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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… Expand
Highly Cited
2013
Highly Cited
2013
Background: The Cys-62/Cys-69 dithiol of Trx1 is predicted to have a profound effect on cell signaling. Results: The Cys-62/Cys… Expand
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Review
2011
Review
2011
Despite the significance of redox post-translational modifications (PTMs) in regulating diverse signal transduction pathways, the… Expand
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Highly Cited
2006
Highly Cited
2006
Thioredoxin is ubiquitous and regulates various target proteins through disulfide bond reduction. We report the structure of… Expand
Highly Cited
2001
Highly Cited
2001
ABSTRACT Helicobacter pylori, an oxygen-sensitive microaerophile, contains an alkyl hydroperoxide reductase homologue (AhpC… Expand
Highly Cited
1998
Highly Cited
1998
We have identified an RNA polymerase sigma factor, σR, that is part of a system that senses and responds to thiol oxidation in… Expand
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… Expand
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… Expand
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Highly Cited
1995
Highly Cited
1995
Human thioredoxin reductase is a dimeric enzyme that catalyzes reduction of the disulfide in oxidized thioredoxin by a mechanism… Expand
Highly Cited
1972
Highly Cited
1972
The biochemical and morphological changes of the yeastlike (Y) form to the mycelial (M) form of Paracoccidioides brasiliensis… Expand