Nutrient chapter

S-allyl-L-cysteine / SAC

Context-specific entity; species, compartment and exposure are stated on each claim.

54 recorded mechanisms · 2 availability situations · 4 preserved sources. Draft and verified records are labeled separately.

Read recorded mechanisms Open recursive mind map

The mechanisms

What the sources say this nutrient does, one relationship at a time. Plain wording comes first; the technical statement follows.

Rat and dog liver/kidney S9 fractions converted SAC to N-acetyl-SAC.
S-allyl-L-cysteine / SAC → N-acetyl-S-allyl-L-cysteine source_derived_draftungraded
Experimental context and source evidence
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"}
Complete structured claim and evidence
The same S9 preparations deacetylated N-acetyl-SAC; SAC also appeared in plasma after intravenous N-acetyl-SAC.
N-acetyl-S-allyl-L-cysteine → S-allyl-L-cysteine / SAC source_derived_draftungraded
Experimental context and source evidence
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"}
Complete structured claim and evidence
SAC sulfoxide was identified among metabolites after SAC administration to rats and dogs.
S-allyl-L-cysteine / SAC → S-allyl-L-cysteine sulfoxide, stereoisomer unspecified source_derived_draftungraded
Experimental context and source evidence
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"}
Complete structured claim and evidence
Very low renal clearance of SAC, below 0.01 L/h/kg, supported extensive reabsorption in rats and dogs.
S-allyl-L-cysteine / SAC → SAC renal reabsorption in rat and dog PK studies source_derived_draftungraded
Experimental context and source evidence
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"}
Complete structured claim and evidence
N-acetyl-SAC decomposed in the detector source and interfered with SAC quantification unless chromatographic separation was used.
N-acetyl-S-allyl-L-cysteine → SAC/NAc-SAC mass-spectrometric source interference source_derived_draftungraded
Experimental context and source evidence
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"}
Complete structured claim and evidence
SAC scavenged superoxide radical anion in the tested chemical system; IC50 was 14.49 mM.
S-allyl-L-cysteine / SAC → Superoxide radical anion source_derived_draftungraded
Experimental context and source evidence
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"}
Complete structured claim and evidence
SAC scavenged hydrogen peroxide in the tested chemical system; IC50 was 68 mM.
S-allyl-L-cysteine / SAC → Hydrogen peroxide source_derived_draftungraded
Experimental context and source evidence
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"}
Complete structured claim and evidence
SAC scavenged hydroxyl radical in the tested chemical system; IC50 was 0.68 mM.
S-allyl-L-cysteine / SAC → Hydroxyl radical source_derived_draftungraded
Experimental context and source evidence
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"}
Complete structured claim and evidence
SAC scavenged singlet molecular oxygen in the tested chemical system; IC50 was 1.93 mM.
S-allyl-L-cysteine / SAC → Singlet molecular oxygen source_derived_draftungraded
Experimental context and source evidence
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"}
Complete structured claim and evidence
SAC scavenged hypochlorous acid / hocl in the tested chemical system; IC50 was 2.86 mM.
S-allyl-L-cysteine / SAC → Hypochlorous acid / HOCl source_derived_draftungraded
Experimental context and source evidence
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"}
Complete structured claim and evidence
SAC scavenged peroxynitrite anion in the tested chemical system; IC50 was 0.80 mM.
S-allyl-L-cysteine / SAC → Peroxynitrite anion source_derived_draftungraded
Experimental context and source evidence
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"}
Complete structured claim and evidence
Ferrozine competition supported SAC binding of Fe2+ in a chemical assay.
S-allyl-L-cysteine / SAC → Ferrous iron source_derived_draftungraded
Experimental context and source evidence
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"}
Complete structured claim and evidence
Electrochemical measurements supported SAC binding of Fe3+; rat-brain assays also showed reduced iron-associated lipid peroxidation.
S-allyl-L-cysteine / SAC → Ferric iron source_derived_draftungraded
Experimental context and source evidence
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"}
Complete structured claim and evidence
SAC administration increased Nrf2 protein and antioxidant-response signaling in the mouse ischemia study.
