S-allyl-L-cysteine / SAC

acting_entity

s-allylcysteine

dose

Not specified in accessed abstract

duration

Not specified in accessed abstract

evidence_access

Primary abstract

experimental_comparison

SAC addition; pathway inhibitor comparisons

experimental_model

Free-fatty-acid-treated HepG2 cells

interpretation_status

Source-derived research curation; not independent primary verification

limitations

The accessed abstract does not resolve the ACC isoform or phosphorylation site.

nutrient_topic

S-allylcysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · S-allyl-L-cysteine / SAC

organism

Homo sapiens

plain_language

A lipid-synthesis enzyme had a separate measured modification.

primary_references

[23465592] S-allyl cysteine attenuates free fatty acid-induced lipogenesis in human HepG2 cells through activation of the AMP-activated protein kinase-dependent pathway. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23465592/ · DOI 10.1016/j.jnutbio.2012.12.006

route

Cell culture

tissue_or_cell_type

Free-fatty-acid-treated HepG2 cells

S-allylcysteine: sulfur signaling, redox responses and cross-nutrient mechanisms (2026-09-20) · lines 194–201

AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Free-fatty-acid-treated HepG2 cells · source_derived_draft · unverified_draft

## s-allylcysteine-acc A lipid-synthesis enzyme had a separate measured modification. SAC treatment increased ACC phosphorylation in HepG2 cells. Model: Free-fatty-acid-treated HepG2 cells Limitations: The accessed abstract does not resolve the ACC isoform or phosphorylation site. Evidence access: Primary abstract [23465592] S-allyl cysteine attenuates free fatty acid-induced lipogenesis in human HepG2 cells through activation of the AMP-activated protein kinase-dependent pathway. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23465592/ · DOI 10.1016/j.jnutbio.2012.12.006 Structured context: {"organism": "Homo sapiens", "tissue_or_cell_type": "Free-fatty-acid-treated HepG2 cells", "dose": "Not specified in accessed abstract", "duration": "Not specified in accessed abstract", "route": "Cell culture", "experimental_comparison": "SAC addition; pathway inhibitor comparisons", "acting_entity": "s-allylcysteine", "interpretation_status": "Source-derived research curation; not independent primary verification"}

acting_entity

s-allylcysteine

dose

Not specified in accessed abstract

duration

Not specified in accessed abstract

evidence_access

Primary abstract

experimental_comparison

SAC addition; pathway inhibitor comparisons

experimental_model

Free-fatty-acid-treated HepG2 cells

interpretation_status

Source-derived research curation; not independent primary verification

limitations

Phosphorylation does not establish direct AMPK binding.

nutrient_topic

S-allylcysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · S-allyl-L-cysteine / SAC

organism

Homo sapiens

plain_language

Energy-regulation signaling changed after exposure.

primary_references

[23465592] S-allyl cysteine attenuates free fatty acid-induced lipogenesis in human HepG2 cells through activation of the AMP-activated protein kinase-dependent pathway. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23465592/ · DOI 10.1016/j.jnutbio.2012.12.006

route

Cell culture

tissue_or_cell_type

Free-fatty-acid-treated HepG2 cells

S-allylcysteine: sulfur signaling, redox responses and cross-nutrient mechanisms (2026-09-20) · lines 185–192

AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Free-fatty-acid-treated HepG2 cells · source_derived_draft · unverified_draft

## s-allylcysteine-ampk Energy-regulation signaling changed after exposure. Adding SAC increased AMPK phosphorylation in fatty-acid-treated human HepG2 cells. Model: Free-fatty-acid-treated HepG2 cells Limitations: Phosphorylation does not establish direct AMPK binding. Evidence access: Primary abstract [23465592] S-allyl cysteine attenuates free fatty acid-induced lipogenesis in human HepG2 cells through activation of the AMP-activated protein kinase-dependent pathway. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23465592/ · DOI 10.1016/j.jnutbio.2012.12.006 Structured context: {"organism": "Homo sapiens", "tissue_or_cell_type": "Free-fatty-acid-treated HepG2 cells", "dose": "Not specified in accessed abstract", "duration": "Not specified in accessed abstract", "route": "Cell culture", "experimental_comparison": "SAC addition; pathway inhibitor comparisons", "acting_entity": "s-allylcysteine", "interpretation_status": "Source-derived research curation; not independent primary verification"}

acting_entity

s-allylcysteine

dose

Not specified in accessed abstract

duration

Not specified in accessed abstract

evidence_access

Primary abstract

experimental_comparison

Purified SAC and black garlic extract tested separately

experimental_model

Bovine aortic endothelial BAE-1 cells

interpretation_status

Source-derived research curation; not independent primary verification

limitations

Bovine cell result; phosphorylation site and human clinical effect not established by the accessed abstract.

nutrient_topic

S-allylcysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · S-allyl-L-cysteine / SAC

organism

Bos taurus

plain_language

A nitric-oxide-producing enzyme connects sulfur signaling to vascular biology.

primary_references

[37062967] Improving endothelial health with food-derived H2S donors: an in vitro study with S-allyl cysteine and with a black-garlic extract enriched in sulfur-containing compounds. · 2023 · https://pubmed.ncbi.nlm.nih.gov/37062967/ · DOI 10.1039/d3fo00412k

route

Cell culture

tissue_or_cell_type

Bovine aortic endothelial BAE-1 cells

S-allylcysteine: sulfur signaling, redox responses and cross-nutrient mechanisms (2026-09-20) · lines 275–282

AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Bovine aortic endothelial BAE-1 cells · source_derived_draft · unverified_draft

## s-allylcysteine-bovine-enos A nitric-oxide-producing enzyme connects sulfur signaling to vascular biology. SAC increased eNOS phosphorylation in BAE-1 cells. Model: Bovine aortic endothelial BAE-1 cells Limitations: Bovine cell result; phosphorylation site and human clinical effect not established by the accessed abstract. Evidence access: Primary abstract [37062967] Improving endothelial health with food-derived H2S donors: an in vitro study with S-allyl cysteine and with a black-garlic extract enriched in sulfur-containing compounds. · 2023 · https://pubmed.ncbi.nlm.nih.gov/37062967/ · DOI 10.1039/d3fo00412k Structured context: {"organism": "Bos taurus", "tissue_or_cell_type": "Bovine aortic endothelial BAE-1 cells", "dose": "Not specified in accessed abstract", "duration": "Not specified in accessed abstract", "route": "Cell culture", "experimental_comparison": "Purified SAC and black garlic extract tested separately", "acting_entity": "s-allylcysteine", "interpretation_status": "Source-derived research curation; not independent primary verification"}

acting_entity

s-allylcysteine

dose

Not specified in accessed abstract

duration

Not specified in accessed abstract

evidence_access

Primary abstract

experimental_comparison

Purified SAC and black garlic extract tested separately

experimental_model

Bovine aortic endothelial BAE-1 cells

interpretation_status

Source-derived research curation; not independent primary verification

limitations

Bovine cells; does not identify direct chemical release versus enzyme-dependent production.

nutrient_topic

S-allylcysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · S-allyl-L-cysteine / SAC

organism

Bos taurus

plain_language

Sulfur signaling was measured in another experimental system.

primary_references

[37062967] Improving endothelial health with food-derived H2S donors: an in vitro study with S-allyl cysteine and with a black-garlic extract enriched in sulfur-containing compounds. · 2023 · https://pubmed.ncbi.nlm.nih.gov/37062967/ · DOI 10.1039/d3fo00412k

route

Cell culture

tissue_or_cell_type

Bovine aortic endothelial BAE-1 cells

S-allylcysteine: sulfur signaling, redox responses and cross-nutrient mechanisms (2026-09-20) · lines 266–273

AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Bovine aortic endothelial BAE-1 cells · source_derived_draft · unverified_draft

## s-allylcysteine-bovine-h2s Sulfur signaling was measured in another experimental system. Purified SAC increased the H2S release readout in bovine aortic endothelial cells. Model: Bovine aortic endothelial BAE-1 cells Limitations: Bovine cells; does not identify direct chemical release versus enzyme-dependent production. Evidence access: Primary abstract [37062967] Improving endothelial health with food-derived H2S donors: an in vitro study with S-allyl cysteine and with a black-garlic extract enriched in sulfur-containing compounds. · 2023 · https://pubmed.ncbi.nlm.nih.gov/37062967/ · DOI 10.1039/d3fo00412k Structured context: {"organism": "Bos taurus", "tissue_or_cell_type": "Bovine aortic endothelial BAE-1 cells", "dose": "Not specified in accessed abstract", "duration": "Not specified in accessed abstract", "route": "Cell culture", "experimental_comparison": "Purified SAC and black garlic extract tested separately", "acting_entity": "s-allylcysteine", "interpretation_status": "Source-derived research curation; not independent primary verification"}

acting_entity

s-allylcysteine

dose

Not specified in accessed abstract

duration

Not specified in accessed abstract

evidence_access

Primary abstract

experimental_comparison

Purified SAC and black garlic extract tested separately

experimental_model

Bovine aortic endothelial BAE-1 cells

interpretation_status

Source-derived research curation; not independent primary verification

limitations

Not proof of lowered human blood pressure or independence from arginine and NOS cofactors.

nutrient_topic

S-allylcysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · S-allyl-L-cysteine / SAC

organism

Bos taurus

plain_language

The downstream gas signal was measured separately.

primary_references

[37062967] Improving endothelial health with food-derived H2S donors: an in vitro study with S-allyl cysteine and with a black-garlic extract enriched in sulfur-containing compounds. · 2023 · https://pubmed.ncbi.nlm.nih.gov/37062967/ · DOI 10.1039/d3fo00412k

route

Cell culture

tissue_or_cell_type

Bovine aortic endothelial BAE-1 cells

S-allylcysteine: sulfur signaling, redox responses and cross-nutrient mechanisms (2026-09-20) · lines 284–291

AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Bovine aortic endothelial BAE-1 cells · source_derived_draft · unverified_draft

## s-allylcysteine-bovine-no The downstream gas signal was measured separately. SAC increased the NO-release readout in BAE-1 cells. Model: Bovine aortic endothelial BAE-1 cells Limitations: Not proof of lowered human blood pressure or independence from arginine and NOS cofactors. Evidence access: Primary abstract [37062967] Improving endothelial health with food-derived H2S donors: an in vitro study with S-allyl cysteine and with a black-garlic extract enriched in sulfur-containing compounds. · 2023 · https://pubmed.ncbi.nlm.nih.gov/37062967/ · DOI 10.1039/d3fo00412k Structured context: {"organism": "Bos taurus", "tissue_or_cell_type": "Bovine aortic endothelial BAE-1 cells", "dose": "Not specified in accessed abstract", "duration": "Not specified in accessed abstract", "route": "Cell culture", "experimental_comparison": "Purified SAC and black garlic extract tested separately", "acting_entity": "s-allylcysteine", "interpretation_status": "Source-derived research curation; not independent primary verification"}

acting_entity

s-allylcysteine

dose

2.24, 3.37 or 4.50 mM SAC

duration

2, 4, 6, 8 or 24 hours

evidence_access

Primary abstract

experimental_comparison

SAC versus untreated cell controls

experimental_model

MCF-7 and MDA-MB-231 breast adenocarcinoma cells

interpretation_status

Source-derived research curation; not independent primary verification

limitations

Abstract does not resolve every time/dose direction; these must be retrieved before assigning a universal signed enzyme edge.

nutrient_topic

S-allylcysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · S-allyl-L-cysteine / SAC

organism

Homo sapiens

plain_language

The cellular background changed the direction of the response.

primary_references

[38397425] S-Allyl-L-Cysteine Affects Cell Proliferation and Expression of H2S-Synthetizing Enzymes in MCF-7 and MDA-MB-231 Adenocarcinoma Cell Lines. · 2024 · https://pubmed.ncbi.nlm.nih.gov/38397425/ · DOI 10.3390/biom14020188

route

Cell culture

tissue_or_cell_type

MCF-7 and MDA-MB-231 breast adenocarcinoma cells

S-allylcysteine: sulfur signaling, redox responses and cross-nutrient mechanisms (2026-09-20) · lines 302–309

AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · MCF-7 and MDA-MB-231 breast adenocarcinoma cells · source_derived_draft · unverified_draft

## s-allylcysteine-breast-cth-cbs-context The cellular background changed the direction of the response. The study reported opposite CTH and CBS expression responses between the two breast cancer cell lines. Model: MCF-7 and MDA-MB-231 breast adenocarcinoma cells Limitations: Abstract does not resolve every time/dose direction; these must be retrieved before assigning a universal signed enzyme edge. Evidence access: Primary abstract [38397425] S-Allyl-L-Cysteine Affects Cell Proliferation and Expression of H2S-Synthetizing Enzymes in MCF-7 and MDA-MB-231 Adenocarcinoma Cell Lines. · 2024 · https://pubmed.ncbi.nlm.nih.gov/38397425/ · DOI 10.3390/biom14020188 Structured context: {"organism": "Homo sapiens", "tissue_or_cell_type": "MCF-7 and MDA-MB-231 breast adenocarcinoma cells", "dose": "2.24, 3.37 or 4.50 mM SAC", "duration": "2, 4, 6, 8 or 24 hours", "route": "Cell culture", "experimental_comparison": "SAC versus untreated cell controls", "acting_entity": "s-allylcysteine", "interpretation_status": "Source-derived research curation; not independent primary verification"}

acting_entity

s-allylcysteine

dose

2.24, 3.37 or 4.50 mM SAC

duration

2, 4, 6, 8 or 24 hours

evidence_access

Primary abstract

experimental_comparison

SAC versus untreated cell controls

experimental_model

MCF-7 and MDA-MB-231 breast adenocarcinoma cells

interpretation_status

Source-derived research curation; not independent primary verification

limitations

High-millimolar cell exposure; mRNA does not establish enzyme flux or net H2S production.

nutrient_topic

S-allylcysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · S-allyl-L-cysteine / SAC

organism

Homo sapiens

plain_language

An enzyme involved in sulfur metabolism changed expression.

