Jump to ContentJump to Main Navigation
Show Summary Details
More options …

Biomolecular Concepts

Editor-in-Chief: Di Cera, Enrico


Covered by Web of Science (BIOSIS Previews)

PubMed Indexed

CiteScore 2018: 3.35

SCImago Journal Rank (SJR) 2018: 1.475
Source Normalized Impact per Paper (SNIP) 2018: 0.825

ICV 2018: 124.31

Open Access
Online
ISSN
1868-503X
See all formats and pricing
More options …
Volume 2, Issue 5

Issues

Oxidative folding: recent developments

András Szarka
  • 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
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Gábor Bánhegyi
  • Department of Medical Chemistry, Molecular Biology and Pathobiochemistry, Semmelweis University, 1444 Budapest, P.O. Box 260, Hungary
  • Email
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
Published Online: 2011-08-30 | DOI: https://doi.org/10.1515/BMC.2011.038

Abstract

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.

Keywords: endoplasmic reticulum; intermembrane space; oxidative folding; periplasm; redox

About the article

Corresponding author


Received: 2011-05-30

Accepted: 2011-07-21

Published Online: 2011-08-30

Published in Print: 2011-10-01


Citation Information: BioMolecular Concepts, Volume 2, Issue 5, Pages 379–390, ISSN (Online) 1868-503X, ISSN (Print) 1868-5021, DOI: https://doi.org/10.1515/BMC.2011.038.

Export Citation

Citing Articles

Here you can find all Crossref-listed publications in which this article is cited. If you would like to receive automatic email messages as soon as this article is cited in other publications, simply activate the “Citation Alert” on the top of this page.

[1]
Tibor Balogh and András Szarka
Orvosi Hetilap, 2015, Volume 156, Number 13, Page 503
[2]
Tibor Balogh, Tamás Lőrincz, Ibolya Stiller, József Mandl, Gábor Bánhegyi, and András Szarka
Pathology & Oncology Research, 2016, Volume 22, Number 2, Page 431
[3]
András Szarka and Tamás Lőrincz
Protoplasma, 2014, Volume 251, Number 3, Page 489

Comments (0)

Please log in or register to comment.
Log in