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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
In this article we introduce a novel polymer platform based on off-stoichiometry thiol-enes (OSTEs), aiming to bridge the gap… 
Highly Cited
2010
Highly Cited
2010
The maleimide motif is widely used for the selective chemical modification of cysteine residues in proteins. Despite widespread… 
Review
2009
Review
2009
Disulfide bond formation is probably involved in the biogenesis of approximately one third of human proteins. A central player in… 
Review
2009
Review
2009
The glutathione (GSH)/glutathione disulfide (GSSG) redox couple is involved in several physiologic processes in plants under both… 
Highly Cited
1983
Highly Cited
1983
N-Acetylcysteine is the drug of choice for the treatment of an acetaminophen overdose. It is thought to provide cysteine for… 
Highly Cited
1965
Highly Cited
1965
The γ1A present in saliva and colostrum exists largely in the form of higher polymers, the major component of which has a…