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Journal ArticleDOI

Glutathione transferases, regulators of cellular metabolism and physiology.

Philip G. Board, +1 more
- 01 May 2013 - 
- Vol. 1830, Iss: 5, pp 3267-3288
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TLDR
Human cytosolic GSTs have emerged as significant regulators of pathways determining cell proliferation and survival and as regulators of ryanodine receptors that are essential for muscle function.
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This article is published in Biochimica et Biophysica Acta.The article was published on 2013-05-01. It has received 336 citations till now. The article focuses on the topics: Glutaredoxin & GPX3.

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Citations
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The role of glutathione reductase and related enzymes on cellular redox homoeostasis network.

TL;DR: The role of glutathione reductase in the regulation, modulation and maintenance of cellular redox homoeostasis, and therapeutic targets to overcome oxidative stress associated cellular disorders are evaluated.
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Glutathione transferases: substrates, inihibitors and pro-drugs in cancer and neurodegenerative diseases

TL;DR: In the last decades, a great deal of research aimed at clarifying the role played by GSTs in drug resistance, at developing inhibitors to counteract this activity but also at exploiting GSTs for prodrugs specific activation in cancer cells.

TheIdentity ofGlutathione S-Transferase B withLigandin, aMajorBinding Protein ofLiver

TL;DR: Evidence ispresented that ligandin, an intracellular protein involved in thebinding of suchanions asbilirubin, indocyanine green, andpenicillin, isidentical toglutathione S-transferase B (EC2.5.1.18), and it was suggested that specificity isdirected towardcompoundswithelectrophilic sites.

Polymorphism in glutathione S-transferase is associated with susceptibility to chemotherapy-induced leukemia

TL;DR: In this article, the authors examined 89 cases of acute myeloid leukemia (t-AML), 420 cases of de novo AML, and 1,022 controls for polymorphisms in GSTM1, GSTT1, and GSTP1 genes.
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.
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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.
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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.
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Structure, function and evolution of glutathione transferases: implications for classification of non-mammalian members of an ancient enzyme superfamily.

TL;DR: Non-mammalian GSTs have been much less well characterized, but have provided a disproportionately large number of three-dimensional structures, thus extending the authors' knowledge of glutathione transferases in mammals.
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Human glutathione S-transferase theta (GSTT1): cDNA cloning and the characterization of a genetic polymorphism.

TL;DR: Characterization of the GSTT1 polymorphism will enable a more accurate assessment of human health risk from synthetic halomethanes and other industrial chemicals.
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