primary_references

[38397425] S-Allyl-L-Cysteine Affects Cell Proliferation and Expression of H2S-Synthetizing Enzymes in MCF-7 and MDA-MB-231 Adenocarcinoma Cell Lines. · 2024 · https://pubmed.ncbi.nlm.nih.gov/38397425/ · DOI 10.3390/biom14020188

route

Cell culture

tissue_or_cell_type

MCF-7 and MDA-MB-231 breast adenocarcinoma cells

S-allylcysteine: sulfur signaling, redox responses and cross-nutrient mechanisms (2026-09-20) · lines 293–300

AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · MCF-7 and MDA-MB-231 breast adenocarcinoma cells · source_derived_draft · unverified_draft

## s-allylcysteine-breast-mpst An enzyme involved in sulfur metabolism changed expression. At 4.50 mM for 24 hours, SAC increased MPST gene expression in both MCF-7 and MDA-MB-231 cells. Model: MCF-7 and MDA-MB-231 breast adenocarcinoma cells Limitations: High-millimolar cell exposure; mRNA does not establish enzyme flux or net H2S production. Evidence access: Primary abstract [38397425] S-Allyl-L-Cysteine Affects Cell Proliferation and Expression of H2S-Synthetizing Enzymes in MCF-7 and MDA-MB-231 Adenocarcinoma Cell Lines. · 2024 · https://pubmed.ncbi.nlm.nih.gov/38397425/ · DOI 10.3390/biom14020188 Structured context: {"organism": "Homo sapiens", "tissue_or_cell_type": "MCF-7 and MDA-MB-231 breast adenocarcinoma cells", "dose": "2.24, 3.37 or 4.50 mM SAC", "duration": "2, 4, 6, 8 or 24 hours", "route": "Cell culture", "experimental_comparison": "SAC versus untreated cell controls", "acting_entity": "s-allylcysteine", "interpretation_status": "Source-derived research curation; not independent primary verification"}

acting_entity

s-allylcysteine

dose

SAC 25 mg/kg; cisplatin dose not retrieved

duration

Single SAC dose for signaling arm; timing not retrieved

evidence_access

Primary abstract

experimental_comparison

SAC with cisplatin versus cisplatin injury controls

experimental_model

Cisplatin-challenged renal cortex and isolated proximal/distal tubules

interpretation_status

Source-derived research curation; not independent primary verification

limitations

Isoforms were not resolved; activity preservation does not demonstrate selenium or riboflavin repletion.

nutrient_topic

S-allylcysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · S-allyl-L-cysteine / SAC

organism

Rattus norvegicus

plain_language

Several antioxidant activities were retained during injury.

primary_references

[24779924] S-allylcysteine prevents cisplatin-induced nephrotoxicity and oxidative stress. · 2014 · https://pubmed.ncbi.nlm.nih.gov/24779924/ · DOI 10.1111/jphp.12263

route

Administration route not specified in accessed abstract

tissue_or_cell_type

Cisplatin-challenged renal cortex and isolated proximal/distal tubules

S-allylcysteine: sulfur signaling, redox responses and cross-nutrient mechanisms (2026-09-20) · lines 356–363

AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Cisplatin-challenged renal cortex and isolated proximal/distal tubules · source_derived_draft · unverified_draft

## s-allylcysteine-cisplatin-antioxidant-enzymes Several antioxidant activities were retained during injury. SAC attenuated cisplatin-associated losses of catalase, GPx and glutathione reductase activities in proximal and distal tubules. Model: Cisplatin-challenged renal cortex and isolated proximal/distal tubules Limitations: Isoforms were not resolved; activity preservation does not demonstrate selenium or riboflavin repletion. Evidence access: Primary abstract [24779924] S-allylcysteine prevents cisplatin-induced nephrotoxicity and oxidative stress. · 2014 · https://pubmed.ncbi.nlm.nih.gov/24779924/ · DOI 10.1111/jphp.12263 Structured context: {"organism": "Rattus norvegicus", "tissue_or_cell_type": "Cisplatin-challenged renal cortex and isolated proximal/distal tubules", "dose": "SAC 25 mg/kg; cisplatin dose not retrieved", "duration": "Single SAC dose for signaling arm; timing not retrieved", "route": "Administration route not specified in accessed abstract", "experimental_comparison": "SAC with cisplatin versus cisplatin injury controls", "acting_entity": "s-allylcysteine", "interpretation_status": "Source-derived research curation; not independent primary verification"}

acting_entity

s-allylcysteine

dose

SAC 25 mg/kg; cisplatin dose not retrieved

duration

Single SAC dose for signaling arm; timing not retrieved

evidence_access

Primary abstract

experimental_comparison

SAC with cisplatin versus cisplatin injury controls

experimental_model

Cisplatin-challenged renal cortex and isolated proximal/distal tubules

interpretation_status

Source-derived research curation; not independent primary verification

limitations

Expression endpoints do not establish direct inhibition of the assembled NADPH oxidase.

nutrient_topic

S-allylcysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · S-allyl-L-cysteine / SAC

organism

Rattus norvegicus

plain_language

Components of a ROS-producing system changed.

primary_references

[24779924] S-allylcysteine prevents cisplatin-induced nephrotoxicity and oxidative stress. · 2014 · https://pubmed.ncbi.nlm.nih.gov/24779924/ · DOI 10.1111/jphp.12263

route

Administration route not specified in accessed abstract

tissue_or_cell_type

Cisplatin-challenged renal cortex and isolated proximal/distal tubules

S-allylcysteine: sulfur signaling, redox responses and cross-nutrient mechanisms (2026-09-20) · lines 347–354

AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Cisplatin-challenged renal cortex and isolated proximal/distal tubules · source_derived_draft · unverified_draft

## s-allylcysteine-cisplatin-nox Components of a ROS-producing system changed. SAC attenuated cisplatin-associated increases in renal p47phox and gp91phox expression. Model: Cisplatin-challenged renal cortex and isolated proximal/distal tubules Limitations: Expression endpoints do not establish direct inhibition of the assembled NADPH oxidase. Evidence access: Primary abstract [24779924] S-allylcysteine prevents cisplatin-induced nephrotoxicity and oxidative stress. · 2014 · https://pubmed.ncbi.nlm.nih.gov/24779924/ · DOI 10.1111/jphp.12263 Structured context: {"organism": "Rattus norvegicus", "tissue_or_cell_type": "Cisplatin-challenged renal cortex and isolated proximal/distal tubules", "dose": "SAC 25 mg/kg; cisplatin dose not retrieved", "duration": "Single SAC dose for signaling arm; timing not retrieved", "route": "Administration route not specified in accessed abstract", "experimental_comparison": "SAC with cisplatin versus cisplatin injury controls", "acting_entity": "s-allylcysteine", "interpretation_status": "Source-derived research curation; not independent primary verification"}

acting_entity

s-allylcysteine

dose

SAC 25 mg/kg; cisplatin dose not retrieved

duration

Single SAC dose for signaling arm; timing not retrieved

evidence_access

Primary abstract

experimental_comparison

SAC with cisplatin versus cisplatin injury controls

experimental_model

Cisplatin-challenged renal cortex and isolated proximal/distal tubules

interpretation_status

Source-derived research curation; not independent primary verification

limitations

Renal protection does not establish preserved antitumor activity or a safe patient combination.

nutrient_topic

S-allylcysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · S-allyl-L-cysteine / SAC

organism

Rattus norvegicus

plain_language

A drug-injury model showed preservation of a defense regulator.

primary_references

[24779924] S-allylcysteine prevents cisplatin-induced nephrotoxicity and oxidative stress. · 2014 · https://pubmed.ncbi.nlm.nih.gov/24779924/ · DOI 10.1111/jphp.12263

route

Administration route not specified in accessed abstract

tissue_or_cell_type

Cisplatin-challenged renal cortex and isolated proximal/distal tubules

S-allylcysteine: sulfur signaling, redox responses and cross-nutrient mechanisms (2026-09-20) · lines 338–345

AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Cisplatin-challenged renal cortex and isolated proximal/distal tubules · source_derived_draft · unverified_draft

## s-allylcysteine-cisplatin-nrf2 A drug-injury model showed preservation of a defense regulator. SAC 25 mg/kg attenuated the cisplatin-associated reduction of renal cortical Nrf2. Model: Cisplatin-challenged renal cortex and isolated proximal/distal tubules Limitations: Renal protection does not establish preserved antitumor activity or a safe patient combination. Evidence access: Primary abstract [24779924] S-allylcysteine prevents cisplatin-induced nephrotoxicity and oxidative stress. · 2014 · https://pubmed.ncbi.nlm.nih.gov/24779924/ · DOI 10.1111/jphp.12263 Structured context: {"organism": "Rattus norvegicus", "tissue_or_cell_type": "Cisplatin-challenged renal cortex and isolated proximal/distal tubules", "dose": "SAC 25 mg/kg; cisplatin dose not retrieved", "duration": "Single SAC dose for signaling arm; timing not retrieved", "route": "Administration route not specified in accessed abstract", "experimental_comparison": "SAC with cisplatin versus cisplatin injury controls", "acting_entity": "s-allylcysteine", "interpretation_status": "Source-derived research curation; not independent primary verification"}

acting_entity

s-allylcysteine

dose

Not specified in accessed abstract

duration

Not specified in accessed abstract

evidence_access

Primary abstract

experimental_comparison

SAC with PhIP challenge and corresponding cell controls

experimental_model

Normal human colonic mucosal epithelial cells exposed to PhIP

interpretation_status

Source-derived research curation; not independent primary verification

limitations

Does not quantify a clinical drug interaction or prove reduced carcinogen activation in people.

nutrient_topic

S-allylcysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · S-allyl-L-cysteine / SAC

organism

Homo sapiens

plain_language

Carcinogen-response signaling changed alongside redox defenses.

primary_references

[35753083] S-Allylcysteine Potently Protects against PhIP-Induced DNA Damage via Nrf2/AhR Signaling Pathway Modulation in Normal Human Colonic Mucosal Epithelial Cells. · 2022 · https://pubmed.ncbi.nlm.nih.gov/35753083/ · DOI 10.1002/mnfr.202101141

route

Cell culture

tissue_or_cell_type

Normal human colonic mucosal epithelial cells exposed to PhIP

S-allylcysteine: sulfur signaling, redox responses and cross-nutrient mechanisms (2026-09-20) · lines 167–174

AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Normal human colonic mucosal epithelial cells exposed to PhIP · source_derived_draft · unverified_draft

## s-allylcysteine-colon-ahr Carcinogen-response signaling changed alongside redox defenses. SAC treatment reduced AhR-pathway signaling during PhIP challenge. Model: Normal human colonic mucosal epithelial cells exposed to PhIP Limitations: Does not quantify a clinical drug interaction or prove reduced carcinogen activation in people. Evidence access: Primary abstract [35753083] S-Allylcysteine Potently Protects against PhIP-Induced DNA Damage via Nrf2/AhR Signaling Pathway Modulation in Normal Human Colonic Mucosal Epithelial Cells. · 2022 · https://pubmed.ncbi.nlm.nih.gov/35753083/ · DOI 10.1002/mnfr.202101141 Structured context: {"organism": "Homo sapiens", "tissue_or_cell_type": "Normal human colonic mucosal epithelial cells exposed to PhIP", "dose": "Not specified in accessed abstract", "duration": "Not specified in accessed abstract", "route": "Cell culture", "experimental_comparison": "SAC with PhIP challenge and corresponding cell controls", "acting_entity": "s-allylcysteine", "interpretation_status": "Source-derived research curation; not independent primary verification"}

acting_entity

s-allylcysteine

dose

Not specified in accessed abstract

duration

Not specified in accessed abstract

evidence_access

Primary abstract

experimental_comparison

SAC with PhIP challenge and corresponding cell controls

experimental_model

Normal human colonic mucosal epithelial cells exposed to PhIP

interpretation_status

Source-derived research curation; not independent primary verification

limitations

The abstract proposes altered KEAP1 association and kinase signaling; causal order is not fully resolved.

nutrient_topic

S-allylcysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · S-allyl-L-cysteine / SAC

organism

Homo sapiens

plain_language

Defense signaling accompanied protection in this cell model.

primary_references

[35753083] S-Allylcysteine Potently Protects against PhIP-Induced DNA Damage via Nrf2/AhR Signaling Pathway Modulation in Normal Human Colonic Mucosal Epithelial Cells. · 2022 · https://pubmed.ncbi.nlm.nih.gov/35753083/ · DOI 10.1002/mnfr.202101141

route

Cell culture

tissue_or_cell_type

Normal human colonic mucosal epithelial cells exposed to PhIP

S-allylcysteine: sulfur signaling, redox responses and cross-nutrient mechanisms (2026-09-20) · lines 158–165

AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Normal human colonic mucosal epithelial cells exposed to PhIP · source_derived_draft · unverified_draft

## s-allylcysteine-colon-nrf2 Defense signaling accompanied protection in this cell model. SAC treatment induced Nrf2/HO-1 signaling during PhIP challenge in human colonic epithelial cells. Model: Normal human colonic mucosal epithelial cells exposed to PhIP Limitations: The abstract proposes altered KEAP1 association and kinase signaling; causal order is not fully resolved. Evidence access: Primary abstract [35753083] S-Allylcysteine Potently Protects against PhIP-Induced DNA Damage via Nrf2/AhR Signaling Pathway Modulation in Normal Human Colonic Mucosal Epithelial Cells. · 2022 · https://pubmed.ncbi.nlm.nih.gov/35753083/ · DOI 10.1002/mnfr.202101141 Structured context: {"organism": "Homo sapiens", "tissue_or_cell_type": "Normal human colonic mucosal epithelial cells exposed to PhIP", "dose": "Not specified in accessed abstract", "duration": "Not specified in accessed abstract", "route": "Cell culture", "experimental_comparison": "SAC with PhIP challenge and corresponding cell controls", "acting_entity": "s-allylcysteine", "interpretation_status": "Source-derived research curation; not independent primary verification"}

acting_entity

s-allylcysteine

dose

Not specified in accessed abstract

duration

Not specified in accessed abstract

evidence_access

Primary abstract

experimental_comparison

SAC with PhIP challenge and corresponding cell controls

experimental_model

Normal human colonic mucosal epithelial cells exposed to PhIP

interpretation_status

Source-derived research curation; not independent primary verification

limitations

The abstract describes the ratio ambiguously as GSH to GSH/GSSG; exact numerator/denominator require full-text clarification. No cysteine donation is inferred.

