insulin-glutathione transhydrogenase activity

Known as: protein-dithiol:NAD(P)+ oxidoreductase activity, protein disulfide reductase activity, protein disulphide reductase activity 
Catalysis of the reaction: protein-dithiol + NAD(P)+ = protein-disulfide + NAD(P)H + H+. [EC:1.8.1.8, MetaCyc:1.6.4.4-RXN]
National Institutes of Health

Papers overview

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Review
2015
Review
2015
SIGNIFICANCE All cells must maintain a balance between oxidants and reductants, while allowing for fluctuations in redox states… (More)
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2013
2013
The mammalian cytosolic thioredoxin system, comprising thioredoxin (Trx), Trx reductase, and NADPH, is the major protein… (More)
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2010
2010
This study was undertaken to evaluate the effects of streptozotocin (STZ)-induced hyperglycemia and insulin-induced hypoglycemia… (More)
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2009
2009
NADPH thioredoxin reductase C (NTRC) is an interesting NTR with a thioredoxin (Trx) domain at the C-terminus, able to conjugate… (More)
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2009
2009
We found that Arabidopsis AtTDX, a heat-stable and plant-specific thioredoxin (Trx)-like protein, exhibits multiple functions… (More)
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Highly Cited
2001
Highly Cited
2001
Helicobacter pylori, an oxygen-sensitive microaerophile, contains an alkyl hydroperoxide reductase homologue (AhpC, HP1563) that… (More)
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Highly Cited
1998
Highly Cited
1998
We have identified an RNA polymerase sigma factor, sigmaR, that is part of a system that senses and responds to thiol oxidation… (More)
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Highly Cited
1996
Highly Cited
1996
In activated human neutrophils a burst of nitric oxide (NO) converts intracellular GSH to S-nitrosoglutathione (GSNO) which is… (More)
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1995
1995
Human thioredoxin reductase is a dimeric enzyme that catalyzes reduction of the disulfide in oxidized thioredoxin by a mechanism… (More)
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1972
1972
The biochemical and morphological changes of the yeastlike (Y) form to the mycelial (M) form of Paracoccidioides brasiliensis… (More)
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