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

Related topics

Related topics

13 relations

Narrower (3)

BdbD protein, Bacillus subtilisCcmg protein, E coliThiol-Disulfide Oxidoreductase
In BloodP4HB geneProcess of secretionantagonists & inhibitors
(More)

Broader (1)

Oxidoreductase

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
2014
Highly Cited
2014
Molybdenum disulfide (MoSâ‚‚) as a broadband saturable absorber for ultra-fast photonics.
The nonlinear optical property of few-layered MoS₂ nanoplatelets synthesized by the hydrothermal exfoliation method was… (More)
Is this relevant?
Highly Cited
2009
Highly Cited
2009
Efficacy of methylcobalamin and folinic acid treatment on glutathione redox status in children with autism.
BACKGROUND Metabolic abnormalities and targeted treatment trials have been reported for several neurobehavioral disorders but are… (More)
  • figure 2
  • figure 1
  • table 1
  • figure 3
Is this relevant?
Highly Cited
2005
Highly Cited
2005
DiANNA: a web server for disulfide connectivity prediction
Correctly predicting the disulfide bond topology in a protein is of crucial importance for the understanding of protein function… (More)
  • figure 1
  • figure 2
Is this relevant?
Review
2003
Review
2003
Protein disulfide bond formation in prokaryotes.
Disulfide bonds formed between pairs of cysteines are important features of the structure of many proteins. Elaborate electron… (More)
Is this relevant?
Highly Cited
2002
Highly Cited
2002
Lead induced oxidative damage and its response to combined administration of alpha-lipoic acid and succimers in rats.
Alpha-lipoic acid (LA) has been reported to be highly effective in improving the thiol capacity of the cells and in reducing lead… (More)
Is this relevant?
Highly Cited
1992
Highly Cited
1992
Crystal structure of transforming growth factor-beta 2: an unusual fold for the superfamily.
The transforming growth factors-beta (TGF-beta 1 through -beta 5) are a family of homodimeric cytokines that regulate… (More)
Is this relevant?
Highly Cited
1983
Highly Cited
1983
Mechanism of action of N-acetylcysteine in the protection against the hepatotoxicity of acetaminophen in rats in vivo.
N-Acetylcysteine is the drug of choice for the treatment of an acetaminophen overdose. It is thought to provide cysteine for… (More)
  • figure 1
  • table I
  • table III
Is this relevant?
Highly Cited
1982
Highly Cited
1982
Isolation of a membrane-bound cofactor for thrombin-catalyzed activation of protein C.
The isolation from rabbit lung of a cofactor for thrombin-catalyzed Protein C activation is described. The lung is perfused to… (More)
  • figure 1
  • figure 2
  • figure 3
  • figure 5
  • figure 4
Is this relevant?
Highly Cited
1979
Highly Cited
1979
Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide.
Thioredoxin from Escherichia coli was shown to catalyze the reduction of insulin disulfides by dithiothreitol. A quantitative… (More)
  • figure 1
  • table II
  • figure 2
  • figure 3
  • table IV
Is this relevant?
Highly Cited
1972
Highly Cited
1972
[37] Reaction of protein sulfhydryl groups with Ellman's reagent.
The reagent 5,5'-dithiobis(2-nitrobenzoic acid) (DTNB) was developed by Ellman as a sulfhydryl reagent. 1 DTNB has been found to… (More)
Is this relevant?