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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… 
National Institutes of Health

Papers overview

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Highly Cited
2011
Highly Cited
2011
We demonstrate here a series of hybrid materials based on thiol-contained polyhedral oligomeric silsesquioxane (POSS-OA/SH) and… 
Highly Cited
1999
Highly Cited
1999
A detailed investigation of the self-assembled monolayers of diphenyl disulfide (DDS), diphenyl diselenide (DDSe), and… 
Highly Cited
1997
Highly Cited
1997
The pressure and/or temperature inactivation of mushroom polyphenoloxidase (PPO) in the absence and presence of EDTA, benzoic… 
Highly Cited
1994
Highly Cited
1994
The disulfide bond location of a homodimeric peptide, prothoracicotropic hormone (PTTH) of the silkworm, Bombyx mori, was… 
Highly Cited
1990
Highly Cited
1990
Neutrophil-specific alloantibodies and the antigens they recognize are important in clinical medicine, but little is known about… 
Highly Cited
1990
Highly Cited
1990
It has been proposed that dithiol-disulfide interchange and oxidation-reduction reactions may play a role in hormone-induced… 
Highly Cited
1989
Highly Cited
1989
The application of free solution capillary electrophoresis (FSCE) to the separation of protein and peptide mixtures is presented… 
Highly Cited
1988
Highly Cited
1988
The level of nonprotein thiols was assayed in individual mammalian cells using flow cytometry. Previous determinations of… 
1976
1976
The derivative of the trypsin-kallikrein inhibitor (Kunitz), TKI+, was prepared with the reactive-site peptide bond Lys-15-Ala-16…