Results 251 to 260 of about 100,115 (305)
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Insect glutathione transferases

Drug Metabolism Reviews, 2011
This article is an overview of the current knowledge of insect glutathione transferases. Three major topics are discussed: the glutathione transferase contributions to insecticide resistance, the polymorphic nature of the insect glutathione transferase superfamily, and a summary of the current structure-function studies on insect glutathione ...
Albert J, Ketterman   +2 more
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Gamma Glutamyl Transferase

Critical Reviews in Clinical Laboratory Sciences, 2001
Serum gamma-glutamyl transferase (GGT) has been widely used as an index of liver dysfunction and marker of alcohol intake. The last few years have seen improvements in these areas and advances in understanding of its physiological role in counteracting oxidative stress by breaking down extracellular glutathione and making its component amino acids ...
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Transferases in Biocatalysis:

2020
Enzymes are nature’s catalyst of choice for the highly selective and efficient coupling of carbohydrates. Enzymatic sugar coupling is a competitive technology for industrial glycosylation reactions, since chemical synthetic routes require extensive use of laborious protection group manipulations and often lack regio- and stereoselectivity.
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Mosquito Glutathione Transferases

2005
The glutathione transferases (glutathione S-transferases, GSTs) are a diverse family of enzymes involved in a wide range of biological processes, many of which involve the conjugation of the tripeptide glutathione to an electrophilic substrate. Relatively little is known about the endogenous substrates of mosquito GSTs, and most studies have focused on
Hilary, Ranson, Janet, Hemingway
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Glutathione S-Transferases

1996
Glutathione (GSH), the most ubiquitous and abundant nonprotein thiol, is essential in numerous detoxification reactions and is therefore considered a chemoprotectant. In the human, levels of GSH range from 30μM in plasma to 3mM in kidney proximal tubules; tumors of various organs can contain up to 10mM GSH [1].
A, Raha, K D, Tew
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Glutathione transferase

2000
Abstract The glutathione transferases (GSTs) are a family of multi-functional proteins which act as enzymes and also as binding proteins in detoxification processes (1-5). GSTs catalyse the nucleophilic attack of the sulfur atom of reduced glutathione by electrophilic groups in a second substrate.
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[62] Animal sialic acid transferases (sialyl-transferases)

1966
Publisher Summary This chapter discusses the synthesis of animal sialic acid transferases (sialyl-transferases). Sialic acids are generally found as constituents of heteropolymers, although one homopolysaccharide, colominic acid is isolated from Escherichia coli K-235.
S. Roseman   +6 more
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The catalytic role of glutathione transferases in heterologous anthocyanin biosynthesis

Nature Catalysis, 2023
Thomas Schwander, Sean Hüppi, Peer
exaly  

Terminal Deoxynucleotidyl Transferase

American Journal of Clinical Pathology, 1980
R B, Johnson, R M, Nakamura
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Glutathione transferases: Nomenclature

Biochemical Pharmacology, 1984
W B, Jakoby, B, Ketterer, B, Mannervik
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