S-allyl-L-cysteine / SAC → Mouse Nrf2 / Nfe2l2 source_derived_draftungraded
Experimental context and source evidence
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"}
Complete structured claim and evidence
Nrf2 knockout mice did not show the ischemic protection observed with systemic SAC in wild-type mice.
Mouse Nrf2 / Nfe2l2 → SAC-associated protection in mouse cerebral ischemia source_derived_draftungraded
Experimental context and source evidence
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"}
Complete structured claim and evidence
A cellular thermal-shift assay supported engagement of KEAP1 by SAC in human colonic epithelial cells.
S-allyl-L-cysteine / SAC → Human KEAP1 source_derived_draftungraded
Experimental context and source evidence
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"}
Complete structured claim and evidence
SAC treatment induced Nrf2/HO-1 signaling during PhIP challenge in human colonic epithelial cells.
S-allyl-L-cysteine / SAC → Human Nrf2 / NFE2L2 source_derived_draftungraded
Experimental context and source evidence
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"}
Complete structured claim and evidence
SAC treatment reduced AhR-pathway signaling during PhIP challenge.
S-allyl-L-cysteine / SAC → Human aryl hydrocarbon receptor / AHR source_derived_draftungraded
Experimental context and source evidence
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"}
Complete structured claim and evidence
The study reported an improved glutathione-related redox ratio with SAC during PhIP exposure.
S-allyl-L-cysteine / SAC → Glutathione redox readout in SAC-treated human colonic cells source_derived_draftungraded
Experimental context and source evidence
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"}
Complete structured claim and evidence
Adding SAC increased AMPK phosphorylation in fatty-acid-treated human HepG2 cells.
S-allyl-L-cysteine / SAC → Human AMP-activated protein kinase complexes source_derived_draftungraded
Experimental context and source evidence
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"}
Complete structured claim and evidence
SAC treatment increased ACC phosphorylation in HepG2 cells.
S-allyl-L-cysteine / SAC → Human acetyl-CoA carboxylase activity, isoform unresolved in assay source_derived_draftungraded
Experimental context and source evidence
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"}
Complete structured claim and evidence
SAC reduced SREBP-1 levels and expression of lipogenic targets including ACC and FAS in HepG2 cells.
S-allyl-L-cysteine / SAC → Sterol regulatory element-binding protein 1 / SREBP-1 source_derived_draftungraded
Experimental context and source evidence
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"}
Complete structured claim and evidence
Pharmacological inhibitor experiments implicated CaMKK and SIRT1 in SAC-associated AMPK signaling.
S-allyl-L-cysteine / SAC → CaMKK/SIRT1-sensitive SAC signaling in HepG2 cells source_derived_draftungraded
Experimental context and source evidence
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"}
Complete structured claim and evidence
SAC inhibited purified recombinant human squalene monooxygenase with an IC50 of 110 micromolar.
S-allyl-L-cysteine / SAC → Human squalene monooxygenase / SQLE source_derived_draftungraded
Experimental context and source evidence
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"}
Complete structured claim and evidence
Thiol-containing reagents, including glutathione, prevented or reversed inhibition in the garlic-compound SQLE assay series.
GSH → Thiol reversal of garlic-compound SQLE inhibition source_derived_draftungraded
Experimental context and source evidence
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"}
Complete structured claim and evidence
SAC pretreatment increased left ventricular CSE activity in infarcted rats from 1.23 to 2.75 micromol/g protein/hour.
S-allyl-L-cysteine / SAC → Rat cystathionine gamma-lyase / Cth source_derived_draftungraded
Experimental context and source evidence
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"}
Complete structured claim and evidence
SAC-treated infarcted rats had higher measured plasma H2S than controls and SAC-plus-PAG rats.
S-allyl-L-cysteine / SAC → Plasma H2S readout in the SAC infarction rat study source_derived_draftungraded
Experimental context and source evidence
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"}
Complete structured claim and evidence
PAG coadministration lowered the SAC-associated CSE activity and eliminated the favorable infarct-size pattern; PAG alone also worsened injury.
