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Antioxid Redox Signal. 2011 Jul 1;15(1):49-66. doi: 10.1089/ars.2010.3575. Epub 2011 Mar 31.

How proteins form disulfide bonds.

Author information

1
de Duve Institute, Université catholique de Louvain, Brussels, Belgium.

Abstract

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.

PMID:
20849374
DOI:
10.1089/ars.2010.3575
[Indexed for MEDLINE]

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