison; its outcomes are not assigned to purified allicin.

primary_references

The effect of garlic supplements on the pharmacokinetics of saquinavir. | 2002 | DOI 10.1086/324351 | PMID 11740713 | https://pubmed.ncbi.nlm.nih.gov/11740713/ | https://doi.org/10.1086/324351

source_locator

Reviewed reference lines 101-101; exact primary location described in quoted passage where extracted.

Allicin: detailed mechanisms of action (reviewed 5 October 2026) · lines 101–101

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 · Editorial study-scope relationship, not experimental causation or chemical composition. · source_derived_draft · unverified_draft

**Saquinavir exposure.** In ten healthy volunteers, a garlic-supplement regimen reduced saquinavir AUC by about 51%, trough concentration by 49%, and peak concentration by 54%. After washout, values had not fully returned to baseline. This is a measured pharmacokinetic interaction with that preparation; combined CYP3A4 and P-glycoprotein induction was not established as its causal mechanism. The magnitude should not be assigned to all garlic foods, purified allicin, or every CYP3A4 substrate. [Piscitelli 2002](https://pubmed.ncbi.nlm.nih.gov/11740713/)

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

Editorial study-scope relationship, not experimental causation or chemical composition.

interpretation_status

Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.

limitations

Unsigned navigation only. Does not assert allicin content, metabolic conversion, causation or intervention equivalence.

plain_language

The garlic-extract-oil-shandong study is a preparation-specific translation comparison; its outcomes are not assigned to purified allicin.

primary_references

Effects of <i>Helicobacter pylori</i> treatment and vitamin and garlic supplementation on gastric cancer incidence and mortality: follow-up of a randomized intervention trial. | 2019 | DOI 10.1136/bmj.l5016 | PMID 31511230 | https://pubmed.ncbi.nlm.nih.gov/31511230/ | https://pmc.ncbi.nlm.nih.gov/articles/PMC6737461/ | https://doi.org/10.1136/bmj.l5016

source_locator

Reviewed reference lines 97-97; exact primary location described in quoted passage where extracted.

Allicin: detailed mechanisms of action (reviewed 5 October 2026) · lines 97–97

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 · Editorial study-scope relationship, not experimental causation or chemical composition. · source_derived_draft · unverified_draft

**Shandong outcomes and formulation.** The factorial trial included 3,365 residents of a high-risk Chinese region. The garlic regimen was two capsules, each containing 200 mg aged garlic extract and 1 mg steam-distilled garlic oil, twice daily for 7.3 years. Over 22.3 years, gastric-cancer incidence was not significantly reduced (adjusted odds ratio 0.81, 95% CI 0.57–1.13), while gastric-cancer mortality was lower (hazard ratio 0.66, 95% CI 0.43–1.00 after rounding). The secondary analysis reports the upper bound as 0.999. Other cancer and cardiovascular-mortality results were not significant. This endpoint-specific, borderline mortality signal must not be replaced with either a blanket null or a cancer-treatment claim. The independently assigned vitamin intervention contained C, E, and selenium; its effects are not garlic effects or proof of garlic–vitamin synergy. [Li 2019](https://pmc.ncbi.nlm.nih.gov/articles/PMC6737461/) [Guo 2020](https://pmc.ncbi.nlm.nih.gov/articles/PMC7320300/)

evidence_access

Primary indexed abstract reviewed; full methods, exact concentrations or species-specific attribution remain unextracted unless explicitly stated in the abstract or separately verified publisher text.

experimental_model

Editorial study-scope relationship, not experimental causation or chemical composition.

interpretation_status

Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.

limitations

Unsigned navigation only. Does not assert allicin content, metabolic conversion, causation or intervention equivalence.

plain_language

The garlic-powder-gardner-2007 study is a preparation-specific translation comparison; its outcomes are not assigned to purified allicin.

primary_references

Effect of raw garlic vs commercial garlic supplements on plasma lipid concentrations in adults with moderate hypercholesterolemia: a randomized clinical trial. | 2007 | DOI 10.1001/archinte.167.4.346 | PMID 17325296 | https://pubmed.ncbi.nlm.nih.gov/17325296/ | https://doi.org/10.1001/archinte.167.4.346

source_locator

Reviewed reference lines 91-91; exact primary location described in quoted passage where extracted.

Allicin: detailed mechanisms of action (reviewed 5 October 2026) · lines 91–91

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 · Editorial study-scope relationship, not experimental causation or chemical composition. · source_derived_draft · unverified_draft

**Cholesterol null.** Gardner randomized 192 adults with moderately elevated LDL cholesterol to raw garlic, garlic powder, aged garlic extract, or placebo for six months. Products equivalent to roughly a four-gram clove were used six days per week and chemically monitored. None significantly improved LDL, HDL, triglycerides, or the total-cholesterol/HDL ratio. This substantial null result should remain visible beside biochemical enzyme findings. It neither disproves every possible formulation nor proves that all positive trials were publication bias. [Gardner 2007](https://pubmed.ncbi.nlm.nih.gov/17325296/)

evidence_access

Primary indexed abstract reviewed; full methods, exact concentrations or species-specific attribution remain unextracted unless explicitly stated in the abstract or separately verified publisher text.

experimental_model

Editorial study-scope relationship, not experimental causation or chemical composition.

interpretation_status

Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.

limitations

Unsigned navigation only. Does not assert allicin content, metabolic conversion, causation or intervention equivalence.

plain_language

The garlic-supplement-josling-2001 study is a preparation-specific translation comparison; its outcomes are not assigned to purified allicin.

primary_references

Preventing the common cold with a garlic supplement: a double-blind, placebo-controlled survey. | 2001 | DOI 10.1007/bf02850113 | PMID 11697022 | https://pubmed.ncbi.nlm.nih.gov/11697022/ | https://doi.org/10.1007/bf02850113

source_locator

Reviewed reference lines 95-95; exact primary location described in quoted passage where extracted.

Allicin: detailed mechanisms of action (reviewed 5 October 2026) · lines 95–95

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 · Editorial study-scope relationship, not experimental causation or chemical composition. · source_derived_draft · unverified_draft

**Cold outcomes differ by preparation.** Josling's trial randomized 146 volunteers for twelve weeks and reported fewer diary-recorded colds with an allicin-containing supplement (24 versus 65 episodes). Nantz tested 2.56 g/day aged garlic extract in 120 participants: the ninety-day cold/flu incidence difference was not significant, although some symptom and activity-impact measures improved. At forty-five days, ex vivo γδ-T-cell and NK-cell proliferation also increased. These are different interventions and endpoints, not a replication of purified allicin efficacy. Neither proves that one specific compound caused the clinical effect. [Josling 2001](https://pubmed.ncbi.nlm.nih.gov/11697022/) [Nantz 2012](https://pubmed.ncbi.nlm.nih.gov/22280901/)

evidence_access

Primary indexed abstract reviewed; full methods, exact concentrations or species-specific attribution remain unextracted unless explicitly stated in the abstract or separately verified publisher text.

experimental_model

Editorial study-scope relationship, not experimental causation or chemical composition.

interpretation_status

Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.

limitations

Unsigned navigation only. Does not assert allicin content, metabolic conversion, causation or intervention equivalence.

plain_language

The raw-garlic-gardner-2007 study is a preparation-specific translation comparison; its outcomes are not assigned to purified allicin.

primary_references

Effect of raw garlic vs commercial garlic supplements on plasma lipid concentrations in adults with moderate hypercholesterolemia: a randomized clinical trial. | 2007 | DOI 10.1001/archinte.167.4.346 | PMID 17325296 | https://pubmed.ncbi.nlm.nih.gov/17325296/ | https://doi.org/10.1001/archinte.167.4.346

source_locator

Reviewed reference lines 91-91; exact primary location described in quoted passage where extracted.