DL-propargylglycine, experimental CSE inhibitor → Cardiac injury response to SAC in infarcted rats source_derived_draftungraded
Experimental context and source evidence
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"}
Complete structured claim and evidence
Purified SAC increased the H2S release readout in bovine aortic endothelial cells.
S-allyl-L-cysteine / SAC → H2S release readout in SAC-treated BAE-1 cells source_derived_draftungraded
Experimental context and source evidence
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"}
Complete structured claim and evidence
SAC increased eNOS phosphorylation in BAE-1 cells.
S-allyl-L-cysteine / SAC → Bovine endothelial nitric oxide synthase / NOS3 source_derived_draftungraded
Experimental context and source evidence
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"}
Complete structured claim and evidence
SAC increased the NO-release readout in BAE-1 cells.
S-allyl-L-cysteine / SAC → NO source_derived_draftungraded
Experimental context and source evidence
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"}
Complete structured claim and evidence
At 4.50 mM for 24 hours, SAC increased MPST gene expression in both MCF-7 and MDA-MB-231 cells.
S-allyl-L-cysteine / SAC → Human mercaptopyruvate sulfurtransferase / MPST source_derived_draftungraded
Experimental context and source evidence
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"}
Complete structured claim and evidence
The study reported opposite CTH and CBS expression responses between the two breast cancer cell lines.
S-allyl-L-cysteine / SAC → Cell-line-dependent CTH/CBS expression response to SAC source_derived_draftungraded
Experimental context and source evidence
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"}
Complete structured claim and evidence
SAC at 20 mM for 72 hours reduced Nrf2 protein in HCC827 and NCI-H1975 lung cancer cells.
S-allyl-L-cysteine / SAC → Human Nrf2 / NFE2L2 source_derived_draftungraded
Experimental context and source evidence
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"}
Complete structured claim and evidence
SAC at 20 mM for 72 hours increased lipid oxidative damage in both tested lung cancer lines.
S-allyl-L-cysteine / SAC → Lipid oxidative damage in SAC-treated lung cancer cells source_derived_draftungraded
Experimental context and source evidence
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"}
Complete structured claim and evidence
SAC at 20 mM for 72 hours increased apoptosis in the tested lung cancer cells.
S-allyl-L-cysteine / SAC → Apoptosis in SAC-treated HCC827/NCI-H1975 cells source_derived_draftungraded
Experimental context and source evidence
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"}
Complete structured claim and evidence
SAC 25 mg/kg attenuated the cisplatin-associated reduction of renal cortical Nrf2.
S-allyl-L-cysteine / SAC → Rat Nrf2 / Nfe2l2 source_derived_draftungraded
Experimental context and source evidence
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"}
Complete structured claim and evidence
SAC attenuated cisplatin-associated increases in renal p47phox and gp91phox expression.
S-allyl-L-cysteine / SAC → Rat renal p47phox/gp91phox abundance during SAC/cisplatin exposure source_derived_draftungraded
Experimental context and source evidence
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"}
Complete structured claim and evidence
SAC attenuated cisplatin-associated losses of catalase, GPx and glutathione reductase activities in proximal and distal tubules.
S-allyl-L-cysteine / SAC → Rat tubular CAT, GPx and GR activities during SAC/cisplatin exposure source_derived_draftungraded
Experimental context and source evidence
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"}
Complete structured claim and evidence
SAC in drinking water increased serum and hepatic GSH during methionine/choline-deficient feeding.
S-allyl-L-cysteine / SAC → Mouse serum/hepatic glutathione during SAC and MCD diet source_derived_draftungraded
Experimental context and source evidence
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"}
Complete structured claim and evidence
SAC reduced hepatic G6PDH and FAS activities and triglyceride accumulation during the deficient diet.
S-allyl-L-cysteine / SAC → Mouse G6PDH/FAS activity during SAC and MCD diet source_derived_draftungraded
Experimental context and source evidence
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"}
Complete structured claim and evidence
SAC showed little effect on tested human CYP1A2 activity over 0.01–1 mM.
S-allyl-L-cysteine / SAC → Human cytochrome P450 1A2 source_derived_draftungraded
Experimental context and source evidence
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"}