nutrient_topic

S-allylcysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · S-allyl-L-cysteine / SAC

organism

Homo sapiens

plain_language

The glutathione readout is retained without inventing a precursor flux.

primary_references

[35753083] S-Allylcysteine Potently Protects against PhIP-Induced DNA Damage via Nrf2/AhR Signaling Pathway Modulation in Normal Human Colonic Mucosal Epithelial Cells. · 2022 · https://pubmed.ncbi.nlm.nih.gov/35753083/ · DOI 10.1002/mnfr.202101141

route

Cell culture

tissue_or_cell_type

Normal human colonic mucosal epithelial cells exposed to PhIP

S-allylcysteine: sulfur signaling, redox responses and cross-nutrient mechanisms (2026-09-20) · lines 176–183

AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Normal human colonic mucosal epithelial cells exposed to PhIP · source_derived_draft · unverified_draft

## s-allylcysteine-colon-redox The glutathione readout is retained without inventing a precursor flux. The study reported an improved glutathione-related redox ratio with SAC during PhIP exposure. Model: Normal human colonic mucosal epithelial cells exposed to PhIP Limitations: The abstract describes the ratio ambiguously as GSH to GSH/GSSG; exact numerator/denominator require full-text clarification. No cysteine donation is inferred. Evidence access: Primary abstract [35753083] S-Allylcysteine Potently Protects against PhIP-Induced DNA Damage via Nrf2/AhR Signaling Pathway Modulation in Normal Human Colonic Mucosal Epithelial Cells. · 2022 · https://pubmed.ncbi.nlm.nih.gov/35753083/ · DOI 10.1002/mnfr.202101141 Structured context: {"organism": "Homo sapiens", "tissue_or_cell_type": "Normal human colonic mucosal epithelial cells exposed to PhIP", "dose": "Not specified in accessed abstract", "duration": "Not specified in accessed abstract", "route": "Cell culture", "experimental_comparison": "SAC with PhIP challenge and corresponding cell controls", "acting_entity": "s-allylcysteine", "interpretation_status": "Source-derived research curation; not independent primary verification"}

acting_entity

s-allylcysteine

dose

SAC 50 mg/kg/day; PAG 10 mg/kg/day

duration

Seven-day pretreatment; assessed 48 hours after infarction

evidence_access

Primary abstract

experimental_comparison

Saline, SAC, SAC plus PAG, and PAG-alone groups

experimental_model

Acute myocardial infarction; left ventricular and plasma measurements

interpretation_status

Source-derived research curation; not independent primary verification

limitations

CSE is CTH; not proof that SAC is directly cleaved to H2S or that enzyme activity increases in people.

nutrient_topic

S-allylcysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · S-allyl-L-cysteine / SAC

organism

Rattus norvegicus

plain_language

A sulfur-producing enzyme changed activity.

primary_references

[17766469] S-allylcysteine mediates cardioprotection in an acute myocardial infarction rat model via a hydrogen sulfide-mediated pathway. · 2007 · https://pubmed.ncbi.nlm.nih.gov/17766469/ · DOI 10.1152/ajpheart.00853.2007

route

Administration route not specified in accessed abstract

tissue_or_cell_type

Acute myocardial infarction; left ventricular and plasma measurements

S-allylcysteine: sulfur signaling, redox responses and cross-nutrient mechanisms (2026-09-20) · lines 239–246

AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Acute myocardial infarction; left ventricular and plasma measurements · source_derived_draft · unverified_draft

## s-allylcysteine-cth-activity A sulfur-producing enzyme changed activity. SAC pretreatment increased left ventricular CSE activity in infarcted rats from 1.23 to 2.75 micromol/g protein/hour. Model: Acute myocardial infarction; left ventricular and plasma measurements Limitations: CSE is CTH; not proof that SAC is directly cleaved to H2S or that enzyme activity increases in people. Evidence access: Primary abstract [17766469] S-allylcysteine mediates cardioprotection in an acute myocardial infarction rat model via a hydrogen sulfide-mediated pathway. · 2007 · https://pubmed.ncbi.nlm.nih.gov/17766469/ · DOI 10.1152/ajpheart.00853.2007 Structured context: {"organism": "Rattus norvegicus", "tissue_or_cell_type": "Acute myocardial infarction; left ventricular and plasma measurements", "dose": "SAC 50 mg/kg/day; PAG 10 mg/kg/day", "duration": "Seven-day pretreatment; assessed 48 hours after infarction", "route": "Administration route not specified in accessed abstract", "experimental_comparison": "Saline, SAC, SAC plus PAG, and PAG-alone groups", "acting_entity": "s-allylcysteine", "interpretation_status": "Source-derived research curation; not independent primary verification"}

acting_entity

s-allylcysteine

dose

SAC 0.01–1 mM; N-acetyl-SAC 1 mM

duration

Probe-specific incubation

evidence_access

Primary full-text HTML, methods/results

experimental_comparison

Test compound versus probe reaction without compound

experimental_model

Pooled human liver microsomes; probe substrate metabolism

interpretation_status

Source-derived research curation; not independent primary verification

limitations

Microsomal assay; not a clinical interaction or induction study.

nutrient_topic

S-allylcysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · S-allyl-L-cysteine / SAC

organism

Human liver preparation

plain_language

A negative enzyme-interaction result is retained.

primary_references

[27725449] Evaluation of the Effects of S-Allyl-L-cysteine, S-Methyl-L-cysteine, trans-S-1-Propenyl-L-cysteine, and Their N-Acetylated and S-Oxidized Metabolites on Human CYP Activities. · 2016 · https://pubmed.ncbi.nlm.nih.gov/27725449/ · DOI 10.1248/bpb.b16-00449

route

In vitro

tissue_or_cell_type

Pooled human liver microsomes; probe substrate metabolism

S-allylcysteine: sulfur signaling, redox responses and cross-nutrient mechanisms (2026-09-20) · lines 383–390

AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Pooled human liver microsomes; probe substrate metabolism · source_derived_draft · unverified_draft

## s-allylcysteine-cyp-null-cyp1a2 A negative enzyme-interaction result is retained. SAC showed little effect on tested human CYP1A2 activity over 0.01–1 mM. Model: Pooled human liver microsomes; probe substrate metabolism Limitations: Microsomal assay; not a clinical interaction or induction study. Evidence access: Primary full-text HTML, methods/results [27725449] Evaluation of the Effects of S-Allyl-L-cysteine, S-Methyl-L-cysteine, trans-S-1-Propenyl-L-cysteine, and Their N-Acetylated and S-Oxidized Metabolites on Human CYP Activities. · 2016 · https://pubmed.ncbi.nlm.nih.gov/27725449/ · DOI 10.1248/bpb.b16-00449 Structured context: {"organism": "Human liver preparation", "tissue_or_cell_type": "Pooled human liver microsomes; probe substrate metabolism", "dose": "SAC 0.01–1 mM; N-acetyl-SAC 1 mM", "duration": "Probe-specific incubation", "route": "In vitro", "experimental_comparison": "Test compound versus probe reaction without compound", "acting_entity": "s-allylcysteine", "interpretation_status": "Source-derived research curation; not independent primary verification"}

acting_entity

s-allylcysteine

dose

SAC 0.01–1 mM; N-acetyl-SAC 1 mM

duration

Probe-specific incubation

evidence_access

Primary full-text HTML, methods/results

experimental_comparison

Test compound versus probe reaction without compound

experimental_model

Pooled human liver microsomes; probe substrate metabolism

interpretation_status

Source-derived research curation; not independent primary verification

limitations

Microsomal assay; not a clinical interaction or induction study.

nutrient_topic

S-allylcysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · S-allyl-L-cysteine / SAC

organism

Human liver preparation

plain_language

A negative enzyme-interaction result is retained.

primary_references

[27725449] Evaluation of the Effects of S-Allyl-L-cysteine, S-Methyl-L-cysteine, trans-S-1-Propenyl-L-cysteine, and Their N-Acetylated and S-Oxidized Metabolites on Human CYP Activities. · 2016 · https://pubmed.ncbi.nlm.nih.gov/27725449/ · DOI 10.1248/bpb.b16-00449

route

In vitro

tissue_or_cell_type

Pooled human liver microsomes; probe substrate metabolism

S-allylcysteine: sulfur signaling, redox responses and cross-nutrient mechanisms (2026-09-20) · lines 401–408

AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Pooled human liver microsomes; probe substrate metabolism · source_derived_draft · unverified_draft

## s-allylcysteine-cyp-null-cyp2c19 A negative enzyme-interaction result is retained. SAC showed little effect on tested human CYP2C19 activity over 0.01–1 mM. Model: Pooled human liver microsomes; probe substrate metabolism Limitations: Microsomal assay; not a clinical interaction or induction study. Evidence access: Primary full-text HTML, methods/results [27725449] Evaluation of the Effects of S-Allyl-L-cysteine, S-Methyl-L-cysteine, trans-S-1-Propenyl-L-cysteine, and Their N-Acetylated and S-Oxidized Metabolites on Human CYP Activities. · 2016 · https://pubmed.ncbi.nlm.nih.gov/27725449/ · DOI 10.1248/bpb.b16-00449 Structured context: {"organism": "Human liver preparation", "tissue_or_cell_type": "Pooled human liver microsomes; probe substrate metabolism", "dose": "SAC 0.01–1 mM; N-acetyl-SAC 1 mM", "duration": "Probe-specific incubation", "route": "In vitro", "experimental_comparison": "Test compound versus probe reaction without compound", "acting_entity": "s-allylcysteine", "interpretation_status": "Source-derived research curation; not independent primary verification"}

acting_entity

s-allylcysteine

dose

SAC 0.01–1 mM; N-acetyl-SAC 1 mM

duration

Probe-specific incubation

evidence_access

Primary full-text HTML, methods/results

experimental_comparison

Test compound versus probe reaction without compound

experimental_model

Pooled human liver microsomes; probe substrate metabolism

interpretation_status

Source-derived research curation; not independent primary verification

limitations

Microsomal assay; not a clinical interaction or induction study.

nutrient_topic

S-allylcysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · S-allyl-L-cysteine / SAC

organism

Human liver preparation

plain_language

A negative enzyme-interaction result is retained.

primary_references

[27725449] Evaluation of the Effects of S-Allyl-L-cysteine, S-Methyl-L-cysteine, trans-S-1-Propenyl-L-cysteine, and Their N-Acetylated and S-Oxidized Metabolites on Human CYP Activities. · 2016 · https://pubmed.ncbi.nlm.nih.gov/27725449/ · DOI 10.1248/bpb.b16-00449

route

In vitro

tissue_or_cell_type

Pooled human liver microsomes; probe substrate metabolism

S-allylcysteine: sulfur signaling, redox responses and cross-nutrient mechanisms (2026-09-20) · lines 392–399

AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Pooled human liver microsomes; probe substrate metabolism · source_derived_draft · unverified_draft

## s-allylcysteine-cyp-null-cyp2c9 A negative enzyme-interaction result is retained. SAC showed little effect on tested human CYP2C9 activity over 0.01–1 mM. Model: Pooled human liver microsomes; probe substrate metabolism Limitations: Microsomal assay; not a clinical interaction or induction study. Evidence access: Primary full-text HTML, methods/results [27725449] Evaluation of the Effects of S-Allyl-L-cysteine, S-Methyl-L-cysteine, trans-S-1-Propenyl-L-cysteine, and Their N-Acetylated and S-Oxidized Metabolites on Human CYP Activities. · 2016 · https://pubmed.ncbi.nlm.nih.gov/27725449/ · DOI 10.1248/bpb.b16-00449 Structured context: {"organism": "Human liver preparation", "tissue_or_cell_type": "Pooled human liver microsomes; probe substrate metabolism", "dose": "SAC 0.01–1 mM; N-acetyl-SAC 1 mM", "duration": "Probe-specific incubation", "route": "In vitro", "experimental_comparison": "Test compound versus probe reaction without compound", "acting_entity": "s-allylcysteine", "interpretation_status": "Source-derived research curation; not independent primary verification"}

acting_entity

s-allylcysteine

dose

SAC 0.01–1 mM; N-acetyl-SAC 1 mM

duration

Probe-specific incubation

evidence_access

Primary full-text HTML, methods/results

experimental_comparison

Test compound versus probe reaction without compound

experimental_model

Pooled human liver microsomes; probe substrate metabolism

interpretation_status

Source-derived research curation; not independent primary verification

limitations

Microsomal assay; not a clinical interaction or induction study.

nutrient_topic

S-allylcysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · S-allyl-L-cysteine / SAC

organism

Human liver preparation

plain_language

A negative enzyme-interaction result is retained.

primary_references

[27725449] Evaluation of the Effects of S-Allyl-L-cysteine, S-Methyl-L-cysteine, trans-S-1-Propenyl-L-cysteine, and Their N-Acetylated and S-Oxidized Metabolites on Human CYP Activities. · 2016 · https://pubmed.ncbi.nlm.nih.gov/27725449/ · DOI 10.1248/bpb.b16-00449

route

In vitro

tissue_or_cell_type

Pooled human liver microsomes; probe substrate metabolism

S-allylcysteine: sulfur signaling, redox responses and cross-nutrient mechanisms (2026-09-20) · lines 410–417

AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Pooled human liver microsomes; probe substrate metabolism · source_derived_draft · unverified_draft

## s-allylcysteine-cyp-null-cyp2d6 A negative enzyme-interaction result is retained. SAC showed little effect on tested human CYP2D6 activity over 0.01–1 mM. Model: Pooled human liver microsomes; probe substrate metabolism Limitations: Microsomal assay; not a clinical interaction or induction study. Evidence access: Primary full-text HTML, methods/results [27725449] Evaluation of the Effects of S-Allyl-L-cysteine, S-Methyl-L-cysteine, trans-S-1-Propenyl-L-cysteine, and Their N-Acetylated and S-Oxidized Metabolites on Human CYP Activities. · 2016 · https://pubmed.ncbi.nlm.nih.gov/27725449/ · DOI 10.1248/bpb.b16-00449 Structured context: {"organism": "Human liver preparation", "tissue_or_cell_type": "Pooled human liver microsomes; probe substrate metabolism", "dose": "SAC 0.01–1 mM; N-acetyl-SAC 1 mM", "duration": "Probe-specific incubation", "route": "In vitro", "experimental_comparison": "Test compound versus probe reaction without compound", "acting_entity": "s-allylcysteine", "interpretation_status": "Source-derived research curation; not independent primary verification"}

acting_entity

s-allylcysteine

dose

SAC 0.01–1 mM; N-acetyl-SAC 1 mM

duration

Probe-specific incubation

evidence_access

Primary full-text HTML, methods/results

experimental_comparison

Test compound versus probe reaction without compound

experimental_model

Pooled human liver microsomes; probe substrate metabolism

interpretation_status

Source-derived research curation; not independent primary verification

limitations

Microsomal assay; not a clinical interaction or induction study.