Allicin: detailed mechanisms of action (reviewed 5 October 2026) · lines 91–91

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 · Editorial study-scope relationship, not experimental causation or chemical composition. · source_derived_draft · unverified_draft

**Cholesterol null.** Gardner randomized 192 adults with moderately elevated LDL cholesterol to raw garlic, garlic powder, aged garlic extract, or placebo for six months. Products equivalent to roughly a four-gram clove were used six days per week and chemically monitored. None significantly improved LDL, HDL, triglycerides, or the total-cholesterol/HDL ratio. This substantial null result should remain visible beside biochemical enzyme findings. It neither disproves every possible formulation nor proves that all positive trials were publication bias. [Gardner 2007](https://pubmed.ncbi.nlm.nih.gov/17325296/)

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

Mouse DRG neurons and pain-related behavior; separate single-channel knockout comparisons.

interpretation_status

Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.

limitations

Participation supported by converging comparisons; the other channel still contributes. Not direct chemical adduct identification in vivo.

plain_language

Allicin engaged the mouse-trpa1-dependent sensory response in mouse channel-loss and neuronal experiments.

primary_references

A single N-terminal cysteine in TRPV1 determines activation by pungent compounds from onion and garlic. | 2008 | DOI 10.1038/nn2056 | PMID 18297068 | https://pubmed.ncbi.nlm.nih.gov/18297068/ | https://pmc.ncbi.nlm.nih.gov/articles/PMC4370189/ | https://doi.org/10.1038/nn2056

source_locator

Reviewed reference lines 71-71; exact primary location described in quoted passage where extracted.

Allicin: detailed mechanisms of action (reviewed 5 October 2026) · lines 71–71

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 · Mouse DRG neurons and pain-related behavior; separate single-channel knockout comparisons. · source_derived_draft · unverified_draft

**Sensory activation.** Experiments identified allicin-dependent activation of TRPA1 and TRPV1. In the later mouse study, allicin stimulated dorsal-root-ganglion neurons and pain-related behavior. Removing either Trpa1 or Trpv1 reduced, but did not abolish, the behavioral response. The channels provide overlapping sensory routes rather than one exclusive receptor. Irritation, chemical burns, and allergic dermatitis are different outcomes. [Macpherson 2005](https://pubmed.ncbi.nlm.nih.gov/15916949/) [Salazar 2008](https://pmc.ncbi.nlm.nih.gov/articles/PMC4370189/)

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

Mouse DRG neurons and pain-related behavior; separate single-channel knockout comparisons.

interpretation_status

Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.

limitations

Participation supported by converging comparisons; the other channel still contributes. Not direct chemical adduct identification in vivo.

plain_language

Allicin engaged the mouse-trpv1-dependent sensory response in mouse channel-loss and neuronal experiments.

primary_references

A single N-terminal cysteine in TRPV1 determines activation by pungent compounds from onion and garlic. | 2008 | DOI 10.1038/nn2056 | PMID 18297068 | https://pubmed.ncbi.nlm.nih.gov/18297068/ | https://pmc.ncbi.nlm.nih.gov/articles/PMC4370189/ | https://doi.org/10.1038/nn2056

source_locator

Reviewed reference lines 71-71; exact primary location described in quoted passage where extracted.

Allicin: detailed mechanisms of action (reviewed 5 October 2026) · lines 71–71

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 · Mouse DRG neurons and pain-related behavior; separate single-channel knockout comparisons. · source_derived_draft · unverified_draft

**Sensory activation.** Experiments identified allicin-dependent activation of TRPA1 and TRPV1. In the later mouse study, allicin stimulated dorsal-root-ganglion neurons and pain-related behavior. Removing either Trpa1 or Trpv1 reduced, but did not abolish, the behavioral response. The channels provide overlapping sensory routes rather than one exclusive receptor. Irritation, chemical burns, and allergic dermatitis are different outcomes. [Macpherson 2005](https://pubmed.ncbi.nlm.nih.gov/15916949/) [Salazar 2008](https://pmc.ncbi.nlm.nih.gov/articles/PMC4370189/)

evidence_access

Primary publisher abstract reviewed; chemical identification only. Detailed reaction conditions, human absorption and therapeutic comparisons were not extracted.

experimental_model

Historical chemical identification; publisher abstract; full reaction conditions not extracted.

interpretation_status

Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.

limitations

No quantified gastrointestinal yield, clinical B1-deficiency rescue, or equivalence to TTFD inferred.

plain_language

Allicin and thiamine form thiamine allyl disulfide, identified as allithiamine in the original chemistry report.

primary_references

ALLITHIAMINE A NEWLY FOUND DERIVATIVE OF VITAMIN B1. I. DISCOVERY OF ALLITHIAMINE | 1954 | https://www.jstage.jst.go.jp/article/biochemistry1922/41/1/41_1_29/_article

source_locator

Reviewed reference lines 61-61; exact primary location described in quoted passage where extracted.

Allicin: detailed mechanisms of action (reviewed 5 October 2026) · lines 61–61

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 · Historical chemical identification; publisher abstract; full reaction conditions not extracted. · source_derived_draft · unverified_draft

**Vitamin B1 chemistry.** The original allithiamine report identified thiamine allyl disulfide as a product of reaction between allicin and thiamine. This creates a real chemical connection to vitamin B1. It does not establish how much forms after eating garlic, clinical correction of thiamine deficiency, or superiority of garlic over thiamine treatment. Allithiamine is distinct from thiamine tetrahydrofurfuryl disulfide and other synthetic derivatives. [Fujiwara 1954](https://www.jstage.jst.go.jp/article/biochemistry1922/41/1/41_1_29/_article)

evidence_access

Primary indexed abstract reviewed; full methods, exact concentrations or species-specific attribution remain unextracted unless explicitly stated in the abstract or separately verified publisher text.

experimental_model

Chemical preparation/transformation scope; media determine product mixture.

interpretation_status

Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.

limitations

DADS/DATS and ajoene remain distinct. This qualitative preparation relationship does not establish human metabolic yield or tissue exposure.

plain_language

Allicin transformation and garlic processing involve chemically distinct e-ajoene; this provenance does not transfer the product's effects to allicin.

primary_references

Products of Allicin Transformation: Ajoenes and Dithiins, Characterization and their Determination by HPLC*. | 1990 | DOI 10.1055/s-2006-960926 | PMID 17221396 | https://pubmed.ncbi.nlm.nih.gov/17221396/ | https://doi.org/10.1055/s-2006-960926

source_locator

Reviewed reference lines 15-15; exact primary location described in quoted passage where extracted.

Allicin: detailed mechanisms of action (reviewed 5 October 2026) · lines 15–15

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 · Chemical preparation/transformation scope; media determine product mixture. · source_derived_draft · unverified_draft

**Distinct sulfur compounds.** Alliin, allicin, diallyl disulfide (DADS), diallyl trisulfide (DATS), E-ajoene, Z-ajoene, and the two vinyldithiin isomers require separate records. Preparation conditions influence the transformation products and ajoene isomer ratio. S-allylcysteine (SAC) has a thioether linkage; S-allylmercaptocysteine (SAMC) is a mixed disulfide. SAMC can arise by reaction with cysteine, whereas SAC is not another name for allicin. Food processing products, biological reaction products, and metabolites should not be collapsed into one chemical family that inherits every member's effects. [Iberl 1990](https://pubmed.ncbi.nlm.nih.gov/17221396/) [Rabinkov 1998](https://pubmed.ncbi.nlm.nih.gov/9528659/)

evidence_access

Primary indexed abstract reviewed; full methods, exact concentrations or species-specific attribution remain unextracted unless explicitly stated in the abstract or separately verified publisher text.

experimental_model

Chemical preparation/transformation scope; media determine product mixture.

interpretation_status

Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.

limitations

DADS/DATS and ajoene remain distinct. This qualitative preparation relationship does not establish human metabolic yield or tissue exposure.

plain_language

Allicin transformation and garlic processing involve chemically distinct z-ajoene; this provenance does not transfer the product's effects to allicin.

primary_references

Products of Allicin Transformation: Ajoenes and Dithiins, Characterization and their Determination by HPLC*. | 1990 | DOI 10.1055/s-2006-960926 | PMID 17221396 | https://pubmed.ncbi.nlm.nih.gov/17221396/ | https://doi.org/10.1055/s-2006-960926

source_locator

Reviewed reference lines 15-15; exact primary location described in quoted passage where extracted.

