Journal
ANTIOXIDANTS & REDOX SIGNALING
Volume 15, Issue 1, Pages 49-66Publisher
MARY ANN LIEBERT, INC
DOI: 10.1089/ars.2010.3575
Keywords
-
Funding
- Belgian Science Policy
- FRS-FNRS
- [P6/05]
Ask authors/readers for more resources
The identification of protein disulfide isomerase, almost 50 years ago, opened the way to the study of oxidative protein folding. Oxidative protein folding refers to the composite process by which a protein recovers both its native structure and its native disulfide bonds. Pathways that form disulfide bonds have now been unraveled in the bacterial periplasm (disulfide bond protein A [DsbA], DsbB, DsbC, DsbG, and DsbD), the endoplasmic reticulum (protein disulfide isomerase and Ero1), and the mitochondrial intermembrane space (Mia40 and Erv1). This review summarizes the current knowledge on disulfide bond formation in both prokaryotes and eukaryotes and highlights the major problems that remain to be solved. Antioxid. Redox Signal. 15, 49-66.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available