nutrient_topic

S-allylcysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · S-allyl-L-cysteine / SAC

organism

Human liver preparation

plain_language

A negative enzyme-interaction result is retained.

primary_references

[27725449] Evaluation of the Effects of S-Allyl-L-cysteine, S-Methyl-L-cysteine, trans-S-1-Propenyl-L-cysteine, and Their N-Acetylated and S-Oxidized Metabolites on Human CYP Activities. · 2016 · https://pubmed.ncbi.nlm.nih.gov/27725449/ · DOI 10.1248/bpb.b16-00449

route

In vitro

tissue_or_cell_type

Pooled human liver microsomes; probe substrate metabolism

S-allylcysteine: sulfur signaling, redox responses and cross-nutrient mechanisms (2026-09-20) · lines 419–426

AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Pooled human liver microsomes; probe substrate metabolism · source_derived_draft · unverified_draft

## s-allylcysteine-cyp-null-cyp3a4 A negative enzyme-interaction result is retained. SAC showed little effect on tested human CYP3A4 activity over 0.01–1 mM. Model: Pooled human liver microsomes; probe substrate metabolism Limitations: Microsomal assay; not a clinical interaction or induction study. Evidence access: Primary full-text HTML, methods/results [27725449] Evaluation of the Effects of S-Allyl-L-cysteine, S-Methyl-L-cysteine, trans-S-1-Propenyl-L-cysteine, and Their N-Acetylated and S-Oxidized Metabolites on Human CYP Activities. · 2016 · https://pubmed.ncbi.nlm.nih.gov/27725449/ · DOI 10.1248/bpb.b16-00449 Structured context: {"organism": "Human liver preparation", "tissue_or_cell_type": "Pooled human liver microsomes; probe substrate metabolism", "dose": "SAC 0.01–1 mM; N-acetyl-SAC 1 mM", "duration": "Probe-specific incubation", "route": "In vitro", "experimental_comparison": "Test compound versus probe reaction without compound", "acting_entity": "s-allylcysteine", "interpretation_status": "Source-derived research curation; not independent primary verification"}

acting_entity

s-allylcysteine

dose

Not specified in accessed abstract

duration

Not specified in accessed abstract

evidence_access

Primary abstract

experimental_comparison

SAC in metal-binding and oxidative challenge assays

experimental_model

Ferrozine, electrochemistry and rat brain homogenate

interpretation_status

Source-derived research curation; not independent primary verification

limitations

No binding constant or dietary iron-absorption effect was available from the accessed abstract.

nutrient_topic

S-allylcysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · S-allyl-L-cysteine / SAC

organism

Cell-free assays and rat brain preparation

plain_language

Iron binding is distinct from radical scavenging.

primary_references

[18422331] Antioxidant and iron-binding properties of curcumin, capsaicin, and S-allylcysteine reduce oxidative stress in rat brain homogenate. · 2008 · https://pubmed.ncbi.nlm.nih.gov/18422331/ · DOI 10.1021/jf0734931

route

In vitro

tissue_or_cell_type

Ferrozine, electrochemistry and rat brain homogenate

S-allylcysteine: sulfur signaling, redox responses and cross-nutrient mechanisms (2026-09-20) · lines 113–120

AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Ferrozine, electrochemistry and rat brain homogenate · source_derived_draft · unverified_draft

## s-allylcysteine-iron-ii-binding Iron binding is distinct from radical scavenging. Ferrozine competition supported SAC binding of Fe2+ in a chemical assay. Model: Ferrozine, electrochemistry and rat brain homogenate Limitations: No binding constant or dietary iron-absorption effect was available from the accessed abstract. Evidence access: Primary abstract [18422331] Antioxidant and iron-binding properties of curcumin, capsaicin, and S-allylcysteine reduce oxidative stress in rat brain homogenate. · 2008 · https://pubmed.ncbi.nlm.nih.gov/18422331/ · DOI 10.1021/jf0734931 Structured context: {"organism": "Cell-free assays and rat brain preparation", "tissue_or_cell_type": "Ferrozine, electrochemistry and rat brain homogenate", "dose": "Not specified in accessed abstract", "duration": "Not specified in accessed abstract", "route": "In vitro", "experimental_comparison": "SAC in metal-binding and oxidative challenge assays", "acting_entity": "s-allylcysteine", "interpretation_status": "Source-derived research curation; not independent primary verification"}

acting_entity

s-allylcysteine

dose

Not specified in accessed abstract

duration

Not specified in accessed abstract

evidence_access

Primary abstract

experimental_comparison

SAC in metal-binding and oxidative challenge assays

experimental_model

Ferrozine, electrochemistry and rat brain homogenate

interpretation_status

Source-derived research curation; not independent primary verification

limitations

Does not establish iron depletion, removal from human tissues or treatment of iron overload.

nutrient_topic

S-allylcysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · S-allyl-L-cysteine / SAC

organism

Cell-free assays and rat brain preparation

plain_language

A second oxidation state was examined.

primary_references

[18422331] Antioxidant and iron-binding properties of curcumin, capsaicin, and S-allylcysteine reduce oxidative stress in rat brain homogenate. · 2008 · https://pubmed.ncbi.nlm.nih.gov/18422331/ · DOI 10.1021/jf0734931

route

In vitro

tissue_or_cell_type

Ferrozine, electrochemistry and rat brain homogenate

S-allylcysteine: sulfur signaling, redox responses and cross-nutrient mechanisms (2026-09-20) · lines 122–129

AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Ferrozine, electrochemistry and rat brain homogenate · source_derived_draft · unverified_draft

## s-allylcysteine-iron-iii-binding A second oxidation state was examined. Electrochemical measurements supported SAC binding of Fe3+; rat-brain assays also showed reduced iron-associated lipid peroxidation. Model: Ferrozine, electrochemistry and rat brain homogenate Limitations: Does not establish iron depletion, removal from human tissues or treatment of iron overload. Evidence access: Primary abstract [18422331] Antioxidant and iron-binding properties of curcumin, capsaicin, and S-allylcysteine reduce oxidative stress in rat brain homogenate. · 2008 · https://pubmed.ncbi.nlm.nih.gov/18422331/ · DOI 10.1021/jf0734931 Structured context: {"organism": "Cell-free assays and rat brain preparation", "tissue_or_cell_type": "Ferrozine, electrochemistry and rat brain homogenate", "dose": "Not specified in accessed abstract", "duration": "Not specified in accessed abstract", "route": "In vitro", "experimental_comparison": "SAC in metal-binding and oxidative challenge assays", "acting_entity": "s-allylcysteine", "interpretation_status": "Source-derived research curation; not independent primary verification"}

acting_entity

s-allylcysteine

dose

Not specified in accessed abstract

duration

Not specified in accessed abstract

evidence_access

Primary abstract

experimental_comparison

SAC with PhIP challenge and corresponding cell controls

experimental_model

Normal human colonic mucosal epithelial cells exposed to PhIP

interpretation_status

Source-derived research curation; not independent primary verification

limitations

Thermal stabilization does not alone identify a binding site, affinity, covalent adduct or purified-protein mechanism.

nutrient_topic

S-allylcysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · S-allyl-L-cysteine / SAC

organism

Homo sapiens

plain_language

A target-engagement assay gives a more direct molecular lead.

primary_references

[35753083] S-Allylcysteine Potently Protects against PhIP-Induced DNA Damage via Nrf2/AhR Signaling Pathway Modulation in Normal Human Colonic Mucosal Epithelial Cells. · 2022 · https://pubmed.ncbi.nlm.nih.gov/35753083/ · DOI 10.1002/mnfr.202101141

route

Cell culture

tissue_or_cell_type

Normal human colonic mucosal epithelial cells exposed to PhIP

S-allylcysteine: sulfur signaling, redox responses and cross-nutrient mechanisms (2026-09-20) · lines 149–156

AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Normal human colonic mucosal epithelial cells exposed to PhIP · source_derived_draft · unverified_draft

## s-allylcysteine-keap1-cetsa A target-engagement assay gives a more direct molecular lead. A cellular thermal-shift assay supported engagement of KEAP1 by SAC in human colonic epithelial cells. Model: Normal human colonic mucosal epithelial cells exposed to PhIP Limitations: Thermal stabilization does not alone identify a binding site, affinity, covalent adduct or purified-protein mechanism. Evidence access: Primary abstract [35753083] S-Allylcysteine Potently Protects against PhIP-Induced DNA Damage via Nrf2/AhR Signaling Pathway Modulation in Normal Human Colonic Mucosal Epithelial Cells. · 2022 · https://pubmed.ncbi.nlm.nih.gov/35753083/ · DOI 10.1002/mnfr.202101141 Structured context: {"organism": "Homo sapiens", "tissue_or_cell_type": "Normal human colonic mucosal epithelial cells exposed to PhIP", "dose": "Not specified in accessed abstract", "duration": "Not specified in accessed abstract", "route": "Cell culture", "experimental_comparison": "SAC with PhIP challenge and corresponding cell controls", "acting_entity": "s-allylcysteine", "interpretation_status": "Source-derived research curation; not independent primary verification"}

acting_entity

s-allylcysteine

dose

10 or 20 mM SAC; mechanistic endpoints 20 mM

duration

24, 48 or 72 hours; mechanistic endpoints 72 hours

evidence_access

Primary abstract

experimental_comparison

SAC; BEAS-2B and A549 comparator cell lines also studied

experimental_model

HCC827 and NCI-H1975 lung cancer cells

interpretation_status

Source-derived research curation; not independent primary verification

limitations

A cell-death endpoint is not a demonstrated cancer treatment in humans.

nutrient_topic

S-allylcysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · S-allyl-L-cysteine / SAC

organism

Homo sapiens

plain_language

Cell death was measured alongside signaling changes.

primary_references

[33136700] S-allylcysteine induces cytotoxic effects in two human lung cancer cell lines via induction of oxidative damage, downregulation of Nrf2 and NF-κB, and apoptosis. · 2021 · https://pubmed.ncbi.nlm.nih.gov/33136700/ · DOI 10.1097/CAD.0000000000001015

route

Cell culture

tissue_or_cell_type

HCC827 and NCI-H1975 lung cancer cells

S-allylcysteine: sulfur signaling, redox responses and cross-nutrient mechanisms (2026-09-20) · lines 329–336

AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · HCC827 and NCI-H1975 lung cancer cells · source_derived_draft · unverified_draft

## s-allylcysteine-lung-apoptosis Cell death was measured alongside signaling changes. SAC at 20 mM for 72 hours increased apoptosis in the tested lung cancer cells. Model: HCC827 and NCI-H1975 lung cancer cells Limitations: A cell-death endpoint is not a demonstrated cancer treatment in humans. Evidence access: Primary abstract [33136700] S-allylcysteine induces cytotoxic effects in two human lung cancer cell lines via induction of oxidative damage, downregulation of Nrf2 and NF-κB, and apoptosis. · 2021 · https://pubmed.ncbi.nlm.nih.gov/33136700/ · DOI 10.1097/CAD.0000000000001015 Structured context: {"organism": "Homo sapiens", "tissue_or_cell_type": "HCC827 and NCI-H1975 lung cancer cells", "dose": "10 or 20 mM SAC; mechanistic endpoints 20 mM", "duration": "24, 48 or 72 hours; mechanistic endpoints 72 hours", "route": "Cell culture", "experimental_comparison": "SAC; BEAS-2B and A549 comparator cell lines also studied", "acting_entity": "s-allylcysteine", "interpretation_status": "Source-derived research curation; not independent primary verification"}

acting_entity

s-allylcysteine

dose

10 or 20 mM SAC; mechanistic endpoints 20 mM

duration

24, 48 or 72 hours; mechanistic endpoints 72 hours

evidence_access

Primary abstract

experimental_comparison

SAC; BEAS-2B and A549 comparator cell lines also studied

experimental_model

HCC827 and NCI-H1975 lung cancer cells

interpretation_status

Source-derived research curation; not independent primary verification

limitations

Very high concentration in malignant cells; not a contradiction of lower-exposure or different-tissue observations.

nutrient_topic

S-allylcysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · S-allyl-L-cysteine / SAC

organism

Homo sapiens

plain_language

A different model showed the opposite Nrf2 response.

primary_references

[33136700] S-allylcysteine induces cytotoxic effects in two human lung cancer cell lines via induction of oxidative damage, downregulation of Nrf2 and NF-κB, and apoptosis. · 2021 · https://pubmed.ncbi.nlm.nih.gov/33136700/ · DOI 10.1097/CAD.0000000000001015

route

Cell culture

tissue_or_cell_type

HCC827 and NCI-H1975 lung cancer cells

S-allylcysteine: sulfur signaling, redox responses and cross-nutrient mechanisms (2026-09-20) · lines 311–318

AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · HCC827 and NCI-H1975 lung cancer cells · source_derived_draft · unverified_draft