Complete structured claim and evidence
SAC showed little effect on tested human CYP2C9 activity over 0.01–1 mM.
S-allyl-L-cysteine / SAC → Human cytochrome P450 2C9 source_derived_draftungraded
Experimental context and source evidence
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"}
Complete structured claim and evidence
SAC showed little effect on tested human CYP2C19 activity over 0.01–1 mM.
S-allyl-L-cysteine / SAC → Human cytochrome P450 2C19 source_derived_draftungraded
Experimental context and source evidence
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"}
Complete structured claim and evidence
SAC showed little effect on tested human CYP2D6 activity over 0.01–1 mM.
S-allyl-L-cysteine / SAC → Human cytochrome P450 2D6 source_derived_draftungraded
Experimental context and source evidence
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"}
Complete structured claim and evidence
SAC showed little effect on tested human CYP3A4 activity over 0.01–1 mM.
S-allyl-L-cysteine / SAC → Human cytochrome P450 3A4 source_derived_draftungraded
Experimental context and source evidence
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"}
Complete structured claim and evidence
N-acetyl-SAC inhibited the CYP2D6 probe reaction by 19% at 1 mM.
N-acetyl-S-allyl-L-cysteine → Human cytochrome P450 2D6 source_derived_draftungraded
Experimental context and source evidence
acting_entity
n-acetyl-s-allylcysteine
dose
SAC 0.01–1 mM; N-acetyl-SAC 1 mM
duration
Probe-specific incubation
evidence_access
Primary full-text HTML, abstract/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
Small in-vitro effect; no patient interaction magnitude.
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 metabolite differed from the parent.
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 428–435
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-nac-cyp2d6 A metabolite differed from the parent. N-acetyl-SAC inhibited the CYP2D6 probe reaction by 19% at 1 mM. Model: Pooled human liver microsomes; probe substrate metabolism Limitations: Small in-vitro effect; no patient interaction magnitude. Evidence access: Primary full-text HTML, abstract/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": "n-acetyl-s-allylcysteine", "interpretation_status": "Source-derived research curation; not independent primary verification"}
Complete structured claim and evidence
The randomized extract trial reported increased blood NO readout after 12 weeks.
Optimized aged black garlic extract in the 2023 hypertension trial → Blood NO readout in the optimized aged black garlic trial source_derived_draftungraded
Experimental context and source evidence
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"}
Complete structured claim and evidence
The same trial found no change in measured endothelial function or inflammatory cytokines.
Optimized aged black garlic extract in the 2023 hypertension trial → Endothelial-function endpoint in the optimized aged black garlic trial source_derived_draftungraded
Experimental context and source evidence
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
Null endpoints coexist with other reported changes; no universal vascular improvement 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 formulation did not improve every measured endpoint.
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 446–453
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-endothelial-null The formulation did not improve every measured endpoint. The same trial found no change in measured endothelial function or inflammatory cytokines. Model: Grade I hypertensive participants receiving antihypertensive treatment Limitations: Null endpoints coexist with other reported changes; no universal vascular improvement is inferred. 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"}
Complete structured claim and evidence
An uncontrolled 12-person nitrate/garlic combination study reported lower systolic pressure after two weeks, persisting at four weeks.
Vascanox HP nitrate/garlic combination studied in 2023 → Blood-pressure readout in the 2023 Vascanox open-label study source_derived_draftungraded
Experimental context and source evidence
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"}
Complete structured claim and evidence
The human CBS catalytic core binds PLP through its active-site lysine; this site is separate from the heme-binding region.
PLP → Human cystathionine beta-synthase / CBS source_derived_draftungraded
Experimental context and source evidence
cross_nutrient
Vitamin B6 and sulfur amino-acid metabolism.
experimental_model
Recombinant truncated human CBS crystallography