Allicin: detailed mechanisms of action (reviewed 5 October 2026) · lines 15–15

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 · Chemical preparation/transformation scope; media determine product mixture. · source_derived_draft · unverified_draft

**Distinct sulfur compounds.** Alliin, allicin, diallyl disulfide (DADS), diallyl trisulfide (DATS), E-ajoene, Z-ajoene, and the two vinyldithiin isomers require separate records. Preparation conditions influence the transformation products and ajoene isomer ratio. S-allylcysteine (SAC) has a thioether linkage; S-allylmercaptocysteine (SAMC) is a mixed disulfide. SAMC can arise by reaction with cysteine, whereas SAC is not another name for allicin. Food processing products, biological reaction products, and metabolites should not be collapsed into one chemical family that inherits every member's effects. [Iberl 1990](https://pubmed.ncbi.nlm.nih.gov/17221396/) [Rabinkov 1998](https://pubmed.ncbi.nlm.nih.gov/9528659/)

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_condition

Cysteine-less construct at corresponding allicin exposure applied · Allicin Condition belongs to the full experimental contrast; do not separate a joint intervention.

experimental_condition

Cysteine-less construct at corresponding allicin exposure expressed · Rat TRPV1 cysteine-less construct with C157 restored Condition belongs to the full experimental contrast; do not separate a joint intervention.

experimental_contrast

{"intervention": "Allicin applied to C157-restored construct", "comparator": "Cysteine-less construct at corresponding allicin exposure", "endpoint": "Restoring C157 to the cysteine-less rat TRPV1 construct restored responsiveness to allicin.", "effect_direction": "increase", "combination": "joint", "conditions": [{"entity_slug": "rat-trpv1-c157-only", "state": "expressed"}, {"entity_slug": "allicin", "state": "applied"}]} Explicit extracted experimental comparison; source-derived draft.

experimental_model

Rat TRPV1 C157-only construct in HEK293; Figure 8.

interpretation_status

Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.

limitations

Interpret only within the recorded preparation, exposure and comparator. The complete source passage retains qualifications; unspecified doses/timing have not been extracted here. No clinical efficacy, nutrient deficiency or unique molecular mediation is inferred.

plain_language

Restoring C157 to the cysteine-less rat TRPV1 construct restored responsiveness to allicin.

primary_references

A single N-terminal cysteine in TRPV1 determines activation by pungent compounds from onion and garlic. | 2008 | DOI 10.1038/nn2056 | PMID 18297068 | https://pubmed.ncbi.nlm.nih.gov/18297068/ | https://pmc.ncbi.nlm.nih.gov/articles/PMC4370189/ | https://doi.org/10.1038/nn2056

source_locator

Reviewed reference lines 73-73; exact primary location described in quoted passage where extracted.

Allicin: detailed mechanisms of action (reviewed 5 October 2026) · lines 73–73

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 · Rat TRPV1 C157-only construct in HEK293; Figure 8. · source_derived_draft · unverified_draft

**A tested TRPV1 cysteine.** In rat TRPV1 expressed in HEK293 cells, the C157A substitution eliminated allicin responsiveness; reinserting C157 into a cysteine-less construct restored it. Capsaicin responsiveness persisted in the relevant mutant controls. A reducing agent reversed activation. This is direct functional evidence for a cysteine-dependent activation mechanism in that construct, not proof that every electrophile makes the same adduct or that the cell line makes the protein human. [Salazar 2008](https://pmc.ncbi.nlm.nih.gov/articles/PMC4370189/)

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_condition

Same mutant patch before allicin expressed · Rat TRPV1 C157A experimental construct Condition belongs to the full experimental contrast; do not separate a joint intervention.

experimental_condition

Same mutant patch before allicin applied · Allicin Condition belongs to the full experimental contrast; do not separate a joint intervention.

experimental_contrast

{"intervention": "Allicin applied to rat-trpv1-c157a", "comparator": "Same mutant patch before allicin", "endpoint": "The rat-trpv1-c157a construct did not show allicin responsiveness while relevant capsaicin responses persisted.", "effect_direction": "no_detected_change", "combination": "joint", "conditions": [{"entity_slug": "rat-trpv1-c157a", "state": "expressed"}, {"entity_slug": "allicin", "state": "applied"}]} Explicit extracted experimental comparison; source-derived draft.

experimental_model

Rat channel variant expressed in HEK293; Figure 8 functional comparison.

interpretation_status

Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.

limitations

No response to allicin, not nonfunctional protein. Human homolog residue numbers are not silently assigned.

plain_language

The rat-trpv1-c157a construct did not show allicin responsiveness while relevant capsaicin responses persisted.

primary_references

A single N-terminal cysteine in TRPV1 determines activation by pungent compounds from onion and garlic. | 2008 | DOI 10.1038/nn2056 | PMID 18297068 | https://pubmed.ncbi.nlm.nih.gov/18297068/ | https://pmc.ncbi.nlm.nih.gov/articles/PMC4370189/ | https://doi.org/10.1038/nn2056

source_locator

Reviewed reference lines 73-73; exact primary location described in quoted passage where extracted.

Allicin: detailed mechanisms of action (reviewed 5 October 2026) · lines 73–73

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 · Rat channel variant expressed in HEK293; Figure 8 functional comparison. · source_derived_draft · unverified_draft

**A tested TRPV1 cysteine.** In rat TRPV1 expressed in HEK293 cells, the C157A substitution eliminated allicin responsiveness; reinserting C157 into a cysteine-less construct restored it. Capsaicin responsiveness persisted in the relevant mutant controls. A reducing agent reversed activation. This is direct functional evidence for a cysteine-dependent activation mechanism in that construct, not proof that every electrophile makes the same adduct or that the cell line makes the protein human. [Salazar 2008](https://pmc.ncbi.nlm.nih.gov/articles/PMC4370189/)

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_condition

Same mutant patch before allicin applied · Allicin Condition belongs to the full experimental contrast; do not separate a joint intervention.

experimental_condition

Same mutant patch before allicin expressed · Rat TRPV1 cysteine-less experimental construct Condition belongs to the full experimental contrast; do not separate a joint intervention.

experimental_contrast

{"intervention": "Allicin applied to rat-trpv1-cysteine-less", "comparator": "Same mutant patch before allicin", "endpoint": "The rat-trpv1-cysteine-less construct did not show allicin responsiveness while relevant capsaicin responses persisted.", "effect_direction": "no_detected_change", "combination": "joint", "conditions": [{"entity_slug": "rat-trpv1-cysteine-less", "state": "expressed"}, {"entity_slug": "allicin", "state": "applied"}]} Explicit extracted experimental comparison; source-derived draft.

experimental_model

Rat channel variant expressed in HEK293; Figure 8 functional comparison.

interpretation_status

Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.

limitations

No response to allicin, not nonfunctional protein. Human homolog residue numbers are not silently assigned.

plain_language

The rat-trpv1-cysteine-less construct did not show allicin responsiveness while relevant capsaicin responses persisted.

primary_references

A single N-terminal cysteine in TRPV1 determines activation by pungent compounds from onion and garlic. | 2008 | DOI 10.1038/nn2056 | PMID 18297068 | https://pubmed.ncbi.nlm.nih.gov/18297068/ | https://pmc.ncbi.nlm.nih.gov/articles/PMC4370189/ | https://doi.org/10.1038/nn2056

source_locator

Reviewed reference lines 73-73; exact primary location described in quoted passage where extracted.

Allicin: detailed mechanisms of action (reviewed 5 October 2026) · lines 73–73

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 · Rat channel variant expressed in HEK293; Figure 8 functional comparison. · source_derived_draft · unverified_draft

**A tested TRPV1 cysteine.** In rat TRPV1 expressed in HEK293 cells, the C157A substitution eliminated allicin responsiveness; reinserting C157 into a cysteine-less construct restored it. Capsaicin responsiveness persisted in the relevant mutant controls. A reducing agent reversed activation. This is direct functional evidence for a cysteine-dependent activation mechanism in that construct, not proof that every electrophile makes the same adduct or that the cell line makes the protein human. [Salazar 2008](https://pmc.ncbi.nlm.nih.gov/articles/PMC4370189/)

evidence_access

Primary indexed abstract reviewed; full methods, exact concentrations or species-specific attribution remain unextracted unless explicitly stated in the abstract or separately verified publisher text.

experimental_model

Garlic sulfur chemistry; spontaneous condensation follows the enzymatic cleavage.

interpretation_status

Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.

limitations

Interpret only within the recorded preparation, exposure and comparator. The complete source passage retains qualifications; unspecified doses/timing have not been extracted here. No clinical efficacy, nutrient deficiency or unique molecular mediation is inferred.

plain_language

Two allylsulfenic-acid molecules condense to allicin with water loss.

primary_references

Two structures of alliinase from Alliium sativum L.: apo form and ternary complex with aminoacrylate reaction intermediate covalently bound to the PLP cofactor. | 2007 | DOI 10.1016/j.jmb.2006.11.041 | PMID 17174334 | https://pubmed.ncbi.nlm.nih.gov/17174334/ | https://doi.org/10.1016/j.jmb.2006.11.041

source_locator

Reviewed reference lines 11-11; exact primary location described in quoted passage where extracted.