## s-allylcysteine-lung-nrf2 A different model showed the opposite Nrf2 response. SAC at 20 mM for 72 hours reduced Nrf2 protein in HCC827 and NCI-H1975 lung cancer cells. Model: HCC827 and NCI-H1975 lung cancer cells Limitations: Very high concentration in malignant cells; not a contradiction of lower-exposure or different-tissue observations. Evidence access: Primary abstract [33136700] S-allylcysteine induces cytotoxic effects in two human lung cancer cell lines via induction of oxidative damage, downregulation of Nrf2 and NF-κB, and apoptosis. · 2021 · https://pubmed.ncbi.nlm.nih.gov/33136700/ · DOI 10.1097/CAD.0000000000001015 Structured context: {"organism": "Homo sapiens", "tissue_or_cell_type": "HCC827 and NCI-H1975 lung cancer cells", "dose": "10 or 20 mM SAC; mechanistic endpoints 20 mM", "duration": "24, 48 or 72 hours; mechanistic endpoints 72 hours", "route": "Cell culture", "experimental_comparison": "SAC; BEAS-2B and A549 comparator cell lines also studied", "acting_entity": "s-allylcysteine", "interpretation_status": "Source-derived research curation; not independent primary verification"}

acting_entity

s-allylcysteine

dose

10 or 20 mM SAC; mechanistic endpoints 20 mM

duration

24, 48 or 72 hours; mechanistic endpoints 72 hours

evidence_access

Primary abstract

experimental_comparison

SAC; BEAS-2B and A549 comparator cell lines also studied

experimental_model

HCC827 and NCI-H1975 lung cancer cells

interpretation_status

Source-derived research curation; not independent primary verification

limitations

Does not establish that usual dietary exposure produces this tissue concentration.

nutrient_topic

S-allylcysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · S-allyl-L-cysteine / SAC

organism

Homo sapiens

plain_language

Oxidative injury increased under this exposure.

primary_references

[33136700] S-allylcysteine induces cytotoxic effects in two human lung cancer cell lines via induction of oxidative damage, downregulation of Nrf2 and NF-κB, and apoptosis. · 2021 · https://pubmed.ncbi.nlm.nih.gov/33136700/ · DOI 10.1097/CAD.0000000000001015

route

Cell culture

tissue_or_cell_type

HCC827 and NCI-H1975 lung cancer cells

S-allylcysteine: sulfur signaling, redox responses and cross-nutrient mechanisms (2026-09-20) · lines 320–327

AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · HCC827 and NCI-H1975 lung cancer cells · source_derived_draft · unverified_draft

## s-allylcysteine-lung-oxidative-injury Oxidative injury increased under this exposure. SAC at 20 mM for 72 hours increased lipid oxidative damage in both tested lung cancer lines. Model: HCC827 and NCI-H1975 lung cancer cells Limitations: Does not establish that usual dietary exposure produces this tissue concentration. Evidence access: Primary abstract [33136700] S-allylcysteine induces cytotoxic effects in two human lung cancer cell lines via induction of oxidative damage, downregulation of Nrf2 and NF-κB, and apoptosis. · 2021 · https://pubmed.ncbi.nlm.nih.gov/33136700/ · DOI 10.1097/CAD.0000000000001015 Structured context: {"organism": "Homo sapiens", "tissue_or_cell_type": "HCC827 and NCI-H1975 lung cancer cells", "dose": "10 or 20 mM SAC; mechanistic endpoints 20 mM", "duration": "24, 48 or 72 hours; mechanistic endpoints 72 hours", "route": "Cell culture", "experimental_comparison": "SAC; BEAS-2B and A549 comparator cell lines also studied", "acting_entity": "s-allylcysteine", "interpretation_status": "Source-derived research curation; not independent primary verification"}

acting_entity

s-allylcysteine

availability_state

nutrient_deficiency Imported condition classification; unverified.

dose

SAC 1 g/L drinking water

duration

Seven weeks

evidence_access

Primary abstract

experimental_comparison

SAC or S-ethylcysteine separately with deficient diet versus diet controls

experimental_model

Methionine/choline-deficient diet; liver and serum measurements

interpretation_status

Source-derived research curation; not independent primary verification

limitations

Does not establish replacement of methionine or choline, or direct donation of cysteine to GSH.

nutrient_topic

S-allylcysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · S-allyl-L-cysteine / SAC

organism

Mus musculus

plain_language

A nutrient-deficiency model connects SAC to glutathione status.

primary_references

[18786595] Alleviative effects of s-allyl cysteine and s-ethyl cysteine on MCD diet-induced hepatotoxicity in mice. · 2008 · https://pubmed.ncbi.nlm.nih.gov/18786595/ · DOI 10.1016/j.fct.2008.08.010

route

Oral drinking water

tissue_or_cell_type

Methionine/choline-deficient diet; liver and serum measurements

trigger_kind

nutrient_deficiency Imported condition classification; unverified.

S-allylcysteine: sulfur signaling, redox responses and cross-nutrient mechanisms (2026-09-20) · lines 365–372

AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Methionine/choline-deficient diet; liver and serum measurements · source_derived_draft · unverified_draft

## s-allylcysteine-mcd-glutathione A nutrient-deficiency model connects SAC to glutathione status. SAC in drinking water increased serum and hepatic GSH during methionine/choline-deficient feeding. Model: Methionine/choline-deficient diet; liver and serum measurements Limitations: Does not establish replacement of methionine or choline, or direct donation of cysteine to GSH. Evidence access: Primary abstract [18786595] Alleviative effects of s-allyl cysteine and s-ethyl cysteine on MCD diet-induced hepatotoxicity in mice. · 2008 · https://pubmed.ncbi.nlm.nih.gov/18786595/ · DOI 10.1016/j.fct.2008.08.010 Structured context: {"organism": "Mus musculus", "tissue_or_cell_type": "Methionine/choline-deficient diet; liver and serum measurements", "dose": "SAC 1 g/L drinking water", "duration": "Seven weeks", "route": "Oral drinking water", "experimental_comparison": "SAC or S-ethylcysteine separately with deficient diet versus diet controls", "acting_entity": "s-allylcysteine", "interpretation_status": "Source-derived research curation; not independent primary verification"}

acting_entity

s-allylcysteine

availability_state

nutrient_deficiency Imported condition classification; unverified.

dose

SAC 1 g/L drinking water

duration

Seven weeks

evidence_access

Primary abstract

experimental_comparison

SAC or S-ethylcysteine separately with deficient diet versus diet controls

experimental_model

Methionine/choline-deficient diet; liver and serum measurements

interpretation_status

Source-derived research curation; not independent primary verification

limitations

Model-specific enzyme activities; not evidence of direct G6PDH binding or a universal NADPH effect.

nutrient_topic

S-allylcysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · S-allyl-L-cysteine / SAC

organism

Mus musculus

plain_language

The response involved lipid metabolism as well as redox markers.

primary_references

[18786595] Alleviative effects of s-allyl cysteine and s-ethyl cysteine on MCD diet-induced hepatotoxicity in mice. · 2008 · https://pubmed.ncbi.nlm.nih.gov/18786595/ · DOI 10.1016/j.fct.2008.08.010

route

Oral drinking water

tissue_or_cell_type

Methionine/choline-deficient diet; liver and serum measurements

trigger_kind

nutrient_deficiency Imported condition classification; unverified.

S-allylcysteine: sulfur signaling, redox responses and cross-nutrient mechanisms (2026-09-20) · lines 374–381

AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Methionine/choline-deficient diet; liver and serum measurements · source_derived_draft · unverified_draft

## s-allylcysteine-mcd-lipogenesis The response involved lipid metabolism as well as redox markers. SAC reduced hepatic G6PDH and FAS activities and triglyceride accumulation during the deficient diet. Model: Methionine/choline-deficient diet; liver and serum measurements Limitations: Model-specific enzyme activities; not evidence of direct G6PDH binding or a universal NADPH effect. Evidence access: Primary abstract [18786595] Alleviative effects of s-allyl cysteine and s-ethyl cysteine on MCD diet-induced hepatotoxicity in mice. · 2008 · https://pubmed.ncbi.nlm.nih.gov/18786595/ · DOI 10.1016/j.fct.2008.08.010 Structured context: {"organism": "Mus musculus", "tissue_or_cell_type": "Methionine/choline-deficient diet; liver and serum measurements", "dose": "SAC 1 g/L drinking water", "duration": "Seven weeks", "route": "Oral drinking water", "experimental_comparison": "SAC or S-ethylcysteine separately with deficient diet versus diet controls", "acting_entity": "s-allylcysteine", "interpretation_status": "Source-derived research curation; not independent primary verification"}

acting_entity

s-allylcysteine

dose

Not specified in accessed abstract

duration

Not specified in accessed abstract

evidence_access

Primary abstract

experimental_comparison

SAC versus ischemic control; wild-type versus Nrf2 knockout

experimental_model

Middle cerebral artery occlusion in wild-type and Nrf2 knockout mice

interpretation_status

Source-derived research curation; not independent primary verification

limitations

No direct binding site or therapeutic human exposure is established by these experiments.

nutrient_topic

S-allylcysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · S-allyl-L-cysteine / SAC

organism

Mus musculus

plain_language

A cellular defense response changed after treatment.

primary_references

[25393425] S-allyl cysteine activates the Nrf2-dependent antioxidant response and protects neurons against ischemic injury in vitro and in vivo. · 2015 · https://pubmed.ncbi.nlm.nih.gov/25393425/ · DOI 10.1111/jnc.12986

route

Systemic administration; precise route not retrieved

tissue_or_cell_type

Middle cerebral artery occlusion in wild-type and Nrf2 knockout mice

S-allylcysteine: sulfur signaling, redox responses and cross-nutrient mechanisms (2026-09-20) · lines 131–138

AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Middle cerebral artery occlusion in wild-type and Nrf2 knockout mice · source_derived_draft · unverified_draft

## s-allylcysteine-mouse-nrf2 A cellular defense response changed after treatment. SAC administration increased Nrf2 protein and antioxidant-response signaling in the mouse ischemia study. Model: Middle cerebral artery occlusion in wild-type and Nrf2 knockout mice Limitations: No direct binding site or therapeutic human exposure is established by these experiments. Evidence access: Primary abstract [25393425] S-allyl cysteine activates the Nrf2-dependent antioxidant response and protects neurons against ischemic injury in vitro and in vivo. · 2015 · https://pubmed.ncbi.nlm.nih.gov/25393425/ · DOI 10.1111/jnc.12986 Structured context: {"organism": "Mus musculus", "tissue_or_cell_type": "Middle cerebral artery occlusion in wild-type and Nrf2 knockout mice", "dose": "Not specified in accessed abstract", "duration": "Not specified in accessed abstract", "route": "Systemic administration; precise route not retrieved", "experimental_comparison": "SAC versus ischemic control; wild-type versus Nrf2 knockout", "acting_entity": "s-allylcysteine", "interpretation_status": "Source-derived research curation; not independent primary verification"}

acting_entity

s-allylcysteine

dose

Rats 5 mg/kg; dogs 2 mg/kg

duration

Single administration

evidence_access

Primary abstract

experimental_comparison

Purified SAC or N-acetyl-SAC; corresponding pharmacokinetic comparisons

experimental_model

Oral/i.v. pharmacokinetics; liver and kidney S9 experiments

interpretation_status

Source-derived research curation; not independent primary verification

limitations

The specific acetyltransferase was not identified in the accessed abstract; do not assign a human enzyme.

nutrient_topic

S-allylcysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · S-allyl-L-cysteine / SAC

organism

Rat and dog

plain_language

Liver and kidney preparations modified the parent compound.

primary_references

[25681129] Metabolism, excretion, and pharmacokinetics of S-allyl-L-cysteine in rats and dogs. · 2015 · https://pubmed.ncbi.nlm.nih.gov/25681129/ · DOI 10.1124/dmd.115.063230

route

Oral or intravenous; S9 incubation separately

tissue_or_cell_type

Oral/i.v. pharmacokinetics; liver and kidney S9 experiments

S-allylcysteine: sulfur signaling, redox responses and cross-nutrient mechanisms (2026-09-20) · lines 14–21

AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Oral/i.v. pharmacokinetics; liver and kidney S9 experiments · source_derived_draft · unverified_draft

## s-allylcysteine-n-acetylation Liver and kidney preparations modified the parent compound. Rat and dog liver/kidney S9 fractions converted SAC to N-acetyl-SAC. Model: Oral/i.v. pharmacokinetics; liver and kidney S9 experiments Limitations: The specific acetyltransferase was not identified in the accessed abstract; do not assign a human enzyme. Evidence access: Primary abstract [25681129] Metabolism, excretion, and pharmacokinetics of S-allyl-L-cysteine in rats and dogs. · 2015 · https://pubmed.ncbi.nlm.nih.gov/25681129/ · DOI 10.1124/dmd.115.063230 Structured context: {"organism": "Rat and dog", "tissue_or_cell_type": "Oral/i.v. pharmacokinetics; liver and kidney S9 experiments", "dose": "Rats 5 mg/kg; dogs 2 mg/kg", "duration": "Single administration", "route": "Oral or intravenous; S9 incubation separately", "experimental_comparison": "Purified SAC or N-acetyl-SAC; corresponding pharmacokinetic comparisons", "acting_entity": "s-allylcysteine", "interpretation_status": "Source-derived research curation; not independent primary verification"}

acting_entity

s-allylcysteine

dose

SAC 50 mg/kg/day; PAG 10 mg/kg/day

duration

Seven-day pretreatment; assessed 48 hours after infarction

evidence_access

Primary abstract

experimental_comparison

Saline, SAC, SAC plus PAG, and PAG-alone groups

experimental_model

Acute myocardial infarction; left ventricular and plasma measurements

interpretation_status

Source-derived research curation; not independent primary verification

limitations

Historical sulfide assay result; exact chemical species and analytical selectivity require full-text assessment.

nutrient_topic

S-allylcysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · S-allyl-L-cysteine / SAC

organism

Rattus norvegicus

plain_language

The sulfur signal had its own measured endpoint.

primary_references

[17766469] S-allylcysteine mediates cardioprotection in an acute myocardial infarction rat model via a hydrogen sulfide-mediated pathway. · 2007 · https://pubmed.ncbi.nlm.nih.gov/17766469/ · DOI 10.1152/ajpheart.00853.2007

route

Administration route not specified in accessed abstract

tissue_or_cell_type

Acute myocardial infarction; left ventricular and plasma measurements

S-allylcysteine: sulfur signaling, redox responses and cross-nutrient mechanisms (2026-09-20) · lines 248–255

AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Acute myocardial infarction; left ventricular and plasma measurements · source_derived_draft · unverified_draft

