Nutrient chapter

Epigallocatechin-3-gallate (EGCG)

The (-)-epigallocatechin-3-gallate compound; distinct from whole green tea, mixed extracts and its conjugated metabolites.

80 recorded mechanisms · 2 availability situations · 8 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.

Surface plasmon resonance supported nanomolar-affinity EGCG binding to 67LR; receptor expression conferred cellular responsiveness.
Epigallocatechin-3-gallate (EGCG) → 67-kDa laminin receptor state / 67LR source_derived_draftungraded
Experimental context and source evidence
experimental_model
Receptor binding and cancer-cell expression experiments.
limitations
67LR is recorded as the receptor state, not equated with all functions of the 37-kDa RPSA precursor.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
A cell-surface receptor can make cells responsive to EGCG.
primary_references
A receptor for green tea polyphenol EGCG. · 2004 · https://pubmed.ncbi.nlm.nih.gov/15024383/ · DOI 10.1038/nsmb743
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 20–26
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Receptor binding and cancer-cell expression experiments. · source_derived_draft · unverified_draft
## egcg-receptor A cell-surface receptor can make cells responsive to EGCG. Surface plasmon resonance supported nanomolar-affinity EGCG binding to 67LR; receptor expression conferred cellular responsiveness. Model: Receptor binding and cancer-cell expression experiments. Limitations: 67LR is recorded as the receptor state, not equated with all functions of the 37-kDa RPSA precursor. Evidence access: primary abstract. A receptor for green tea polyphenol EGCG. · 2004 · https://pubmed.ncbi.nlm.nih.gov/15024383/ · DOI 10.1038/nsmb743
Complete structured claim and evidence
A genetic screen identified eEF1A as a component of 67LR-dependent EGCG signaling.
67-kDa laminin receptor state / 67LR → Eukaryotic elongation factor 1A family source_derived_draftungraded
Experimental context and source evidence
experimental_model
Genetic screen, cell signaling and experimental tumor-growth models.
limitations
Pathway dependency in these models does not establish human cancer treatment or a dietary threshold.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
The surface signal depends on an intracellular relay.
primary_references
Green tea polyphenol epigallocatechin-3-gallate signaling pathway through 67-kDa laminin receptor. · 2008 · https://pubmed.ncbi.nlm.nih.gov/18079119/ · DOI 10.1074/jbc.m707892200
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 28–34
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Genetic screen, cell signaling and experimental tumor-growth models. · source_derived_draft · unverified_draft
## egcg-eef1a The surface signal depends on an intracellular relay. A genetic screen identified eEF1A as a component of 67LR-dependent EGCG signaling. Model: Genetic screen, cell signaling and experimental tumor-growth models. Limitations: Pathway dependency in these models does not establish human cancer treatment or a dietary threshold. Evidence access: primary abstract. Green tea polyphenol epigallocatechin-3-gallate signaling pathway through 67-kDa laminin receptor. · 2008 · https://pubmed.ncbi.nlm.nih.gov/18079119/ · DOI 10.1074/jbc.m707892200
Complete structured claim and evidence
EGCG dephosphorylated MYPT1 Thr696 through 67LR and eEF1A.
Epigallocatechin-3-gallate (EGCG) → MYPT1 Thr696 phosphorylation source_derived_draftungraded
Experimental context and source evidence
experimental_model
Genetic screen, cell signaling and experimental tumor-growth models.
limitations
Pathway dependency in these models does not establish human cancer treatment or a dietary threshold.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
EGCG removed an inhibitory phosphorylation mark in this pathway.
primary_references
Green tea polyphenol epigallocatechin-3-gallate signaling pathway through 67-kDa laminin receptor. · 2008 · https://pubmed.ncbi.nlm.nih.gov/18079119/ · DOI 10.1074/jbc.m707892200
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 36–42
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Genetic screen, cell signaling and experimental tumor-growth models. · source_derived_draft · unverified_draft
## egcg-mypt EGCG removed an inhibitory phosphorylation mark in this pathway. EGCG dephosphorylated MYPT1 Thr696 through 67LR and eEF1A. Model: Genetic screen, cell signaling and experimental tumor-growth models. Limitations: Pathway dependency in these models does not establish human cancer treatment or a dietary threshold. Evidence access: primary abstract. Green tea polyphenol epigallocatechin-3-gallate signaling pathway through 67-kDa laminin receptor. · 2008 · https://pubmed.ncbi.nlm.nih.gov/18079119/ · DOI 10.1074/jbc.m707892200
Complete structured claim and evidence
MYPT1 dephosphorylation accompanied activation of myosin phosphatase.
Epigallocatechin-3-gallate (EGCG) → Myosin phosphatase activity source_derived_draftungraded
Experimental context and source evidence
experimental_model
Genetic screen, cell signaling and experimental tumor-growth models.
limitations
Pathway dependency in these models does not establish human cancer treatment or a dietary threshold.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
Changing MYPT1 changed phosphatase activity.
primary_references
Green tea polyphenol epigallocatechin-3-gallate signaling pathway through 67-kDa laminin receptor. · 2008 · https://pubmed.ncbi.nlm.nih.gov/18079119/ · DOI 10.1074/jbc.m707892200
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 44–50
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Genetic screen, cell signaling and experimental tumor-growth models. · source_derived_draft · unverified_draft
## egcg-phosphatase Changing MYPT1 changed phosphatase activity. MYPT1 dephosphorylation accompanied activation of myosin phosphatase. Model: Genetic screen, cell signaling and experimental tumor-growth models. Limitations: Pathway dependency in these models does not establish human cancer treatment or a dietary threshold. Evidence access: primary abstract. Green tea polyphenol epigallocatechin-3-gallate signaling pathway through 67-kDa laminin receptor. · 2008 · https://pubmed.ncbi.nlm.nih.gov/18079119/ · DOI 10.1074/jbc.m707892200
Complete structured claim and evidence
Silencing MYPT1, eEF1A or 67LR abrogated EGCG-mediated tumor-growth inhibition in the tested models.
Myosin phosphatase targeting subunit 1 family / MYPT1 → Tumor growth in EGCG experimental models source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
experimental_model
Genetic screen, cell signaling and experimental tumor-growth models.
limitations
Pathway dependency in these models does not establish human cancer treatment or a dietary threshold.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
Removing pathway components prevented the observed response.
primary_references
Green tea polyphenol epigallocatechin-3-gallate signaling pathway through 67-kDa laminin receptor. · 2008 · https://pubmed.ncbi.nlm.nih.gov/18079119/ · DOI 10.1074/jbc.m707892200
trigger_kind
machinery_impairment Imported condition classification; unverified.
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 52–58
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Genetic screen, cell signaling and experimental tumor-growth models. · source_derived_draft · unverified_draft
## egcg-machinery Removing pathway components prevented the observed response. Silencing MYPT1, eEF1A or 67LR abrogated EGCG-mediated tumor-growth inhibition in the tested models. Model: Genetic screen, cell signaling and experimental tumor-growth models. Limitations: Pathway dependency in these models does not establish human cancer treatment or a dietary threshold. Evidence access: primary abstract. Green tea polyphenol epigallocatechin-3-gallate signaling pathway through 67-kDa laminin receptor. · 2008 · https://pubmed.ncbi.nlm.nih.gov/18079119/ · DOI 10.1074/jbc.m707892200
Complete structured claim and evidence
EGCG activation of 67LR increased cGMP, a rate-limiting signal for cell death in the model.
67-kDa laminin receptor state / 67LR → Cyclic guanosine monophosphate source_derived_draftungraded
Experimental context and source evidence
experimental_model
Cancer-cell experiments and mouse xenografts in the 2013 study.
limitations
Preclinical combination experiments; normal-cell selectivity in tested preparations is not universal safety.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
The receptor signal passed through cGMP.
primary_references
67-kDa laminin receptor increases cGMP to induce cancer-selective apoptosis. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23348740/ · DOI 10.1172/jci64768
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 60–66
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Cancer-cell experiments and mouse xenografts in the 2013 study. · source_derived_draft · unverified_draft
## egcg-cgmp The receptor signal passed through cGMP. EGCG activation of 67LR increased cGMP, a rate-limiting signal for cell death in the model. Model: Cancer-cell experiments and mouse xenografts in the 2013 study. Limitations: Preclinical combination experiments; normal-cell selectivity in tested preparations is not universal safety. Evidence access: primary abstract. 67-kDa laminin receptor increases cGMP to induce cancer-selective apoptosis. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23348740/ · DOI 10.1172/jci64768
Complete structured claim and evidence
The cGMP-dependent death pathway engaged PKC delta and acid sphingomyelinase.
Cyclic guanosine monophosphate → Protein kinase C delta family source_derived_draftungraded
Experimental context and source evidence
experimental_model
Cancer-cell experiments and mouse xenografts in the 2013 study.
limitations
Preclinical combination experiments; normal-cell selectivity in tested preparations is not universal safety.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
cGMP connected the receptor to a lipid-signaling enzyme.
primary_references
67-kDa laminin receptor increases cGMP to induce cancer-selective apoptosis. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23348740/ · DOI 10.1172/jci64768
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 68–74
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Cancer-cell experiments and mouse xenografts in the 2013 study. · source_derived_draft · unverified_draft
## egcg-pkcd cGMP connected the receptor to a lipid-signaling enzyme. The cGMP-dependent death pathway engaged PKC delta and acid sphingomyelinase. Model: Cancer-cell experiments and mouse xenografts in the 2013 study. Limitations: Preclinical combination experiments; normal-cell selectivity in tested preparations is not universal safety. Evidence access: primary abstract. 67-kDa laminin receptor increases cGMP to induce cancer-selective apoptosis. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23348740/ · DOI 10.1172/jci64768
Complete structured claim and evidence
Acid sphingomyelinase participated downstream of PKC delta in 67LR-dependent cell death.
Acid sphingomyelinase family → Apoptosis in specified EGCG cancer models source_derived_draftungraded
Experimental context and source evidence
experimental_model
Cancer-cell experiments and mouse xenografts in the 2013 study.
limitations
Preclinical combination experiments; normal-cell selectivity in tested preparations is not universal safety.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
Lipid breakdown was part of the experimental death signal.
primary_references
67-kDa laminin receptor increases cGMP to induce cancer-selective apoptosis. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23348740/ · DOI 10.1172/jci64768
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 76–82
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Cancer-cell experiments and mouse xenografts in the 2013 study. · source_derived_draft · unverified_draft
## egcg-asm Lipid breakdown was part of the experimental death signal. Acid sphingomyelinase participated downstream of PKC delta in 67LR-dependent cell death. Model: Cancer-cell experiments and mouse xenografts in the 2013 study. Limitations: Preclinical combination experiments; normal-cell selectivity in tested preparations is not universal safety. Evidence access: primary abstract. 67-kDa laminin receptor increases cGMP to induce cancer-selective apoptosis. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23348740/ · DOI 10.1172/jci64768
Complete structured claim and evidence
Overexpressed PDE5 attenuated the cGMP-dependent anticancer signal.
Phosphodiesterase 5 family → Apoptosis in specified EGCG cancer models source_derived_draftungraded
Experimental context and source evidence
experimental_model
Cancer-cell experiments and mouse xenografts in the 2013 study.
limitations
Preclinical combination experiments; normal-cell selectivity in tested preparations is not universal safety.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
An enzyme that removes cGMP can limit the response.
primary_references
67-kDa laminin receptor increases cGMP to induce cancer-selective apoptosis. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23348740/ · DOI 10.1172/jci64768
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 84–90
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Cancer-cell experiments and mouse xenografts in the 2013 study. · source_derived_draft · unverified_draft
## egcg-pde5 An enzyme that removes cGMP can limit the response. Overexpressed PDE5 attenuated the cGMP-dependent anticancer signal. Model: Cancer-cell experiments and mouse xenografts in the 2013 study. Limitations: Preclinical combination experiments; normal-cell selectivity in tested preparations is not universal safety. Evidence access: primary abstract. 67-kDa laminin receptor increases cGMP to induce cancer-selective apoptosis. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23348740/ · DOI 10.1172/jci64768
Complete structured claim and evidence
PDE5 inhibition with vardenafil potentiated EGCG-dependent apoptosis and prolonged survival in a mouse xenograft experiment.
Vardenafil → Apoptosis in specified EGCG cancer models source_derived_draftungraded
Experimental context and source evidence
experimental_model
Cancer-cell experiments and mouse xenografts in the 2013 study.
limitations
Preclinical combination experiments; normal-cell selectivity in tested preparations is not universal safety.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
Blocking the opposing enzyme strengthened the response in these models.
primary_references
67-kDa laminin receptor increases cGMP to induce cancer-selective apoptosis. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23348740/ · DOI 10.1172/jci64768
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 92–98
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Cancer-cell experiments and mouse xenografts in the 2013 study. · source_derived_draft · unverified_draft
## egcg-vardenafil Blocking the opposing enzyme strengthened the response in these models. PDE5 inhibition with vardenafil potentiated EGCG-dependent apoptosis and prolonged survival in a mouse xenograft experiment. Model: Cancer-cell experiments and mouse xenografts in the 2013 study. Limitations: Preclinical combination experiments; normal-cell selectivity in tested preparations is not universal safety. Evidence access: primary abstract. 67-kDa laminin receptor increases cGMP to induce cancer-selective apoptosis. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23348740/ · DOI 10.1172/jci64768
Complete structured claim and evidence
EGCG rapidly increased Tollip expression; 67LR silencing or antibody blockade prevented this.
Epigallocatechin-3-gallate (EGCG) → Tollip expression source_derived_draftungraded
Experimental context and source evidence
experimental_model
Macrophage LPS-response experiments, EGCG 1 micromolar; organism not assigned from abstract.
limitations
Family nodes preserve the unresolved species. This is not evidence of treating systemic human inflammation.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
EGCG increased a brake on inflammatory signaling.
primary_references
TLR4 signaling inhibitory pathway induced by green tea polyphenol epigallocatechin-3-gallate through 67-kDa laminin receptor. · 2010 · https://pubmed.ncbi.nlm.nih.gov/20511545/ · DOI 10.4049/jimmunol.0903742
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 100–106
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Macrophage LPS-response experiments, EGCG 1 micromolar; organism not assigned from abstract. · source_derived_draft · unverified_draft
## egcg-tollip EGCG increased a brake on inflammatory signaling. EGCG rapidly increased Tollip expression; 67LR silencing or antibody blockade prevented this. Model: Macrophage LPS-response experiments, EGCG 1 micromolar; organism not assigned from abstract. Limitations: Family nodes preserve the unresolved species. This is not evidence of treating systemic human inflammation. Evidence access: primary abstract. TLR4 signaling inhibitory pathway induced by green tea polyphenol epigallocatechin-3-gallate through 67-kDa laminin receptor. · 2010 · https://pubmed.ncbi.nlm.nih.gov/20511545/ · DOI 10.4049/jimmunol.0903742
Complete structured claim and evidence
EGCG reduced TLR4 expression through 67LR.
Epigallocatechin-3-gallate (EGCG) → TLR4 expression source_derived_draftungraded
Experimental context and source evidence
experimental_model
Macrophage LPS-response experiments, EGCG 1 micromolar; organism not assigned from abstract.
limitations
Family nodes preserve the unresolved species. This is not evidence of treating systemic human inflammation.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
The cells expressed less of the tested inflammatory receptor.
primary_references
TLR4 signaling inhibitory pathway induced by green tea polyphenol epigallocatechin-3-gallate through 67-kDa laminin receptor. · 2010 · https://pubmed.ncbi.nlm.nih.gov/20511545/ · DOI 10.4049/jimmunol.0903742
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 108–114
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Macrophage LPS-response experiments, EGCG 1 micromolar; organism not assigned from abstract. · source_derived_draft · unverified_draft
## egcg-tlr4 The cells expressed less of the tested inflammatory receptor. EGCG reduced TLR4 expression through 67LR. Model: Macrophage LPS-response experiments, EGCG 1 micromolar; organism not assigned from abstract. Limitations: Family nodes preserve the unresolved species. This is not evidence of treating systemic human inflammation. Evidence access: primary abstract. TLR4 signaling inhibitory pathway induced by green tea polyphenol epigallocatechin-3-gallate through 67-kDa laminin receptor. · 2010 · https://pubmed.ncbi.nlm.nih.gov/20511545/ · DOI 10.4049/jimmunol.0903742
Complete structured claim and evidence
Tollip silencing impaired EGCG inhibition of TLR4 signaling.
Toll-interacting protein family / Tollip → TLR4 downstream inflammatory signaling source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
experimental_model
Macrophage LPS-response experiments, EGCG 1 micromolar; organism not assigned from abstract.
limitations
Family nodes preserve the unresolved species. This is not evidence of treating systemic human inflammation.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
The anti-inflammatory response depended on Tollip.
primary_references
TLR4 signaling inhibitory pathway induced by green tea polyphenol epigallocatechin-3-gallate through 67-kDa laminin receptor. · 2010 · https://pubmed.ncbi.nlm.nih.gov/20511545/ · DOI 10.4049/jimmunol.0903742
trigger_kind
machinery_impairment Imported condition classification; unverified.
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 116–122
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Macrophage LPS-response experiments, EGCG 1 micromolar; organism not assigned from abstract. · source_derived_draft · unverified_draft
## egcg-tollip-gate The anti-inflammatory response depended on Tollip. Tollip silencing impaired EGCG inhibition of TLR4 signaling. Model: Macrophage LPS-response experiments, EGCG 1 micromolar; organism not assigned from abstract. Limitations: Family nodes preserve the unresolved species. This is not evidence of treating systemic human inflammation. Evidence access: primary abstract. TLR4 signaling inhibitory pathway induced by green tea polyphenol epigallocatechin-3-gallate through 67-kDa laminin receptor. · 2010 · https://pubmed.ncbi.nlm.nih.gov/20511545/ · DOI 10.4049/jimmunol.0903742
Complete structured claim and evidence