Allicin: detailed mechanisms of action (reviewed 5 October 2026) · lines 11–11

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 · Garlic sulfur chemistry; spontaneous condensation follows the enzymatic cleavage. · source_derived_draft · unverified_draft

**Alliinase and vitamin B6.** Garlic alliinase is a plant pyridoxal-5′-phosphate (PLP)-dependent enzyme, not a human enzyme. Structural studies resolved its cofactor-containing active site, an apo form, and a PLP-bound aminoacrylate intermediate. Alliin cleavage produces allylsulfenic acid and an aminoacrylate intermediate; the latter yields pyruvate and ammonia. Two allylsulfenic acid molecules condense to allicin with water loss. This links allicin formation to B6 chemistry in the plant. It does not show that taking B6 increases allicin production in a person. [Kuettner 2002](https://pubmed.ncbi.nlm.nih.gov/12235163/) [Shimon 2007](https://pubmed.ncbi.nlm.nih.gov/17174334/)

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_condition

Allicin-activated channel before DTT prior exposure · Allicin Condition belongs to the full experimental contrast; do not separate a joint intervention.

experimental_condition

Allicin-activated channel before DTT added · Dithiothreitol / DTT Condition belongs to the full experimental contrast; do not separate a joint intervention.

experimental_contrast

{"intervention": "DTT after allicin", "comparator": "Allicin-activated channel before DTT", "endpoint": "A reducing agent reversed allicin-evoked TRPV1 activation in the patch assay.", "effect_direction": "decrease", "combination": "joint", "conditions": [{"entity_slug": "dithiothreitol", "state": "added"}, {"entity_slug": "allicin", "state": "prior exposure"}]} Explicit extracted experimental comparison; source-derived draft.

experimental_model

Rat TRPV1 in HEK293; DTT addition after allicin exposure.

interpretation_status

Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.

limitations

Experimental reducing agent, not an oral treatment recommendation.

plain_language

A reducing agent reversed allicin-evoked TRPV1 activation in the patch assay.

primary_references

A single N-terminal cysteine in TRPV1 determines activation by pungent compounds from onion and garlic. | 2008 | DOI 10.1038/nn2056 | PMID 18297068 | https://pubmed.ncbi.nlm.nih.gov/18297068/ | https://pmc.ncbi.nlm.nih.gov/articles/PMC4370189/ | https://doi.org/10.1038/nn2056

source_locator

Reviewed reference lines 73-73; exact primary location described in quoted passage where extracted.

Allicin: detailed mechanisms of action (reviewed 5 October 2026) · lines 73–73

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 · Rat TRPV1 in HEK293; DTT addition after allicin exposure. · source_derived_draft · unverified_draft

**A tested TRPV1 cysteine.** In rat TRPV1 expressed in HEK293 cells, the C157A substitution eliminated allicin responsiveness; reinserting C157 into a cysteine-less construct restored it. Capsaicin responsiveness persisted in the relevant mutant controls. A reducing agent reversed activation. This is direct functional evidence for a cysteine-dependent activation mechanism in that construct, not proof that every electrophile makes the same adduct or that the cell line makes the protein human. [Salazar 2008](https://pmc.ncbi.nlm.nih.gov/articles/PMC4370189/)

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_condition

Same allicin exposure without added GSH present · Allicin Condition belongs to the full experimental contrast; do not separate a joint intervention.

experimental_condition

Same allicin exposure without added GSH added extracellularly · GSH Condition belongs to the full experimental contrast; do not separate a joint intervention.

experimental_contrast

{"intervention": "Allicin plus 1 mM extracellular GSH", "comparator": "Same allicin exposure without added GSH", "endpoint": "Added extracellular glutathione reduced injury from allicin in Human A549/Beas-2B epithelial cultures.", "effect_direction": "decrease", "combination": "joint", "conditions": [{"entity_slug": "glutathione", "state": "added extracellularly"}, {"entity_slug": "allicin", "state": "present"}]} Explicit extracted experimental comparison; source-derived draft.

experimental_model

Human A549/Beas-2B epithelial cultures; 1 mM extracellular GSH, direct allicin exposure; metabolic/LDH assays.

interpretation_status

Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.

limitations

Quenching changes free exposure; it is not proof of intracellular repair or a validated physiological plasma GSH level.

plain_language

Added extracellular glutathione reduced injury from allicin in Human A549/Beas-2B epithelial cultures.

primary_references

Diallylthiosulfinate (Allicin), a Volatile Antimicrobial from Garlic (Allium sativum), Kills Human Lung Pathogenic Bacteria, Including MDR Strains, as a Vapor. | 2017 | DOI 10.3390/molecules22101711 | PMID 29023413 | https://pubmed.ncbi.nlm.nih.gov/29023413/ | https://pmc.ncbi.nlm.nih.gov/articles/PMC6151386/ | https://doi.org/10.3390/molecules22101711

source_locator

Reviewed reference lines 65-65; exact primary location described in quoted passage where extracted.

Allicin: detailed mechanisms of action (reviewed 5 October 2026) · lines 65–65

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 A549/Beas-2B epithelial cultures; 1 mM extracellular GSH, direct allicin exposure; metabolic/LDH assays. · source_derived_draft · unverified_draft

**Laboratory antimicrobial activity.** Purified allicin inhibited multiple tested respiratory bacterial isolates, including some resistant to clinical antibiotics; susceptibility varied by organism and assay. The same investigation measured mammalian-cell and rat-lung-slice toxicity. Added glutathione reduced toxicity in those models. The experimental 1-mM glutathione condition must not be presented as a validated normal plasma concentration or a safe inhalation regimen. Luminal or surface accessibility is a hypothesis about delivery, not a calculation proving efficacy from nominal dose divided by fluid volume. [Reiter 2017](https://pmc.ncbi.nlm.nih.gov/articles/PMC6151386/)

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_condition

Same allicin exposure without added GSH present · Allicin Condition belongs to the full experimental contrast; do not separate a joint intervention.

experimental_condition

Same allicin exposure without added GSH added extracellularly · GSH Condition belongs to the full experimental contrast; do not separate a joint intervention.

experimental_contrast

{"intervention": "Allicin plus 1 mM extracellular GSH", "comparator": "Same allicin exposure without added GSH", "endpoint": "Added extracellular glutathione reduced injury from allicin in Rat precision-cut lung slices.", "effect_direction": "decrease", "combination": "joint", "conditions": [{"entity_slug": "glutathione", "state": "added extracellularly"}, {"entity_slug": "allicin", "state": "present"}]} Explicit extracted experimental comparison; source-derived draft.

experimental_model

Rat precision-cut lung slices; 1 mM extracellular GSH, direct allicin exposure; metabolic/LDH assays.

interpretation_status

Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.

limitations

Quenching changes free exposure; it is not proof of intracellular repair or a validated physiological plasma GSH level.

plain_language

Added extracellular glutathione reduced injury from allicin in Rat precision-cut lung slices.

primary_references

Diallylthiosulfinate (Allicin), a Volatile Antimicrobial from Garlic (Allium sativum), Kills Human Lung Pathogenic Bacteria, Including MDR Strains, as a Vapor. | 2017 | DOI 10.3390/molecules22101711 | PMID 29023413 | https://pubmed.ncbi.nlm.nih.gov/29023413/ | https://pmc.ncbi.nlm.nih.gov/articles/PMC6151386/ | https://doi.org/10.3390/molecules22101711

source_locator

Reviewed reference lines 65-65; exact primary location described in quoted passage where extracted.

