Glutathione-insulin transhydrogenase

Known as: Glutathione:protein-disulfide oxidoreductase, Thiol-Protein Disulfide Oxidoreductase, insulin reductase 
An enzyme that catalyzes the reduction of a protein-disulfide in the presence of glutathione, forming a protein-dithiol. Insulin is one of its… (More)
National Institutes of Health

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Highly Cited
2014
Highly Cited
2014
The nonlinear optical property of few-layered MoS₂ nanoplatelets synthesized by the hydrothermal exfoliation method was… (More)
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Highly Cited
2009
Highly Cited
2009
BACKGROUND Metabolic abnormalities and targeted treatment trials have been reported for several neurobehavioral disorders but are… (More)
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Highly Cited
2005
Highly Cited
2005
Correctly predicting the disulfide bond topology in a protein is of crucial importance for the understanding of protein function… (More)
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Review
2003
Review
2003
Disulfide bonds formed between pairs of cysteines are important features of the structure of many proteins. Elaborate electron… (More)
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Highly Cited
2002
Highly Cited
2002
Alpha-lipoic acid (LA) has been reported to be highly effective in improving the thiol capacity of the cells and in reducing lead… (More)
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Highly Cited
1992
Highly Cited
1992
The transforming growth factors-beta (TGF-beta 1 through -beta 5) are a family of homodimeric cytokines that regulate… (More)
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Highly Cited
1983
Highly Cited
1983
N-Acetylcysteine is the drug of choice for the treatment of an acetaminophen overdose. It is thought to provide cysteine for… (More)
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Highly Cited
1982
Highly Cited
1982
The isolation from rabbit lung of a cofactor for thrombin-catalyzed Protein C activation is described. The lung is perfused to… (More)
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Highly Cited
1979
Highly Cited
1979
Thioredoxin from Escherichia coli was shown to catalyze the reduction of insulin disulfides by dithiothreitol. A quantitative… (More)
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Highly Cited
1972
Highly Cited
1972
The reagent 5,5'-dithiobis(2-nitrobenzoic acid) (DTNB) was developed by Ellman as a sulfhydryl reagent. 1 DTNB has been found to… (More)
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