EGCG inhibited bovine DHFR with slow tight binding, Ki 0.109 micromolar.
Epigallocatechin-3-gallate (EGCG) → Bovine dihydrofolate reductase / DHFR source_derived_draftungraded
Experimental context and source evidence
experimental_model
Purified bovine/chicken DHFR and lymphoma-cell experiments; human DHFR interaction was modeled computationally.
limitations
Do not relabel the purified enzymes as human DHFR or infer that normal tea intake causes folate deficiency.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
EGCG inhibited a folate-processing enzyme in a purified animal preparation.
primary_references
The antifolate activity of tea catechins. · 2005 · https://pubmed.ncbi.nlm.nih.gov/15781612/ · DOI 10.1158/0008-5472.can-04-3469
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 124–130
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Purified bovine/chicken DHFR and lymphoma-cell experiments; human DHFR interaction was modeled computationally. · source_derived_draft · unverified_draft
## egcg-bovine-dhfr EGCG inhibited a folate-processing enzyme in a purified animal preparation. EGCG inhibited bovine DHFR with slow tight binding, Ki 0.109 micromolar. Model: Purified bovine/chicken DHFR and lymphoma-cell experiments; human DHFR interaction was modeled computationally. Limitations: Do not relabel the purified enzymes as human DHFR or infer that normal tea intake causes folate deficiency. Evidence access: primary abstract. The antifolate activity of tea catechins. · 2005 · https://pubmed.ncbi.nlm.nih.gov/15781612/ · DOI 10.1158/0008-5472.can-04-3469
Complete structured claim and evidence
Chicken DHFR showed reversible competitive inhibition, Ki 10.3 micromolar.
Epigallocatechin-3-gallate (EGCG) → Chicken dihydrofolate reductase / DHFR source_derived_draftungraded
Experimental context and source evidence
experimental_model
Purified bovine/chicken DHFR and lymphoma-cell experiments; human DHFR interaction was modeled computationally.
limitations
Do not relabel the purified enzymes as human DHFR or infer that normal tea intake causes folate deficiency.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
Even enzyme preparations from different species behaved differently.
primary_references
The antifolate activity of tea catechins. · 2005 · https://pubmed.ncbi.nlm.nih.gov/15781612/ · DOI 10.1158/0008-5472.can-04-3469
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 132–138
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Purified bovine/chicken DHFR and lymphoma-cell experiments; human DHFR interaction was modeled computationally. · source_derived_draft · unverified_draft
## egcg-chicken-dhfr Even enzyme preparations from different species behaved differently. Chicken DHFR showed reversible competitive inhibition, Ki 10.3 micromolar. Model: Purified bovine/chicken DHFR and lymphoma-cell experiments; human DHFR interaction was modeled computationally. Limitations: Do not relabel the purified enzymes as human DHFR or infer that normal tea intake causes folate deficiency. Evidence access: primary abstract. The antifolate activity of tea catechins. · 2005 · https://pubmed.ncbi.nlm.nih.gov/15781612/ · DOI 10.1158/0008-5472.can-04-3469
Complete structured claim and evidence
Folate depletion increased lymphoma-cell sensitivity to EGCG; the reported growth IC50 was 20 micromolar.
Folate (vitamin B9) → Proliferation of EGCG-exposed lymphoma cells source_derived_draftungraded
Experimental context and source evidence
availability_state
nutrient_deficiency Imported condition classification; unverified.
experimental_model
Purified bovine/chicken DHFR and lymphoma-cell experiments; human DHFR interaction was modeled computationally.
limitations
Do not relabel the purified enzymes as human DHFR or infer that normal tea intake causes folate deficiency.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
Low folate made the cultured cells more sensitive.
primary_references
The antifolate activity of tea catechins. · 2005 · https://pubmed.ncbi.nlm.nih.gov/15781612/ · DOI 10.1158/0008-5472.can-04-3469
trigger_kind
nutrient_deficiency Imported condition classification; unverified.
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 140–146
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Purified bovine/chicken DHFR and lymphoma-cell experiments; human DHFR interaction was modeled computationally. · source_derived_draft · unverified_draft
## egcg-folate-low Low folate made the cultured cells more sensitive. Folate depletion increased lymphoma-cell sensitivity to EGCG; the reported growth IC50 was 20 micromolar. Model: Purified bovine/chicken DHFR and lymphoma-cell experiments; human DHFR interaction was modeled computationally. Limitations: Do not relabel the purified enzymes as human DHFR or infer that normal tea intake causes folate deficiency. Evidence access: primary abstract. The antifolate activity of tea catechins. · 2005 · https://pubmed.ncbi.nlm.nih.gov/15781612/ · DOI 10.1158/0008-5472.can-04-3469
Complete structured claim and evidence
Hypoxanthine plus thymidine attenuated EGCG growth inhibition, consistent with involvement of folate-dependent nucleotide supply.
Hypoxanthine → Proliferation of EGCG-exposed lymphoma cells source_derived_draftungraded
Experimental context and source evidence
experimental_model
Purified bovine/chicken DHFR and lymphoma-cell experiments; human DHFR interaction was modeled computationally.
limitations
Rescue supports pathway involvement but does not prove DHFR is the only target.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
Supplying salvage-pathway ingredients partly bypassed the growth effect.
primary_references
The antifolate activity of tea catechins. · 2005 · https://pubmed.ncbi.nlm.nih.gov/15781612/ · DOI 10.1158/0008-5472.can-04-3469
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 148–154
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Purified bovine/chicken DHFR and lymphoma-cell experiments; human DHFR interaction was modeled computationally. · source_derived_draft · unverified_draft
## egcg-salvage Supplying salvage-pathway ingredients partly bypassed the growth effect. Hypoxanthine plus thymidine attenuated EGCG growth inhibition, consistent with involvement of folate-dependent nucleotide supply. Model: Purified bovine/chicken DHFR and lymphoma-cell experiments; human DHFR interaction was modeled computationally. Limitations: Rescue supports pathway involvement but does not prove DHFR is the only target. Evidence access: primary abstract. The antifolate activity of tea catechins. · 2005 · https://pubmed.ncbi.nlm.nih.gov/15781612/ · DOI 10.1158/0008-5472.can-04-3469
Complete structured claim and evidence
In 39 women studied for 30 days, folate stayed in the normal range across EGCG-containing-extract groups, including groups receiving clomiphene or letrozole.
Green tea extract, study-specific mixture → Serum folate concentration source_derived_draftungraded
Experimental context and source evidence
experimental_model
Women aged 18–40; all groups received extract; selected MTHFR and DHFR genotypes considered.
limitations
No extract-free control, pregnancy outcome or long-term depletion test. Abstract dose terminology is inconsistent; no pure-EGCG dose is inferred.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
This short human study did not reproduce folate depletion.
primary_references
Evaluating the Effect of Epigallocatechin Gallate (EGCG) in Reducing Folate Levels in Reproductive Aged Women by MTHFR and DHFR Genotype in Combination With Letrozole or Clomiphene. · 2025 · https://pubmed.ncbi.nlm.nih.gov/40077973/ · DOI 10.1111/cts.70189
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 156–162
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Women aged 18–40; all groups received extract; selected MTHFR and DHFR genotypes considered. · source_derived_draft · unverified_draft
## egcg-human-folate This short human study did not reproduce folate depletion. In 39 women studied for 30 days, folate stayed in the normal range across EGCG-containing-extract groups, including groups receiving clomiphene or letrozole. Model: Women aged 18–40; all groups received extract; selected MTHFR and DHFR genotypes considered. Limitations: No extract-free control, pregnancy outcome or long-term depletion test. Abstract dose terminology is inconsistent; no pure-EGCG dose is inferred. Evidence access: primary abstract. Evaluating the Effect of Epigallocatechin Gallate (EGCG) in Reducing Folate Levels in Reproductive Aged Women by MTHFR and DHFR Genotype in Combination With Letrozole or Clomiphene. · 2025 · https://pubmed.ncbi.nlm.nih.gov/40077973/ · DOI 10.1111/cts.70189
Complete structured claim and evidence
EGCG inhibited human liver cytosolic COMT-mediated catechol-estrogen methylation, IC50 0.07 micromolar, with mixed inhibition.
Epigallocatechin-3-gallate (EGCG) → Human catechol O-methyltransferase / COMT source_derived_draftungraded
Experimental context and source evidence
experimental_model
Human liver cytosol and metabolite comparisons.
limitations
Assay potency does not establish brain, liver or whole-body inhibition after ingestion.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
A liver preparation showed inhibition of a methyl-transfer enzyme.
primary_references
Inhibition of human liver catechol-O-methyltransferase by tea catechins and their metabolites: structure-activity relationship and molecular-modeling studies. · 2005 · https://pubmed.ncbi.nlm.nih.gov/15857617/ · DOI 10.1016/j.bcp.2005.01.024
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 164–170
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human liver cytosol and metabolite comparisons. · source_derived_draft · unverified_draft
## egcg-comt-invitro A liver preparation showed inhibition of a methyl-transfer enzyme. EGCG inhibited human liver cytosolic COMT-mediated catechol-estrogen methylation, IC50 0.07 micromolar, with mixed inhibition. Model: Human liver cytosol and metabolite comparisons. Limitations: Assay potency does not establish brain, liver or whole-body inhibition after ingestion. Evidence access: primary abstract. Inhibition of human liver catechol-O-methyltransferase by tea catechins and their metabolites: structure-activity relationship and molecular-modeling studies. · 2005 · https://pubmed.ncbi.nlm.nih.gov/15857617/ · DOI 10.1016/j.bcp.2005.01.024
Complete structured claim and evidence
4″-O-methyl-EGCG retained COMT inhibitory activity, IC50 0.10 micromolar.
4″-O-methyl-EGCG → Human catechol O-methyltransferase / COMT source_derived_draftungraded
Experimental context and source evidence
experimental_model
Human liver cytosol; catechol-estrogen assay.
limitations
Do not assume metabolites have identical tissue exposure or activity to EGCG.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
A methylated metabolite also affected the enzyme in vitro.
primary_references
Inhibition of human liver catechol-O-methyltransferase by tea catechins and their metabolites: structure-activity relationship and molecular-modeling studies. · 2005 · https://pubmed.ncbi.nlm.nih.gov/15857617/ · DOI 10.1016/j.bcp.2005.01.024
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 172–178
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human liver cytosol; catechol-estrogen assay. · source_derived_draft · unverified_draft
## egcg-comt-metabolite A methylated metabolite also affected the enzyme in vitro. 4″-O-methyl-EGCG retained COMT inhibitory activity, IC50 0.10 micromolar. Model: Human liver cytosol; catechol-estrogen assay. Limitations: Do not assume metabolites have identical tissue exposure or activity to EGCG. Evidence access: primary abstract. Inhibition of human liver catechol-O-methyltransferase by tea catechins and their metabolites: structure-activity relationship and molecular-modeling studies. · 2005 · https://pubmed.ncbi.nlm.nih.gov/15857617/ · DOI 10.1016/j.bcp.2005.01.024
Complete structured claim and evidence
After 750 mg EGCG in 24 volunteers, erythrocyte COMT activity increased by 24% at two hours rather than decreasing.
Epigallocatechin-3-gallate (EGCG) → Human erythrocyte COMT activity source_derived_draftungraded
Experimental context and source evidence
experimental_model
Single exposure; 14 women and 10 men; COMT genotype assessment.
limitations
Red-cell activity at one time point is not a measurement of brain or liver COMT. No general catecholamine or fat-burning claim follows.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
The measured human red-cell result did not match a simple inhibition prediction.
primary_references
The activity of catechol-O-methyltransferase (COMT) is not impaired by high doses of epigallocatechin-3-gallate (EGCG) in vivo. · 2014 · https://pubmed.ncbi.nlm.nih.gov/24972245/ · DOI 10.1016/j.ejphar.2014.06.014
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 180–186
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Single exposure; 14 women and 10 men; COMT genotype assessment. · source_derived_draft · unverified_draft
## egcg-comt-human The measured human red-cell result did not match a simple inhibition prediction. After 750 mg EGCG in 24 volunteers, erythrocyte COMT activity increased by 24% at two hours rather than decreasing. Model: Single exposure; 14 women and 10 men; COMT genotype assessment. Limitations: Red-cell activity at one time point is not a measurement of brain or liver COMT. No general catecholamine or fat-burning claim follows. Evidence access: primary abstract. The activity of catechol-O-methyltransferase (COMT) is not impaired by high doses of epigallocatechin-3-gallate (EGCG) in vivo. · 2014 · https://pubmed.ncbi.nlm.nih.gov/24972245/ · DOI 10.1016/j.ejphar.2014.06.014
Complete structured claim and evidence
In 30 women with low iron stores, 150 and 300 mg EGCG reduced relative nonheme-iron absorption by 14% and 27%; the 300 mg comparison with placebo was significant.
Epigallocatechin-3-gallate (EGCG) → Nonheme iron absorption source_derived_draftungraded
Experimental context and source evidence
experimental_model
Randomized double-blind three-period crossover; eight days per period; stable iron isotopes.
limitations
The reassuring paper title does not negate its significant high-dose result. Low-dose impact in healthy iron-replete people was an author extrapolation, not the studied population.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
EGCG reduced iron absorption at the higher tested dose.
primary_references
Epigallocatechin gallate (EGCG) (TEAVIGO) does not impair nonhaem-iron absorption in man. · 2005 · https://pubmed.ncbi.nlm.nih.gov/16008116/ · DOI 10.1016/j.phymed.2004.07.001
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 188–194
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Randomized double-blind three-period crossover; eight days per period; stable iron isotopes. · source_derived_draft · unverified_draft
## egcg-iron EGCG reduced iron absorption at the higher tested dose. In 30 women with low iron stores, 150 and 300 mg EGCG reduced relative nonheme-iron absorption by 14% and 27%; the 300 mg comparison with placebo was significant. Model: Randomized double-blind three-period crossover; eight days per period; stable iron isotopes. Limitations: The reassuring paper title does not negate its significant high-dose result. Low-dose impact in healthy iron-replete people was an author extrapolation, not the studied population. Evidence access: primary abstract. Epigallocatechin gallate (EGCG) (TEAVIGO) does not impair nonhaem-iron absorption in man. · 2005 · https://pubmed.ncbi.nlm.nih.gov/16008116/ · DOI 10.1016/j.phymed.2004.07.001
Complete structured claim and evidence
EGCG inhibited chicken liver FAS through rapid reversible and slower irreversible components; rapid 50% inhibition occurred at 52 micromolar.
Epigallocatechin-3-gallate (EGCG) → Chicken fatty acid synthase / FASN source_derived_draftungraded
Experimental context and source evidence
experimental_model
Chicken liver FAS; biochemical kinetics.
limitations
Not a human weight-loss trial or a direct measurement of human FASN.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
EGCG acted on a lipid-synthesis enzyme in a purified preparation.
primary_references
Green tea epigallocatechin gallate: a natural inhibitor of fatty-acid synthase. · 2001 · https://pubmed.ncbi.nlm.nih.gov/11700039/ · DOI 10.1006/bbrc.2001.5923
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 196–202
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Chicken liver FAS; biochemical kinetics. · source_derived_draft · unverified_draft
## egcg-fasn EGCG acted on a lipid-synthesis enzyme in a purified preparation. EGCG inhibited chicken liver FAS through rapid reversible and slower irreversible components; rapid 50% inhibition occurred at 52 micromolar. Model: Chicken liver FAS; biochemical kinetics. Limitations: Not a human weight-loss trial or a direct measurement of human FASN. Evidence access: primary abstract. Green tea epigallocatechin gallate: a natural inhibitor of fatty-acid synthase. · 2001 · https://pubmed.ncbi.nlm.nih.gov/11700039/ · DOI 10.1006/bbrc.2001.5923
Complete structured claim and evidence
NADPH protected against inhibition, and ketoacyl-reductase experiments supported competition near the NADPH-binding function.
NADPH → Chicken fatty acid synthase / FASN source_derived_draftungraded
Experimental context and source evidence
experimental_model
Purified chicken FAS kinetics.
limitations
This does not show that niacin supplementation cancels EGCG or improves a clinical outcome.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
The enzyme’s reducing cofactor altered EGCG inhibition.
primary_references
Green tea epigallocatechin gallate: a natural inhibitor of fatty-acid synthase. · 2001 · https://pubmed.ncbi.nlm.nih.gov/11700039/ · DOI 10.1006/bbrc.2001.5923
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 204–210
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Purified chicken FAS kinetics. · source_derived_draft · unverified_draft
## egcg-fasn-nadph The enzyme’s reducing cofactor altered EGCG inhibition. NADPH protected against inhibition, and ketoacyl-reductase experiments supported competition near the NADPH-binding function. Model: Purified chicken FAS kinetics. Limitations: This does not show that niacin supplementation cancels EGCG or improves a clinical outcome. Evidence access: primary abstract. Green tea epigallocatechin gallate: a natural inhibitor of fatty-acid synthase. · 2001 · https://pubmed.ncbi.nlm.nih.gov/11700039/ · DOI 10.1006/bbrc.2001.5923
Complete structured claim and evidence
EGCG showed ATP-competitive inhibition with Ki 380 nanomolar in the reported enzyme assay.
Epigallocatechin-3-gallate (EGCG) → Phosphoinositide 3-kinase family source_derived_draftungraded
Experimental context and source evidence
experimental_model
Biochemical kinase assays plus MDA-MB-231 and A549 cell experiments.
limitations
PI3K isoform is not assigned from abstract; docking is a model, not a solved ligand structure.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
EGCG competed with the enzyme’s energy substrate.
primary_references
Epigallocatechin gallate (EGCG), a major component of green tea, is a dual phosphoinositide-3-kinase/mTOR inhibitor. · 2011 · https://pubmed.ncbi.nlm.nih.gov/21300025/ · DOI 10.1016/j.bbrc.2011.02.010
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 212–218
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Biochemical kinase assays plus MDA-MB-231 and A549 cell experiments. · source_derived_draft · unverified_draft
## egcg-pi3k EGCG competed with the enzyme’s energy substrate. EGCG showed ATP-competitive inhibition with Ki 380 nanomolar in the reported enzyme assay. Model: Biochemical kinase assays plus MDA-MB-231 and A549 cell experiments. Limitations: PI3K isoform is not assigned from abstract; docking is a model, not a solved ligand structure. Evidence access: primary abstract. Epigallocatechin gallate (EGCG), a major component of green tea, is a dual phosphoinositide-3-kinase/mTOR inhibitor. · 2011 · https://pubmed.ncbi.nlm.nih.gov/21300025/ · DOI 10.1016/j.bbrc.2011.02.010
Complete structured claim and evidence
EGCG showed ATP-competitive inhibition with Ki 320 nanomolar in the reported enzyme assay.
Epigallocatechin-3-gallate (EGCG) → Human mechanistic target of rapamycin kinase / MTOR source_derived_draftungraded
Experimental context and source evidence
experimental_model
Biochemical kinase assays plus MDA-MB-231 and A549 cell experiments.
limitations
PI3K isoform is not assigned from abstract; docking is a model, not a solved ligand structure.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
EGCG competed with the enzyme’s energy substrate.
