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glutathione-insulin transhydrogenase activity

Known as: glutathione--insulin transhydrogenase activity, thiol-protein disulphide oxidoreductase activity, insulin reductase activity 
Catalysis of the reaction: 2 glutathione + protein-disulfide = oxidized glutathione + protein-dithiol. [EC:1.8.4.2]
National Institutes of Health

Papers overview

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Highly Cited
2010
Highly Cited
2010
Reduction-responsive biodegradable micelles were developed from disulfide-linked dextran-b-poly(epsilon-caprolactone) diblock… Expand
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Highly Cited
2009
Highly Cited
2009
The nutrient conditions present in abandoned coal mine drainages create an extreme environment where defensive and offensive… Expand
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Highly Cited
2008
Highly Cited
2008
Salt stress impairs reactive oxygen species (ROS) and methylglyoxal (MG) detoxification systems, and causes oxidative damage to… Expand
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Highly Cited
2003
Highly Cited
2003
Thioredoxin (Trx1) is a redox-active protein containing two active site cysteines (Cys-32 and Cys-35) that cycle between the… Expand
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Highly Cited
1998
Highly Cited
1998
Thiol-disulfide exchange reactions are required for many aspects of cellular metabolism including the folding of disulfide-bonded… Expand
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Highly Cited
1998
Highly Cited
1998
We have reported previously that diethyldithio-carbamate (DDC) and pyrrolidine dithiocarbamate (PDTC) induce apoptosis in rat… Expand
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Review
1997
Review
1997
In these studies we have shown that reaction of a peptide-α-thioacid with an aryl disulfide gives a product with mass consistent… Expand
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Highly Cited
1995
Highly Cited
1995
A dynamic rheometer was used to characterize the effect of glutathione, potassium bromate, and two ascorbic acid isomers on the… Expand
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Highly Cited
1993
Highly Cited
1993
An antiparallel coiled-coil has been designed and characterized as a model for studying protein folding and assembly. This… Expand
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Highly Cited
1978
Highly Cited
1978
A heterobifunctional reagent, N-succinimidyl 3-(2-pyridyldithio)propionate, was synthesized. Its N-hydroxysuccinimide ester group… Expand
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