Allicin: detailed mechanisms of action (reviewed 5 October 2026) · lines 65–65

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 · Rat precision-cut lung slices; 1 mM extracellular GSH, direct allicin exposure; metabolic/LDH assays. · source_derived_draft · unverified_draft

**Laboratory antimicrobial activity.** Purified allicin inhibited multiple tested respiratory bacterial isolates, including some resistant to clinical antibiotics; susceptibility varied by organism and assay. The same investigation measured mammalian-cell and rat-lung-slice toxicity. Added glutathione reduced toxicity in those models. The experimental 1-mM glutathione condition must not be presented as a validated normal plasma concentration or a safe inhalation regimen. Luminal or surface accessibility is a hypothesis about delivery, not a calculation proving efficacy from nominal dose divided by fluid volume. [Reiter 2017](https://pmc.ncbi.nlm.nih.gov/articles/PMC6151386/)

evidence_access

Primary indexed abstract reviewed; full methods, exact concentrations or species-specific attribution remain unextracted unless explicitly stated in the abstract or separately verified publisher text.

experimental_condition

Allicin-inhibited enzyme without effective reductant prior inhibitory exposure · Allicin Condition belongs to the full experimental contrast; do not separate a joint intervention.

experimental_condition

Allicin-inhibited enzyme without effective reductant added · GSH Condition belongs to the full experimental contrast; do not separate a joint intervention.

experimental_contrast

{"intervention": "GSH addition after allicin inhibition", "comparator": "Allicin-inhibited enzyme without effective reductant", "endpoint": "Glutathione restored activity of allicin-inhibited papain.", "effect_direction": "increase", "combination": "joint", "conditions": [{"entity_slug": "allicin", "state": "prior inhibitory exposure"}, {"entity_slug": "glutathione", "state": "added"}]} Explicit extracted experimental comparison; source-derived draft.

experimental_model

Purified enzyme, prior allicin inhibition, reductant comparison.

interpretation_status

Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.

limitations

Interpret only within the recorded preparation, exposure and comparator. The complete source passage retains qualifications; unspecified doses/timing have not been extracted here. No clinical efficacy, nutrient deficiency or unique molecular mediation is inferred.

plain_language

Glutathione restored activity of allicin-inhibited papain.

primary_references

The mode of action of allicin: trapping of radicals and interaction with thiol containing proteins. | 1998 | DOI 10.1016/s0304-4165(97)00104-9 | PMID 9528659 | https://pubmed.ncbi.nlm.nih.gov/9528659/ | https://doi.org/10.1016/s0304-4165(97)00104-9

source_locator

Reviewed reference lines 41-41; exact primary location described in quoted passage where extracted.

Allicin: detailed mechanisms of action (reviewed 5 October 2026) · lines 41–41

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 · Purified enzyme, prior allicin inhibition, reductant comparison. · source_derived_draft · unverified_draft

**Enzyme inhibition and reversal differ by target.** The early purified-enzyme study observed inhibition of papain, bacterial NADP-dependent alcohol dehydrogenase, and horse-liver NAD-dependent alcohol dehydrogenase. Thiols could reactivate the enzymes, but not interchangeably: glutathione restored papain activity, whereas it did not restore the tested bacterial dehydrogenase under those conditions. Dithiothreitol or mercaptoethanol had different reversal profiles. Covalent inhibition is therefore not equivalent to unrecoverable injury, and a general glutathione rescue cannot be assumed for every enzyme. [Rabinkov 1998](https://pubmed.ncbi.nlm.nih.gov/9528659/)

evidence_access

Primary indexed abstract reviewed; full methods, exact concentrations or species-specific attribution remain unextracted unless explicitly stated in the abstract or separately verified publisher text.

experimental_condition

Allicin-inhibited enzyme without effective reductant prior inhibitory exposure · Allicin Condition belongs to the full experimental contrast; do not separate a joint intervention.

experimental_condition

Allicin-inhibited enzyme without effective reductant added · GSH Condition belongs to the full experimental contrast; do not separate a joint intervention.

experimental_contrast

{"intervention": "GSH addition after allicin inhibition", "comparator": "Allicin-inhibited enzyme without effective reductant", "endpoint": "Glutathione did not restore the allicin-inhibited bacterial dehydrogenase in the tested assay.", "effect_direction": "no_detected_change", "combination": "joint", "conditions": [{"entity_slug": "allicin", "state": "prior inhibitory exposure"}, {"entity_slug": "glutathione", "state": "added"}]} Explicit extracted experimental comparison; source-derived draft.

experimental_model

Purified enzyme, prior allicin inhibition, reductant comparison.

interpretation_status

Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.

limitations

Interpret only within the recorded preparation, exposure and comparator. The complete source passage retains qualifications; unspecified doses/timing have not been extracted here. No clinical efficacy, nutrient deficiency or unique molecular mediation is inferred.

plain_language

Glutathione did not restore the allicin-inhibited bacterial dehydrogenase in the tested assay.

primary_references

The mode of action of allicin: trapping of radicals and interaction with thiol containing proteins. | 1998 | DOI 10.1016/s0304-4165(97)00104-9 | PMID 9528659 | https://pubmed.ncbi.nlm.nih.gov/9528659/ | https://doi.org/10.1016/s0304-4165(97)00104-9

source_locator

Reviewed reference lines 41-41; exact primary location described in quoted passage where extracted.

Allicin: detailed mechanisms of action (reviewed 5 October 2026) · lines 41–41

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 · Purified enzyme, prior allicin inhibition, reductant comparison. · source_derived_draft · unverified_draft

**Enzyme inhibition and reversal differ by target.** The early purified-enzyme study observed inhibition of papain, bacterial NADP-dependent alcohol dehydrogenase, and horse-liver NAD-dependent alcohol dehydrogenase. Thiols could reactivate the enzymes, but not interchangeably: glutathione restored papain activity, whereas it did not restore the tested bacterial dehydrogenase under those conditions. Dithiothreitol or mercaptoethanol had different reversal profiles. Covalent inhibition is therefore not equivalent to unrecoverable injury, and a general glutathione rescue cannot be assumed for every enzyme. [Rabinkov 1998](https://pubmed.ncbi.nlm.nih.gov/9528659/)

availability_state

machinery_impairment Imported condition classification; unverified.

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_condition

Wild-type with the same allicin exposure deleted · Mouse Trpa1 ion channel Condition belongs to the full experimental contrast; do not separate a joint intervention.

experimental_condition

Wild-type with the same allicin exposure present · Allicin Condition belongs to the full experimental contrast; do not separate a joint intervention.

experimental_contrast

{"intervention": "mouse-trpa1 deletion with allicin", "comparator": "Wild-type with the same allicin exposure", "endpoint": "Loss of mouse-trpa1 reduced but did not abolish allicin-evoked pain-related behavior.", "effect_direction": "decrease", "combination": "joint", "conditions": [{"entity_slug": "mouse-trpa1", "state": "deleted"}, {"entity_slug": "allicin", "state": "present"}]} Explicit extracted experimental comparison; source-derived draft.

experimental_model

Mouse single-gene knockout compared with its wild-type littermate background.

interpretation_status

Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.

limitations

No double-knockout inference; behavioral assay, not proof of human allergy or burns.

plain_language

Loss of mouse-trpa1 reduced but did not abolish allicin-evoked pain-related behavior.

primary_references

A single N-terminal cysteine in TRPV1 determines activation by pungent compounds from onion and garlic. | 2008 | DOI 10.1038/nn2056 | PMID 18297068 | https://pubmed.ncbi.nlm.nih.gov/18297068/ | https://pmc.ncbi.nlm.nih.gov/articles/PMC4370189/ | https://doi.org/10.1038/nn2056

source_locator

Reviewed reference lines 71-71; exact primary location described in quoted passage where extracted.

trigger_kind

machinery_impairment Imported condition classification; unverified.

Allicin: detailed mechanisms of action (reviewed 5 October 2026) · lines 71–71

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 · Mouse single-gene knockout compared with its wild-type littermate background. · source_derived_draft · unverified_draft

**Sensory activation.** Experiments identified allicin-dependent activation of TRPA1 and TRPV1. In the later mouse study, allicin stimulated dorsal-root-ganglion neurons and pain-related behavior. Removing either Trpa1 or Trpv1 reduced, but did not abolish, the behavioral response. The channels provide overlapping sensory routes rather than one exclusive receptor. Irritation, chemical burns, and allergic dermatitis are different outcomes. [Macpherson 2005](https://pubmed.ncbi.nlm.nih.gov/15916949/) [Salazar 2008](https://pmc.ncbi.nlm.nih.gov/articles/PMC4370189/)

availability_state

machinery_impairment Imported condition classification; unverified.