primary_references
Epigallocatechin gallate (EGCG), a major component of green tea, is a dual phosphoinositide-3-kinase/mTOR inhibitor. · 2011 · https://pubmed.ncbi.nlm.nih.gov/21300025/ · DOI 10.1016/j.bbrc.2011.02.010
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 220–226
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Biochemical kinase assays plus MDA-MB-231 and A549 cell experiments. · source_derived_draft · unverified_draft
## egcg-mtor EGCG competed with the enzyme’s energy substrate. EGCG showed ATP-competitive inhibition with Ki 320 nanomolar in the reported enzyme assay. Model: Biochemical kinase assays plus MDA-MB-231 and A549 cell experiments. Limitations: PI3K isoform is not assigned from abstract; docking is a model, not a solved ligand structure. Evidence access: primary abstract. Epigallocatechin gallate (EGCG), a major component of green tea, is a dual phosphoinositide-3-kinase/mTOR inhibitor. · 2011 · https://pubmed.ncbi.nlm.nih.gov/21300025/ · DOI 10.1016/j.bbrc.2011.02.010
Complete structured claim and evidence
EGCG reduced AKT Ser473 phosphorylation alongside proliferation in the tested cancer cells.
Epigallocatechin-3-gallate (EGCG) → AKT Ser473 phosphorylation source_derived_draftungraded
Experimental context and source evidence
experimental_model
MDA-MB-231 and A549 cells.
limitations
A pathway readout does not establish a unique causal target or human anticancer efficacy.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
Downstream growth signaling changed in the cell experiments.
primary_references
Epigallocatechin gallate (EGCG), a major component of green tea, is a dual phosphoinositide-3-kinase/mTOR inhibitor. · 2011 · https://pubmed.ncbi.nlm.nih.gov/21300025/ · DOI 10.1016/j.bbrc.2011.02.010
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 228–234
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · MDA-MB-231 and A549 cells. · source_derived_draft · unverified_draft
## egcg-akt Downstream growth signaling changed in the cell experiments. EGCG reduced AKT Ser473 phosphorylation alongside proliferation in the tested cancer cells. Model: MDA-MB-231 and A549 cells. Limitations: A pathway readout does not establish a unique causal target or human anticancer efficacy. Evidence access: primary abstract. Epigallocatechin gallate (EGCG), a major component of green tea, is a dual phosphoinositide-3-kinase/mTOR inhibitor. · 2011 · https://pubmed.ncbi.nlm.nih.gov/21300025/ · DOI 10.1016/j.bbrc.2011.02.010
Complete structured claim and evidence
The kinase panel reported EGCG inhibition with IC50 0.33 micromolar.
Epigallocatechin-3-gallate (EGCG) → Dual-specificity tyrosine-phosphorylation regulated kinase 1A family source_derived_draftungraded
Experimental context and source evidence
experimental_model
Panel of 28 protein kinases.
limitations
Two inhibited kinases in this panel do not establish selectivity across the entire kinome.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
A kinase-panel experiment identified another target.
primary_references
The specificities of protein kinase inhibitors: an update. · 2003 · https://pubmed.ncbi.nlm.nih.gov/12534346/ · DOI 10.1042/bj20021535
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 236–242
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Panel of 28 protein kinases. · source_derived_draft · unverified_draft
## egcg-dyrk A kinase-panel experiment identified another target. The kinase panel reported EGCG inhibition with IC50 0.33 micromolar. Model: Panel of 28 protein kinases. Limitations: Two inhibited kinases in this panel do not establish selectivity across the entire kinome. Evidence access: primary abstract. The specificities of protein kinase inhibitors: an update. · 2003 · https://pubmed.ncbi.nlm.nih.gov/12534346/ · DOI 10.1042/bj20021535
Complete structured claim and evidence
The kinase panel reported EGCG inhibition with IC50 1.0 micromolar.
Epigallocatechin-3-gallate (EGCG) → PRAK / MAPK-activated protein kinase 5 family source_derived_draftungraded
Experimental context and source evidence
experimental_model
Panel of 28 protein kinases.
limitations
Two inhibited kinases in this panel do not establish selectivity across the entire kinome.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
A kinase-panel experiment identified another target.
primary_references
The specificities of protein kinase inhibitors: an update. · 2003 · https://pubmed.ncbi.nlm.nih.gov/12534346/ · DOI 10.1042/bj20021535
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 244–250
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Panel of 28 protein kinases. · source_derived_draft · unverified_draft
## egcg-prak A kinase-panel experiment identified another target. The kinase panel reported EGCG inhibition with IC50 1.0 micromolar. Model: Panel of 28 protein kinases. Limitations: Two inhibited kinases in this panel do not establish selectivity across the entire kinome. Evidence access: primary abstract. The specificities of protein kinase inhibitors: an update. · 2003 · https://pubmed.ncbi.nlm.nih.gov/12534346/ · DOI 10.1042/bj20021535
Complete structured claim and evidence
EGCG competitively inhibited DNMT activity in nuclear extracts, Ki 6.89 micromolar.
Epigallocatechin-3-gallate (EGCG) → DNA cytosine methyltransferase family source_derived_draftungraded
Experimental context and source evidence
experimental_model
Nuclear-extract enzyme assay; molecular docking was also reported.
limitations
The extract assay is not purified DNMT1-specific proof; modeled binding contacts remain predictions.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
EGCG affected a DNA-methylation assay.
primary_references
Tea polyphenol (-)-epigallocatechin-3-gallate inhibits DNA methyltransferase and reactivates methylation-silenced genes in cancer cell lines. · 2003 · https://pubmed.ncbi.nlm.nih.gov/14633667/
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 252–258
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Nuclear-extract enzyme assay; molecular docking was also reported. · source_derived_draft · unverified_draft
## egcg-dnmt EGCG affected a DNA-methylation assay. EGCG competitively inhibited DNMT activity in nuclear extracts, Ki 6.89 micromolar. Model: Nuclear-extract enzyme assay; molecular docking was also reported. Limitations: The extract assay is not purified DNMT1-specific proof; modeled binding contacts remain predictions. Evidence access: primary abstract. Tea polyphenol (-)-epigallocatechin-3-gallate inhibits DNA methyltransferase and reactivates methylation-silenced genes in cancer cell lines. · 2003 · https://pubmed.ncbi.nlm.nih.gov/14633667/
Complete structured claim and evidence
At 5–50 micromolar for 12–144 hours, EGCG reduced methylation-specific signals at p16, RARbeta, MGMT and hMLH1 promoters in KYSE 510 cells.
Epigallocatechin-3-gallate (EGCG) → Promoter CpG methylation in specified cancer cells source_derived_draftungraded
Experimental context and source evidence
experimental_model
Human esophageal cancer cells; PCR methylation assays.
limitations
Not a universal epigenome reset or evidence that demethylation is always beneficial.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
Some silenced cancer-cell genes showed changes in promoter methylation.
primary_references
Tea polyphenol (-)-epigallocatechin-3-gallate inhibits DNA methyltransferase and reactivates methylation-silenced genes in cancer cell lines. · 2003 · https://pubmed.ncbi.nlm.nih.gov/14633667/
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 260–266
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human esophageal cancer cells; PCR methylation assays. · source_derived_draft · unverified_draft
## egcg-cpg Some silenced cancer-cell genes showed changes in promoter methylation. At 5–50 micromolar for 12–144 hours, EGCG reduced methylation-specific signals at p16, RARbeta, MGMT and hMLH1 promoters in KYSE 510 cells. Model: Human esophageal cancer cells; PCR methylation assays. Limitations: Not a universal epigenome reset or evidence that demethylation is always beneficial. Evidence access: primary abstract. Tea polyphenol (-)-epigallocatechin-3-gallate inhibits DNA methyltransferase and reactivates methylation-silenced genes in cancer cell lines. · 2003 · https://pubmed.ncbi.nlm.nih.gov/14633667/
Complete structured claim and evidence
The promoter changes accompanied gene mRNA re-expression; RARbeta and hMLH1 protein re-expression was detected.
Epigallocatechin-3-gallate (EGCG) → Expression of methylation-silenced genes in cancer cells source_derived_draftungraded
Experimental context and source evidence
experimental_model
Cancer-cell expression assays.
limitations
Dietary exposure and human disease outcomes were not established.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
The study also checked gene expression, beyond a methylation signal.
primary_references
Tea polyphenol (-)-epigallocatechin-3-gallate inhibits DNA methyltransferase and reactivates methylation-silenced genes in cancer cell lines. · 2003 · https://pubmed.ncbi.nlm.nih.gov/14633667/
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 268–274
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Cancer-cell expression assays. · source_derived_draft · unverified_draft
## egcg-reactivation The study also checked gene expression, beyond a methylation signal. The promoter changes accompanied gene mRNA re-expression; RARbeta and hMLH1 protein re-expression was detected. Model: Cancer-cell expression assays. Limitations: Dietary exposure and human disease outcomes were not established. Evidence access: primary abstract. Tea polyphenol (-)-epigallocatechin-3-gallate inhibits DNA methyltransferase and reactivates methylation-silenced genes in cancer cell lines. · 2003 · https://pubmed.ncbi.nlm.nih.gov/14633667/
Complete structured claim and evidence
The 2022 study assigned hepatic EGCG sulfation to SULT1A1.
Human sulfotransferase 1A1 / SULT1A1 → Epigallocatechin-3-gallate (EGCG) source_derived_draftungraded
Experimental context and source evidence
experimental_model
Human liver/intestinal cytosol, enzyme assignment and a human ingestion pharmacokinetic study.
limitations
Formation rate and metabolite exposure do not prove identical biological effects of free and conjugated EGCG.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
One study identifies this enzyme as a route for processing EGCG.
primary_references
4″-Sulfation Is the Major Metabolic Pathway of Epigallocatechin-3-gallate in Humans: Characterization of Metabolites, Enzymatic Analysis, and Pharmacokinetic Profiling. · 2022 · https://pubmed.ncbi.nlm.nih.gov/35786898/ · DOI 10.1021/acs.jafc.2c02150
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 276–282
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human liver/intestinal cytosol, enzyme assignment and a human ingestion pharmacokinetic study. · source_derived_draft · unverified_draft
## egcg-sult1a1-substrate One study identifies this enzyme as a route for processing EGCG. The 2022 study assigned hepatic EGCG sulfation to SULT1A1. Model: Human liver/intestinal cytosol, enzyme assignment and a human ingestion pharmacokinetic study. Limitations: Formation rate and metabolite exposure do not prove identical biological effects of free and conjugated EGCG. Evidence access: primary abstract. 4″-Sulfation Is the Major Metabolic Pathway of Epigallocatechin-3-gallate in Humans: Characterization of Metabolites, Enzymatic Analysis, and Pharmacokinetic Profiling. · 2022 · https://pubmed.ncbi.nlm.nih.gov/35786898/ · DOI 10.1021/acs.jafc.2c02150
Complete structured claim and evidence
The same study assigned intestinal EGCG sulfation to SULT1A3.
Human sulfotransferase 1A3 / SULT1A3 → Epigallocatechin-3-gallate (EGCG) source_derived_draftungraded
Experimental context and source evidence
experimental_model
Human liver/intestinal cytosol, enzyme assignment and a human ingestion pharmacokinetic study.
limitations
Formation rate and metabolite exposure do not prove identical biological effects of free and conjugated EGCG.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
A different enzyme contributed in the intestinal preparation.
primary_references
4″-Sulfation Is the Major Metabolic Pathway of Epigallocatechin-3-gallate in Humans: Characterization of Metabolites, Enzymatic Analysis, and Pharmacokinetic Profiling. · 2022 · https://pubmed.ncbi.nlm.nih.gov/35786898/ · DOI 10.1021/acs.jafc.2c02150
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 284–290
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human liver/intestinal cytosol, enzyme assignment and a human ingestion pharmacokinetic study. · source_derived_draft · unverified_draft
## egcg-sult1a3 A different enzyme contributed in the intestinal preparation. The same study assigned intestinal EGCG sulfation to SULT1A3. Model: Human liver/intestinal cytosol, enzyme assignment and a human ingestion pharmacokinetic study. Limitations: Formation rate and metabolite exposure do not prove identical biological effects of free and conjugated EGCG. Evidence access: primary abstract. 4″-Sulfation Is the Major Metabolic Pathway of Epigallocatechin-3-gallate in Humans: Characterization of Metabolites, Enzymatic Analysis, and Pharmacokinetic Profiling. · 2022 · https://pubmed.ncbi.nlm.nih.gov/35786898/ · DOI 10.1021/acs.jafc.2c02150
Complete structured claim and evidence
Human plasma EGCG-4″-sulfate Cmax was 177.9 nM versus 233.5 nM free EGCG; AUC was 715.2 versus 664.1 nM·h.
Epigallocatechin-3-gallate (EGCG) → EGCG-4″-sulfate source_derived_draftungraded
Experimental context and source evidence
experimental_model
Human liver/intestinal cytosol, enzyme assignment and a human ingestion pharmacokinetic study.
limitations
Formation rate and metabolite exposure do not prove identical biological effects of free and conjugated EGCG.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
A conjugated metabolite reached exposure comparable to free EGCG.
primary_references
4″-Sulfation Is the Major Metabolic Pathway of Epigallocatechin-3-gallate in Humans: Characterization of Metabolites, Enzymatic Analysis, and Pharmacokinetic Profiling. · 2022 · https://pubmed.ncbi.nlm.nih.gov/35786898/ · DOI 10.1021/acs.jafc.2c02150
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 292–298
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human liver/intestinal cytosol, enzyme assignment and a human ingestion pharmacokinetic study. · source_derived_draft · unverified_draft
## egcg-sulfate-exposure A conjugated metabolite reached exposure comparable to free EGCG. Human plasma EGCG-4″-sulfate Cmax was 177.9 nM versus 233.5 nM free EGCG; AUC was 715.2 versus 664.1 nM·h. Model: Human liver/intestinal cytosol, enzyme assignment and a human ingestion pharmacokinetic study. Limitations: Formation rate and metabolite exposure do not prove identical biological effects of free and conjugated EGCG. Evidence access: primary abstract. 4″-Sulfation Is the Major Metabolic Pathway of Epigallocatechin-3-gallate in Humans: Characterization of Metabolites, Enzymatic Analysis, and Pharmacokinetic Profiling. · 2022 · https://pubmed.ncbi.nlm.nih.gov/35786898/ · DOI 10.1021/acs.jafc.2c02150
Complete structured claim and evidence
The 2016 SULT1A1 allostery study explicitly reported that EGCG was not a SULT1A1 substrate but was sulfonated by SULT2A1.
Human sulfotransferase 1A1 / SULT1A1 → Epigallocatechin-3-gallate (EGCG) source_derived_draftungraded
Experimental context and source evidence
experimental_model
Equilibrium binding and pre-steady-state human SULT enzyme experiments.
limitations
This differs from the later SULT1A1 assignment; assay and product-identification differences require comparison.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
An earlier enzyme study gives a different substrate assignment.
primary_references
Isozyme Specific Allosteric Regulation of Human Sulfotransferase 1A1. · 2016 · https://pubmed.ncbi.nlm.nih.gov/27356022/ · DOI 10.1021/acs.biochem.6b00401
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 300–306
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Equilibrium binding and pre-steady-state human SULT enzyme experiments. · source_derived_draft · unverified_draft
## egcg-sult-not-substrate An earlier enzyme study gives a different substrate assignment. The 2016 SULT1A1 allostery study explicitly reported that EGCG was not a SULT1A1 substrate but was sulfonated by SULT2A1. Model: Equilibrium binding and pre-steady-state human SULT enzyme experiments. Limitations: This differs from the later SULT1A1 assignment; assay and product-identification differences require comparison. Evidence access: primary abstract. Isozyme Specific Allosteric Regulation of Human Sulfotransferase 1A1. · 2016 · https://pubmed.ncbi.nlm.nih.gov/27356022/ · DOI 10.1021/acs.biochem.6b00401
Complete structured claim and evidence
EGCG stabilized the closed SULT1A1 active-site cap, slowed nucleotide release and inhibited turnover; nucleotide-bound enzyme showed 17-fold tighter EGCG binding.
Epigallocatechin-3-gallate (EGCG) → Human sulfotransferase 1A1 / SULT1A1 source_derived_draftungraded
Experimental context and source evidence
experimental_model
Allosteric binding/kinetic model; weak active-site binding also observed.
limitations
Substrate status and inhibition are separate questions; not proof of altered melatonin or hormone levels in people.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
EGCG can trap this enzyme in a slower-cycling state.
primary_references
Isozyme Specific Allosteric Regulation of Human Sulfotransferase 1A1. · 2016 · https://pubmed.ncbi.nlm.nih.gov/27356022/ · DOI 10.1021/acs.biochem.6b00401
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 308–314
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Allosteric binding/kinetic model; weak active-site binding also observed. · source_derived_draft · unverified_draft
## egcg-sult-cap EGCG can trap this enzyme in a slower-cycling state. EGCG stabilized the closed SULT1A1 active-site cap, slowed nucleotide release and inhibited turnover; nucleotide-bound enzyme showed 17-fold tighter EGCG binding. Model: Allosteric binding/kinetic model; weak active-site binding also observed. Limitations: Substrate status and inhibition are separate questions; not proof of altered melatonin or hormone levels in people. Evidence access: primary abstract. Isozyme Specific Allosteric Regulation of Human Sulfotransferase 1A1. · 2016 · https://pubmed.ncbi.nlm.nih.gov/27356022/ · DOI 10.1021/acs.biochem.6b00401
Complete structured claim and evidence
Human fecal fermentation converted EGCG through ester hydrolysis, ring opening/fission and subsequent reactions to phenolic acids, including 4-phenylbutyric and hydroxyphenylpropionic acids.
Epigallocatechin-3-gallate (EGCG) → EGCG-derived microbial phenolic metabolite pool source_derived_draftungraded
Experimental context and source evidence
experimental_model
In-vitro human gut-community fermentation and UHPLC-Q-Orbitrap-MS.
limitations
Metabolite detection in fermentation does not demonstrate systemic human exposure or benefit.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
Gut microbes can turn EGCG into chemically different compounds.
primary_references
Reciprocal Interactions between Epigallocatechin-3-gallate (EGCG) and Human Gut Microbiota In Vitro. · 2020 · https://pubmed.ncbi.nlm.nih.gov/32808768/ · DOI 10.1021/acs.jafc.0c03587
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 316–322
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · In-vitro human gut-community fermentation and UHPLC-Q-Orbitrap-MS. · source_derived_draft · unverified_draft
## egcg-microbial-conversion Gut microbes can turn EGCG into chemically different compounds. Human fecal fermentation converted EGCG through ester hydrolysis, ring opening/fission and subsequent reactions to phenolic acids, including 4-phenylbutyric and hydroxyphenylpropionic acids. Model: In-vitro human gut-community fermentation and UHPLC-Q-Orbitrap-MS. Limitations: Metabolite detection in fermentation does not demonstrate systemic human exposure or benefit. Evidence access: primary abstract. Reciprocal Interactions between Epigallocatechin-3-gallate (EGCG) and Human Gut Microbiota In Vitro. · 2020 · https://pubmed.ncbi.nlm.nih.gov/32808768/ · DOI 10.1021/acs.jafc.0c03587
Complete structured claim and evidence
EGCG-exposed fermentations showed increases in Bacteroides, Christensenellaceae and Bifidobacterium and decreases in selected other taxa.
Epigallocatechin-3-gallate (EGCG) → Gut microbial community composition in fermentation assays source_derived_draftungraded
Experimental context and source evidence
experimental_model
