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enzyme-thiol transhydrogenase (glutathione-disulfide) activity

Known as: enzyme-thiol transhydrogenase (glutathione-disulphide) activity, enzyme-thiol transhydrogenase (oxidized-glutathione) activity, xanthine-dehydrogenase:glutathione-disulfide S-oxidoreductase activity 
Catalysis of the reaction: oxidized glutathione + [xanthine dehydrogenase] = reduced glutathione + xanthine-oxidase. [EC:1.8.4.7, MetaCyc:1.8.4.7-RXN… 
National Institutes of Health

Papers overview

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Highly Cited
2014
Highly Cited
2014
The multifunctional role of oleylamine (OAm) as a versatile and flexible reagent in synthesis as well as a desired surface ligand… 
Highly Cited
2011
Highly Cited
2011
An explorative study of the Thiol-Yne Coupling (TYC) reaction has been carried out using an aliphatic (1-octyne) and an aromatic… 
Review
2010
Review
2010
Chemoselective ligation techniques enable the selective modification of proteins and other biomolecules in dilute aqueous… 
Review
2005
Review
2005
A large number of proteins contain free thiols that can be modified by the formation of internal disulphides or by mixed… 
Highly Cited
1993
Highly Cited
1993
Glutathione (GSH) is the major nonprotein thiol that can protect cells from damage due to electrophilic alkylating agents by… 
Highly Cited
1981
Highly Cited
1981
Two-electron reduced glutathione reductase from yeast reacted with iodoacetamide is alkylated almost exclusively in the nascent…