## s-allylcysteine-rat-h2s The sulfur signal had its own measured endpoint. SAC-treated infarcted rats had higher measured plasma H2S than controls and SAC-plus-PAG rats. Model: Acute myocardial infarction; left ventricular and plasma measurements Limitations: Historical sulfide assay result; exact chemical species and analytical selectivity require full-text assessment. Evidence access: Primary abstract [17766469] S-allylcysteine mediates cardioprotection in an acute myocardial infarction rat model via a hydrogen sulfide-mediated pathway. · 2007 · https://pubmed.ncbi.nlm.nih.gov/17766469/ · DOI 10.1152/ajpheart.00853.2007 Structured context: {"organism": "Rattus norvegicus", "tissue_or_cell_type": "Acute myocardial infarction; left ventricular and plasma measurements", "dose": "SAC 50 mg/kg/day; PAG 10 mg/kg/day", "duration": "Seven-day pretreatment; assessed 48 hours after infarction", "route": "Administration route not specified in accessed abstract", "experimental_comparison": "Saline, SAC, SAC plus PAG, and PAG-alone groups", "acting_entity": "s-allylcysteine", "interpretation_status": "Source-derived research curation; not independent primary verification"}

acting_entity

s-allylcysteine

dose

Rats 5 mg/kg; dogs 2 mg/kg

duration

Single administration

evidence_access

Primary abstract

experimental_comparison

Purified SAC or N-acetyl-SAC; corresponding pharmacokinetic comparisons

experimental_model

Oral/i.v. pharmacokinetics; liver and kidney S9 experiments

interpretation_status

Source-derived research curation; not independent primary verification

limitations

Animal oral bioavailability exceeded 90%; dog half-life was about 12 hours. These are not human kinetic estimates.

nutrient_topic

S-allylcysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · S-allyl-L-cysteine / SAC

organism

Rat and dog

plain_language

Kidney handling helps explain persistence in blood.

primary_references

[25681129] Metabolism, excretion, and pharmacokinetics of S-allyl-L-cysteine in rats and dogs. · 2015 · https://pubmed.ncbi.nlm.nih.gov/25681129/ · DOI 10.1124/dmd.115.063230

route

Oral or intravenous; S9 incubation separately

tissue_or_cell_type

Oral/i.v. pharmacokinetics; liver and kidney S9 experiments

S-allylcysteine: sulfur signaling, redox responses and cross-nutrient mechanisms (2026-09-20) · lines 41–48

AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Oral/i.v. pharmacokinetics; liver and kidney S9 experiments · source_derived_draft · unverified_draft

## s-allylcysteine-renal-reabsorption Kidney handling helps explain persistence in blood. Very low renal clearance of SAC, below 0.01 L/h/kg, supported extensive reabsorption in rats and dogs. Model: Oral/i.v. pharmacokinetics; liver and kidney S9 experiments Limitations: Animal oral bioavailability exceeded 90%; dog half-life was about 12 hours. These are not human kinetic estimates. Evidence access: Primary abstract [25681129] Metabolism, excretion, and pharmacokinetics of S-allyl-L-cysteine in rats and dogs. · 2015 · https://pubmed.ncbi.nlm.nih.gov/25681129/ · DOI 10.1124/dmd.115.063230 Structured context: {"organism": "Rat and dog", "tissue_or_cell_type": "Oral/i.v. pharmacokinetics; liver and kidney S9 experiments", "dose": "Rats 5 mg/kg; dogs 2 mg/kg", "duration": "Single administration", "route": "Oral or intravenous; S9 incubation separately", "experimental_comparison": "Purified SAC or N-acetyl-SAC; corresponding pharmacokinetic comparisons", "acting_entity": "s-allylcysteine", "interpretation_status": "Source-derived research curation; not independent primary verification"}

acting_entity

s-allylcysteine

dose

Rats 5 mg/kg; dogs 2 mg/kg

duration

Single administration

evidence_access

Primary abstract

experimental_comparison

Purified SAC or N-acetyl-SAC; corresponding pharmacokinetic comparisons

experimental_model

Oral/i.v. pharmacokinetics; liver and kidney S9 experiments

interpretation_status

Source-derived research curation; not independent primary verification

limitations

Sulfoxide stereochemistry and responsible enzyme were not resolved in the accessed abstract.

nutrient_topic

S-allylcysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · S-allyl-L-cysteine / SAC

organism

Rat and dog

plain_language

Oxidation creates another chemically distinct species.

primary_references

[25681129] Metabolism, excretion, and pharmacokinetics of S-allyl-L-cysteine in rats and dogs. · 2015 · https://pubmed.ncbi.nlm.nih.gov/25681129/ · DOI 10.1124/dmd.115.063230

route

Oral or intravenous; S9 incubation separately

tissue_or_cell_type

Oral/i.v. pharmacokinetics; liver and kidney S9 experiments

S-allylcysteine: sulfur signaling, redox responses and cross-nutrient mechanisms (2026-09-20) · lines 32–39

AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Oral/i.v. pharmacokinetics; liver and kidney S9 experiments · source_derived_draft · unverified_draft

## s-allylcysteine-s-oxidation Oxidation creates another chemically distinct species. SAC sulfoxide was identified among metabolites after SAC administration to rats and dogs. Model: Oral/i.v. pharmacokinetics; liver and kidney S9 experiments Limitations: Sulfoxide stereochemistry and responsible enzyme were not resolved in the accessed abstract. Evidence access: Primary abstract [25681129] Metabolism, excretion, and pharmacokinetics of S-allyl-L-cysteine in rats and dogs. · 2015 · https://pubmed.ncbi.nlm.nih.gov/25681129/ · DOI 10.1124/dmd.115.063230 Structured context: {"organism": "Rat and dog", "tissue_or_cell_type": "Oral/i.v. pharmacokinetics; liver and kidney S9 experiments", "dose": "Rats 5 mg/kg; dogs 2 mg/kg", "duration": "Single administration", "route": "Oral or intravenous; S9 incubation separately", "experimental_comparison": "Purified SAC or N-acetyl-SAC; corresponding pharmacokinetic comparisons", "acting_entity": "s-allylcysteine", "interpretation_status": "Source-derived research curation; not independent primary verification"}

acting_entity

s-allylcysteine

dose

Assay-specific millimolar IC50 values

duration

Not specified in accessed abstract

evidence_access

Primary abstract

experimental_comparison

SAC concentration series versus corresponding reference scavengers

experimental_model

Reactive-species scavenging systems

interpretation_status

Source-derived research curation; not independent primary verification

limitations

Assay potency is not an achieved human tissue concentration.

nutrient_topic

S-allylcysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · S-allyl-L-cysteine / SAC

organism

Cell-free chemical assays

plain_language

Direct chemistry has a measured concentration requirement.

primary_references

[17576034] S-allylcysteine scavenges singlet oxygen and hypochlorous acid and protects LLC-PK(1) cells of potassium dichromate-induced toxicity. · 2007 · https://pubmed.ncbi.nlm.nih.gov/17576034/ · DOI 10.1016/j.fct.2007.05.002

route

In vitro

tissue_or_cell_type

Reactive-species scavenging systems

S-allylcysteine: sulfur signaling, redox responses and cross-nutrient mechanisms (2026-09-20) · lines 95–102

AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Reactive-species scavenging systems · source_derived_draft · unverified_draft

## s-allylcysteine-scavenging-hocl Direct chemistry has a measured concentration requirement. SAC scavenged hypochlorous acid / hocl in the tested chemical system; IC50 was 2.86 mM. Model: Reactive-species scavenging systems Limitations: Assay potency is not an achieved human tissue concentration. Evidence access: Primary abstract [17576034] S-allylcysteine scavenges singlet oxygen and hypochlorous acid and protects LLC-PK(1) cells of potassium dichromate-induced toxicity. · 2007 · https://pubmed.ncbi.nlm.nih.gov/17576034/ · DOI 10.1016/j.fct.2007.05.002 Structured context: {"organism": "Cell-free chemical assays", "tissue_or_cell_type": "Reactive-species scavenging systems", "dose": "Assay-specific millimolar IC50 values", "duration": "Not specified in accessed abstract", "route": "In vitro", "experimental_comparison": "SAC concentration series versus corresponding reference scavengers", "acting_entity": "s-allylcysteine", "interpretation_status": "Source-derived research curation; not independent primary verification"}

acting_entity

s-allylcysteine

dose

Assay-specific millimolar IC50 values

duration

Not specified in accessed abstract

evidence_access

Primary abstract

experimental_comparison

SAC concentration series versus corresponding reference scavengers

experimental_model

Reactive-species scavenging systems

interpretation_status

Source-derived research curation; not independent primary verification

limitations

Assay potency is not an achieved human tissue concentration.

nutrient_topic

S-allylcysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · S-allyl-L-cysteine / SAC

organism

Cell-free chemical assays

plain_language

Direct chemistry has a measured concentration requirement.

primary_references

[17576034] S-allylcysteine scavenges singlet oxygen and hypochlorous acid and protects LLC-PK(1) cells of potassium dichromate-induced toxicity. · 2007 · https://pubmed.ncbi.nlm.nih.gov/17576034/ · DOI 10.1016/j.fct.2007.05.002

route

In vitro

tissue_or_cell_type

Reactive-species scavenging systems

S-allylcysteine: sulfur signaling, redox responses and cross-nutrient mechanisms (2026-09-20) · lines 77–84

AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Reactive-species scavenging systems · source_derived_draft · unverified_draft

## s-allylcysteine-scavenging-hydroxyl Direct chemistry has a measured concentration requirement. SAC scavenged hydroxyl radical in the tested chemical system; IC50 was 0.68 mM. Model: Reactive-species scavenging systems Limitations: Assay potency is not an achieved human tissue concentration. Evidence access: Primary abstract [17576034] S-allylcysteine scavenges singlet oxygen and hypochlorous acid and protects LLC-PK(1) cells of potassium dichromate-induced toxicity. · 2007 · https://pubmed.ncbi.nlm.nih.gov/17576034/ · DOI 10.1016/j.fct.2007.05.002 Structured context: {"organism": "Cell-free chemical assays", "tissue_or_cell_type": "Reactive-species scavenging systems", "dose": "Assay-specific millimolar IC50 values", "duration": "Not specified in accessed abstract", "route": "In vitro", "experimental_comparison": "SAC concentration series versus corresponding reference scavengers", "acting_entity": "s-allylcysteine", "interpretation_status": "Source-derived research curation; not independent primary verification"}

acting_entity

s-allylcysteine

dose

Assay-specific millimolar IC50 values

duration

Not specified in accessed abstract

evidence_access

Primary abstract

experimental_comparison

SAC concentration series versus corresponding reference scavengers

experimental_model

Reactive-species scavenging systems

interpretation_status

Source-derived research curation; not independent primary verification

limitations

Assay potency is not an achieved human tissue concentration.

nutrient_topic

S-allylcysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · S-allyl-L-cysteine / SAC

organism

Cell-free chemical assays

plain_language

Direct chemistry has a measured concentration requirement.

primary_references

[17576034] S-allylcysteine scavenges singlet oxygen and hypochlorous acid and protects LLC-PK(1) cells of potassium dichromate-induced toxicity. · 2007 · https://pubmed.ncbi.nlm.nih.gov/17576034/ · DOI 10.1016/j.fct.2007.05.002

route

In vitro

tissue_or_cell_type

Reactive-species scavenging systems

S-allylcysteine: sulfur signaling, redox responses and cross-nutrient mechanisms (2026-09-20) · lines 68–75

AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Reactive-species scavenging systems · source_derived_draft · unverified_draft

## s-allylcysteine-scavenging-peroxide Direct chemistry has a measured concentration requirement. SAC scavenged hydrogen peroxide in the tested chemical system; IC50 was 68 mM. Model: Reactive-species scavenging systems Limitations: Assay potency is not an achieved human tissue concentration. Evidence access: Primary abstract [17576034] S-allylcysteine scavenges singlet oxygen and hypochlorous acid and protects LLC-PK(1) cells of potassium dichromate-induced toxicity. · 2007 · https://pubmed.ncbi.nlm.nih.gov/17576034/ · DOI 10.1016/j.fct.2007.05.002 Structured context: {"organism": "Cell-free chemical assays", "tissue_or_cell_type": "Reactive-species scavenging systems", "dose": "Assay-specific millimolar IC50 values", "duration": "Not specified in accessed abstract", "route": "In vitro", "experimental_comparison": "SAC concentration series versus corresponding reference scavengers", "acting_entity": "s-allylcysteine", "interpretation_status": "Source-derived research curation; not independent primary verification"}

acting_entity

s-allylcysteine

dose

Assay-specific millimolar IC50 values

duration

Not specified in accessed abstract

evidence_access

Primary abstract

experimental_comparison

SAC concentration series versus corresponding reference scavengers

experimental_model

Reactive-species scavenging systems

interpretation_status

Source-derived research curation; not independent primary verification

limitations

Assay potency is not an achieved human tissue concentration.

nutrient_topic

S-allylcysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · S-allyl-L-cysteine / SAC

organism

Cell-free chemical assays

plain_language

Direct chemistry has a measured concentration requirement.

primary_references

[17576034] S-allylcysteine scavenges singlet oxygen and hypochlorous acid and protects LLC-PK(1) cells of potassium dichromate-induced toxicity. · 2007 · https://pubmed.ncbi.nlm.nih.gov/17576034/ · DOI 10.1016/j.fct.2007.05.002

route

In vitro

tissue_or_cell_type

Reactive-species scavenging systems

S-allylcysteine: sulfur signaling, redox responses and cross-nutrient mechanisms (2026-09-20) · lines 104–111

AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Reactive-species scavenging systems · source_derived_draft · unverified_draft

## s-allylcysteine-scavenging-peroxynitrite Direct chemistry has a measured concentration requirement. SAC scavenged peroxynitrite anion in the tested chemical system; IC50 was 0.80 mM. Model: Reactive-species scavenging systems Limitations: Assay potency is not an achieved human tissue concentration. Evidence access: Primary abstract [17576034] S-allylcysteine scavenges singlet oxygen and hypochlorous acid and protects LLC-PK(1) cells of potassium dichromate-induced toxicity. · 2007 · https://pubmed.ncbi.nlm.nih.gov/17576034/ · DOI 10.1016/j.fct.2007.05.002 Structured context: {"organism": "Cell-free chemical assays", "tissue_or_cell_type": "Reactive-species scavenging systems", "dose": "Assay-specific millimolar IC50 values", "duration": "Not specified in accessed abstract", "route": "In vitro", "experimental_comparison": "SAC concentration series versus corresponding reference scavengers", "acting_entity": "s-allylcysteine", "interpretation_status": "Source-derived research curation; not independent primary verification"}

acting_entity

s-allylcysteine

dose

Assay-specific millimolar IC50 values

duration

Not specified in accessed abstract

evidence_access

Primary abstract

experimental_comparison

SAC concentration series versus corresponding reference scavengers

experimental_model

Reactive-species scavenging systems

interpretation_status

Source-derived research curation; not independent primary verification

limitations

Assay potency is not an achieved human tissue concentration.