In-vitro fermentation with microbiome profiling.
limitations
Taxon shifts and metabolite correlations do not establish a universally beneficial microbiome in humans.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
EGCG also changed the experimental microbial community.
primary_references
Reciprocal Interactions between Epigallocatechin-3-gallate (EGCG) and Human Gut Microbiota In Vitro. · 2020 · https://pubmed.ncbi.nlm.nih.gov/32808768/ · DOI 10.1021/acs.jafc.0c03587
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 324–330
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · In-vitro fermentation with microbiome profiling. · source_derived_draft · unverified_draft
## egcg-microbiome EGCG also changed the experimental microbial community. EGCG-exposed fermentations showed increases in Bacteroides, Christensenellaceae and Bifidobacterium and decreases in selected other taxa. Model: In-vitro fermentation with microbiome profiling. Limitations: Taxon shifts and metabolite correlations do not establish a universally beneficial microbiome in humans. Evidence access: primary abstract. Reciprocal Interactions between Epigallocatechin-3-gallate (EGCG) and Human Gut Microbiota In Vitro. · 2020 · https://pubmed.ncbi.nlm.nih.gov/32808768/ · DOI 10.1021/acs.jafc.0c03587
Complete structured claim and evidence
EGCG-associated peroxide formation and CHO cytotoxicity differed substantially among seven culture media.
Epigallocatechin-3-gallate (EGCG) → Hydrogen peroxide source_derived_draftungraded
Experimental context and source evidence
experimental_model
CHO cells and cell-culture medium comparisons.
limitations
Culture autooxidation cannot be generalized to all tissues or used to dismiss every cell experiment.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
EGCG can generate peroxide under some laboratory conditions.
primary_references
Different cytotoxic and clastogenic effects of epigallocatechin gallate in various cell-culture media due to variable rates of its oxidation in the culture medium. · 2007 · https://pubmed.ncbi.nlm.nih.gov/17851114/ · DOI 10.1016/j.mrgentox.2007.07.009
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 332–338
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · CHO cells and cell-culture medium comparisons. · source_derived_draft · unverified_draft
## egcg-peroxide EGCG can generate peroxide under some laboratory conditions. EGCG-associated peroxide formation and CHO cytotoxicity differed substantially among seven culture media. Model: CHO cells and cell-culture medium comparisons. Limitations: Culture autooxidation cannot be generalized to all tissues or used to dismiss every cell experiment. Evidence access: primary abstract. Different cytotoxic and clastogenic effects of epigallocatechin gallate in various cell-culture media due to variable rates of its oxidation in the culture medium. · 2007 · https://pubmed.ncbi.nlm.nih.gov/17851114/ · DOI 10.1016/j.mrgentox.2007.07.009
Complete structured claim and evidence
Added catalase substantially reduced EGCG cytotoxicity in the culture comparison.
Experimental catalase preparation → EGCG cytotoxicity in CHO cell cultures source_derived_draftungraded
Experimental context and source evidence
experimental_model
CHO-cell experiments.
limitations
Rescue implicates peroxide in this setting; it does not establish oral catalase or antioxidant combinations as treatment.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
Removing peroxide reduced the observed cell injury.
primary_references
Different cytotoxic and clastogenic effects of epigallocatechin gallate in various cell-culture media due to variable rates of its oxidation in the culture medium. · 2007 · https://pubmed.ncbi.nlm.nih.gov/17851114/ · DOI 10.1016/j.mrgentox.2007.07.009
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 340–346
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · CHO-cell experiments. · source_derived_draft · unverified_draft
## egcg-catalase Removing peroxide reduced the observed cell injury. Added catalase substantially reduced EGCG cytotoxicity in the culture comparison. Model: CHO-cell experiments. Limitations: Rescue implicates peroxide in this setting; it does not establish oral catalase or antioxidant combinations as treatment. Evidence access: primary abstract. Different cytotoxic and clastogenic effects of epigallocatechin gallate in various cell-culture media due to variable rates of its oxidation in the culture medium. · 2007 · https://pubmed.ncbi.nlm.nih.gov/17851114/ · DOI 10.1016/j.mrgentox.2007.07.009
Complete structured claim and evidence
EGCG bound unfolded amyloid-beta and alpha-synuclein and redirected assembly toward unstructured, relatively nontoxic oligomers in the experimental system.
Epigallocatechin-3-gallate (EGCG) → Amyloid fibril formation in specified assays source_derived_draftungraded
Experimental context and source evidence
experimental_model
Biophysical and cell-based aggregation experiments.
limitations
Not evidence of preventing or treating human neurodegenerative disease.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
EGCG changed how these proteins assembled.
primary_references
EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers. · 2008 · https://pubmed.ncbi.nlm.nih.gov/18511942/ · DOI 10.1038/nsmb.1437
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 348–354
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Biophysical and cell-based aggregation experiments. · source_derived_draft · unverified_draft
## egcg-amyloid-initiation EGCG changed how these proteins assembled. EGCG bound unfolded amyloid-beta and alpha-synuclein and redirected assembly toward unstructured, relatively nontoxic oligomers in the experimental system. Model: Biophysical and cell-based aggregation experiments. Limitations: Not evidence of preventing or treating human neurodegenerative disease. Evidence access: primary abstract. EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers. · 2008 · https://pubmed.ncbi.nlm.nih.gov/18511942/ · DOI 10.1038/nsmb.1437
Complete structured claim and evidence
EGCG bound mature fibrils and remodeled them into smaller amorphous aggregates without measured release of monomers or small diffusible oligomers.
Epigallocatechin-3-gallate (EGCG) → Amyloid-beta fibrils, sequence specified by study source_derived_draftungraded
Experimental context and source evidence
experimental_model
Mature amyloid-beta and alpha-synuclein fibril preparations.
limitations
This does not show removal of deposits from a human brain.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
EGCG changed pre-existing aggregates in a laboratory experiment.
primary_references
EGCG remodels mature alpha-synuclein and amyloid-beta fibrils and reduces cellular toxicity. · 2010 · https://pubmed.ncbi.nlm.nih.gov/20385841/ · DOI 10.1073/pnas.0910723107
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 356–362
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Mature amyloid-beta and alpha-synuclein fibril preparations. · source_derived_draft · unverified_draft
## egcg-ab-remodel EGCG changed pre-existing aggregates in a laboratory experiment. EGCG bound mature fibrils and remodeled them into smaller amorphous aggregates without measured release of monomers or small diffusible oligomers. Model: Mature amyloid-beta and alpha-synuclein fibril preparations. Limitations: This does not show removal of deposits from a human brain. Evidence access: primary abstract. EGCG remodels mature alpha-synuclein and amyloid-beta fibrils and reduces cellular toxicity. · 2010 · https://pubmed.ncbi.nlm.nih.gov/20385841/ · DOI 10.1073/pnas.0910723107
Complete structured claim and evidence
EGCG bound mature fibrils and remodeled them into smaller amorphous aggregates without measured release of monomers or small diffusible oligomers.
Epigallocatechin-3-gallate (EGCG) → Alpha-synuclein fibrils source_derived_draftungraded
Experimental context and source evidence
experimental_model
Mature amyloid-beta and alpha-synuclein fibril preparations.
limitations
This does not show removal of deposits from a human brain.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
EGCG changed pre-existing aggregates in a laboratory experiment.
primary_references
EGCG remodels mature alpha-synuclein and amyloid-beta fibrils and reduces cellular toxicity. · 2010 · https://pubmed.ncbi.nlm.nih.gov/20385841/ · DOI 10.1073/pnas.0910723107
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 364–370
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Mature amyloid-beta and alpha-synuclein fibril preparations. · source_derived_draft · unverified_draft
## egcg-as-remodel EGCG changed pre-existing aggregates in a laboratory experiment. EGCG bound mature fibrils and remodeled them into smaller amorphous aggregates without measured release of monomers or small diffusible oligomers. Model: Mature amyloid-beta and alpha-synuclein fibril preparations. Limitations: This does not show removal of deposits from a human brain. Evidence access: primary abstract. EGCG remodels mature alpha-synuclein and amyloid-beta fibrils and reduces cellular toxicity. · 2010 · https://pubmed.ncbi.nlm.nih.gov/20385841/ · DOI 10.1073/pnas.0910723107
Complete structured claim and evidence
Remodeled aggregates had lower toxicity in the tested cell assay.
Epigallocatechin-3-gallate (EGCG) → Amyloid aggregate toxicity in cell assays source_derived_draftungraded
Experimental context and source evidence
experimental_model
Cell toxicity comparison of treated versus untreated fibrils.
limitations
Assay result, not clinical cognitive improvement.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
The remodeled material was less harmful in that assay.
primary_references
EGCG remodels mature alpha-synuclein and amyloid-beta fibrils and reduces cellular toxicity. · 2010 · https://pubmed.ncbi.nlm.nih.gov/20385841/ · DOI 10.1073/pnas.0910723107
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 372–378
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Cell toxicity comparison of treated versus untreated fibrils. · source_derived_draft · unverified_draft
## egcg-aggregate-toxicity The remodeled material was less harmful in that assay. Remodeled aggregates had lower toxicity in the tested cell assay. Model: Cell toxicity comparison of treated versus untreated fibrils. Limitations: Assay result, not clinical cognitive improvement. Evidence access: primary abstract. EGCG remodels mature alpha-synuclein and amyloid-beta fibrils and reduces cellular toxicity. · 2010 · https://pubmed.ncbi.nlm.nih.gov/20385841/ · DOI 10.1073/pnas.0910723107
Complete structured claim and evidence
Remodeling of the tested mature amyloid preparations depended on EGCG autooxidation.
Oxidized EGCG reaction products, unresolved mixture → Amyloid-beta fibrils, sequence specified by study source_derived_draftungraded
Experimental context and source evidence
experimental_model
Amyloid-beta 1–40 and IAPP/Sup35 fragment preparations.
limitations
Fragment and in-vitro oxidation contexts limit generalization.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
The oxidation state helped determine aggregate remodeling.
primary_references
Toward the molecular mechanism(s) by which EGCG treatment remodels mature amyloid fibrils. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23611538/ · DOI 10.1021/ja3115696
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 380–386
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Amyloid-beta 1–40 and IAPP/Sup35 fragment preparations. · source_derived_draft · unverified_draft
## egcg-oxidation-remodel The oxidation state helped determine aggregate remodeling. Remodeling of the tested mature amyloid preparations depended on EGCG autooxidation. Model: Amyloid-beta 1–40 and IAPP/Sup35 fragment preparations. Limitations: Fragment and in-vitro oxidation contexts limit generalization. Evidence access: primary abstract. Toward the molecular mechanism(s) by which EGCG treatment remodels mature amyloid fibrils. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23611538/ · DOI 10.1021/ja3115696
Complete structured claim and evidence
Both oxidized and unoxidized EGCG bound fibrils and prevented Thioflavin T binding.
Epigallocatechin-3-gallate (EGCG) → Thioflavin T fibril-binding signal source_derived_draftungraded
Experimental context and source evidence
experimental_model
Fibril binding/assay-interference experiments.
limitations
Use independent structural and toxicity measurements to distinguish remodeling from dye displacement.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
A lower dye signal alone can be mistaken for less amyloid.
primary_references
Toward the molecular mechanism(s) by which EGCG treatment remodels mature amyloid fibrils. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23611538/ · DOI 10.1021/ja3115696
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 388–394
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Fibril binding/assay-interference experiments. · source_derived_draft · unverified_draft
## egcg-tht A lower dye signal alone can be mistaken for less amyloid. Both oxidized and unoxidized EGCG bound fibrils and prevented Thioflavin T binding. Model: Fibril binding/assay-interference experiments. Limitations: Use independent structural and toxicity measurements to distinguish remodeling from dye displacement. Evidence access: primary abstract. Toward the molecular mechanism(s) by which EGCG treatment remodels mature amyloid fibrils. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23611538/ · DOI 10.1021/ja3115696
Complete structured claim and evidence
EGCG blocked bortezomib-mediated anticancer effects in the reported models.
Epigallocatechin-3-gallate (EGCG) → Antitumor activity of bortezomib in specified models source_derived_draftungraded
Experimental context and source evidence
experimental_model
Myeloma/glioblastoma cell experiments and animal models in the 2009 Blood study.
limitations
Preclinical findings; no human coadministration outcome trial. Chemical form and simultaneous concentrations matter.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
One research group found that EGCG weakened this cancer drug.
primary_references
Green tea polyphenols block the anticancer effects of bortezomib and other boronic acid-based proteasome inhibitors. · 2009 · https://pubmed.ncbi.nlm.nih.gov/19190249/ · DOI 10.1182/blood-2008-07-171389
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 396–402
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Myeloma/glioblastoma cell experiments and animal models in the 2009 Blood study. · source_derived_draft · unverified_draft
## egcg-bortezomib-antagonism One research group found that EGCG weakened this cancer drug. EGCG blocked bortezomib-mediated anticancer effects in the reported models. Model: Myeloma/glioblastoma cell experiments and animal models in the 2009 Blood study. Limitations: Preclinical findings; no human coadministration outcome trial. Chemical form and simultaneous concentrations matter. Evidence access: primary abstract. Green tea polyphenols block the anticancer effects of bortezomib and other boronic acid-based proteasome inhibitors. · 2009 · https://pubmed.ncbi.nlm.nih.gov/19190249/ · DOI 10.1182/blood-2008-07-171389
Complete structured claim and evidence
Direct EGCG–bortezomib reaction prevented proteasome inhibition and downstream stress/death responses; tested nonboronic inhibitors did not show the same antagonism.
Epigallocatechin-3-gallate (EGCG) → Bortezomib-mediated proteasome inhibition source_derived_draftungraded
Experimental context and source evidence
experimental_model
Myeloma/glioblastoma cell experiments and animal models in the 2009 Blood study.
limitations
Preclinical findings; no human coadministration outcome trial. Chemical form and simultaneous concentrations matter.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
The proposed interference starts with drug chemistry.
primary_references
Green tea polyphenols block the anticancer effects of bortezomib and other boronic acid-based proteasome inhibitors. · 2009 · https://pubmed.ncbi.nlm.nih.gov/19190249/ · DOI 10.1182/blood-2008-07-171389
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 404–410
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Myeloma/glioblastoma cell experiments and animal models in the 2009 Blood study. · source_derived_draft · unverified_draft
## egcg-bortezomib-proteasome The proposed interference starts with drug chemistry. Direct EGCG–bortezomib reaction prevented proteasome inhibition and downstream stress/death responses; tested nonboronic inhibitors did not show the same antagonism. Model: Myeloma/glioblastoma cell experiments and animal models in the 2009 Blood study. Limitations: Preclinical findings; no human coadministration outcome trial. Chemical form and simultaneous concentrations matter. Evidence access: primary abstract. Green tea polyphenols block the anticancer effects of bortezomib and other boronic acid-based proteasome inhibitors. · 2009 · https://pubmed.ncbi.nlm.nih.gov/19190249/ · DOI 10.1182/blood-2008-07-171389
Complete structured claim and evidence
NMR and cell experiments characterized boronate and borate EGCG–bortezomib derivatives; adduct stability depended on structural features.
Epigallocatechin-3-gallate (EGCG) → Bortezomib source_derived_draftungraded
Experimental context and source evidence
experimental_model
Chemical characterization and cell assays.
limitations
A boronic-acid drug is not interchangeable with dietary boron.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
The chemical interaction has evidence beyond a pathway diagram.
primary_references
Molecular characterization of the boron adducts of the proteasome inhibitor bortezomib with epigallocatechin-3-gallate and related polyphenols. · 2015 · https://pubmed.ncbi.nlm.nih.gov/25669488/ · DOI 10.1039/c4ob02512a
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 412–418
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Chemical characterization and cell assays. · source_derived_draft · unverified_draft
## egcg-boronate The chemical interaction has evidence beyond a pathway diagram. NMR and cell experiments characterized boronate and borate EGCG–bortezomib derivatives; adduct stability depended on structural features. Model: Chemical characterization and cell assays. Limitations: A boronic-acid drug is not interchangeable with dietary boron. Evidence access: primary abstract. Molecular characterization of the boron adducts of the proteasome inhibitor bortezomib with epigallocatechin-3-gallate and related polyphenols. · 2015 · https://pubmed.ncbi.nlm.nih.gov/25669488/ · DOI 10.1039/c4ob02512a
Complete structured claim and evidence
A separate 2009 KM3 myeloma-cell study reported synergistic apoptosis with EGCG plus bortezomib.
Epigallocatechin-3-gallate (EGCG) → Antitumor activity of bortezomib in specified models source_derived_draftungraded
Experimental context and source evidence
experimental_model
KM3 myeloma cells; associated NF-kappaB/caspase pathway readouts.
limitations
Dose, timing and model were not harmonized with the antagonism study; no universal direction can be assigned.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
Another study reported a stronger combination effect.
primary_references
Potentiation of (-)-epigallocatechin-3-gallate-induced apoptosis by bortezomib in multiple myeloma cells. · 2009 · https://pubmed.ncbi.nlm.nih.gov/20011976/ · DOI 10.1093/abbs/gmp094
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 420–426
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · KM3 myeloma cells; associated NF-kappaB/caspase pathway readouts. · source_derived_draft · unverified_draft
## egcg-bortezomib-synergy Another study reported a stronger combination effect. A separate 2009 KM3 myeloma-cell study reported synergistic apoptosis with EGCG plus bortezomib. Model: KM3 myeloma cells; associated NF-kappaB/caspase pathway readouts. Limitations: Dose, timing and model were not harmonized with the antagonism study; no universal direction can be assigned. Evidence access: primary abstract. Potentiation of (-)-epigallocatechin-3-gallate-induced apoptosis by bortezomib in multiple myeloma cells. · 2009 · https://pubmed.ncbi.nlm.nih.gov/20011976/ · DOI 10.1093/abbs/gmp094
Complete structured claim and evidence
In CWR22 xenografts, EGCG above 200 micromolar at bortezomib administration abolished measured antitumor activity.
Epigallocatechin-3-gallate (EGCG) → Antitumor activity of bortezomib in specified models source_derived_draftungraded
Experimental context and source evidence
experimental_model
Immunocompromised mice; bortezomib 0.8 mg/kg IV twice weekly.
