Oxidative Protein Folding in Vitro: A Study of the Cooperation between Quiescin-Sulfhydryl Oxidase and Protein Disulfide Isomerase
Author:
Affiliation:
1. Department of Chemistry and Biochemistry, University of Delaware, Newark, Delaware 19716
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi801604x
Reference73 articles.
1. Ero1p: A Novel and Ubiquitous Protein with an Essential Role in Oxidative Protein Folding in the Endoplasmic Reticulum
2. The ERO1 Gene of Yeast Is Required for Oxidation of Protein Dithiols in the Endoplasmic Reticulum
3. Homology between Egg White Sulfhydryl Oxidase and Quiescin Q6 Defines a New Class of Flavin-linked Sulfhydryl Oxidases
4. Rat Seminal Vesicle FAD-dependent Sulfhydryl Oxidase
5. Tissue-specific Expression and Dimerization of the Endoplasmic Reticulum Oxidoreductase Ero1β
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