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_condition

Wild-type with the same allicin exposure deleted · Mouse transient receptor potential vanilloid 1 / Trpv1 Condition belongs to the full experimental contrast; do not separate a joint intervention.

experimental_condition

Wild-type with the same allicin exposure present · Allicin Condition belongs to the full experimental contrast; do not separate a joint intervention.

experimental_contrast

{"intervention": "mouse-trpv1 deletion with allicin", "comparator": "Wild-type with the same allicin exposure", "endpoint": "Loss of mouse-trpv1 reduced but did not abolish allicin-evoked pain-related behavior.", "effect_direction": "decrease", "combination": "joint", "conditions": [{"entity_slug": "mouse-trpv1", "state": "deleted"}, {"entity_slug": "allicin", "state": "present"}]} Explicit extracted experimental comparison; source-derived draft.

experimental_model

Mouse single-gene knockout compared with its wild-type littermate background.

interpretation_status

Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.

limitations

No double-knockout inference; behavioral assay, not proof of human allergy or burns.

plain_language

Loss of mouse-trpv1 reduced but did not abolish allicin-evoked pain-related behavior.

primary_references

A single N-terminal cysteine in TRPV1 determines activation by pungent compounds from onion and garlic. | 2008 | DOI 10.1038/nn2056 | PMID 18297068 | https://pubmed.ncbi.nlm.nih.gov/18297068/ | https://pmc.ncbi.nlm.nih.gov/articles/PMC4370189/ | https://doi.org/10.1038/nn2056

source_locator

Reviewed reference lines 71-71; exact primary location described in quoted passage where extracted.

trigger_kind

machinery_impairment Imported condition classification; unverified.

Allicin: detailed mechanisms of action (reviewed 5 October 2026) · lines 71–71

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 · Mouse single-gene knockout compared with its wild-type littermate background. · source_derived_draft · unverified_draft

**Sensory activation.** Experiments identified allicin-dependent activation of TRPA1 and TRPV1. In the later mouse study, allicin stimulated dorsal-root-ganglion neurons and pain-related behavior. Removing either Trpa1 or Trpv1 reduced, but did not abolish, the behavioral response. The channels provide overlapping sensory routes rather than one exclusive receptor. Irritation, chemical burns, and allergic dermatitis are different outcomes. [Macpherson 2005](https://pubmed.ncbi.nlm.nih.gov/15916949/) [Salazar 2008](https://pmc.ncbi.nlm.nih.gov/articles/PMC4370189/)

availability_state

machinery_impairment Imported condition classification; unverified.

evidence_access

Primary indexed abstract reviewed; full methods, exact concentrations or species-specific attribution remain unextracted unless explicitly stated in the abstract or separately verified publisher text.

experimental_condition

Yeast comparator without that deletion at matched allicin exposure deleted · Saccharomyces cerevisiae high-affinity copper transporter / Ctr1 Condition belongs to the full experimental contrast; do not separate a joint intervention.

experimental_condition

Yeast comparator without that deletion at matched allicin exposure present · Allicin Condition belongs to the full experimental contrast; do not separate a joint intervention.

experimental_contrast

{"intervention": "yeast-ctr1 deletion with allicin", "comparator": "Yeast comparator without that deletion at matched allicin exposure", "endpoint": "Deletion of yeast-ctr1 increased yeast sensitivity to allicin.", "effect_direction": "decrease", "combination": "joint", "conditions": [{"entity_slug": "yeast-ctr1", "state": "deleted"}, {"entity_slug": "allicin", "state": "present"}]} Explicit extracted experimental comparison; source-derived draft.

experimental_model

Saccharomyces cerevisiae deletion screen; primary abstract; exact dose and exposure duration unextracted.

interpretation_status

Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.

limitations

Hypersensitivity does not prove direct binding to the deleted protein or distinguish metal uptake from metalloprotein dysfunction.

plain_language

Deletion of yeast-ctr1 increased yeast sensitivity to allicin.

primary_references

A Mini HIP HOP Assay Uncovers a Central Role for Copper and Zinc in the Antifungal Mode of Action of Allicin. | 2017 | DOI 10.1021/acs.jafc.7b00250 | PMID 28421744 | https://pubmed.ncbi.nlm.nih.gov/28421744/ | https://doi.org/10.1021/acs.jafc.7b00250

source_locator

Reviewed reference lines 59-59; exact primary location described in quoted passage where extracted.

trigger_kind

machinery_impairment Imported condition classification; unverified.

Allicin: detailed mechanisms of action (reviewed 5 October 2026) · lines 59–59

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 · Saccharomyces cerevisiae deletion screen; primary abstract; exact dose and exposure duration unextracted. · source_derived_draft · unverified_draft

**Yeast metal requirements.** In a chemical-genetic screen of Saccharomyces cerevisiae, loss of CTR1, MAC1, or ZAP1 increased sensitivity to allicin; copper or zinc additions rescued the relevant sensitized phenotypes. This supports involvement of metal acquisition or metalloprotein function but does not discriminate those alternatives. It is not direct proof that allicin binds each protein, chelates all intracellular copper, or causes human mineral deficiency. Exact supplementation concentrations and all strain-specific contrasts remain unextracted from the accessible abstract. [Prescott and Panaretou 2017](https://pubmed.ncbi.nlm.nih.gov/28421744/)

availability_state

machinery_impairment Imported condition classification; unverified.

evidence_access

Primary indexed abstract reviewed; full methods, exact concentrations or species-specific attribution remain unextracted unless explicitly stated in the abstract or separately verified publisher text.

experimental_condition

Yeast comparator without that deletion at matched allicin exposure present · Allicin Condition belongs to the full experimental contrast; do not separate a joint intervention.

experimental_condition

Yeast comparator without that deletion at matched allicin exposure deleted · Saccharomyces cerevisiae copper-responsive transcription factor / Mac1 Condition belongs to the full experimental contrast; do not separate a joint intervention.

experimental_contrast

{"intervention": "yeast-mac1 deletion with allicin", "comparator": "Yeast comparator without that deletion at matched allicin exposure", "endpoint": "Deletion of yeast-mac1 increased yeast sensitivity to allicin.", "effect_direction": "decrease", "combination": "joint", "conditions": [{"entity_slug": "yeast-mac1", "state": "deleted"}, {"entity_slug": "allicin", "state": "present"}]} Explicit extracted experimental comparison; source-derived draft.

experimental_model

Saccharomyces cerevisiae deletion screen; primary abstract; exact dose and exposure duration unextracted.

interpretation_status

Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.

limitations

Hypersensitivity does not prove direct binding to the deleted protein or distinguish metal uptake from metalloprotein dysfunction.

plain_language

Deletion of yeast-mac1 increased yeast sensitivity to allicin.

primary_references

A Mini HIP HOP Assay Uncovers a Central Role for Copper and Zinc in the Antifungal Mode of Action of Allicin. | 2017 | DOI 10.1021/acs.jafc.7b00250 | PMID 28421744 | https://pubmed.ncbi.nlm.nih.gov/28421744/ | https://doi.org/10.1021/acs.jafc.7b00250

source_locator

Reviewed reference lines 59-59; exact primary location described in quoted passage where extracted.

trigger_kind

machinery_impairment Imported condition classification; unverified.