limitations
Concentration-specific animal findings do not establish a human safety threshold.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
A follow-up found antagonism at very high simultaneous exposure.
primary_references
Preclinical evaluation of the antitumor activity of bortezomib in combination with vitamin C or with epigallocatechin gallate, a component of green tea. · 2011 · https://pubmed.ncbi.nlm.nih.gov/21400028/ · DOI 10.1007/s00280-011-1591-2
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 428–434
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Immunocompromised mice; bortezomib 0.8 mg/kg IV twice weekly. · source_derived_draft · unverified_draft
## egcg-bortezomib-high A follow-up found antagonism at very high simultaneous exposure. In CWR22 xenografts, EGCG above 200 micromolar at bortezomib administration abolished measured antitumor activity. Model: Immunocompromised mice; bortezomib 0.8 mg/kg IV twice weekly. Limitations: Concentration-specific animal findings do not establish a human safety threshold. Evidence access: primary abstract. Preclinical evaluation of the antitumor activity of bortezomib in combination with vitamin C or with epigallocatechin gallate, a component of green tea. · 2011 · https://pubmed.ncbi.nlm.nih.gov/21400028/ · DOI 10.1007/s00280-011-1591-2
Complete structured claim and evidence
At EGCG 11–16 micromolar, the same model showed no antagonism; tumor-growth inhibition was 63.5% versus 53.9–58.9% with bortezomib alone.
Epigallocatechin-3-gallate (EGCG) → Antitumor activity of bortezomib in specified models source_derived_draftungraded
Experimental context and source evidence
experimental_model
CWR22 xenograft exposure comparison.
limitations
Not proof of clinical synergy or unrestricted safe coadministration.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
The drug interaction was not identical at every concentration.
primary_references
Preclinical evaluation of the antitumor activity of bortezomib in combination with vitamin C or with epigallocatechin gallate, a component of green tea. · 2011 · https://pubmed.ncbi.nlm.nih.gov/21400028/ · DOI 10.1007/s00280-011-1591-2
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 436–442
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · CWR22 xenograft exposure comparison. · source_derived_draft · unverified_draft
## egcg-bortezomib-lower The drug interaction was not identical at every concentration. At EGCG 11–16 micromolar, the same model showed no antagonism; tumor-growth inhibition was 63.5% versus 53.9–58.9% with bortezomib alone. Model: CWR22 xenograft exposure comparison. Limitations: Not proof of clinical synergy or unrestricted safe coadministration. Evidence access: primary abstract. Preclinical evaluation of the antitumor activity of bortezomib in combination with vitamin C or with epigallocatechin gallate, a component of green tea. · 2011 · https://pubmed.ncbi.nlm.nih.gov/21400028/ · DOI 10.1007/s00280-011-1591-2
Complete structured claim and evidence
Oral vitamin C at 40 or 500 mg/kg did not antagonize bortezomib in the same mouse experiment.
L-Ascorbic acid → Antitumor activity of bortezomib in specified models source_derived_draftungraded
Experimental context and source evidence
experimental_model
CWR22 xenograft model.
limitations
Species, route and exposure matter; this comparison does not justify combining supplements with cancer treatment.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
Another nutrient comparator did not reproduce high-EGCG antagonism.
primary_references
Preclinical evaluation of the antitumor activity of bortezomib in combination with vitamin C or with epigallocatechin gallate, a component of green tea. · 2011 · https://pubmed.ncbi.nlm.nih.gov/21400028/ · DOI 10.1007/s00280-011-1591-2
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 444–450
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · CWR22 xenograft model. · source_derived_draft · unverified_draft
## egcg-bortezomib-vitc Another nutrient comparator did not reproduce high-EGCG antagonism. Oral vitamin C at 40 or 500 mg/kg did not antagonize bortezomib in the same mouse experiment. Model: CWR22 xenograft model. Limitations: Species, route and exposure matter; this comparison does not justify combining supplements with cancer treatment. Evidence access: primary abstract. Preclinical evaluation of the antitumor activity of bortezomib in combination with vitamin C or with epigallocatechin gallate, a component of green tea. · 2011 · https://pubmed.ncbi.nlm.nih.gov/21400028/ · DOI 10.1007/s00280-011-1591-2
Complete structured claim and evidence
Adding 30 mg ascorbic acid to 250 mL tea increased EGCG recovery after simulated digestion to 54%, versus at most 10% without protective formulation.
L-Ascorbic acid → EGCG recovery after simulated digestion source_derived_draftungraded
Experimental context and source evidence
experimental_model
In-vitro gastric/small-intestinal digestion with HPLC recovery.
limitations
Recovery is chemical survival, not measured human absorption or clinical synergy.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
Vitamin C protected EGCG in a simulated digestive system.
primary_references
Common tea formulations modulate in vitro digestive recovery of green tea catechins. · 2007 · https://pubmed.ncbi.nlm.nih.gov/17688297/ · DOI 10.1002/mnfr.200700086
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 452–458
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · In-vitro gastric/small-intestinal digestion with HPLC recovery. · source_derived_draft · unverified_draft
## egcg-vitc-stability Vitamin C protected EGCG in a simulated digestive system. Adding 30 mg ascorbic acid to 250 mL tea increased EGCG recovery after simulated digestion to 54%, versus at most 10% without protective formulation. Model: In-vitro gastric/small-intestinal digestion with HPLC recovery. Limitations: Recovery is chemical survival, not measured human absorption or clinical synergy. Evidence access: primary abstract. Common tea formulations modulate in vitro digestive recovery of green tea catechins. · 2007 · https://pubmed.ncbi.nlm.nih.gov/17688297/ · DOI 10.1002/mnfr.200700086
Complete structured claim and evidence
In a 30-person crossover study, fasting produced more than 3.5-fold higher free-EGCG peak concentrations than fed administration.
Polyphenon E green tea catechin mixture → Free EGCG plasma exposure source_derived_draftungraded
Experimental context and source evidence
experimental_model
Polyphenon E providing 400, 800 or 1200 mg EGCG; 10 subjects per dose group.
limitations
Mixture and high experimental doses; greater exposure is not a recommendation to take extracts fasting. Nausea was most frequent at 1200 mg fasting.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
Food changed how much free EGCG reached the blood.
primary_references
Effects of dosing condition on the oral bioavailability of green tea catechins after single-dose administration of Polyphenon E in healthy individuals. · 2005 · https://pubmed.ncbi.nlm.nih.gov/15958649/ · DOI 10.1158/1078-0432.ccr-04-2549
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 460–466
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Polyphenon E providing 400, 800 or 1200 mg EGCG; 10 subjects per dose group. · source_derived_draft · unverified_draft
## egcg-fasting Food changed how much free EGCG reached the blood. In a 30-person crossover study, fasting produced more than 3.5-fold higher free-EGCG peak concentrations than fed administration. Model: Polyphenon E providing 400, 800 or 1200 mg EGCG; 10 subjects per dose group. Limitations: Mixture and high experimental doses; greater exposure is not a recommendation to take extracts fasting. Nausea was most frequent at 1200 mg fasting. Evidence access: primary abstract. Effects of dosing condition on the oral bioavailability of green tea catechins after single-dose administration of Polyphenon E in healthy individuals. · 2005 · https://pubmed.ncbi.nlm.nih.gov/15958649/ · DOI 10.1158/1078-0432.ccr-04-2549
Complete structured claim and evidence
After 700 mL/day green tea for 14 days, nadolol Cmax and AUC fell by 85.3% and 85.0% in 10 healthy volunteers; renal clearance was unchanged.
Green tea beverage, study-specific mixture → Nadolol plasma exposure source_derived_draftungraded
Experimental context and source evidence
experimental_model
30 mg nadolol after tea versus water.
limitations
This human experiment tested tea, not isolated EGCG.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
Whole green tea substantially reduced exposure to nadolol.
primary_references
Green tea ingestion greatly reduces plasma concentrations of nadolol in healthy subjects. · 2014 · https://pubmed.ncbi.nlm.nih.gov/24419562/ · DOI 10.1038/clpt.2013.241
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 468–474
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · 30 mg nadolol after tea versus water. · source_derived_draft · unverified_draft
## egcg-nadolol-human Whole green tea substantially reduced exposure to nadolol. After 700 mL/day green tea for 14 days, nadolol Cmax and AUC fell by 85.3% and 85.0% in 10 healthy volunteers; renal clearance was unchanged. Model: 30 mg nadolol after tea versus water. Limitations: This human experiment tested tea, not isolated EGCG. Evidence access: primary abstract. Green tea ingestion greatly reduces plasma concentrations of nadolol in healthy subjects. · 2014 · https://pubmed.ncbi.nlm.nih.gov/24419562/ · DOI 10.1038/clpt.2013.241
Complete structured claim and evidence
Green tea attenuated nadolol-associated blood-pressure reduction in the volunteer study.
Green tea beverage, study-specific mixture → Blood-pressure lowering response to nadolol source_derived_draftungraded
Experimental context and source evidence
experimental_model
Same 10-person tea/water comparison.
limitations
Not a study of cardiovascular events or isolated EGCG.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
The pharmacokinetic interaction also affected a drug response.
primary_references
Green tea ingestion greatly reduces plasma concentrations of nadolol in healthy subjects. · 2014 · https://pubmed.ncbi.nlm.nih.gov/24419562/ · DOI 10.1038/clpt.2013.241
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 476–482
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Same 10-person tea/water comparison. · source_derived_draft · unverified_draft
## egcg-nadolol-bp The pharmacokinetic interaction also affected a drug response. Green tea attenuated nadolol-associated blood-pressure reduction in the volunteer study. Model: Same 10-person tea/water comparison. Limitations: Not a study of cardiovascular events or isolated EGCG. Evidence access: primary abstract. Green tea ingestion greatly reduces plasma concentrations of nadolol in healthy subjects. · 2014 · https://pubmed.ncbi.nlm.nih.gov/24419562/ · DOI 10.1038/clpt.2013.241
Complete structured claim and evidence
Green tea inhibited OATP1A2-mediated nadolol uptake in HEK293 transport assays, supporting a possible intestinal explanation.
Green tea beverage, study-specific mixture → Human OATP1A2 / SLCO1A2 source_derived_draftungraded
Experimental context and source evidence
experimental_model
OATP1A2-transfected cells; nadolol transport Km 84.3 micromolar.
limitations
The clinical study did not directly prove intestinal OATP1A2 inhibition.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
A transporter experiment supplies a candidate mechanism.
primary_references
Green tea ingestion greatly reduces plasma concentrations of nadolol in healthy subjects. · 2014 · https://pubmed.ncbi.nlm.nih.gov/24419562/ · DOI 10.1038/clpt.2013.241
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 484–490
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · OATP1A2-transfected cells; nadolol transport Km 84.3 micromolar. · source_derived_draft · unverified_draft
## egcg-oatp A transporter experiment supplies a candidate mechanism. Green tea inhibited OATP1A2-mediated nadolol uptake in HEK293 transport assays, supporting a possible intestinal explanation. Model: OATP1A2-transfected cells; nadolol transport Km 84.3 micromolar. Limitations: The clinical study did not directly prove intestinal OATP1A2 inhibition. Evidence access: primary abstract. Green tea ingestion greatly reduces plasma concentrations of nadolol in healthy subjects. · 2014 · https://pubmed.ncbi.nlm.nih.gov/24419562/ · DOI 10.1038/clpt.2013.241
Complete structured claim and evidence
EGCG pretreatment reduced rat nadolol Cmax by 53% and AUC by 51%, with weaker blood-pressure control.
Epigallocatechin-3-gallate (EGCG) → Nadolol plasma exposure source_derived_draftungraded
Experimental context and source evidence
experimental_model
Male spontaneously hypertensive rats; EGCG 10 mg/kg/day for 14 days and nadolol 10 mg/kg on day 14.
limitations
Rat transcription/exposure results; mRNA changes do not establish transporter protein activity or a human effect size.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
Purified EGCG also changed nadolol exposure in an animal study.
primary_references
Oral epigallocatechin gallate reduces intestinal nadolol absorption via modulation of Oatp1a5 and Oct1 transcriptional levels in spontaneously hypertensive rats. · 2021 · https://pubmed.ncbi.nlm.nih.gov/34303263/ · DOI 10.1016/j.phymed.2021.153623
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 492–498
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Male spontaneously hypertensive rats; EGCG 10 mg/kg/day for 14 days and nadolol 10 mg/kg on day 14. · source_derived_draft · unverified_draft
## egcg-nadolol-rat Purified EGCG also changed nadolol exposure in an animal study. EGCG pretreatment reduced rat nadolol Cmax by 53% and AUC by 51%, with weaker blood-pressure control. Model: Male spontaneously hypertensive rats; EGCG 10 mg/kg/day for 14 days and nadolol 10 mg/kg on day 14. Limitations: Rat transcription/exposure results; mRNA changes do not establish transporter protein activity or a human effect size. Evidence access: primary abstract. Oral epigallocatechin gallate reduces intestinal nadolol absorption via modulation of Oatp1a5 and Oct1 transcriptional levels in spontaneously hypertensive rats. · 2021 · https://pubmed.ncbi.nlm.nih.gov/34303263/ · DOI 10.1016/j.phymed.2021.153623
Complete structured claim and evidence
EGCG pretreatment reduced the specified transporter mRNA by a reported 4.03-fold.
Epigallocatechin-3-gallate (EGCG) → Rat ileal Oatp1a5 mRNA expression source_derived_draftungraded
Experimental context and source evidence
experimental_model
Male spontaneously hypertensive rats; EGCG 10 mg/kg/day for 14 days and nadolol 10 mg/kg on day 14.
limitations
Rat transcription/exposure results; mRNA changes do not establish transporter protein activity or a human effect size.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
The study measured a transporter-expression change.
primary_references
Oral epigallocatechin gallate reduces intestinal nadolol absorption via modulation of Oatp1a5 and Oct1 transcriptional levels in spontaneously hypertensive rats. · 2021 · https://pubmed.ncbi.nlm.nih.gov/34303263/ · DOI 10.1016/j.phymed.2021.153623
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 500–506
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Male spontaneously hypertensive rats; EGCG 10 mg/kg/day for 14 days and nadolol 10 mg/kg on day 14. · source_derived_draft · unverified_draft
## egcg-ileal-oatp The study measured a transporter-expression change. EGCG pretreatment reduced the specified transporter mRNA by a reported 4.03-fold. Model: Male spontaneously hypertensive rats; EGCG 10 mg/kg/day for 14 days and nadolol 10 mg/kg on day 14. Limitations: Rat transcription/exposure results; mRNA changes do not establish transporter protein activity or a human effect size. Evidence access: primary abstract. Oral epigallocatechin gallate reduces intestinal nadolol absorption via modulation of Oatp1a5 and Oct1 transcriptional levels in spontaneously hypertensive rats. · 2021 · https://pubmed.ncbi.nlm.nih.gov/34303263/ · DOI 10.1016/j.phymed.2021.153623
Complete structured claim and evidence
EGCG pretreatment reduced the specified transporter mRNA by a reported 4.03-fold.
Epigallocatechin-3-gallate (EGCG) → Rat ileal Oct1 mRNA expression source_derived_draftungraded
Experimental context and source evidence
experimental_model
Male spontaneously hypertensive rats; EGCG 10 mg/kg/day for 14 days and nadolol 10 mg/kg on day 14.
limitations
Rat transcription/exposure results; mRNA changes do not establish transporter protein activity or a human effect size.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
The study measured a transporter-expression change.
primary_references
Oral epigallocatechin gallate reduces intestinal nadolol absorption via modulation of Oatp1a5 and Oct1 transcriptional levels in spontaneously hypertensive rats. · 2021 · https://pubmed.ncbi.nlm.nih.gov/34303263/ · DOI 10.1016/j.phymed.2021.153623
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 508–514
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Male spontaneously hypertensive rats; EGCG 10 mg/kg/day for 14 days and nadolol 10 mg/kg on day 14. · source_derived_draft · unverified_draft
## egcg-ileal-oct The study measured a transporter-expression change. EGCG pretreatment reduced the specified transporter mRNA by a reported 4.03-fold. Model: Male spontaneously hypertensive rats; EGCG 10 mg/kg/day for 14 days and nadolol 10 mg/kg on day 14. Limitations: Rat transcription/exposure results; mRNA changes do not establish transporter protein activity or a human effect size. Evidence access: primary abstract. Oral epigallocatechin gallate reduces intestinal nadolol absorption via modulation of Oatp1a5 and Oct1 transcriptional levels in spontaneously hypertensive rats. · 2021 · https://pubmed.ncbi.nlm.nih.gov/34303263/ · DOI 10.1016/j.phymed.2021.153623
Complete structured claim and evidence
EGCG pretreatment reduced the specified transporter mRNA by a reported 8.01-fold.
Epigallocatechin-3-gallate (EGCG) → Rat ileal P-glycoprotein mRNA expression source_derived_draftungraded
Experimental context and source evidence
experimental_model
Male spontaneously hypertensive rats; EGCG 10 mg/kg/day for 14 days and nadolol 10 mg/kg on day 14.
limitations
Rat transcription/exposure results; mRNA changes do not establish transporter protein activity or a human effect size.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
The study measured a transporter-expression change.
primary_references
Oral epigallocatechin gallate reduces intestinal nadolol absorption via modulation of Oatp1a5 and Oct1 transcriptional levels in spontaneously hypertensive rats. · 2021 · https://pubmed.ncbi.nlm.nih.gov/34303263/ · DOI 10.1016/j.phymed.2021.153623
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 516–522
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Male spontaneously hypertensive rats; EGCG 10 mg/kg/day for 14 days and nadolol 10 mg/kg on day 14. · source_derived_draft · unverified_draft
## egcg-ileal-pgp The study measured a transporter-expression change. EGCG pretreatment reduced the specified transporter mRNA by a reported 8.01-fold. Model: Male spontaneously hypertensive rats; EGCG 10 mg/kg/day for 14 days and nadolol 10 mg/kg on day 14. Limitations: Rat transcription/exposure results; mRNA changes do not establish transporter protein activity or a human effect size. Evidence access: primary abstract. Oral epigallocatechin gallate reduces intestinal nadolol absorption via modulation of Oatp1a5 and Oct1 transcriptional levels in spontaneously hypertensive rats. · 2021 · https://pubmed.ncbi.nlm.nih.gov/34303263/ · DOI 10.1016/j.phymed.2021.153623
Complete structured claim and evidence
EGCG pretreatment reduced the specified transporter mRNA by a reported 2.66-fold.
Epigallocatechin-3-gallate (EGCG) → Rat hepatic Oct1 mRNA expression source_derived_draftungraded
Experimental context and source evidence
experimental_model
Male spontaneously hypertensive rats; EGCG 10 mg/kg/day for 14 days and nadolol 10 mg/kg on day 14.
limitations
Rat transcription/exposure results; mRNA changes do not establish transporter protein activity or a human effect size.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
The study measured a transporter-expression change.
primary_references
Oral epigallocatechin gallate reduces intestinal nadolol absorption via modulation of Oatp1a5 and Oct1 transcriptional levels in spontaneously hypertensive rats. · 2021 · https://pubmed.ncbi.nlm.nih.gov/34303263/ · DOI 10.1016/j.phymed.2021.153623
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 524–530