limitations
The crystallized human construct lacks the C-terminal regulatory region.
nutrient_topic
Vitamin B6 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin B6
organism
Homo sapiens
plain_language
CBS uses active vitamin B6 in its catalytic site.
primary_references
[b6-cbs-2001] Structure of human cystathionine beta-synthase: a unique pyridoxal 5'-phosphate-dependent heme protein. (2001). https://pmc.ncbi.nlm.nih.gov/articles/PMC149156/ DOI: 10.1093/emboj/20.15.3910
tissue_or_cell_type
Purified recombinant protein; no intact tissue
Vitamin B6: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 505–515
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant truncated human CBS crystallography · source_derived_draft · unverified_draft
### b6-met-cbs-plp The human CBS catalytic core binds PLP through its active-site lysine; this site is separate from the heme-binding region. Condition category: normal nutrient_topic: Vitamin B6 research collection; topical membership is not evidence of a direct dietary effect. plain_language: CBS uses active vitamin B6 in its catalytic site. organism: Homo sapiens tissue_or_cell_type: Purified recombinant protein; no intact tissue experimental_model: Recombinant truncated human CBS crystallography limitations: The crystallized human construct lacks the C-terminal regulatory region. cross_nutrient: Vitamin B6 and sulfur amino-acid metabolism. [b6-cbs-2001] Structure of human cystathionine beta-synthase: a unique pyridoxal 5'-phosphate-dependent heme protein. (2001). https://pmc.ncbi.nlm.nih.gov/articles/PMC149156/ DOI: 10.1093/emboj/20.15.3910
Complete structured claim and evidence
PLP binds human CTH at Lys212 in an active site assembled from adjacent subunits.
PLP → Human cystathionine gamma-lyase / CTH source_derived_draftungraded
Experimental context and source evidence
cross_nutrient
Second PLP-dependent step of sulfur amino-acid transsulfuration.
evidence_location
Apo, PLP and PLP-PAG structural comparisons
experimental_model
Purified human CTH apo/holo crystal structures and assays
limitations
Purified-enzyme evidence does not define dietary requirements or cellular PLP thresholds.
nutrient_topic
Vitamin B6 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin B6
organism
Homo sapiens
plain_language
CTH needs an assembled B6-binding catalytic site.
primary_references
[b6-cth-structure-2009] Structural Basis for the Inhibition Mechanism of Human Cystathionine gamma-Lyase, an Enzyme Responsible for the Production of H2S (2009). https://doi.org/10.1074/jbc.M805459200 DOI: 10.1074/jbc.M805459200
tissue_or_cell_type
Purified recombinant protein; no intact tissue
Vitamin B6: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 541–552
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified human CTH apo/holo crystal structures and assays · source_derived_draft · unverified_draft
### b6-met-cth-plp PLP binds human CTH at Lys212 in an active site assembled from adjacent subunits. Condition category: normal nutrient_topic: Vitamin B6 research collection; topical membership is not evidence of a direct dietary effect. plain_language: CTH needs an assembled B6-binding catalytic site. organism: Homo sapiens tissue_or_cell_type: Purified recombinant protein; no intact tissue experimental_model: Purified human CTH apo/holo crystal structures and assays limitations: Purified-enzyme evidence does not define dietary requirements or cellular PLP thresholds. cross_nutrient: Second PLP-dependent step of sulfur amino-acid transsulfuration. evidence_location: Apo, PLP and PLP-PAG structural comparisons [b6-cth-structure-2009] Structural Basis for the Inhibition Mechanism of Human Cystathionine gamma-Lyase, an Enzyme Responsible for the Production of H2S (2009). https://doi.org/10.1074/jbc.M805459200 DOI: 10.1074/jbc.M805459200
Complete structured claim and evidence
Glutamate-cysteine ligase joins glutamate and cysteine to form gamma-glutamylcysteine in the first glutathione-synthesis step.
Human glutamate-cysteine ligase catalytic subunit / GCLC → Gamma-glutamylcysteine source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/30581542.fulltext.txt", "locator": "Primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "77cf6674cf9b9bc140a228588a53c937966fd3a67397c1c4970221c5cc58a0b1", "start_char": 762, "end_char": 1092, "text_sha256": "927fa13b085700c20b578ecabc7c8c17a66ea4600b90809e3061d12bcaea3849"}
experimental_model
Human enzyme mutagenesis, kinetics and molecular dynamics
exposure
S-loop variants; established biosynthetic reactions described in the introduction
limitations
