Human cytosolic glutathione-S-transferases: quantitative analysis of expression, comparative analysis of structures and inhibition strategies of isozymes involved in drug resistance-Reference-Cited by-同舟云学术

Human cytosolic glutathione-S-transferases: quantitative analysis of expression, comparative analysis of structures and inhibition strategies of isozymes involved in drug resistance

Published:2017-07-03 Issue:3 Volume:49 Page:318-337
ISSN:0360-2532
Container-title:Drug Metabolism Reviews
language:en
Short-container-title:Drug Metabolism Reviews

Author:

Mohana Krishnamoorthy¹,Achary Anant¹

Affiliation:

1. Department of Biotechnology, Centre for Research, Kamaraj College of Engineering and Technology, Virudhunagar, India

Publisher

Informa UK Limited

Subject

Pharmacology (medical),General Pharmacology, Toxicology and Pharmaceutics

Link

https://www.tandfonline.com/doi/pdf/10.1080/03602532.2017.1343343

Reference165 articles.

1. Identification of an N-capping box that affects the α6-helix propensity in glutathione S-transferase superfamily proteins: a role for an invariant aspartic residue

2. The glutathione-binding site in glutathione S-transferases. Investigation of the cysteinyl, glycyl and γ-glutamyl domains

3. Regulation of JNK signaling by GSTp

4. The role of tyrosine-9 and the C-terminal helix in the catalytic mechanism of Alpha-class glutathione S-transferases

5. Functional analysis of the evolutionarily conserved proline 53 residue inProteus mirabilisglutathione transferase B1-1

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