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Male spontaneously hypertensive rats; EGCG 10 mg/kg/day for 14 days and nadolol 10 mg/kg on day 14. · source_derived_draft · unverified_draft
## egcg-hepatic-oct The study measured a transporter-expression change. EGCG pretreatment reduced the specified transporter mRNA by a reported 2.66-fold. Model: Male spontaneously hypertensive rats; EGCG 10 mg/kg/day for 14 days and nadolol 10 mg/kg on day 14. Limitations: Rat transcription/exposure results; mRNA changes do not establish transporter protein activity or a human effect size. Evidence access: primary abstract. Oral epigallocatechin gallate reduces intestinal nadolol absorption via modulation of Oatp1a5 and Oct1 transcriptional levels in spontaneously hypertensive rats. · 2021 · https://pubmed.ncbi.nlm.nih.gov/34303263/ · DOI 10.1016/j.phymed.2021.153623
Complete structured claim and evidence
EGCG pretreatment reduced the specified transporter mRNA by a reported 2.61-fold.
Epigallocatechin-3-gallate (EGCG) → Rat hepatic P-glycoprotein mRNA expression source_derived_draftungraded
Experimental context and source evidence
experimental_model
Male spontaneously hypertensive rats; EGCG 10 mg/kg/day for 14 days and nadolol 10 mg/kg on day 14.
limitations
Rat transcription/exposure results; mRNA changes do not establish transporter protein activity or a human effect size.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
The study measured a transporter-expression change.
primary_references
Oral epigallocatechin gallate reduces intestinal nadolol absorption via modulation of Oatp1a5 and Oct1 transcriptional levels in spontaneously hypertensive rats. · 2021 · https://pubmed.ncbi.nlm.nih.gov/34303263/ · DOI 10.1016/j.phymed.2021.153623
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 532–538
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Male spontaneously hypertensive rats; EGCG 10 mg/kg/day for 14 days and nadolol 10 mg/kg on day 14. · source_derived_draft · unverified_draft
## egcg-hepatic-pgp The study measured a transporter-expression change. EGCG pretreatment reduced the specified transporter mRNA by a reported 2.61-fold. Model: Male spontaneously hypertensive rats; EGCG 10 mg/kg/day for 14 days and nadolol 10 mg/kg on day 14. Limitations: Rat transcription/exposure results; mRNA changes do not establish transporter protein activity or a human effect size. Evidence access: primary abstract. Oral epigallocatechin gallate reduces intestinal nadolol absorption via modulation of Oatp1a5 and Oct1 transcriptional levels in spontaneously hypertensive rats. · 2021 · https://pubmed.ncbi.nlm.nih.gov/34303263/ · DOI 10.1016/j.phymed.2021.153623
Complete structured claim and evidence
In the 12-month randomized trial, 26/513 extract recipients (5.1%) developed moderate-or-greater liver-test abnormalities; odds ratio versus placebo was 7.0 (95% CI 2.4–20.3).
Green tea extract, study-specific mixture → Serum liver-enzyme elevations source_derived_draftungraded
Experimental context and source evidence
experimental_model
1021 analyzed women with normal baseline enzymes; 513 extract and 508 placebo.
limitations
An extract trial does not isolate EGCG as the sole causal constituent or estimate risk from ordinary tea drinking.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
Concentrated extract increased liver-test abnormalities in this trial.
primary_references
Effect of Green Tea Supplements on Liver Enzyme Elevation: Results from a Randomized Intervention Study in the United States. · 2017 · https://pubmed.ncbi.nlm.nih.gov/28765194/ · DOI 10.1158/1940-6207.capr-17-0160
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 540–546
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · 1021 analyzed women with normal baseline enzymes; 513 extract and 508 placebo. · source_derived_draft · unverified_draft
## egcg-liver-rct Concentrated extract increased liver-test abnormalities in this trial. In the 12-month randomized trial, 26/513 extract recipients (5.1%) developed moderate-or-greater liver-test abnormalities; odds ratio versus placebo was 7.0 (95% CI 2.4–20.3). Model: 1021 analyzed women with normal baseline enzymes; 513 extract and 508 placebo. Limitations: An extract trial does not isolate EGCG as the sole causal constituent or estimate risk from ordinary tea drinking. Evidence access: primary abstract. Effect of Green Tea Supplements on Liver Enzyme Elevation: Results from a Randomized Intervention Study in the United States. · 2017 · https://pubmed.ncbi.nlm.nih.gov/28765194/ · DOI 10.1158/1940-6207.capr-17-0160
Complete structured claim and evidence
ALT decreased after stopping extract and increased after rechallenge in affected participants.
Green tea extract, study-specific mixture → Serum liver-enzyme elevations source_derived_draftungraded
Experimental context and source evidence
experimental_model
Trial dechallenge/rechallenge observations.
limitations
These observations do not establish a single molecular injury pathway.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
Stopping and restarting strengthened the link to the extract.
primary_references
Effect of Green Tea Supplements on Liver Enzyme Elevation: Results from a Randomized Intervention Study in the United States. · 2017 · https://pubmed.ncbi.nlm.nih.gov/28765194/ · DOI 10.1158/1940-6207.capr-17-0160
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 548–554
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Trial dechallenge/rechallenge observations. · source_derived_draft · unverified_draft
## egcg-liver-rechallenge Stopping and restarting strengthened the link to the extract. ALT decreased after stopping extract and increased after rechallenge in affected participants. Model: Trial dechallenge/rechallenge observations. Limitations: These observations do not establish a single molecular injury pathway. Evidence access: primary abstract. Effect of Green Tea Supplements on Liver Enzyme Elevation: Results from a Randomized Intervention Study in the United States. · 2017 · https://pubmed.ncbi.nlm.nih.gov/28765194/ · DOI 10.1158/1940-6207.capr-17-0160
Complete structured claim and evidence
HLA-B*35:01 was present in 72% of 40 adjudicated green-tea liver-injury cases, versus 11% in population controls.
Human HLA-B*35:01 allele → Green-tea-associated liver injury source_derived_draftungraded
Experimental context and source evidence
experimental_model
Drug-Induced Liver Injury Network selected case series; 95% hepatocellular, 35% severe, three transplants.
limitations
Selected cases are not an incidence estimate; association does not prove antigen presentation or deterministic injury in carriers.
nutrient_topic
EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
plain_language
A genetic association suggests an immune contribution to some liver injuries.
primary_references
HLA-B*35:01 and Green Tea-Induced Liver Injury. · 2021 · https://pubmed.ncbi.nlm.nih.gov/32892374/ · DOI 10.1002/hep.31538
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 556–562
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Drug-Induced Liver Injury Network selected case series; 95% hepatocellular, 35% severe, three transplants. · source_derived_draft · unverified_draft
## egcg-hla A genetic association suggests an immune contribution to some liver injuries. HLA-B*35:01 was present in 72% of 40 adjudicated green-tea liver-injury cases, versus 11% in population controls. Model: Drug-Induced Liver Injury Network selected case series; 95% hepatocellular, 35% severe, three transplants. Limitations: Selected cases are not an incidence estimate; association does not prove antigen presentation or deterministic injury in carriers. Evidence access: primary abstract. HLA-B*35:01 and Green Tea-Induced Liver Injury. · 2021 · https://pubmed.ncbi.nlm.nih.gov/32892374/ · DOI 10.1002/hep.31538
Complete structured claim and evidence
Human soluble COMT structures resolve bound SAM.
Human catechol O-methyltransferase / COMT → S-Adenosyl-L-methionine source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/chlorogenic_acid-research/18486144.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "9cafbfc9353f49fab9919bc64608f21f445ace4b190771e44088a5a746e5a6e3", "start_char": 0, "end_char": 1961, "text_sha256": "9cafbfc9353f49fab9919bc64608f21f445ace4b190771e44088a5a746e5a6e3"}
experimental_model
Human soluble COMT crystallography and deposited structure 3BWM
exposure
SAM and 3,5-dinitrocatechol-bound crystals; deposited Mg ion
limitations
Structural cofactor connection, not a CGA-magnesium supplementation trial. Human and rat COMT specificity differs; deposition includes an inhibitor analog rather than CGA.
nutrient_topic
Chlorogenic acid research collection; topical membership is not evidence of a direct dietary effect. · Chlorogenic acid / 5-O-caffeoylquinic acid
organism
Homo sapiens
plain_language
The shared methyl donor links COMT to methionine-cycle metabolism.
primary_references
[chlorogenic_acid-p18486144] Crystal structures of human 108V and 108M catechol O-methyltransferase. (2008). https://pubmed.ncbi.nlm.nih.gov/18486144/ DOI: 10.1016/j.jmb.2008.04.040
tissue_or_cell_type
Purified soluble COMT
Chlorogenic acid: metabolism, signaling and nutrient connections (2026-09-17) · lines 841–852
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human soluble COMT crystallography and deposited structure 3BWM · source_derived_draft · unverified_draft
### chlorogenic_acid-human-comt-sam Human soluble COMT structures resolve bound SAM. Condition category: normal nutrient_topic: Chlorogenic acid research collection; topical membership is not evidence of a direct dietary effect. plain_language: The shared methyl donor links COMT to methionine-cycle metabolism. organism: Homo sapiens tissue_or_cell_type: Purified soluble COMT experimental_model: Human soluble COMT crystallography and deposited structure 3BWM limitations: Structural cofactor connection, not a CGA-magnesium supplementation trial. Human and rat COMT specificity differs; deposition includes an inhibitor analog rather than CGA. exposure: SAM and 3,5-dinitrocatechol-bound crystals; deposited Mg ion evidence_span: {"source_cache": "artifacts/chlorogenic_acid-research/18486144.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "9cafbfc9353f49fab9919bc64608f21f445ace4b190771e44088a5a746e5a6e3", "start_char": 0, "end_char": 1961, "text_sha256": "9cafbfc9353f49fab9919bc64608f21f445ace4b190771e44088a5a746e5a6e3"} [chlorogenic_acid-p18486144] Crystal structures of human 108V and 108M catechol O-methyltransferase. (2008). https://pubmed.ncbi.nlm.nih.gov/18486144/ DOI: 10.1016/j.jmb.2008.04.040
Complete structured claim and evidence
The human COMT structure 3BWM includes bound magnesium alongside SAM and the catechol analog.
Human catechol O-methyltransferase / COMT → Mg2+ source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/chlorogenic_acid-research/3BWM.cif", "source_url": "https://files.rcsb.org/download/3BWM.cif", "locator": "Primary deposited structure 3BWM chemical-component loop; zero-based end-exclusive Unicode offsets", "file_sha256": "debe2736e6c5affecce595281fac469cd424ab6e91a5d908ec89d9460f60e4f6", "start_char": 11428, "end_char": 13476, "text_sha256": "98319e36f43f3fe147a2b9a2444809c31b0e14ae68e789fe3c1a8303fd8da8bc"}
experimental_model
Human soluble COMT crystallography and deposited structure 3BWM
exposure
SAM and 3,5-dinitrocatechol-bound crystals; deposited Mg ion
limitations
Structural cofactor connection, not a CGA-magnesium supplementation trial. Human and rat COMT specificity differs; deposition includes an inhibitor analog rather than CGA.
nutrient_topic
Chlorogenic acid research collection; topical membership is not evidence of a direct dietary effect. · Chlorogenic acid / 5-O-caffeoylquinic acid
organism
Homo sapiens
plain_language
Magnesium is part of the measured enzyme complex; this does not prove that CGA depletes magnesium.
primary_references
[chlorogenic_acid-p18486144] Crystal structures of human 108V and 108M catechol O-methyltransferase. (2008). https://pubmed.ncbi.nlm.nih.gov/18486144/ DOI: 10.1016/j.jmb.2008.04.040
tissue_or_cell_type
Purified soluble COMT
Chlorogenic acid: metabolism, signaling and nutrient connections (2026-09-17) · lines 854–865
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human soluble COMT crystallography and deposited structure 3BWM · source_derived_draft · unverified_draft
### chlorogenic_acid-human-comt-mg The human COMT structure 3BWM includes bound magnesium alongside SAM and the catechol analog. Condition category: normal nutrient_topic: Chlorogenic acid research collection; topical membership is not evidence of a direct dietary effect. plain_language: Magnesium is part of the measured enzyme complex; this does not prove that CGA depletes magnesium. organism: Homo sapiens tissue_or_cell_type: Purified soluble COMT experimental_model: Human soluble COMT crystallography and deposited structure 3BWM limitations: Structural cofactor connection, not a CGA-magnesium supplementation trial. Human and rat COMT specificity differs; deposition includes an inhibitor analog rather than CGA. exposure: SAM and 3,5-dinitrocatechol-bound crystals; deposited Mg ion evidence_span: {"source_cache": "artifacts/chlorogenic_acid-research/3BWM.cif", "source_url": "https://files.rcsb.org/download/3BWM.cif", "locator": "Primary deposited structure 3BWM chemical-component loop; zero-based end-exclusive Unicode offsets", "file_sha256": "debe2736e6c5affecce595281fac469cd424ab6e91a5d908ec89d9460f60e4f6", "start_char": 11428, "end_char": 13476, "text_sha256": "98319e36f43f3fe147a2b9a2444809c31b0e14ae68e789fe3c1a8303fd8da8bc"} [chlorogenic_acid-p18486144] Crystal structures of human 108V and 108M catechol O-methyltransferase. (2008). https://pubmed.ncbi.nlm.nih.gov/18486144/ DOI: 10.1016/j.jmb.2008.04.040
Complete structured claim and evidence
DHFR reduces folic acid to dihydrofolate before further reduction to tetrahydrofolate.
Human dihydrofolate reductase / DHFR → Folic acid source_derived_draftungraded
Experimental context and source evidence
experimental_model
Fresh human liver extracts from six donors and rat comparison
exposure
Folic acid substrate with NADPH
limitations
Reaction identity; liver rates cannot define a universal intake ceiling.
nutrient_topic
Folate and folic acid research collection; topical membership is not evidence of a direct dietary effect. · Folate (vitamin B9)
organism
Homo sapiens
plain_language
Folic acid needs a reduction step before it becomes usable folate.
primary_references
[bailey2009] The extremely slow and variable activity of dihydrofolate reductase in human liver and its implications for high folic acid intake (2009). https://pubmed.ncbi.nlm.nih.gov/19706381/ DOI: 10.1073/pnas.0902072106
tissue_or_cell_type
Liver enzyme preparations
Folate and folic acid: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 351–361
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Fresh human liver extracts from six donors and rat comparison · source_derived_draft · unverified_draft
### folate-dhfr-folic-acid-first-reduction DHFR reduces folic acid to dihydrofolate before further reduction to tetrahydrofolate. Condition category: normal nutrient_topic: Folate and folic acid research collection; topical membership is not evidence of a direct dietary effect. plain_language: Folic acid needs a reduction step before it becomes usable folate. organism: Homo sapiens tissue_or_cell_type: Liver enzyme preparations experimental_model: Fresh human liver extracts from six donors and rat comparison limitations: Reaction identity; liver rates cannot define a universal intake ceiling. exposure: Folic acid substrate with NADPH [bailey2009] The extremely slow and variable activity of dihydrofolate reductase in human liver and its implications for high folic acid intake (2009). https://pubmed.ncbi.nlm.nih.gov/19706381/ DOI: 10.1073/pnas.0902072106
Complete structured claim and evidence
Human liver DHFR converted 7,8-dihydrofolate to tetrahydrofolate in NADPH-containing assays.
Human dihydrofolate reductase / DHFR → 7,8-Dihydrofolate source_derived_draftungraded
Experimental context and source evidence
experimental_model
Fresh human liver extracts from six donors and rat comparison
exposure
DHF substrate; THF quantified by HPLC
limitations
Assay chemistry, not an outcome study.
nutrient_topic
Folate and folic acid research collection; topical membership is not evidence of a direct dietary effect. · Folate (vitamin B9)
organism
Homo sapiens
plain_language
DHFR regenerates reduced folate from DHF.
primary_references
[bailey2009] The extremely slow and variable activity of dihydrofolate reductase in human liver and its implications for high folic acid intake (2009). https://pubmed.ncbi.nlm.nih.gov/19706381/ DOI: 10.1073/pnas.0902072106
tissue_or_cell_type
Liver extracts
Folate and folic acid: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 363–373
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Fresh human liver extracts from six donors and rat comparison · source_derived_draft · unverified_draft
### folate-dhfr-dhf-recycling Human liver DHFR converted 7,8-dihydrofolate to tetrahydrofolate in NADPH-containing assays. Condition category: normal nutrient_topic: Folate and folic acid research collection; topical membership is not evidence of a direct dietary effect. plain_language: DHFR regenerates reduced folate from DHF. organism: Homo sapiens tissue_or_cell_type: Liver extracts experimental_model: Fresh human liver extracts from six donors and rat comparison limitations: Assay chemistry, not an outcome study. exposure: DHF substrate; THF quantified by HPLC [bailey2009] The extremely slow and variable activity of dihydrofolate reductase in human liver and its implications for high folic acid intake (2009). https://pubmed.ncbi.nlm.nih.gov/19706381/ DOI: 10.1073/pnas.0902072106
Complete structured claim and evidence
Folic-acid reduction per gram of six human livers averaged less than 2% of rat liver activity at physiological pH, with nearly fivefold human variation.
Human dihydrofolate reductase / DHFR → Folic acid source_derived_draftungraded
Experimental context and source evidence
experimental_model
Fresh human liver extracts from six donors and rat comparison
exposure
Matched ex-vivo activity assay
limitations
Small tissue series; neither whole-body clearance nor harm was measured.
nutrient_topic
Folate and folic acid research collection; topical membership is not evidence of a direct dietary effect. · Folate (vitamin B9)
organism
Homo sapiens and Rattus norvegicus comparison
plain_language
Human liver processing was slow and varied between samples.
primary_references
[bailey2009] The extremely slow and variable activity of dihydrofolate reductase in human liver and its implications for high folic acid intake (2009). https://pubmed.ncbi.nlm.nih.gov/19706381/ DOI: 10.1073/pnas.0902072106
tissue_or_cell_type
Fresh liver extracts
Folate and folic acid: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 375–385
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Fresh human liver extracts from six donors and rat comparison · source_derived_draft · unverified_draft
### folate-human-liver-folic-acid-slow-processing Folic-acid reduction per gram of six human livers averaged less than 2% of rat liver activity at physiological pH, with nearly fivefold human variation. Condition category: normal nutrient_topic: Folate and folic acid research collection; topical membership is not evidence of a direct dietary effect. plain_language: Human liver processing was slow and varied between samples. organism: Homo sapiens and Rattus norvegicus comparison tissue_or_cell_type: Fresh liver extracts experimental_model: Fresh human liver extracts from six donors and rat comparison limitations: Small tissue series; neither whole-body clearance nor harm was measured. exposure: Matched ex-vivo activity assay [bailey2009] The extremely slow and variable activity of dihydrofolate reductase in human liver and its implications for high folic acid intake (2009). https://pubmed.ncbi.nlm.nih.gov/19706381/ DOI: 10.1073/pnas.0902072106
Complete structured claim and evidence
DHFR knockdown decreased intracellular BH4 and increased BH2 in the cell systems.
Mouse endothelial Dhfr knockdown → Endothelial BH4-to-BH2 ratio, model specified source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/citrulline-research/19666465.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "b1ef76ebbd312932011edd1b0f9f428026a4e4cdd53301bd66f99eaf543e77af", "start_char": 0, "end_char": 1716, "text_sha256": "b1ef76ebbd312932011edd1b0f9f428026a4e4cdd53301bd66f99eaf543e77af"}