Reaction descriptions are background chemistry in a primary enzyme paper, not evidence that sulforaphane corrects inherited GSS deficiency.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human GSS
plain_language
The induced machinery still needs its amino-acid building blocks.
primary_references
[sulforaphane-p30581542] Genetic Mutations in the S-loop of Human Glutathione Synthetase: Links Between Substrate Binding, Active Site Structure and Allostery. (2019). https://pubmed.ncbi.nlm.nih.gov/30581542/ DOI: 10.1016/j.csbj.2018.11.008
tissue_or_cell_type
Glutathione synthesis and substrate binding
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 840–851
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human enzyme mutagenesis, kinetics and molecular dynamics · source_derived_draft · unverified_draft
### sulforaphane-gcl-first-step Glutamate-cysteine ligase joins glutamate and cysteine to form gamma-glutamylcysteine in the first glutathione-synthesis step. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: The induced machinery still needs its amino-acid building blocks. organism: Human GSS tissue_or_cell_type: Glutathione synthesis and substrate binding experimental_model: Human enzyme mutagenesis, kinetics and molecular dynamics limitations: Reaction descriptions are background chemistry in a primary enzyme paper, not evidence that sulforaphane corrects inherited GSS deficiency. exposure: S-loop variants; established biosynthetic reactions described in the introduction evidence_span: {"source_cache": "artifacts/sulforaphane-research/30581542.fulltext.txt", "locator": "Primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "77cf6674cf9b9bc140a228588a53c937966fd3a67397c1c4970221c5cc58a0b1", "start_char": 762, "end_char": 1092, "text_sha256": "927fa13b085700c20b578ecabc7c8c17a66ea4600b90809e3061d12bcaea3849"} [sulforaphane-p30581542] Genetic Mutations in the S-loop of Human Glutathione Synthetase: Links Between Substrate Binding, Active Site Structure and Allostery. (2019). https://pubmed.ncbi.nlm.nih.gov/30581542/ DOI: 10.1016/j.csbj.2018.11.008
Complete structured claim and evidence
The GSR catalytic cycle transfers reducing equivalents from flavin to the Cys58-Cys63 active-site disulfide before glutathione-disulfide reduction.
FAD → Glutathione reductase / GSR source_derived_draftungraded
Experimental context and source evidence
cross_nutrient
B2-derived cofactor bridges NADPH and the glutathione system.
evidence_location
Results: NADPH binding; Fig 1 consensus cycle; GSH/GSSG complexes
experimental_model
Purified human glutathione reductase crystals with natural substrates, 0.95-1.1-A resolution, chemically reduced controls.
exposure
Purified-enzyme assay
limitations
Mechanism integrates natural-substrate structures with prior kinetic work; transient intermediates were not all directly trapped here.
nutrient_topic
Riboflavin research collection; topical membership is not evidence of a direct dietary effect. · Riboflavin (vitamin B2)
organism
Homo sapiens
plain_language
FAD relays electrons through enzyme cysteines.
primary_references
[berkholz2008] Catalytic cycle of human glutathione reductase near 1 A resolution. (2008). https://pubmed.ncbi.nlm.nih.gov/18638483/ DOI: 10.1016/j.jmb.2008.06.083
tissue_or_cell_type
Purified human GSR
Riboflavin: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 1318–1330
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified human glutathione reductase crystals with natural substrates, 0.95-1.1-A resolution, chemically reduced controls. · source_derived_draft · unverified_draft
### b2-gsr-flavin-disulfide-relay The GSR catalytic cycle transfers reducing equivalents from flavin to the Cys58-Cys63 active-site disulfide before glutathione-disulfide reduction. Condition category: normal nutrient_topic: Riboflavin research collection; topical membership is not evidence of a direct dietary effect. plain_language: FAD relays electrons through enzyme cysteines. organism: Homo sapiens tissue_or_cell_type: Purified human GSR experimental_model: Purified human glutathione reductase crystals with natural substrates, 0.95-1.1-A resolution, chemically reduced controls. limitations: Mechanism integrates natural-substrate structures with prior kinetic work; transient intermediates were not all directly trapped here. exposure: Purified-enzyme assay cross_nutrient: B2-derived cofactor bridges NADPH and the glutathione system. evidence_location: Results: NADPH binding; Fig 1 consensus cycle; GSH/GSSG complexes [berkholz2008] Catalytic cycle of human glutathione reductase near 1 A resolution. (2008). https://pubmed.ncbi.nlm.nih.gov/18638483/ DOI: 10.1016/j.jmb.2008.06.083
Complete structured claim and evidence

