Independence of the Chaperone Activity of Protein Disulfide Isomerase from Its Thioredoxin-like Active Site
Open Access
- 1 July 1995
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 270 (29) , 17078-17080
- https://doi.org/10.1074/jbc.270.29.17078
Abstract
No abstract availableKeywords
This publication has 24 references indexed in Scilit:
- Protein disulphide isomerase: building bridges in protein foldingTrends in Biochemical Sciences, 1994
- Enzymatic Catalysis of Disulfide FormationProtein Expression and Purification, 1994
- Protein disulfide isomerase is both an enzyme and a chaperoneThe FASEB Journal, 1993
- The essential function of yeast protein disulfide isomerase does not reside in its isomerase activityCell, 1993
- Protein folding in the cellNature, 1992
- Effect of protein and peptide inhibitors on the activity of protein disulfide-isomeraseBiochemistry, 1991
- The reactivities and ionization properties of the active-site dithiol groups of mammalian protein disulphide-isomeraseBiochemical Journal, 1991
- Guanidine hydrochloride denaturation studies of mutant forms of staphylococcal nucleaseJournal of Cellular Biochemistry, 1986
- Factors affecting the folding and association of flounder muscle glyceraldehyde-3-phosphate dehydrogenase, in vitroBiochemistry, 1974
- Tissue sulfhydryl groupsArchives of Biochemistry and Biophysics, 1959