Editor-in-Chief: Di Cera, Enrico
Covered by Web of Science (BIOSIS Previews)
CiteScore 2018: 3.35
SCImago Journal Rank (SJR) 2018: 1.475
Source Normalized Impact per Paper (SNIP) 2018: 0.825
ICV 2018: 124.31
Oxidative folding: recent developments
- Department of Applied Biotechnology and Food Science, Laboratory of Biochemistry and Molecular Biology, Budapest University of Technology and Economics, 1111 Budapest, Hungary
- Pathobiochemistry Research Group of Hungarian Academy of Sciences and Semmelweis University, 1444 Budapest, P.O. Box 260, Hungary
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- De Gruyter OnlineGoogle Scholar
Disulfide bond formation in proteins is an effective tool of both structure stabilization and redox regulation. The prokaryotic periplasm and the endoplasmic reticulum of eukaryotes were long considered as the only compartments for enzyme mediated formation of stable disulfide bonds. Recently, the mitochondrial intermembrane space has emerged as the third protein-oxidizing compartment. The classic view on the mechanism of oxidative folding in the endoplasmic reticulum has also been reshaped by new observations. Moreover, besides the structure stabilizing function, reversible disulfide bridge formation in some proteins of the endoplasmic reticulum, seems to play a regulatory role. This review briefly summarizes the present knowledge of the redox systems supporting oxidative folding, emphasizing recent developments.
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