(+)-Catechin 3-Gallate

(+)-Catechin 3-Gallate is a lipid of Polyketides (PK) class. (+)-catechin 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. (+)-catechin 3-gallate often locates in Solitary microtubule component of centriole or axonemal complex, Palmar surface, Glial and peritoneal. The associated genes with (+)-Catechin 3-Gallate are Homologous Gene and TSC1 gene.

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Introduction

To understand associated biological information of (+)-Catechin 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 (+)-Catechin 3-Gallate?

(+)-Catechin 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 (+)-Catechin 3-Gallate

MeSH term MeSH ID Detail
Cicatrix D002921 9 associated lipids
Total 1

PubChem Associated disorders and diseases

What pathways are associated with (+)-Catechin 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 (+)-Catechin 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 (+)-Catechin 3-Gallate?


Related references are published most in these journals:

Function Cross reference Weighted score Related literatures

What lipids are associated with (+)-Catechin 3-Gallate?

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

What genes are associated with (+)-Catechin 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 (+)-Catechin 3-Gallate?

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

NCBI Entrez Crosslinks

All references with (+)-Catechin 3-Gallate

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Authors Title Published Journal PubMed Link
Strobel P et al. Myricetin, quercetin and catechin-gallate inhibit glucose uptake in isolated rat adipocytes. 2005 Biochem. J. pmid:15469417
Hong J et al. Effects of purified green and black tea polyphenols on cyclooxygenase- and lipoxygenase-dependent metabolism of arachidonic acid in human colon mucosa and colon tumor tissues. 2001 Biochem. Pharmacol. pmid:11705450
Chen D et al. Inhibition of human liver catechol-O-methyltransferase by tea catechins and their metabolites: structure-activity relationship and molecular-modeling studies. 2005 Biochem. Pharmacol. pmid:15857617
Wu AZ et al. Antiarrhythmic effects of (-)-epicatechin-3-gallate, a novel sodium channel agonist in cultured neonatal rat ventricular myocytes. 2013 Biochem. Pharmacol. pmid:23116965
Wang X et al. The galloyl moiety of green tea catechins is the critical structural feature to inhibit fatty-acid synthase. 2003 Biochem. Pharmacol. pmid:14599562
Ochiai H et al. Epigallocatechin-3-gallate is an inhibitor of Na+, K(+)-ATPase by favoring the E1 conformation. 2009 Biochem. Pharmacol. pmid:19539611
Feng W et al. Green tea catechins are potent sensitizers of ryanodine receptor type 1 (RyR1). 2010 Biochem. Pharmacol. pmid:20471964
Kamihira-Ishijima M et al. Inhibitory mechanism of pancreatic amyloid fibril formation: formation of the complex between tea catechins and the fragment of residues 22-27. 2012 Biochemistry pmid:23205879
Navarro-Perán E et al. Kinetics of the inhibition of bovine liver dihydrofolate reductase by tea catechins: origin of slow-binding inhibition and pH studies. 2005 Biochemistry pmid:15895994
Liu S et al. Theaflavin derivatives in black tea and catechin derivatives in green tea inhibit HIV-1 entry by targeting gp41. 2005 Biochim. Biophys. Acta pmid:15823507