experimental_model
DHFR knockdown/inhibition and controlled GTPCH-expression cell experiments
exposure
Methotrexate or RNA interference; comparison with GTPCH knockdown
limitations
Mouse models; DHFR also handles folate, but this study does not make folate and BH4 interchangeable.
nutrient_topic
Citrulline research collection; topical membership is not evidence of a direct dietary effect. · L-Citrulline
organism
Mouse endothelial and NIH-3T3-based experimental cell systems
plain_language
Recycling quality matters, not just the total amount of pterin.
primary_references
[citrulline-p19666465] Critical role for tetrahydrobiopterin recycling by dihydrofolate reductase in regulation of endothelial nitric-oxide synthase coupling: relative importance of the de novo biopterin synthesis versus salvage pathways. (2009). https://pubmed.ncbi.nlm.nih.gov/19666465/ DOI: 10.1074/jbc.m109.041483
tissue_or_cell_type
BH4/BH2 balance and NOS coupling
trigger_kind
machinery_impairment Imported condition classification; unverified.
Citrulline: arginine recycling, nitrogen disposal and nutrient connections (2026-09-17) · lines 775–786
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · DHFR knockdown/inhibition and controlled GTPCH-expression cell experiments · source_derived_draft · unverified_draft
### citrulline-dhfr-ratio DHFR knockdown decreased intracellular BH4 and increased BH2 in the cell systems. Condition category: machinery_impairment nutrient_topic: Citrulline research collection; topical membership is not evidence of a direct dietary effect. plain_language: Recycling quality matters, not just the total amount of pterin. organism: Mouse endothelial and NIH-3T3-based experimental cell systems tissue_or_cell_type: BH4/BH2 balance and NOS coupling experimental_model: DHFR knockdown/inhibition and controlled GTPCH-expression cell experiments limitations: Mouse models; DHFR also handles folate, but this study does not make folate and BH4 interchangeable. exposure: Methotrexate or RNA interference; comparison with GTPCH knockdown evidence_span: {"source_cache": "artifacts/citrulline-research/19666465.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "b1ef76ebbd312932011edd1b0f9f428026a4e4cdd53301bd66f99eaf543e77af", "start_char": 0, "end_char": 1716, "text_sha256": "b1ef76ebbd312932011edd1b0f9f428026a4e4cdd53301bd66f99eaf543e77af"} [citrulline-p19666465] Critical role for tetrahydrobiopterin recycling by dihydrofolate reductase in regulation of endothelial nitric-oxide synthase coupling: relative importance of the de novo biopterin synthesis versus salvage pathways. (2009). https://pubmed.ncbi.nlm.nih.gov/19666465/ DOI: 10.1074/jbc.m109.041483
Complete structured claim and evidence
DHFR loss increased eNOS-dependent superoxide while reducing NO production.
Mouse endothelial Dhfr knockdown → Endothelial nitric oxide synthase uncoupling, model specified source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/citrulline-research/19666465.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "b1ef76ebbd312932011edd1b0f9f428026a4e4cdd53301bd66f99eaf543e77af", "start_char": 0, "end_char": 1716, "text_sha256": "b1ef76ebbd312932011edd1b0f9f428026a4e4cdd53301bd66f99eaf543e77af"}
experimental_model
DHFR knockdown/inhibition and controlled GTPCH-expression cell experiments
exposure
Methotrexate or RNA interference; comparison with GTPCH knockdown
limitations
Mouse models; DHFR also handles folate, but this study does not make folate and BH4 interchangeable.
nutrient_topic
Citrulline research collection; topical membership is not evidence of a direct dietary effect. · L-Citrulline
organism
Mouse endothelial and NIH-3T3-based experimental cell systems
plain_language
A damaged cofactor balance can change the enzyme output.
primary_references
[citrulline-p19666465] Critical role for tetrahydrobiopterin recycling by dihydrofolate reductase in regulation of endothelial nitric-oxide synthase coupling: relative importance of the de novo biopterin synthesis versus salvage pathways. (2009). https://pubmed.ncbi.nlm.nih.gov/19666465/ DOI: 10.1074/jbc.m109.041483
tissue_or_cell_type
BH4/BH2 balance and NOS coupling
trigger_kind
machinery_impairment Imported condition classification; unverified.
Citrulline: arginine recycling, nitrogen disposal and nutrient connections (2026-09-17) · lines 788–799
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · DHFR knockdown/inhibition and controlled GTPCH-expression cell experiments · source_derived_draft · unverified_draft
### citrulline-dhfr-uncoupling DHFR loss increased eNOS-dependent superoxide while reducing NO production. Condition category: machinery_impairment nutrient_topic: Citrulline research collection; topical membership is not evidence of a direct dietary effect. plain_language: A damaged cofactor balance can change the enzyme output. organism: Mouse endothelial and NIH-3T3-based experimental cell systems tissue_or_cell_type: BH4/BH2 balance and NOS coupling experimental_model: DHFR knockdown/inhibition and controlled GTPCH-expression cell experiments limitations: Mouse models; DHFR also handles folate, but this study does not make folate and BH4 interchangeable. exposure: Methotrexate or RNA interference; comparison with GTPCH knockdown evidence_span: {"source_cache": "artifacts/citrulline-research/19666465.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "b1ef76ebbd312932011edd1b0f9f428026a4e4cdd53301bd66f99eaf543e77af", "start_char": 0, "end_char": 1716, "text_sha256": "b1ef76ebbd312932011edd1b0f9f428026a4e4cdd53301bd66f99eaf543e77af"} [citrulline-p19666465] Critical role for tetrahydrobiopterin recycling by dihydrofolate reductase in regulation of endothelial nitric-oxide synthase coupling: relative importance of the de novo biopterin synthesis versus salvage pathways. (2009). https://pubmed.ncbi.nlm.nih.gov/19666465/ DOI: 10.1074/jbc.m109.041483
Complete structured claim and evidence
Added ascorbic acid significantly counteracted the inhibition of radiolabeled nonheme iron absorption caused by sodium phytate in wheat-roll meals.
L-Ascorbic acid → Nonheme iron absorption source_derived_draftungraded
Experimental context and source evidence
cross_nutrient
Meal composition modifies the vitamin C/iron interaction.
experimental_model
Human alternate-day paired radiolabeled wheat-roll experiments.
exposure
Seven sodium phytate levels spanning 2–250 mg expressed as phytate phosphorus, with and without ascorbic acid; 55Fe/59Fe labels. Exact C dose and participant count are not extracted from the abstract.
limitations
Single-meal tracer result; does not prove full cancellation of inhibition or long-term correction of anemia.
nutrient_topic
Vitamin C research collection; topical membership is not evidence of a direct dietary effect. · Vitamin C
organism
Homo sapiens
plain_language
Vitamin C helped offset an iron-absorption inhibitor in the tested meals.
primary_references
[c-hallberg1989] Iron absorption in man: ascorbic acid and dose-dependent inhibition by phytate (1989). https://pubmed.ncbi.nlm.nih.gov/2911999/ DOI: 10.1093/ajcn/49.1.140
tissue_or_cell_type
Human blood or whole-person endpoints
Vitamin C: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 1580–1591
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human alternate-day paired radiolabeled wheat-roll experiments. · source_derived_draft · unverified_draft
### c-phytate-iron-inhibition-counteraction Added ascorbic acid significantly counteracted the inhibition of radiolabeled nonheme iron absorption caused by sodium phytate in wheat-roll meals. Condition category: normal nutrient_topic: Vitamin C research collection; topical membership is not evidence of a direct dietary effect. plain_language: Vitamin C helped offset an iron-absorption inhibitor in the tested meals. organism: Homo sapiens tissue_or_cell_type: Human blood or whole-person endpoints experimental_model: Human alternate-day paired radiolabeled wheat-roll experiments. limitations: Single-meal tracer result; does not prove full cancellation of inhibition or long-term correction of anemia. exposure: Seven sodium phytate levels spanning 2–250 mg expressed as phytate phosphorus, with and without ascorbic acid; 55Fe/59Fe labels. Exact C dose and participant count are not extracted from the abstract. cross_nutrient: Meal composition modifies the vitamin C/iron interaction. [c-hallberg1989] Iron absorption in man: ascorbic acid and dose-dependent inhibition by phytate (1989). https://pubmed.ncbi.nlm.nih.gov/2911999/ DOI: 10.1093/ajcn/49.1.140
Complete structured claim and evidence
Iron absorption was significantly higher when tea was consumed one hour after the meal than when consumed simultaneously (P=0.046).
Nonheme dietary iron → Nonheme iron absorption source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/iron-research/29046302.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "3a01f467e543b56e182ef6acfe15ca9d65474590ef9490bc698f864765588366", "start_char": 0, "end_char": 1971, "text_sha256": "3a01f467e543b56e182ef6acfe15ca9d65474590ef9490bc698f864765588366"}
experimental_model
Three-period stable-isotope meal experiment
exposure
Labeled porridge with water, simultaneous tea or tea one hour later
limitations
Acute fractional absorption endpoint; not a long-term anemia trial or proof that all tea preparations have equal effects.
nutrient_topic
Iron research collection; topical membership is not evidence of a direct dietary effect. · Iron
organism
12 iron-replete nonanemic women
plain_language
The timing of a meal inhibitor changed how much iron was absorbed.
primary_references
[iron-p29046302] A 1-h time interval between a meal containing iron and consumption of tea attenuates the inhibitory effects on iron absorption: a controlled trial in a cohort of healthy UK women using a stable iron isotope. (2017). https://pubmed.ncbi.nlm.nih.gov/29046302/ DOI: 10.3945/ajcn.117.161364
tissue_or_cell_type
Intestinal nonheme iron absorption
Iron: absorption, trafficking, iron-dependent enzymes and nutrient interactions (2026-09-17) · lines 1005–1016
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Three-period stable-isotope meal experiment · source_derived_draft · unverified_draft
### iron-tea-timing Iron absorption was significantly higher when tea was consumed one hour after the meal than when consumed simultaneously (P=0.046). Condition category: normal nutrient_topic: Iron research collection; topical membership is not evidence of a direct dietary effect. plain_language: The timing of a meal inhibitor changed how much iron was absorbed. organism: 12 iron-replete nonanemic women tissue_or_cell_type: Intestinal nonheme iron absorption experimental_model: Three-period stable-isotope meal experiment limitations: Acute fractional absorption endpoint; not a long-term anemia trial or proof that all tea preparations have equal effects. exposure: Labeled porridge with water, simultaneous tea or tea one hour later evidence_span: {"source_cache": "artifacts/iron-research/29046302.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "3a01f467e543b56e182ef6acfe15ca9d65474590ef9490bc698f864765588366", "start_char": 0, "end_char": 1971, "text_sha256": "3a01f467e543b56e182ef6acfe15ca9d65474590ef9490bc698f864765588366"} [iron-p29046302] A 1-h time interval between a meal containing iron and consumption of tea attenuates the inhibitory effects on iron absorption: a controlled trial in a cohort of healthy UK women using a stable iron isotope. (2017). https://pubmed.ncbi.nlm.nih.gov/29046302/ DOI: 10.3945/ajcn.117.161364
Complete structured claim and evidence
COMT-mediated O-methylation of CGA contributed to the coupled-assay response.
COMT preparation used in dietary-catechol methylation assay, organism not specified in abstract → Chlorogenic acid / 5-O-caffeoylquinic acid source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/chlorogenic_acid-research/16081510.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e93fafd7946f8a4aea30ff3ee9ef05e303f9154eb947410fca8e63c6521a4170", "start_char": 0, "end_char": 2008, "text_sha256": "e93fafd7946f8a4aea30ff3ee9ef05e303f9154eb947410fca8e63c6521a4170"}
experimental_model
Coupled catechol-methylation/DNA-methylation assays and breast-cancer cell experiments
exposure
CGA DNMT1 IC50 0.9 micromolar in the coupled assay; compounds tested up to 20 micromolar
limitations
These concentrations and coupled-reaction conditions do not establish whole-body methyl-donor depletion, anticancer benefit or vitamin deficiency after food intake. COMT-mediated SAH generation is distinct from direct competitive binding to DNMT1.
nutrient_topic
Chlorogenic acid research collection; topical membership is not evidence of a direct dietary effect. · Chlorogenic acid / 5-O-caffeoylquinic acid
organism
Human DNMT1 and MCF-7/MDA-MB-231 cells; COMT preparation species unresolved in abstract
plain_language
Metabolizing a catechol connects it to methyl-group chemistry.
primary_references
[chlorogenic_acid-p16081510] Inhibition of DNA methylation by caffeic acid and chlorogenic acid, two common catechol-containing coffee polyphenols. (2006). https://pubmed.ncbi.nlm.nih.gov/16081510/ DOI: 10.1093/carcin/bgi206
tissue_or_cell_type
Cell-free methyltransferase reactions and cultured cancer cells
Chlorogenic acid: metabolism, signaling and nutrient connections (2026-09-17) · lines 776–787
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Coupled catechol-methylation/DNA-methylation assays and breast-cancer cell experiments · source_derived_draft · unverified_draft
### chlorogenic_acid-comt-cga COMT-mediated O-methylation of CGA contributed to the coupled-assay response. Condition category: normal nutrient_topic: Chlorogenic acid research collection; topical membership is not evidence of a direct dietary effect. plain_language: Metabolizing a catechol connects it to methyl-group chemistry. organism: Human DNMT1 and MCF-7/MDA-MB-231 cells; COMT preparation species unresolved in abstract tissue_or_cell_type: Cell-free methyltransferase reactions and cultured cancer cells experimental_model: Coupled catechol-methylation/DNA-methylation assays and breast-cancer cell experiments limitations: These concentrations and coupled-reaction conditions do not establish whole-body methyl-donor depletion, anticancer benefit or vitamin deficiency after food intake. COMT-mediated SAH generation is distinct from direct competitive binding to DNMT1. exposure: CGA DNMT1 IC50 0.9 micromolar in the coupled assay; compounds tested up to 20 micromolar evidence_span: {"source_cache": "artifacts/chlorogenic_acid-research/16081510.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e93fafd7946f8a4aea30ff3ee9ef05e303f9154eb947410fca8e63c6521a4170", "start_char": 0, "end_char": 2008, "text_sha256": "e93fafd7946f8a4aea30ff3ee9ef05e303f9154eb947410fca8e63c6521a4170"} [chlorogenic_acid-p16081510] Inhibition of DNA methylation by caffeic acid and chlorogenic acid, two common catechol-containing coffee polyphenols. (2006). https://pubmed.ncbi.nlm.nih.gov/16081510/ DOI: 10.1093/carcin/bgi206
Complete structured claim and evidence
SULT1A1 had the strongest tested sulfating activity toward 6-hydroxymelatonin.
Human sulfotransferase 1A1 / SULT1A1 → 6-Sulfatoxymelatonin / aMT6s source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/melatonin-research/26577053.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "ab887dc7012d5f393de52ecf842b67282d51b61bac705b9ab187c1a3e24331d5", "start_char": 0, "end_char": 1378, "text_sha256": "ab887dc7012d5f393de52ecf842b67282d51b61bac705b9ab187c1a3e24331d5"}
experimental_model
Thirteen human SULT enzymes, labeled cells and tissue cytosols
exposure
6-hydroxymelatonin and N-acetylserotonin substrates; sulfate metabolic labeling
limitations
Enzyme ranking applies to tested conditions. Sulfation is a separate step from P450 hydroxylation; no dietary sulfur threshold was established.
nutrient_topic
Melatonin research collection; topical membership is not evidence of a direct dietary effect. · Melatonin
organism
Human recombinant enzymes, HepG2 and Caco-2 cells
plain_language
The hydroxylated metabolite undergoes another reaction before common urinary measurement.
primary_references
[melatonin-p26577053] Sulfation of 6-hydroxymelatonin, N-acetylserotonin and 4-hydroxyramelteon by the human cytosolic sulfotransferases (SULTs). (2016). https://pubmed.ncbi.nlm.nih.gov/26577053/ DOI: 10.3109/00498254.2015.1107656
tissue_or_cell_type
Sulfate conjugation
Melatonin: synthesis, receptors, circadian timing and nutrient interactions (2026-09-17) · lines 630–641
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Thirteen human SULT enzymes, labeled cells and tissue cytosols · source_derived_draft · unverified_draft
### melatonin-sult1a1 SULT1A1 had the strongest tested sulfating activity toward 6-hydroxymelatonin. Condition category: normal nutrient_topic: Melatonin research collection; topical membership is not evidence of a direct dietary effect. plain_language: The hydroxylated metabolite undergoes another reaction before common urinary measurement. organism: Human recombinant enzymes, HepG2 and Caco-2 cells tissue_or_cell_type: Sulfate conjugation experimental_model: Thirteen human SULT enzymes, labeled cells and tissue cytosols limitations: Enzyme ranking applies to tested conditions. Sulfation is a separate step from P450 hydroxylation; no dietary sulfur threshold was established. exposure: 6-hydroxymelatonin and N-acetylserotonin substrates; sulfate metabolic labeling evidence_span: {"source_cache": "artifacts/melatonin-research/26577053.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "ab887dc7012d5f393de52ecf842b67282d51b61bac705b9ab187c1a3e24331d5", "start_char": 0, "end_char": 1378, "text_sha256": "ab887dc7012d5f393de52ecf842b67282d51b61bac705b9ab187c1a3e24331d5"} [melatonin-p26577053] Sulfation of 6-hydroxymelatonin, N-acetylserotonin and 4-hydroxyramelteon by the human cytosolic sulfotransferases (SULTs). (2016). https://pubmed.ncbi.nlm.nih.gov/26577053/ DOI: 10.3109/00498254.2015.1107656
Complete structured claim and evidence
Human SULT1A1 catalyzed curcumin sulfation.
Human sulfotransferase 1A1 / SULT1A1 → Curcumin sulfate source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/curcumin-research/11815407.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "028fbc6d7e7e728f7e52970df07c8e9b04053abe4799669798d593369d2c23b8", "start_char": 0, "end_char": 2113, "text_sha256": "028fbc6d7e7e728f7e52970df07c8e9b04053abe4799669798d593369d2c23b8"}
experimental_model
Human and rat tissue fractions and enzyme assays
exposure
Curcumin incubated with tissue fractions or purified sulfotransferases
limitations
Ex-vivo metabolism does not measure whole-person bioavailability. Isoforms are specified only where experimentally identified.
nutrient_topic
Curcumin research collection; topical membership is not evidence of a direct dietary effect. · Curcumin
organism
Human assays below; rat experiments not merged
plain_language
This enzyme adds a sulfate group to curcumin.
primary_references
[curcumin-p11815407] Metabolism of the cancer chemopreventive agent curcumin in human and rat intestine. (2002). https://pubmed.ncbi.nlm.nih.gov/11815407/
tissue_or_cell_type
Intestinal and hepatic microsomes and cytosol
Curcumin: metabolism, signaling and nutrient connections (2026-09-17) · lines 112–123
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human and rat tissue fractions and enzyme assays · source_derived_draft · unverified_draft
### curcumin-sult1a1 Human SULT1A1 catalyzed curcumin sulfation. Condition category: normal nutrient_topic: Curcumin research collection; topical membership is not evidence of a direct dietary effect. plain_language: This enzyme adds a sulfate group to curcumin. organism: Human assays below; rat experiments not merged tissue_or_cell_type: Intestinal and hepatic microsomes and cytosol experimental_model: Human and rat tissue fractions and enzyme assays limitations: Ex-vivo metabolism does not measure whole-person bioavailability. Isoforms are specified only where experimentally identified. exposure: Curcumin incubated with tissue fractions or purified sulfotransferases evidence_span: {"source_cache": "artifacts/curcumin-research/11815407.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "028fbc6d7e7e728f7e52970df07c8e9b04053abe4799669798d593369d2c23b8", "start_char": 0, "end_char": 2113, "text_sha256": "028fbc6d7e7e728f7e52970df07c8e9b04053abe4799669798d593369d2c23b8"} [curcumin-p11815407] Metabolism of the cancer chemopreventive agent curcumin in human and rat intestine. (2002). https://pubmed.ncbi.nlm.nih.gov/11815407/
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.

