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Book ChapterDOI

The Isoenzymes of Glutathione Transferase

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This article is published in Advances in Enzymology and Related Areas of Molecular Biology.The article was published on 2006-11-22. It has received 855 citations till now.

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Journal ArticleDOI

The glutathione S-transferase supergene family: regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance.

TL;DR: The biochemical functions of GST are described to show how individual isoenzymes contribute to resistance to carcinogens, antitumor drugs, environmental pollutants, and products of oxidative stress, and to allow identification of factors that may modulate resistance to specific noxious chemicals.
Journal ArticleDOI

The importance of glutathione in human disease.

TL;DR: An overview of the biological importance of GSH at the level of the cell and organism can be found in this article, where the authors provide a review of the most prevalent non-protein thiol in animal cells.
Journal ArticleDOI

Glutathione transferases--structure and catalytic activity.

TL;DR: The glutathione transferases are recognized as important catalysts in the biotransformation of xenobiotics, including drugs as well as environmental pollutants, and numerous transferases from mammalian tissues, insects, and plants have been isolated and characterized.
Journal ArticleDOI

The molecular basis of insecticide resistance in mosquitoes.

TL;DR: This paper reviews what is currently known about insecticide resistance conferred by metabolic or target site changes in mosquitoes.
Journal ArticleDOI

Glutathione S-Transferase Polymorphisms and Their Biological Consequences

TL;DR: Two supergene families encode proteins with glutathione S-transferase (GST) activity that detoxify a variety of electrophilic compounds, including oxidized lipid, DNA and catechol products generated by reactive oxygen species-induced damage to intracellular molecules.
References
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Journal ArticleDOI

Glutathione S-transferases. The first enzymatic step in mercapturic acid formation.

TL;DR: The purification of homogeneous glutathione S-transferases B and C from rat liver is described, and only transferases A and C are immunologically related.
Journal ArticleDOI

Why genes in pieces

Book ChapterDOI

The role of glutathione and glutathione S-transferases in the metabolism of chemical carcinogens and other electrophilic agents.

TL;DR: The knowledge of the way in which mutagens and carcinogens are metabolized is essential to a better understanding of their mode of action and of the processes for their detoxication.
Journal ArticleDOI

Purification from pig liver of a protein which protects liposomes and biomembranes from peroxidative degradation and exhibits glutathione peroxidase activity on phosphatidylcholine hydroperoxides.

TL;DR: The cell sap from pig liver contains a protein which protects phosphatidylcholine liposomes and biomembranes from peroxidative degradation in the presence of glutathione, and this protein appears to be distinct from the selenoenzyme glutATHioneperoxidase and from any known glutathion S-transferase.
Journal ArticleDOI

The refined structure of the selenoenzyme glutathione peroxidase at 0.2-nm resolution.

TL;DR: A general picture of a minimal reaction mechanism, in good agreement with functional and structural data, is proposed and a reasonable model of glutathione binding is presented.
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