Epicatechin-3-gallate

Epicatechin-3-gallate is a lipid of Polyketides (PK) class. Epicatechin-3-gallate is associated with abnormalities such as Epilepsy and Megalencephaly. The involved functions are known as Docking, Drug Interactions, inhibitors, Oxidation and Inflammation Process. Epicatechin-3-gallate often locates in Solitary microtubule component of centriole or axonemal complex, Palmar surface, Glial and peritoneal. The associated genes with Epicatechin-3-gallate are Homologous Gene and TSC1 gene.

Cross Reference

Introduction

To understand associated biological information of Epicatechin-3-gallate, we collected biological information of abnormalities, associated pathways, cellular/molecular locations, biological functions, related genes/proteins, lipids and common seen animal/experimental models with organized paragraphs from literatures.

What diseases are associated with Epicatechin-3-gallate?

Epicatechin-3-gallate is suspected in Epilepsy, Megalencephaly and other diseases in descending order of the highest number of associated sentences.

Related references are mostly published in these journals:

Disease Cross reference Weighted score Related literature
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Possible diseases from mapped MeSH terms on references

We collected disease MeSH terms mapped to the references associated with Epicatechin-3-gallate

MeSH term MeSH ID Detail
Colonic Neoplasms D003110 161 associated lipids
Cicatrix D002921 9 associated lipids
Total 2

PubChem Associated disorders and diseases

What pathways are associated with Epicatechin-3-gallate

There are no associated biomedical information in the current reference collection.

PubChem Biomolecular Interactions and Pathways

Link to PubChem Biomolecular Interactions and Pathways

What cellular locations are associated with Epicatechin-3-gallate?

Related references are published most in these journals:

Location Cross reference Weighted score Related literatures
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What functions are associated with Epicatechin-3-gallate?


Related references are published most in these journals:

Function Cross reference Weighted score Related literatures

What lipids are associated with Epicatechin-3-gallate?

There are no associated biomedical information in the current reference collection.

What genes are associated with Epicatechin-3-gallate?

Related references are published most in these journals:


Gene Cross reference Weighted score Related literatures

What common seen animal models are associated with Epicatechin-3-gallate?

There are no associated biomedical information in the current reference collection.

NCBI Entrez Crosslinks

All references with Epicatechin-3-gallate

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Authors Title Published Journal PubMed Link
You Y et al. Identification of major phenolic compounds of Chinese water chestnut and their antioxidant activity. 2007 Molecules pmid:17851436
Huang CC et al. (-)-Epicatechin-3-gallate, a green tea polyphenol is a potent agent against UVB-induced damage in HaCaT keratinocytes. 2007 Molecules pmid:17960092
Noda Y and Peterson DG Structure-reactivity relationships of flavan-3-ols on product generation in aqueous glucose/glycine model systems. 2007 J. Agric. Food Chem. pmid:17394338
Thephinlap C et al. Epigallocatechin-3-gallate and epicatechin-3-gallate from green tea decrease plasma non-transferrin bound iron and erythrocyte oxidative stress. 2007 Med Chem pmid:17504202
Kyle JA et al. Effects of infusion time and addition of milk on content and absorption of polyphenols from black tea. 2007 J. Agric. Food Chem. pmid:17489604
Landis-Piwowar KR et al. Methylation suppresses the proteasome-inhibitory function of green tea polyphenols. 2007 J. Cell. Physiol. pmid:17477351
Kusano R et al. Structures of epicatechin gallate trimer and tetramer produced by enzymatic oxidation. 2007 Chem. Pharm. Bull. pmid:18057757
Cho KN et al. Green tea catechin (-)-epicatechin gallate induces tumour suppressor protein ATF3 via EGR-1 activation. 2007 Eur. J. Cancer pmid:17764926
Lo HM et al. Tea polyphenols inhibit rat vascular smooth muscle cell adhesion and migration on collagen and laminin via interference with cell-ECM interaction. 2007 J. Biomed. Sci. pmid:17436062
Sharma SK et al. Green tea catechins potentiate triclosan binding to enoyl-ACP reductase from Plasmodium falciparum (PfENR). 2007 J. Med. Chem. pmid:17263522