(+)-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
Ikeda I et al. Tea catechins with a galloyl moiety suppress postprandial hypertriacylglycerolemia by delaying lymphatic transport of dietary fat in rats. 2005 J. Nutr. pmid:15671206
Huang CC et al. Protective effects of (-)-epicatechin-3-gallate on UVA-induced damage in HaCaT keratinocytes. 2005 Arch. Dermatol. Res. pmid:15726391
Mukai K et al. Structure-activity relationship of the tocopherol-regeneration reaction by catechins. 2005 Free Radic. Biol. Med. pmid:15808422
Feucht W et al. Flavanols in somatic cell division and male meiosis of tea (Camellia sinensis) anthers. 2005 Plant Biol (Stuttg) pmid:15822012
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
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
Anderson JC et al. Synthesis and antibacterial activity of hydrolytically stable (-)-epicatechin gallate analogues for the modulation of beta-lactam resistance in Staphylococcus aureus. 2005 Bioorg. Med. Chem. Lett. pmid:15863332
El Bedoui J et al. Catechins prevent vascular smooth muscle cell invasion by inhibiting MT1-MMP activity and MMP-2 expression. 2005 Cardiovasc. Res. pmid:15885676
Anger DL et al. Heteroactivation of cytochrome P450 1A1 by teas and tea polyphenols. 2005 Br. J. Pharmacol. pmid:15895106
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