Availability and dependencies

Each situation shows the normal role first, then what the sources report under a specific condition. A shortfall in the diet, a fault in the machinery, and a low blood reading are kept separate because they are not the same thing.

Nrf2 removal changes the SAC ischemia response

Condition: machinery_impairment · Nrf2 knockout during experimental ischemia.

Normal role: Nrf2 organizes antioxidant-response transcription.

Recorded consequence: SAC-associated protection was absent.

Scope: Mouse cerebral ischemia.

CSE inhibitor changes SAC-associated cardiac protection

Condition: machinery_impairment · PAG alone or with SAC before infarction.

Normal role: CTH contributes to endogenous sulfur metabolism.

Recorded consequence: Enzyme activity and injury outcomes changed.

Scope: Rat myocardial infarction.

The sources

Every document behind this chapter is preserved word for word. Open one to read it in full with its recorded conflicts marked in place.

Riboflavin: mechanisms, deficiency and nutrient interactions (2026-09-17)AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · unverified_draftRead preserved source
S-allylcysteine: sulfur signaling, redox responses and cross-nutrient mechanisms (2026-09-20)AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · unverified_draftRead preserved source
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17)AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · unverified_draftRead preserved source
Vitamin B6: mechanisms, deficiency and nutrient interactions (2026-09-17)AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · unverified_draftRead preserved source

Recorded disagreements

Where two sources say different things, both are kept and the difference is explained. You can discuss a disagreement or propose a mechanism that might account for it.

Open questions in this collection

Questions the curators could not answer from the sources in front of them, kept here with the reason each one is still open. These are gaps in this collection, not findings or proof that no one has studied them.

Chapters are assembled from supplied drafts and curated literature summaries. Statements remain unverified against the primary studies, and the ledger is not medical advice.

Evidence, AI assistance and curation standards

S-allyl-L-cysteine / SAC

The mechanisms

Rat and dog liver/kidney S9 fractions converted SAC to N-acetyl-SAC.

The same S9 preparations deacetylated N-acetyl-SAC; SAC also appeared in plasma after intravenous N-acetyl-SAC.

SAC sulfoxide was identified among metabolites after SAC administration to rats and dogs.

Very low renal clearance of SAC, below 0.01 L/h/kg, supported extensive reabsorption in rats and dogs.

N-acetyl-SAC decomposed in the detector source and interfered with SAC quantification unless chromatographic separation was used.

SAC scavenged superoxide radical anion in the tested chemical system; IC50 was 14.49 mM.

SAC scavenged hydrogen peroxide in the tested chemical system; IC50 was 68 mM.

SAC scavenged hydroxyl radical in the tested chemical system; IC50 was 0.68 mM.

SAC scavenged singlet molecular oxygen in the tested chemical system; IC50 was 1.93 mM.

SAC scavenged hypochlorous acid / hocl in the tested chemical system; IC50 was 2.86 mM.

SAC scavenged peroxynitrite anion in the tested chemical system; IC50 was 0.80 mM.

Ferrozine competition supported SAC binding of Fe2+ in a chemical assay.

Electrochemical measurements supported SAC binding of Fe3+; rat-brain assays also showed reduced iron-associated lipid peroxidation.