Allicin: detailed mechanisms of action (reviewed 5 October 2026) · lines 59–59

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 · Saccharomyces cerevisiae deletion screen; primary abstract; exact dose and exposure duration unextracted. · source_derived_draft · unverified_draft

**Yeast metal requirements.** In a chemical-genetic screen of Saccharomyces cerevisiae, loss of CTR1, MAC1, or ZAP1 increased sensitivity to allicin; copper or zinc additions rescued the relevant sensitized phenotypes. This supports involvement of metal acquisition or metalloprotein function but does not discriminate those alternatives. It is not direct proof that allicin binds each protein, chelates all intracellular copper, or causes human mineral deficiency. Exact supplementation concentrations and all strain-specific contrasts remain unextracted from the accessible abstract. [Prescott and Panaretou 2017](https://pubmed.ncbi.nlm.nih.gov/28421744/)

availability_state

machinery_impairment Imported condition classification; unverified.

evidence_access

Primary indexed abstract reviewed; full methods, exact concentrations or species-specific attribution remain unextracted unless explicitly stated in the abstract or separately verified publisher text.

experimental_condition

Yeast comparator without that deletion at matched allicin exposure deleted · Saccharomyces cerevisiae zinc-responsive transcription factor / Zap1 Condition belongs to the full experimental contrast; do not separate a joint intervention.

experimental_condition

Yeast comparator without that deletion at matched allicin exposure present · Allicin Condition belongs to the full experimental contrast; do not separate a joint intervention.

experimental_contrast

{"intervention": "yeast-zap1 deletion with allicin", "comparator": "Yeast comparator without that deletion at matched allicin exposure", "endpoint": "Deletion of yeast-zap1 increased yeast sensitivity to allicin.", "effect_direction": "decrease", "combination": "joint", "conditions": [{"entity_slug": "yeast-zap1", "state": "deleted"}, {"entity_slug": "allicin", "state": "present"}]} Explicit extracted experimental comparison; source-derived draft.

experimental_model

Saccharomyces cerevisiae deletion screen; primary abstract; exact dose and exposure duration unextracted.

interpretation_status

Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.

limitations

Hypersensitivity does not prove direct binding to the deleted protein or distinguish metal uptake from metalloprotein dysfunction.

plain_language

Deletion of yeast-zap1 increased yeast sensitivity to allicin.

primary_references

A Mini HIP HOP Assay Uncovers a Central Role for Copper and Zinc in the Antifungal Mode of Action of Allicin. | 2017 | DOI 10.1021/acs.jafc.7b00250 | PMID 28421744 | https://pubmed.ncbi.nlm.nih.gov/28421744/ | https://doi.org/10.1021/acs.jafc.7b00250

source_locator

Reviewed reference lines 59-59; exact primary location described in quoted passage where extracted.

trigger_kind

machinery_impairment Imported condition classification; unverified.

Allicin: detailed mechanisms of action (reviewed 5 October 2026) · lines 59–59

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 · Saccharomyces cerevisiae deletion screen; primary abstract; exact dose and exposure duration unextracted. · source_derived_draft · unverified_draft

**Yeast metal requirements.** In a chemical-genetic screen of Saccharomyces cerevisiae, loss of CTR1, MAC1, or ZAP1 increased sensitivity to allicin; copper or zinc additions rescued the relevant sensitized phenotypes. This supports involvement of metal acquisition or metalloprotein function but does not discriminate those alternatives. It is not direct proof that allicin binds each protein, chelates all intracellular copper, or causes human mineral deficiency. Exact supplementation concentrations and all strain-specific contrasts remain unextracted from the accessible abstract. [Prescott and Panaretou 2017](https://pubmed.ncbi.nlm.nih.gov/28421744/)

evidence_access

Primary indexed abstract reviewed; full methods, exact concentrations or species-specific attribution remain unextracted unless explicitly stated in the abstract or separately verified publisher text.

experimental_condition

Same sensitized yeast with allicin without added metal added in relevant mutant background · Copper(II) ion Condition belongs to the full experimental contrast; do not separate a joint intervention.

experimental_condition

Same sensitized yeast with allicin without added metal present · Allicin Condition belongs to the full experimental contrast; do not separate a joint intervention.

experimental_contrast

{"intervention": "Metal addition to the corresponding sensitized allicin-exposed yeast", "comparator": "Same sensitized yeast with allicin without added metal", "endpoint": "Added copper-ii reversed the relevant metal-defence-mutant hypersensitivity to allicin in yeast.", "effect_direction": "increase", "combination": "joint", "conditions": [{"entity_slug": "copper-ii", "state": "added in relevant mutant background"}, {"entity_slug": "allicin", "state": "present"}]} Explicit extracted experimental comparison; source-derived draft.

experimental_model

Saccharomyces cerevisiae sensitized-mutant rescue; accessible abstract; exact individual strain-dose mapping not fully extracted.

interpretation_status

Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.

limitations

Abstract reports copper/zinc rescue but does not provide all strain-specific values. No human mineral-deficiency or supplementation claim.

plain_language

Added copper-ii reversed the relevant metal-defence-mutant hypersensitivity to allicin in yeast.

primary_references

A Mini HIP HOP Assay Uncovers a Central Role for Copper and Zinc in the Antifungal Mode of Action of Allicin. | 2017 | DOI 10.1021/acs.jafc.7b00250 | PMID 28421744 | https://pubmed.ncbi.nlm.nih.gov/28421744/ | https://doi.org/10.1021/acs.jafc.7b00250

source_locator

Reviewed reference lines 59-59; exact primary location described in quoted passage where extracted.

Allicin: detailed mechanisms of action (reviewed 5 October 2026) · lines 59–59

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 · Saccharomyces cerevisiae sensitized-mutant rescue; accessible abstract; exact individual strain-dose mapping not fully extracted. · source_derived_draft · unverified_draft

**Yeast metal requirements.** In a chemical-genetic screen of Saccharomyces cerevisiae, loss of CTR1, MAC1, or ZAP1 increased sensitivity to allicin; copper or zinc additions rescued the relevant sensitized phenotypes. This supports involvement of metal acquisition or metalloprotein function but does not discriminate those alternatives. It is not direct proof that allicin binds each protein, chelates all intracellular copper, or causes human mineral deficiency. Exact supplementation concentrations and all strain-specific contrasts remain unextracted from the accessible abstract. [Prescott and Panaretou 2017](https://pubmed.ncbi.nlm.nih.gov/28421744/)

evidence_access

Primary indexed abstract reviewed; full methods, exact concentrations or species-specific attribution remain unextracted unless explicitly stated in the abstract or separately verified publisher text.

experimental_condition

Same sensitized yeast with allicin without added metal added in relevant mutant background · Zinc(II) ion Condition belongs to the full experimental contrast; do not separate a joint intervention.

experimental_condition

Same sensitized yeast with allicin without added metal present · Allicin Condition belongs to the full experimental contrast; do not separate a joint intervention.

experimental_contrast

{"intervention": "Metal addition to the corresponding sensitized allicin-exposed yeast", "comparator": "Same sensitized yeast with allicin without added metal", "endpoint": "Added zinc-ion reversed the relevant metal-defence-mutant hypersensitivity to allicin in yeast.", "effect_direction": "increase", "combination": "joint", "conditions": [{"entity_slug": "zinc-ion", "state": "added in relevant mutant background"}, {"entity_slug": "allicin", "state": "present"}]} Explicit extracted experimental comparison; source-derived draft.

experimental_model

Saccharomyces cerevisiae sensitized-mutant rescue; accessible abstract; exact individual strain-dose mapping not fully extracted.

interpretation_status

Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.

limitations

Abstract reports copper/zinc rescue but does not provide all strain-specific values. No human mineral-deficiency or supplementation claim.

plain_language

Added zinc-ion reversed the relevant metal-defence-mutant hypersensitivity to allicin in yeast.

primary_references

A Mini HIP HOP Assay Uncovers a Central Role for Copper and Zinc in the Antifungal Mode of Action of Allicin. | 2017 | DOI 10.1021/acs.jafc.7b00250 | PMID 28421744 | https://pubmed.ncbi.nlm.nih.gov/28421744/ | https://doi.org/10.1021/acs.jafc.7b00250

source_locator

Reviewed reference lines 59-59; exact primary location described in quoted passage where extracted.

Allicin: detailed mechanisms of action (reviewed 5 October 2026) · lines 59–59

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 · Saccharomyces cerevisiae sensitized-mutant rescue; accessible abstract; exact individual strain-dose mapping not fully extracted. · source_derived_draft · unverified_draft

**Yeast metal requirements.** In a chemical-genetic screen of Saccharomyces cerevisiae, loss of CTR1, MAC1, or ZAP1 increased sensitivity to allicin; copper or zinc additions rescued the relevant sensitized phenotypes. This supports involvement of metal acquisition or metalloprotein function but does not discriminate those alternatives. It is not direct proof that allicin binds each protein, chelates all intracellular copper, or causes human mineral deficiency. Exact supplementation concentrations and all strain-specific contrasts remain unextracted from the accessible abstract. [Prescott and Panaretou 2017](https://pubmed.ncbi.nlm.nih.gov/28421744/)

availability_state

machinery_impairment Imported condition classification; unverified.