Loss of 67LR/eEF1A/MYPT1 machinery blocks experimental response

Condition: machinery_impairment · Silencing a required signaling component.

Normal role: The intact pathway and nutrient conditions support the comparator response.

Recorded consequence: EGCG-mediated tumor-growth inhibition was abrogated in the reported models.

Scope: Preclinical experiment; inspect linked evidence.

Tollip loss weakens experimental TLR4 inhibition

Condition: machinery_impairment · Tollip RNA interference in macrophages.

Normal role: The intact pathway and nutrient conditions support the comparator response.

Recorded consequence: EGCG inhibition of TLR4 signaling was impaired.

Scope: Preclinical experiment; inspect linked evidence.

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.

Chlorogenic acid: metabolism, signaling 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
Citrulline: arginine recycling, nitrogen disposal 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
Curcumin: metabolism, signaling 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
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18)AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · unverified_draftRead preserved source
Folate and folic acid: 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
Iron: absorption, trafficking, iron-dependent enzymes 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
Melatonin: synthesis, receptors, circadian timing 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
Vitamin C: 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.

EGCG and SULT1A1: opposing substrate assignmentsThe 2016 paper explicitly reports EGCG is not a SULT1A1 substrate; the 2022 paper assigns hepatic sulfation to SULT1A1. These are competing published substrate assignments, not an authoring correction.Read the recorded disagreement
EGCG plus bortezomib: antagonism versus potentiation in preclinical studiesTwo 2009 studies report opposing combination outcomes, including myeloma models. They were not matched for concentration, timing or cell system, so this is an unresolved literature disagreement rather than proof of same-condition incompatibility.Read the recorded disagreement

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

Epigallocatechin-3-gallate (EGCG)

The mechanisms

Surface plasmon resonance supported nanomolar-affinity EGCG binding to 67LR; receptor expression conferred cellular responsiveness.

A genetic screen identified eEF1A as a component of 67LR-dependent EGCG signaling.

EGCG dephosphorylated MYPT1 Thr696 through 67LR and eEF1A.

MYPT1 dephosphorylation accompanied activation of myosin phosphatase.

Silencing MYPT1, eEF1A or 67LR abrogated EGCG-mediated tumor-growth inhibition in the tested models.

EGCG activation of 67LR increased cGMP, a rate-limiting signal for cell death in the model.

The cGMP-dependent death pathway engaged PKC delta and acid sphingomyelinase.

Acid sphingomyelinase participated downstream of PKC delta in 67LR-dependent cell death.

Overexpressed PDE5 attenuated the cGMP-dependent anticancer signal.

PDE5 inhibition with vardenafil potentiated EGCG-dependent apoptosis and prolonged survival in a mouse xenograft experiment.

EGCG rapidly increased Tollip expression; 67LR silencing or antibody blockade prevented this.

EGCG reduced TLR4 expression through 67LR.

Tollip silencing impaired EGCG inhibition of TLR4 signaling.

EGCG inhibited bovine DHFR with slow tight binding, Ki 0.109 micromolar.

Chicken DHFR showed reversible competitive inhibition, Ki 10.3 micromolar.

Folate depletion increased lymphoma-cell sensitivity to EGCG; the reported growth IC50 was 20 micromolar.

Hypoxanthine plus thymidine attenuated EGCG growth inhibition, consistent with involvement of folate-dependent nucleotide supply.

In 39 women studied for 30 days, folate stayed in the normal range across EGCG-containing-extract groups, including groups receiving clomiphene or letrozole.

EGCG inhibited human liver cytosolic COMT-mediated catechol-estrogen methylation, IC50 0.07 micromolar, with mixed inhibition.

4″-O-methyl-EGCG retained COMT inhibitory activity, IC50 0.10 micromolar.

After 750 mg EGCG in 24 volunteers, erythrocyte COMT activity increased by 24% at two hours rather than decreasing.

In 30 women with low iron stores, 150 and 300 mg EGCG reduced relative nonheme-iron absorption by 14% and 27%; the 300 mg comparison with placebo was significant.

EGCG inhibited chicken liver FAS through rapid reversible and slower irreversible components; rapid 50% inhibition occurred at 52 micromolar.

NADPH protected against inhibition, and ketoacyl-reductase experiments supported competition near the NADPH-binding function.

EGCG showed ATP-competitive inhibition with Ki 380 nanomolar in the reported enzyme assay.

EGCG showed ATP-competitive inhibition with Ki 320 nanomolar in the reported enzyme assay.

EGCG reduced AKT Ser473 phosphorylation alongside proliferation in the tested cancer cells.

The kinase panel reported EGCG inhibition with IC50 0.33 micromolar.

The kinase panel reported EGCG inhibition with IC50 1.0 micromolar.

EGCG competitively inhibited DNMT activity in nuclear extracts, Ki 6.89 micromolar.

At 5–50 micromolar for 12–144 hours, EGCG reduced methylation-specific signals at p16, RARbeta, MGMT and hMLH1 promoters in KYSE 510 cells.

The promoter changes accompanied gene mRNA re-expression; RARbeta and hMLH1 protein re-expression was detected.

The 2022 study assigned hepatic EGCG sulfation to SULT1A1.

The same study assigned intestinal EGCG sulfation to SULT1A3.

Human plasma EGCG-4″-sulfate Cmax was 177.9 nM versus 233.5 nM free EGCG; AUC was 715.2 versus 664.1 nM·h.

The 2016 SULT1A1 allostery study explicitly reported that EGCG was not a SULT1A1 substrate but was sulfonated by SULT2A1.

EGCG stabilized the closed SULT1A1 active-site cap, slowed nucleotide release and inhibited turnover; nucleotide-bound enzyme showed 17-fold tighter EGCG binding.

Human fecal fermentation converted EGCG through ester hydrolysis, ring opening/fission and subsequent reactions to phenolic acids, including 4-phenylbutyric and hydroxyphenylpropionic acids.

EGCG-exposed fermentations showed increases in Bacteroides, Christensenellaceae and Bifidobacterium and decreases in selected other taxa.

EGCG-associated peroxide formation and CHO cytotoxicity differed substantially among seven culture media.

Added catalase substantially reduced EGCG cytotoxicity in the culture comparison.

EGCG bound unfolded amyloid-beta and alpha-synuclein and redirected assembly toward unstructured, relatively nontoxic oligomers in the experimental system.

EGCG bound mature fibrils and remodeled them into smaller amorphous aggregates without measured release of monomers or small diffusible oligomers.

EGCG bound mature fibrils and remodeled them into smaller amorphous aggregates without measured release of monomers or small diffusible oligomers.

Remodeled aggregates had lower toxicity in the tested cell assay.

Remodeling of the tested mature amyloid preparations depended on EGCG autooxidation.

Both oxidized and unoxidized EGCG bound fibrils and prevented Thioflavin T binding.

EGCG blocked bortezomib-mediated anticancer effects in the reported models.

Direct EGCG–bortezomib reaction prevented proteasome inhibition and downstream stress/death responses; tested nonboronic inhibitors did not show the same antagonism.

NMR and cell experiments characterized boronate and borate EGCG–bortezomib derivatives; adduct stability depended on structural features.

A separate 2009 KM3 myeloma-cell study reported synergistic apoptosis with EGCG plus bortezomib.

In CWR22 xenografts, EGCG above 200 micromolar at bortezomib administration abolished measured antitumor activity.

At EGCG 11–16 micromolar, the same model showed no antagonism; tumor-growth inhibition was 63.5% versus 53.9–58.9% with bortezomib alone.

Oral vitamin C at 40 or 500 mg/kg did not antagonize bortezomib in the same mouse experiment.

Adding 30 mg ascorbic acid to 250 mL tea increased EGCG recovery after simulated digestion to 54%, versus at most 10% without protective formulation.

In a 30-person crossover study, fasting produced more than 3.5-fold higher free-EGCG peak concentrations than fed administration.

After 700 mL/day green tea for 14 days, nadolol Cmax and AUC fell by 85.3% and 85.0% in 10 healthy volunteers; renal clearance was unchanged.

Green tea attenuated nadolol-associated blood-pressure reduction in the volunteer study.

Green tea inhibited OATP1A2-mediated nadolol uptake in HEK293 transport assays, supporting a possible intestinal explanation.

EGCG pretreatment reduced rat nadolol Cmax by 53% and AUC by 51%, with weaker blood-pressure control.

EGCG pretreatment reduced the specified transporter mRNA by a reported 4.03-fold.

EGCG pretreatment reduced the specified transporter mRNA by a reported 4.03-fold.

EGCG pretreatment reduced the specified transporter mRNA by a reported 8.01-fold.

EGCG pretreatment reduced the specified transporter mRNA by a reported 2.66-fold.

EGCG pretreatment reduced the specified transporter mRNA by a reported 2.61-fold.

In the 12-month randomized trial, 26/513 extract recipients (5.1%) developed moderate-or-greater liver-test abnormalities; odds ratio versus placebo was 7.0 (95% CI 2.4–20.3).

ALT decreased after stopping extract and increased after rechallenge in affected participants.

HLA-B*35:01 was present in 72% of 40 adjudicated green-tea liver-injury cases, versus 11% in population controls.

Human soluble COMT structures resolve bound SAM.

The human COMT structure 3BWM includes bound magnesium alongside SAM and the catechol analog.

DHFR reduces folic acid to dihydrofolate before further reduction to tetrahydrofolate.

Human liver DHFR converted 7,8-dihydrofolate to tetrahydrofolate in NADPH-containing assays.

Folic-acid reduction per gram of six human livers averaged less than 2% of rat liver activity at physiological pH, with nearly fivefold human variation.

DHFR knockdown decreased intracellular BH4 and increased BH2 in the cell systems.

DHFR loss increased eNOS-dependent superoxide while reducing NO production.

Added ascorbic acid significantly counteracted the inhibition of radiolabeled nonheme iron absorption caused by sodium phytate in wheat-roll meals.

Iron absorption was significantly higher when tea was consumed one hour after the meal than when consumed simultaneously (P=0.046).

COMT-mediated O-methylation of CGA contributed to the coupled-assay response.