nutrient_topic

S-allylcysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · S-allyl-L-cysteine / SAC

organism

Cell-free chemical assays

plain_language

Direct chemistry has a measured concentration requirement.

primary_references

[17576034] S-allylcysteine scavenges singlet oxygen and hypochlorous acid and protects LLC-PK(1) cells of potassium dichromate-induced toxicity. · 2007 · https://pubmed.ncbi.nlm.nih.gov/17576034/ · DOI 10.1016/j.fct.2007.05.002

route

In vitro

tissue_or_cell_type

Reactive-species scavenging systems

S-allylcysteine: sulfur signaling, redox responses and cross-nutrient mechanisms (2026-09-20) · lines 86–93

AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Reactive-species scavenging systems · source_derived_draft · unverified_draft

## s-allylcysteine-scavenging-singlet Direct chemistry has a measured concentration requirement. SAC scavenged singlet molecular oxygen in the tested chemical system; IC50 was 1.93 mM. Model: Reactive-species scavenging systems Limitations: Assay potency is not an achieved human tissue concentration. Evidence access: Primary abstract [17576034] S-allylcysteine scavenges singlet oxygen and hypochlorous acid and protects LLC-PK(1) cells of potassium dichromate-induced toxicity. · 2007 · https://pubmed.ncbi.nlm.nih.gov/17576034/ · DOI 10.1016/j.fct.2007.05.002 Structured context: {"organism": "Cell-free chemical assays", "tissue_or_cell_type": "Reactive-species scavenging systems", "dose": "Assay-specific millimolar IC50 values", "duration": "Not specified in accessed abstract", "route": "In vitro", "experimental_comparison": "SAC concentration series versus corresponding reference scavengers", "acting_entity": "s-allylcysteine", "interpretation_status": "Source-derived research curation; not independent primary verification"}

acting_entity

s-allylcysteine

dose

Assay-specific millimolar IC50 values

duration

Not specified in accessed abstract

evidence_access

Primary abstract

experimental_comparison

SAC concentration series versus corresponding reference scavengers

experimental_model

Reactive-species scavenging systems

interpretation_status

Source-derived research curation; not independent primary verification

limitations

Assay potency is not an achieved human tissue concentration.

nutrient_topic

S-allylcysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · S-allyl-L-cysteine / SAC

organism

Cell-free chemical assays

plain_language

Direct chemistry has a measured concentration requirement.

primary_references

[17576034] S-allylcysteine scavenges singlet oxygen and hypochlorous acid and protects LLC-PK(1) cells of potassium dichromate-induced toxicity. · 2007 · https://pubmed.ncbi.nlm.nih.gov/17576034/ · DOI 10.1016/j.fct.2007.05.002

route

In vitro

tissue_or_cell_type

Reactive-species scavenging systems

S-allylcysteine: sulfur signaling, redox responses and cross-nutrient mechanisms (2026-09-20) · lines 59–66

AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Reactive-species scavenging systems · source_derived_draft · unverified_draft

## s-allylcysteine-scavenging-superoxide Direct chemistry has a measured concentration requirement. SAC scavenged superoxide radical anion in the tested chemical system; IC50 was 14.49 mM. Model: Reactive-species scavenging systems Limitations: Assay potency is not an achieved human tissue concentration. Evidence access: Primary abstract [17576034] S-allylcysteine scavenges singlet oxygen and hypochlorous acid and protects LLC-PK(1) cells of potassium dichromate-induced toxicity. · 2007 · https://pubmed.ncbi.nlm.nih.gov/17576034/ · DOI 10.1016/j.fct.2007.05.002 Structured context: {"organism": "Cell-free chemical assays", "tissue_or_cell_type": "Reactive-species scavenging systems", "dose": "Assay-specific millimolar IC50 values", "duration": "Not specified in accessed abstract", "route": "In vitro", "experimental_comparison": "SAC concentration series versus corresponding reference scavengers", "acting_entity": "s-allylcysteine", "interpretation_status": "Source-derived research curation; not independent primary verification"}

acting_entity

s-allylcysteine

dose

SAC IC50 110 micromolar

duration

Time-dependent inhibition; duration not retrieved

evidence_access

Primary abstract

experimental_comparison

SAC and other compounds tested individually; thiol reversal experiments

experimental_model

Purified recombinant squalene monooxygenase assay

interpretation_status

Source-derived research curation; not independent primary verification

limitations

Enzyme-assay potency does not establish inhibition at oral human exposures; not interchangeable with HMGCR inhibition.

nutrient_topic

S-allylcysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · S-allyl-L-cysteine / SAC

organism

Human recombinant protein

plain_language

A downstream cholesterol enzyme was tested directly.

primary_references

[11385050] Garlic and garlic-derived compounds inhibit human squalene monooxygenase. · 2001 · https://pubmed.ncbi.nlm.nih.gov/11385050/ · DOI 10.1093/jn/131.6.1662

route

Cell-free enzyme assay

tissue_or_cell_type

Purified recombinant squalene monooxygenase assay

S-allylcysteine: sulfur signaling, redox responses and cross-nutrient mechanisms (2026-09-20) · lines 221–228

AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Purified recombinant squalene monooxygenase assay · source_derived_draft · unverified_draft

## s-allylcysteine-sqle A downstream cholesterol enzyme was tested directly. SAC inhibited purified recombinant human squalene monooxygenase with an IC50 of 110 micromolar. Model: Purified recombinant squalene monooxygenase assay Limitations: Enzyme-assay potency does not establish inhibition at oral human exposures; not interchangeable with HMGCR inhibition. Evidence access: Primary abstract [11385050] Garlic and garlic-derived compounds inhibit human squalene monooxygenase. · 2001 · https://pubmed.ncbi.nlm.nih.gov/11385050/ · DOI 10.1093/jn/131.6.1662 Structured context: {"organism": "Human recombinant protein", "tissue_or_cell_type": "Purified recombinant squalene monooxygenase assay", "dose": "SAC IC50 110 micromolar", "duration": "Time-dependent inhibition; duration not retrieved", "route": "Cell-free enzyme assay", "experimental_comparison": "SAC and other compounds tested individually; thiol reversal experiments", "acting_entity": "s-allylcysteine", "interpretation_status": "Source-derived research curation; not independent primary verification"}

acting_entity

s-allylcysteine

dose

Not specified in accessed abstract

duration

Not specified in accessed abstract

evidence_access

Primary abstract

experimental_comparison

SAC addition; pathway inhibitor comparisons

experimental_model

Free-fatty-acid-treated HepG2 cells

interpretation_status

Source-derived research curation; not independent primary verification

limitations

SREBP-1 isoform and direct molecular target are unresolved in the accessed abstract.

nutrient_topic

S-allylcysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · S-allyl-L-cysteine / SAC

organism

Homo sapiens

plain_language

The lipid-production program changed as well as kinase activity.

primary_references

[23465592] S-allyl cysteine attenuates free fatty acid-induced lipogenesis in human HepG2 cells through activation of the AMP-activated protein kinase-dependent pathway. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23465592/ · DOI 10.1016/j.jnutbio.2012.12.006

route

Cell culture

tissue_or_cell_type

Free-fatty-acid-treated HepG2 cells

S-allylcysteine: sulfur signaling, redox responses and cross-nutrient mechanisms (2026-09-20) · lines 203–210

AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Free-fatty-acid-treated HepG2 cells · source_derived_draft · unverified_draft

## s-allylcysteine-srebp The lipid-production program changed as well as kinase activity. SAC reduced SREBP-1 levels and expression of lipogenic targets including ACC and FAS in HepG2 cells. Model: Free-fatty-acid-treated HepG2 cells Limitations: SREBP-1 isoform and direct molecular target are unresolved in the accessed abstract. Evidence access: Primary abstract [23465592] S-allyl cysteine attenuates free fatty acid-induced lipogenesis in human HepG2 cells through activation of the AMP-activated protein kinase-dependent pathway. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23465592/ · DOI 10.1016/j.jnutbio.2012.12.006 Structured context: {"organism": "Homo sapiens", "tissue_or_cell_type": "Free-fatty-acid-treated HepG2 cells", "dose": "Not specified in accessed abstract", "duration": "Not specified in accessed abstract", "route": "Cell culture", "experimental_comparison": "SAC addition; pathway inhibitor comparisons", "acting_entity": "s-allylcysteine", "interpretation_status": "Source-derived research curation; not independent primary verification"}

acting_entity

s-allylcysteine

dose

Not specified in accessed abstract

duration

Not specified in accessed abstract

evidence_access

Primary abstract

experimental_comparison

SAC addition; pathway inhibitor comparisons

experimental_model

Free-fatty-acid-treated HepG2 cells

interpretation_status

Source-derived research curation; not independent primary verification

limitations

Abstract does not specify CaMKK isoform, inhibitor selectivity or direct SIRT1 activation. No NAD or calcium depletion is demonstrated.

nutrient_topic

S-allylcysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · S-allyl-L-cysteine / SAC

organism

Homo sapiens

plain_language

Upstream pathway perturbations identify dependencies to investigate.

primary_references

[23465592] S-allyl cysteine attenuates free fatty acid-induced lipogenesis in human HepG2 cells through activation of the AMP-activated protein kinase-dependent pathway. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23465592/ · DOI 10.1016/j.jnutbio.2012.12.006

route

Cell culture

tissue_or_cell_type

Free-fatty-acid-treated HepG2 cells

S-allylcysteine: sulfur signaling, redox responses and cross-nutrient mechanisms (2026-09-20) · lines 212–219

AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Free-fatty-acid-treated HepG2 cells · source_derived_draft · unverified_draft

## s-allylcysteine-upstream-kinase Upstream pathway perturbations identify dependencies to investigate. Pharmacological inhibitor experiments implicated CaMKK and SIRT1 in SAC-associated AMPK signaling. Model: Free-fatty-acid-treated HepG2 cells Limitations: Abstract does not specify CaMKK isoform, inhibitor selectivity or direct SIRT1 activation. No NAD or calcium depletion is demonstrated. Evidence access: Primary abstract [23465592] S-allyl cysteine attenuates free fatty acid-induced lipogenesis in human HepG2 cells through activation of the AMP-activated protein kinase-dependent pathway. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23465592/ · DOI 10.1016/j.jnutbio.2012.12.006 Structured context: {"organism": "Homo sapiens", "tissue_or_cell_type": "Free-fatty-acid-treated HepG2 cells", "dose": "Not specified in accessed abstract", "duration": "Not specified in accessed abstract", "route": "Cell culture", "experimental_comparison": "SAC addition; pathway inhibitor comparisons", "acting_entity": "s-allylcysteine", "interpretation_status": "Source-derived research curation; not independent primary verification"}

acting_entity

n-acetyl-s-allylcysteine

dose

Rats 5 mg/kg; dogs 2 mg/kg

duration

Single administration

evidence_access

Primary abstract

experimental_comparison

Purified SAC or N-acetyl-SAC; corresponding pharmacokinetic comparisons

experimental_model

Oral/i.v. pharmacokinetics; liver and kidney S9 experiments

interpretation_status

Source-derived research curation; not independent primary verification

limitations

Rat/dog finding, not a quantified human recycling rate.

nutrient_topic

S-allylcysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · S-allyl-L-cysteine / SAC

organism

Rat and dog

plain_language

The measured conversion could run back toward SAC.

primary_references

[25681129] Metabolism, excretion, and pharmacokinetics of S-allyl-L-cysteine in rats and dogs. · 2015 · https://pubmed.ncbi.nlm.nih.gov/25681129/ · DOI 10.1124/dmd.115.063230

route

Oral or intravenous; S9 incubation separately

tissue_or_cell_type

Oral/i.v. pharmacokinetics; liver and kidney S9 experiments

S-allylcysteine: sulfur signaling, redox responses and cross-nutrient mechanisms (2026-09-20) · lines 23–30

AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Oral/i.v. pharmacokinetics; liver and kidney S9 experiments · source_derived_draft · unverified_draft

## s-allylcysteine-deacetylation The measured conversion could run back toward SAC. The same S9 preparations deacetylated N-acetyl-SAC; SAC also appeared in plasma after intravenous N-acetyl-SAC. Model: Oral/i.v. pharmacokinetics; liver and kidney S9 experiments Limitations: Rat/dog finding, not a quantified human recycling rate. Evidence access: Primary abstract [25681129] Metabolism, excretion, and pharmacokinetics of S-allyl-L-cysteine in rats and dogs. · 2015 · https://pubmed.ncbi.nlm.nih.gov/25681129/ · DOI 10.1124/dmd.115.063230 Structured context: {"organism": "Rat and dog", "tissue_or_cell_type": "Oral/i.v. pharmacokinetics; liver and kidney S9 experiments", "dose": "Rats 5 mg/kg; dogs 2 mg/kg", "duration": "Single administration", "route": "Oral or intravenous; S9 incubation separately", "experimental_comparison": "Purified SAC or N-acetyl-SAC; corresponding pharmacokinetic comparisons", "acting_entity": "n-acetyl-s-allylcysteine", "interpretation_status": "Source-derived research curation; not independent primary verification"}

acting_entity

n-acetyl-s-allylcysteine

dose

Calibration and source-fragmentation experiment

duration

Analytical assay

evidence_access

Primary abstract

experimental_comparison

SAC and metabolite standards with chromatographic separation

experimental_model

LC-MS/MS assay validation

interpretation_status

Source-derived research curation; not independent primary verification

limitations

Analytical artifact, not biological conversion or an increase in in-vivo SAC.

nutrient_topic

S-allylcysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · S-allyl-L-cysteine / SAC

organism

Rat plasma analytical matrix

plain_language

A metabolite can make an analytical SAC signal misleading.

