(-)-Epigallocatechin

(-)-Epigallocatechin is a lipid of Polyketides (PK) class. The involved functions are known as Protective Agents, inhibitors, Process, Drug Kinetics and Fermentation. (-)-epigallocatechin often locates in Hepatic, Blood, Membrane, Back and apical membrane. The associated genes with (-)-Epigallocatechin are ADRBK1 gene and FASTK Gene. The related lipids are 1,2-dilinolenoyl-3-(4-aminobutyryl)propane-1,2,3-triol. The related experimental models are Rodent Model and Transgenic Model.

Cross Reference

Introduction

To understand associated biological information of (-)-Epigallocatechin, 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 (-)-Epigallocatechin?

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

Possible diseases from mapped MeSH terms on references

We collected disease MeSH terms mapped to the references associated with (-)-Epigallocatechin

MeSH term MeSH ID Detail
Body Weight D001835 333 associated lipids
Lung Neoplasms D008175 171 associated lipids
Adenocarcinoma D000230 166 associated lipids
Hemolysis D006461 131 associated lipids
Pancreatic Neoplasms D010190 77 associated lipids
Mammary Neoplasms, Experimental D008325 67 associated lipids
Liver Diseases D008107 31 associated lipids
Glioblastoma D005909 27 associated lipids
Total 8

PubChem Associated disorders and diseases

What pathways are associated with (-)-Epigallocatechin

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 (-)-Epigallocatechin?

Related references are published most in these journals:

Location Cross reference Weighted score Related literatures
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What functions are associated with (-)-Epigallocatechin?


Related references are published most in these journals:

Function Cross reference Weighted score Related literatures

What lipids are associated with (-)-Epigallocatechin?

Related references are published most in these journals:

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What genes are associated with (-)-Epigallocatechin?

Related references are published most in these journals:


Gene Cross reference Weighted score Related literatures

What common seen animal models are associated with (-)-Epigallocatechin?

Rodent Model

Rodent Model are used in the study 'Dietary (-)-epicatechin as a potent inhibitor of βγ-secretase amyloid precursor protein processing.' (Cox CJ et al., 2015) and Rodent Model are used in the study 'Effects of dosing condition on the oral bioavailability of green tea catechins after single-dose administration of Polyphenon E in healthy individuals.' (Chow HH et al., 2005).

Transgenic Model

Transgenic Model are used in the study 'Dietary (-)-epicatechin as a potent inhibitor of βγ-secretase amyloid precursor protein processing.' (Cox CJ et al., 2015).

Related references are published most in these journals:

Model Cross reference Weighted score Related literatures
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NCBI Entrez Crosslinks

All references with (-)-Epigallocatechin

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Authors Title Published Journal PubMed Link
Alemdaroglu NC et al. Inhibition of folic acid uptake by catechins and tea extracts in Caco-2 cells. 2007 Planta Med. pmid:17117344
Koyama Y et al. Effects of green tea on gene expression of hepatic gluconeogenic enzymes in vivo. 2004 Planta Med. pmid:15549673
Dauer A et al. Polymeric proanthocyanidins from the bark of Hamamelis virginiana. 2003 Planta Med. pmid:12567291
Shim JS et al. The effects of panduratin A isolated from Kaempferia pandurata on the expression of matrix metalloproteinase-1 and type-1 procollagen in human skin fibroblasts. 2008 Planta Med. pmid:18253916
Kuo YC et al. Isolation and immunomodulatory effect of flavonoids from Syzygium samarangense. 2004 Planta Med. pmid:15643565
Kao CC et al. Green tea catechins: inhibitors of glycerol-3-phosphate dehydrogenase. 2010 Planta Med. pmid:19937554
Kuzuhara T et al. Green tea catechins inhibit the endonuclease activity of influenza A virus RNA polymerase. 2009 PLoS Curr pmid:20025206
Wang P et al. Limitations of MTT and MTS-based assays for measurement of antiproliferative activity of green tea polyphenols. 2010 PLoS ONE pmid:20419137
Sun Z et al. Phosphorylation of Nrf2 at multiple sites by MAP kinases has a limited contribution in modulating the Nrf2-dependent antioxidant response. 2009 PLoS ONE pmid:19668370
Fujimura Y et al. Metabolomics-driven nutraceutical evaluation of diverse green tea cultivars. 2011 PLoS ONE pmid:21853132