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Glutathione S-transferases, structure, regulation, and therapeutic implications

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Rushmore, T.H., Pickett, C.B.·1993·Journal of Biological Chemistry

Abstract

The glutathione S-transferases (GSTs)' are a family of enzymes that catalyze the nucleophilic addition of the thiol of reduced glutathione to a variety of electrophiles (1-9). In addition, the GSTs bind with varying affinities a variety of hydrophobic compounds such as heme, bilirubin, polycyclic aromatic hydrocarbons, and dexamethasone (1-9). It is now generally accepted that the GSTs are encoded by at least five different gene families (9-12). Four of the gene families encode the cytosolic GSTs whereas the fifth en-codes a microsomal form of the enzyme (13, 14). In this review, we have focused on three GST research areas: 1) structure-function analysis of GSTs; 2) regulation of GST expression; and 3) GSTs as therapeutic targets in disease. Since our review will not be com-prehensive, we would like to direct the reader to several excellent recent reviews focusing on various aspects of GSTs (4,8,9).

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Metadata

Authors
Rushmore, T. H., & Pickett, C. B.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1993-06
Volume
268
Issue
16
Pages
11475-11478
ISSN
0021-9258 (ISSN-L)
OpenAlex
W1486158855
Cited by
405
References
0
FWCI
8.99
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Glutathione S-transferases, structure, regulation, and therapeutic implications. https://app.cochat.ai/papers/10.1016/s0021-9258(19)50219-8
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Rushmore, T. H., & Pickett, C. B. (1993). Glutathione S-transferases, structure, regulation, and therapeutic implications. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(19)50219-8

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.