A common polymorphic variant of UGT 1A5 displays increased activity due to optimized cofactor binding-Reference-Cited by-同舟云学术

A common polymorphic variant of UGT 1A5 displays increased activity due to optimized cofactor binding

Published:2018-05-22 Issue:11 Volume:592 Page:1837-1846
ISSN:0014-5793
Container-title:FEBS Letters
language:en
Short-container-title:FEBS Lett

Author:

Yang Fan¹,Machalz David²,Wang Sisi¹,Li Zhengyi¹,Wolber Gerhard²,Bureik Matthias¹^ORCID

Affiliation:

1. School of Pharmaceutical Science and Technology Health Sciences Platform Tianjin University China

2. Pharmaceutical and Medicinal Chemistry Computer‐Aided Drug Design Institute of Pharmacy Free University Berlin Germany

Publisher

Wiley

Subject

Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/1873-3468.13072

Reference41 articles.

1. Revisiting the Latency of Uridine Diphosphate-Glucuronosyltransferases (UGTs)—How Does the Endoplasmic Reticulum Membrane Influence Their Function?

2. Pharmacogenomics of Human Uridine Diphospho-Glucuronosyltransferases and Clinical Implications

3. S-Glucuronidation of 7-mercapto-4-methylcoumarin by human UDP glycosyltransferases in genetically engineered fission yeast cells

4. A novel method for the production of N‐ and O‐glucuronides using recombinant fission yeast (Schizosaccharomyces pombe);Buchheit D;Drug Metab Rev,2010

5. Production of Ibuprofen Acyl Glucosides by Human UGT2B7

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