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.

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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
Vaidyanathan JB and Walle T Cellular uptake and efflux of the tea flavonoid (-)epicatechin-3-gallate in the human intestinal cell line Caco-2. 2003 J. Pharmacol. Exp. Ther. pmid:12970388
Kadowaki M et al. Presence or absence of a gallate moiety on catechins affects their cellular transport. 2008 J. Pharm. Pharmacol. pmid:18718123
Yokozawa T et al. (-)-Epicatechin 3-O-gallate ameliorates the damages related to peroxynitrite production by mechanisms distinct from those of other free radical inhibitors. 2004 J. Pharm. Pharmacol. pmid:15005882
Nakamura H et al. Green tea catechin inhibits lipopolysaccharide-induced bone resorption in vivo. 2010 J. Periodont. Res. pmid:19602116
Hayes CJ et al. Synthesis and preliminary anticancer activity studies of C4 and C8-modified derivatives of catechin gallate (CG) and epicatechin gallate (ECG). 2006 J. Org. Chem. pmid:17168588
Kobayashi K et al. Strong Inhibition of Secretory Sphingomyelinase by Catechins, Particularly by (-)-Epicatechin 3-O-Gallate and (-)-3'-O-Methylepigallocatechin 3-O-Gallate. 2016 J. Nutr. Sci. Vitaminol. pmid:27264097
Minoda K et al. Influence of the galloyl moiety in tea catechins on binding affinity for human serum albumin. 2010 J. Nutr. Sci. Vitaminol. pmid:21228505
Manna S et al. Tea polyphenols can restrict benzo[a]pyrene-induced lung carcinogenesis by altered expression of p53-associated genes and H-ras, c-myc and cyclin D1. 2009 J. Nutr. Biochem. pmid:18656336
Hosokawa Y et al. Catechins inhibit CXCL10 production from oncostatin M-stimulated human gingival fibroblasts. 2010 J. Nutr. Biochem. pmid:19616927
Zhu W et al. A-type ECG and EGCG dimers disturb the structure of 3T3-L1 cell membrane and strongly inhibit its differentiation by targeting peroxisome proliferator-activated receptor γ with miR-27 involved mechanism. 2015 J. Nutr. Biochem. pmid:26145192