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_condition

Wild-type yeast at the same allicin exposure deleted · Saccharomyces cerevisiae glutathione reductase / Glr1 Condition belongs to the full experimental contrast; do not separate a joint intervention.

experimental_condition

Wild-type yeast at the same allicin exposure present · Allicin Condition belongs to the full experimental contrast; do not separate a joint intervention.

experimental_contrast

{"intervention": "yeast-glr1 deletion with allicin", "comparator": "Wild-type yeast at the same allicin exposure", "endpoint": "Loss of yeast-glr1 increased susceptibility in the allicin arm of the yeast chemical-genetic comparison.", "effect_direction": "decrease", "combination": "joint", "conditions": [{"entity_slug": "yeast-glr1", "state": "deleted"}, {"entity_slug": "allicin", "state": "present"}]} Explicit extracted experimental comparison; source-derived draft.

experimental_model

Saccharomyces cerevisiae; separate gene deletions and allicin exposures compared with an analogue; Figure 3.

interpretation_status

Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.

limitations

Keep dose and compound distinctions: analogue effects cannot substitute for allicin. Not a human nutrient-deficiency phenotype.

plain_language

Loss of yeast-glr1 increased susceptibility in the allicin arm of the yeast chemical-genetic comparison.

primary_references

The Sulfilimine Analogue of Allicin, <i>S</i>-Allyl-<i>S</i>-(<i>S</i>-allyl)-<i>N</i>-Cyanosulfilimine, Is Antimicrobial and Reacts with Glutathione. | 2020 | DOI 10.3390/antiox9111086 | PMID 33158268 | https://pubmed.ncbi.nlm.nih.gov/33158268/ | https://pmc.ncbi.nlm.nih.gov/articles/PMC7694261/ | https://doi.org/10.3390/antiox9111086

source_locator

Reviewed reference lines 49-49; exact primary location described in quoted passage where extracted.

trigger_kind

machinery_impairment Imported condition classification; unverified.

Allicin: detailed mechanisms of action (reviewed 5 October 2026) · lines 49–49

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 · Saccharomyces cerevisiae; separate gene deletions and allicin exposures compared with an analogue; Figure 3. · source_derived_draft · unverified_draft

**Redox-defense impairment.** A study comparing allicin with a sulfilimine analogue included allicin-exposed Saccharomyces cerevisiae mutants. The GLR1, ZWF1, and YAP1 perturbations connect susceptibility to glutathione recycling, NADPH supply, and stress regulation; effects depended on concentration and compound. The analogue was more potent in some low-concentration comparisons, and its results must not be copied onto allicin. TRX2 loss had a much smaller effect in this system. Human B2 deficiency, G6PD deficiency, or selenium status cannot be assigned the yeast phenotype without direct evidence. [Horn 2020](https://pmc.ncbi.nlm.nih.gov/articles/PMC7694261/)

availability_state

machinery_impairment Imported condition classification; unverified.

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_condition

Wild-type yeast at the same allicin exposure deleted · Saccharomyces cerevisiae oxidative-stress transcription factor / Yap1 Condition belongs to the full experimental contrast; do not separate a joint intervention.

experimental_condition

Wild-type yeast at the same allicin exposure present · Allicin Condition belongs to the full experimental contrast; do not separate a joint intervention.

experimental_contrast

{"intervention": "yeast-yap1 deletion with allicin", "comparator": "Wild-type yeast at the same allicin exposure", "endpoint": "Loss of yeast-yap1 increased susceptibility in the allicin arm of the yeast chemical-genetic comparison.", "effect_direction": "decrease", "combination": "joint", "conditions": [{"entity_slug": "yeast-yap1", "state": "deleted"}, {"entity_slug": "allicin", "state": "present"}]} Explicit extracted experimental comparison; source-derived draft.

experimental_model

Saccharomyces cerevisiae; separate gene deletions and allicin exposures compared with an analogue; Figure 3.

interpretation_status

Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.

limitations

Keep dose and compound distinctions: analogue effects cannot substitute for allicin. Not a human nutrient-deficiency phenotype.

plain_language

Loss of yeast-yap1 increased susceptibility in the allicin arm of the yeast chemical-genetic comparison.

primary_references

The Sulfilimine Analogue of Allicin, <i>S</i>-Allyl-<i>S</i>-(<i>S</i>-allyl)-<i>N</i>-Cyanosulfilimine, Is Antimicrobial and Reacts with Glutathione. | 2020 | DOI 10.3390/antiox9111086 | PMID 33158268 | https://pubmed.ncbi.nlm.nih.gov/33158268/ | https://pmc.ncbi.nlm.nih.gov/articles/PMC7694261/ | https://doi.org/10.3390/antiox9111086

source_locator

Reviewed reference lines 49-49; exact primary location described in quoted passage where extracted.

trigger_kind

machinery_impairment Imported condition classification; unverified.

Allicin: detailed mechanisms of action (reviewed 5 October 2026) · lines 49–49

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 · Saccharomyces cerevisiae; separate gene deletions and allicin exposures compared with an analogue; Figure 3. · source_derived_draft · unverified_draft

**Redox-defense impairment.** A study comparing allicin with a sulfilimine analogue included allicin-exposed Saccharomyces cerevisiae mutants. The GLR1, ZWF1, and YAP1 perturbations connect susceptibility to glutathione recycling, NADPH supply, and stress regulation; effects depended on concentration and compound. The analogue was more potent in some low-concentration comparisons, and its results must not be copied onto allicin. TRX2 loss had a much smaller effect in this system. Human B2 deficiency, G6PD deficiency, or selenium status cannot be assigned the yeast phenotype without direct evidence. [Horn 2020](https://pmc.ncbi.nlm.nih.gov/articles/PMC7694261/)

availability_state

machinery_impairment Imported condition classification; unverified.

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_condition

Wild-type yeast at the same allicin exposure present · Allicin Condition belongs to the full experimental contrast; do not separate a joint intervention.

experimental_condition

Wild-type yeast at the same allicin exposure deleted · Saccharomyces cerevisiae glucose-6-phosphate dehydrogenase / Zwf1 Condition belongs to the full experimental contrast; do not separate a joint intervention.

experimental_contrast

{"intervention": "yeast-zwf1 deletion with allicin", "comparator": "Wild-type yeast at the same allicin exposure", "endpoint": "Loss of yeast-zwf1 increased susceptibility in the allicin arm of the yeast chemical-genetic comparison.", "effect_direction": "decrease", "combination": "joint", "conditions": [{"entity_slug": "yeast-zwf1", "state": "deleted"}, {"entity_slug": "allicin", "state": "present"}]} Explicit extracted experimental comparison; source-derived draft.

experimental_model

Saccharomyces cerevisiae; separate gene deletions and allicin exposures compared with an analogue; Figure 3.

interpretation_status

Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.

limitations

Keep dose and compound distinctions: analogue effects cannot substitute for allicin. Not a human nutrient-deficiency phenotype.

plain_language

Loss of yeast-zwf1 increased susceptibility in the allicin arm of the yeast chemical-genetic comparison.

primary_references

The Sulfilimine Analogue of Allicin, <i>S</i>-Allyl-<i>S</i>-(<i>S</i>-allyl)-<i>N</i>-Cyanosulfilimine, Is Antimicrobial and Reacts with Glutathione. | 2020 | DOI 10.3390/antiox9111086 | PMID 33158268 | https://pubmed.ncbi.nlm.nih.gov/33158268/ | https://pmc.ncbi.nlm.nih.gov/articles/PMC7694261/ | https://doi.org/10.3390/antiox9111086

source_locator

Reviewed reference lines 49-49; exact primary location described in quoted passage where extracted.

trigger_kind

machinery_impairment Imported condition classification; unverified.

Allicin: detailed mechanisms of action (reviewed 5 October 2026) · lines 49–49

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 · Saccharomyces cerevisiae; separate gene deletions and allicin exposures compared with an analogue; Figure 3. · source_derived_draft · unverified_draft

**Redox-defense impairment.** A study comparing allicin with a sulfilimine analogue included allicin-exposed Saccharomyces cerevisiae mutants. The GLR1, ZWF1, and YAP1 perturbations connect susceptibility to glutathione recycling, NADPH supply, and stress regulation; effects depended on concentration and compound. The analogue was more potent in some low-concentration comparisons, and its results must not be copied onto allicin. TRX2 loss had a much smaller effect in this system. Human B2 deficiency, G6PD deficiency, or selenium status cannot be assigned the yeast phenotype without direct evidence. [Horn 2020](https://pmc.ncbi.nlm.nih.gov/articles/PMC7694261/)