SAC administration increased Nrf2 protein and antioxidant-response signaling in the mouse ischemia study.

Nrf2 knockout mice did not show the ischemic protection observed with systemic SAC in wild-type mice.

A cellular thermal-shift assay supported engagement of KEAP1 by SAC in human colonic epithelial cells.

SAC treatment induced Nrf2/HO-1 signaling during PhIP challenge in human colonic epithelial cells.

SAC treatment reduced AhR-pathway signaling during PhIP challenge.

The study reported an improved glutathione-related redox ratio with SAC during PhIP exposure.

Adding SAC increased AMPK phosphorylation in fatty-acid-treated human HepG2 cells.

SAC treatment increased ACC phosphorylation in HepG2 cells.

SAC reduced SREBP-1 levels and expression of lipogenic targets including ACC and FAS in HepG2 cells.

Pharmacological inhibitor experiments implicated CaMKK and SIRT1 in SAC-associated AMPK signaling.

SAC inhibited purified recombinant human squalene monooxygenase with an IC50 of 110 micromolar.

Thiol-containing reagents, including glutathione, prevented or reversed inhibition in the garlic-compound SQLE assay series.

SAC pretreatment increased left ventricular CSE activity in infarcted rats from 1.23 to 2.75 micromol/g protein/hour.

SAC-treated infarcted rats had higher measured plasma H2S than controls and SAC-plus-PAG rats.

PAG coadministration lowered the SAC-associated CSE activity and eliminated the favorable infarct-size pattern; PAG alone also worsened injury.

Purified SAC increased the H2S release readout in bovine aortic endothelial cells.

SAC increased eNOS phosphorylation in BAE-1 cells.

SAC increased the NO-release readout in BAE-1 cells.

At 4.50 mM for 24 hours, SAC increased MPST gene expression in both MCF-7 and MDA-MB-231 cells.

The study reported opposite CTH and CBS expression responses between the two breast cancer cell lines.

SAC at 20 mM for 72 hours reduced Nrf2 protein in HCC827 and NCI-H1975 lung cancer cells.

SAC at 20 mM for 72 hours increased lipid oxidative damage in both tested lung cancer lines.

SAC at 20 mM for 72 hours increased apoptosis in the tested lung cancer cells.

SAC 25 mg/kg attenuated the cisplatin-associated reduction of renal cortical Nrf2.

SAC attenuated cisplatin-associated increases in renal p47phox and gp91phox expression.

SAC attenuated cisplatin-associated losses of catalase, GPx and glutathione reductase activities in proximal and distal tubules.

SAC in drinking water increased serum and hepatic GSH during methionine/choline-deficient feeding.

SAC reduced hepatic G6PDH and FAS activities and triglyceride accumulation during the deficient diet.

SAC showed little effect on tested human CYP1A2 activity over 0.01–1 mM.

SAC showed little effect on tested human CYP2C9 activity over 0.01–1 mM.

SAC showed little effect on tested human CYP2C19 activity over 0.01–1 mM.

SAC showed little effect on tested human CYP2D6 activity over 0.01–1 mM.

SAC showed little effect on tested human CYP3A4 activity over 0.01–1 mM.

N-acetyl-SAC inhibited the CYP2D6 probe reaction by 19% at 1 mM.

The randomized extract trial reported increased blood NO readout after 12 weeks.

The same trial found no change in measured endothelial function or inflammatory cytokines.

An uncontrolled 12-person nitrate/garlic combination study reported lower systolic pressure after two weeks, persisting at four weeks.

The human CBS catalytic core binds PLP through its active-site lysine; this site is separate from the heme-binding region.

PLP binds human CTH at Lys212 in an active site assembled from adjacent subunits.

Glutamate-cysteine ligase joins glutamate and cysteine to form gamma-glutamylcysteine in the first glutathione-synthesis step.

The GSR catalytic cycle transfers reducing equivalents from flavin to the Cys58-Cys63 active-site disulfide before glutathione-disulfide reduction.

Availability and dependencies

The sources

Recorded disagreements

Open questions in this collection