Article
Competition between glutathione and protein thiols for disulphide-bond formation.
Nature cell biology - 1 Jul 1999
Cuozzo J W, Kaiser C A
Abstract excerpt
It has long been assumed that the oxidized form of glutathione, the tripeptide glutamate-cysteine-glycine, is a source of oxidizing equivalents needed for the formation of disulphide bonds in proteins within the endoplasmic reticulum (ER), although the in vivo function of glutathione in the ER has never been studied directly. Here we show that the major pathway for oxidation in the yeast ER, defined by the...
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