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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2015
2015
Diallyl trisulfide (DATS) reacts rapidly with glutathione (GSH) to release H2S through thiol-disulfide exchange followed by allyl… (More)
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2009
2009
The nutrient conditions present in abandoned coal mine drainages create an extreme environment where defensive and offensive… (More)
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2006
2006
Low molecular weight thiol/disulfide redox pools are dependent upon extracellular cysteine (Cys) availability. We determined… (More)
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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… (More)
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2002
2002
GC-MS analysis of the anal sac secretion from the hooded skunk, Mephitis macroura, showed the following seven major components… (More)
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2000
2000
The protein subunit of Escherichia coli ribonuclease P (which has a cysteine residue at position 113) and its single cysteine… (More)
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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… (More)
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Review
1996
Review
1996
This bioessay aims to explain the different effects of maternal ageing and postovulatory oocyte ageing on mammalian oocytes… (More)
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1980
1980
This is a study on the histochemical and electron microscope findings of the intracellular inclusions in a case of meningothelial… (More)
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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… (More)
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