primary_references

[28561204] Oral Administration of (S)-Allyl-l-Cysteine and Aged Garlic Extract to Rats: Determination of Metabolites and Their Pharmacokinetics. · 2017 · https://pubmed.ncbi.nlm.nih.gov/28561204/ · DOI 10.1055/s-0043-111895

route

Ex vivo

tissue_or_cell_type

LC-MS/MS assay validation

S-allylcysteine: sulfur signaling, redox responses and cross-nutrient mechanisms (2026-09-20) · lines 50–57

AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · LC-MS/MS assay validation · source_derived_draft · unverified_draft

## s-allylcysteine-analytical-interference A metabolite can make an analytical SAC signal misleading. N-acetyl-SAC decomposed in the detector source and interfered with SAC quantification unless chromatographic separation was used. Model: LC-MS/MS assay validation Limitations: Analytical artifact, not biological conversion or an increase in in-vivo SAC. Evidence access: Primary abstract [28561204] Oral Administration of (S)-Allyl-l-Cysteine and Aged Garlic Extract to Rats: Determination of Metabolites and Their Pharmacokinetics. · 2017 · https://pubmed.ncbi.nlm.nih.gov/28561204/ · DOI 10.1055/s-0043-111895 Structured context: {"organism": "Rat plasma analytical matrix", "tissue_or_cell_type": "LC-MS/MS assay validation", "dose": "Calibration and source-fragmentation experiment", "duration": "Analytical assay", "route": "Ex vivo", "experimental_comparison": "SAC and metabolite standards with chromatographic separation", "acting_entity": "n-acetyl-s-allylcysteine", "interpretation_status": "Source-derived research curation; not independent primary verification"}

acting_entity

optimized-aged-black-garlic-2023

dose

Optimized aged black garlic extract providing 0.25 mg SAC/day

duration

Twelve weeks

evidence_access

Primary abstract

experimental_comparison

Randomized triple-blind placebo-controlled extract trial

experimental_model

Grade I hypertensive participants receiving antihypertensive treatment

interpretation_status

Source-derived research curation; not independent primary verification

limitations

SAC-standardized extract, not purified SAC. Background antihypertensives continued; reported blood NO is a study assay endpoint.

nutrient_topic

S-allylcysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · S-allyl-L-cysteine / SAC

organism

Homo sapiens

plain_language

Human formulation evidence is available, with ingredient attribution unresolved.

primary_references

[37686723] Antihypertensive Effects of an Optimized Aged Garlic Extract in Subjects with Grade I Hypertension and Antihypertensive Drug Therapy: A Randomized, Triple-Blind Controlled Trial. · 2023 · https://pubmed.ncbi.nlm.nih.gov/37686723/ · DOI 10.3390/nu15173691

route

Oral

tissue_or_cell_type

Grade I hypertensive participants receiving antihypertensive treatment

S-allylcysteine: sulfur signaling, redox responses and cross-nutrient mechanisms (2026-09-20) · lines 437–444

AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Grade I hypertensive participants receiving antihypertensive treatment · source_derived_draft · unverified_draft

## s-allylcysteine-extract-no Human formulation evidence is available, with ingredient attribution unresolved. The randomized extract trial reported increased blood NO readout after 12 weeks. Model: Grade I hypertensive participants receiving antihypertensive treatment Limitations: SAC-standardized extract, not purified SAC. Background antihypertensives continued; reported blood NO is a study assay endpoint. Evidence access: Primary abstract [37686723] Antihypertensive Effects of an Optimized Aged Garlic Extract in Subjects with Grade I Hypertension and Antihypertensive Drug Therapy: A Randomized, Triple-Blind Controlled Trial. · 2023 · https://pubmed.ncbi.nlm.nih.gov/37686723/ · DOI 10.3390/nu15173691 Structured context: {"organism": "Homo sapiens", "tissue_or_cell_type": "Grade I hypertensive participants receiving antihypertensive treatment", "dose": "Optimized aged black garlic extract providing 0.25 mg SAC/day", "duration": "Twelve weeks", "route": "Oral", "experimental_comparison": "Randomized triple-blind placebo-controlled extract trial", "acting_entity": "optimized-aged-black-garlic-2023", "interpretation_status": "Source-derived research curation; not independent primary verification"}

acting_entity

mouse-nfe2l2

availability_state

machinery_impairment Imported condition classification; unverified.

dose

Not specified in accessed abstract

duration

Not specified in accessed abstract

evidence_access

Primary abstract

experimental_comparison

SAC versus ischemic control; wild-type versus Nrf2 knockout

experimental_model

Middle cerebral artery occlusion in wild-type and Nrf2 knockout mice

interpretation_status

Source-derived research curation; not independent primary verification

limitations

Necessity in this model; not proof that every SAC effect requires Nrf2.

nutrient_topic

S-allylcysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · S-allyl-L-cysteine / SAC

organism

Mus musculus

plain_language

Removing the pathway changed the response to SAC.

primary_references

[25393425] S-allyl cysteine activates the Nrf2-dependent antioxidant response and protects neurons against ischemic injury in vitro and in vivo. · 2015 · https://pubmed.ncbi.nlm.nih.gov/25393425/ · DOI 10.1111/jnc.12986

route

Systemic administration; precise route not retrieved

tissue_or_cell_type

Middle cerebral artery occlusion in wild-type and Nrf2 knockout mice

trigger_kind

machinery_impairment Imported condition classification; unverified.

S-allylcysteine: sulfur signaling, redox responses and cross-nutrient mechanisms (2026-09-20) · lines 140–147

AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Middle cerebral artery occlusion in wild-type and Nrf2 knockout mice · source_derived_draft · unverified_draft

## s-allylcysteine-mouse-nrf2-required Removing the pathway changed the response to SAC. Nrf2 knockout mice did not show the ischemic protection observed with systemic SAC in wild-type mice. Model: Middle cerebral artery occlusion in wild-type and Nrf2 knockout mice Limitations: Necessity in this model; not proof that every SAC effect requires Nrf2. Evidence access: Primary abstract [25393425] S-allyl cysteine activates the Nrf2-dependent antioxidant response and protects neurons against ischemic injury in vitro and in vivo. · 2015 · https://pubmed.ncbi.nlm.nih.gov/25393425/ · DOI 10.1111/jnc.12986 Structured context: {"organism": "Mus musculus", "tissue_or_cell_type": "Middle cerebral artery occlusion in wild-type and Nrf2 knockout mice", "dose": "Not specified in accessed abstract", "duration": "Not specified in accessed abstract", "route": "Systemic administration; precise route not retrieved", "experimental_comparison": "SAC versus ischemic control; wild-type versus Nrf2 knockout", "acting_entity": "mouse-nfe2l2", "interpretation_status": "Source-derived research curation; not independent primary verification"}

acting_entity

vascanox-hp-2023

dose

Vascanox HP combination; constituent doses not retrieved

duration

Four weeks

evidence_access

Primary abstract

experimental_comparison

Within-person baseline; no placebo or factorial comparison

experimental_model

Twelve participants completing an open-label combination study

interpretation_status

Source-derived research curation; not independent primary verification

limitations

No placebo or ingredient-factorial arms: cannot establish SAC contribution, nitrate contribution, interaction or synergy.

nutrient_topic

S-allylcysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · S-allyl-L-cysteine / SAC

organism

Homo sapiens

plain_language

A cross-compound human lead remains available without assigning the effect to SAC.

primary_references

[37849591] Effects of S-Allylcysteine-Rich Garlic Extract and Dietary Inorganic Nitrate Formula on Blood Pressure and Salivary Nitric Oxide: An Open-Label Clinical Trial Among Hypertensive Subjects. · 2023 · https://pubmed.ncbi.nlm.nih.gov/37849591/ · DOI 10.7759/cureus.45369

route

Oral

tissue_or_cell_type

Twelve participants completing an open-label combination study

S-allylcysteine: sulfur signaling, redox responses and cross-nutrient mechanisms (2026-09-20) · lines 455–462

AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Twelve participants completing an open-label combination study · source_derived_draft · unverified_draft

## s-allylcysteine-nitrate-combination A cross-compound human lead remains available without assigning the effect to SAC. An uncontrolled 12-person nitrate/garlic combination study reported lower systolic pressure after two weeks, persisting at four weeks. Model: Twelve participants completing an open-label combination study Limitations: No placebo or ingredient-factorial arms: cannot establish SAC contribution, nitrate contribution, interaction or synergy. Evidence access: Primary abstract [37849591] Effects of S-Allylcysteine-Rich Garlic Extract and Dietary Inorganic Nitrate Formula on Blood Pressure and Salivary Nitric Oxide: An Open-Label Clinical Trial Among Hypertensive Subjects. · 2023 · https://pubmed.ncbi.nlm.nih.gov/37849591/ · DOI 10.7759/cureus.45369 Structured context: {"organism": "Homo sapiens", "tissue_or_cell_type": "Twelve participants completing an open-label combination study", "dose": "Vascanox HP combination; constituent doses not retrieved", "duration": "Four weeks", "route": "Oral", "experimental_comparison": "Within-person baseline; no placebo or factorial comparison", "acting_entity": "vascanox-hp-2023", "interpretation_status": "Source-derived research curation; not independent primary verification"}

acting_entity

dl-propargylglycine

availability_state

machinery_impairment Imported condition classification; unverified.

dose

SAC 50 mg/kg/day; PAG 10 mg/kg/day

duration

Seven-day pretreatment; assessed 48 hours after infarction

evidence_access

Primary abstract

experimental_comparison

Saline, SAC, SAC plus PAG, and PAG-alone groups

experimental_model

Acute myocardial infarction; left ventricular and plasma measurements

interpretation_status

Source-derived research curation; not independent primary verification

limitations

Pharmacological interference, not a selective genetic proof; PAG-alone injury complicates attribution.

nutrient_topic

S-allylcysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · S-allyl-L-cysteine / SAC

organism

Rattus norvegicus

plain_language

Blocking the proposed pathway altered the outcome, with an important inhibitor control.

primary_references

[17766469] S-allylcysteine mediates cardioprotection in an acute myocardial infarction rat model via a hydrogen sulfide-mediated pathway. · 2007 · https://pubmed.ncbi.nlm.nih.gov/17766469/ · DOI 10.1152/ajpheart.00853.2007

route

Administration route not specified in accessed abstract

tissue_or_cell_type

Acute myocardial infarction; left ventricular and plasma measurements

trigger_kind

machinery_impairment Imported condition classification; unverified.

S-allylcysteine: sulfur signaling, redox responses and cross-nutrient mechanisms (2026-09-20) · lines 257–264

AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Acute myocardial infarction; left ventricular and plasma measurements · source_derived_draft · unverified_draft

## s-allylcysteine-pag-response Blocking the proposed pathway altered the outcome, with an important inhibitor control. PAG coadministration lowered the SAC-associated CSE activity and eliminated the favorable infarct-size pattern; PAG alone also worsened injury. Model: Acute myocardial infarction; left ventricular and plasma measurements Limitations: Pharmacological interference, not a selective genetic proof; PAG-alone injury complicates attribution. Evidence access: Primary abstract [17766469] S-allylcysteine mediates cardioprotection in an acute myocardial infarction rat model via a hydrogen sulfide-mediated pathway. · 2007 · https://pubmed.ncbi.nlm.nih.gov/17766469/ · DOI 10.1152/ajpheart.00853.2007 Structured context: {"organism": "Rattus norvegicus", "tissue_or_cell_type": "Acute myocardial infarction; left ventricular and plasma measurements", "dose": "SAC 50 mg/kg/day; PAG 10 mg/kg/day", "duration": "Seven-day pretreatment; assessed 48 hours after infarction", "route": "Administration route not specified in accessed abstract", "experimental_comparison": "Saline, SAC, SAC plus PAG, and PAG-alone groups", "acting_entity": "dl-propargylglycine", "interpretation_status": "Source-derived research curation; not independent primary verification"}

acting_entity

glutathione

dose

SAC IC50 110 micromolar

duration

Time-dependent inhibition; duration not retrieved

evidence_access

Primary abstract

experimental_comparison

SAC and other compounds tested individually; thiol reversal experiments

experimental_model

Purified recombinant squalene monooxygenase assay

interpretation_status

Source-derived research curation; not independent primary verification

limitations

The abstract groups several inhibitors. SAC-specific reversal magnitude and a covalent site are not separately established; dithiols were more effective than monothiols.

nutrient_topic

S-allylcysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · S-allyl-L-cysteine / SAC

organism

Human recombinant protein

plain_language

The enzyme result connects to thiol chemistry.

primary_references

[11385050] Garlic and garlic-derived compounds inhibit human squalene monooxygenase. · 2001 · https://pubmed.ncbi.nlm.nih.gov/11385050/ · DOI 10.1093/jn/131.6.1662

route

Cell-free enzyme assay

tissue_or_cell_type

Purified recombinant squalene monooxygenase assay

S-allylcysteine: sulfur signaling, redox responses and cross-nutrient mechanisms (2026-09-20) · lines 230–237

AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Purified recombinant squalene monooxygenase assay · source_derived_draft · unverified_draft

## s-allylcysteine-sqle-thiol-reversal The enzyme result connects to thiol chemistry. Thiol-containing reagents, including glutathione, prevented or reversed inhibition in the garlic-compound SQLE assay series. Model: Purified recombinant squalene monooxygenase assay Limitations: The abstract groups several inhibitors. SAC-specific reversal magnitude and a covalent site are not separately established; dithiols were more effective than monothiols. Evidence access: Primary abstract [11385050] Garlic and garlic-derived compounds inhibit human squalene monooxygenase. · 2001 · https://pubmed.ncbi.nlm.nih.gov/11385050/ · DOI 10.1093/jn/131.6.1662 Structured context: {"organism": "Human recombinant protein", "tissue_or_cell_type": "Purified recombinant squalene monooxygenase assay", "dose": "SAC IC50 110 micromolar", "duration": "Time-dependent inhibition; duration not retrieved", "route": "Cell-free enzyme assay", "experimental_comparison": "SAC and other compounds tested individually; thiol reversal experiments", "acting_entity": "glutathione", "interpretation_status": "Source-derived research curation; not independent primary verification"}