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Disulfides as redox switches : from molecular mechanisms to functional significance

Wouters, Merridee A., Fan, Samuel W. and Haworth, Naomi L. 2010, Disulfides as redox switches : from molecular mechanisms to functional significance, Antioxidants and redox signalling, vol. 12, no. 1, pp. 53-91.

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Title Disulfides as redox switches : from molecular mechanisms to functional significance
Author(s) Wouters, Merridee A.
Fan, Samuel W.
Haworth, Naomi L.
Journal name Antioxidants and redox signalling
Volume number 12
Issue number 1
Start page 53
End page 91
Total pages 39
Publisher Mary Ann Liebert Inc. Publishers
Place of publication New Rochelle, N. Y.
Publication date 2010-01
ISSN 1523-0864
1557-7716
Summary The molecular mechanisms underlying thiol-based redox control are poorly defined. Disulfide bonds between Cys residues are commonly thought to confer extra rigidity and stability to their resident protein, forming a type of proteinaceous spot weld. Redox biologists have been redefining the role of disulfides over the last 30–40 years. Disulfides are now known to form in the cytosol under conditions of oxidative stress. Isomerization of extracellular disulfides is also emerging as an important regulator of protein function. The current paradigm is that the disulfide proteome consists of two subproteomes: a structural group and a redox-sensitive group. The redoxsensitive group is less stable and often associated with regions of stress in protein structures. Some characterized redox-active disulfides are the helical CXXC motif, often associated with thioredoxin-fold proteins; and forbidden disulfides, a group of metastable disulfides that disobey elucidated rules of protein stereochemistry. Here we discuss the role of redox-active disulfides as switches in proteins.
Notes This is a copy of an article published in the Antioxidants and Redox Signaling © 2010 Mary Ann Liebert, Inc.; Antioxidants and Redox Signaling is available online at: http://online.liebertpub.com.
Language eng
Field of Research 060199 - Biochemistry and Cell Biology not elsewhere classified
Socio Economic Objective 970106 - Expanding Knowledge in the Biological Sciences
HERDC Research category C1.1 Refereed article in a scholarly journal
Copyright notice ©2010, Mary Ann Liebert Publishers
Persistent URL http://hdl.handle.net/10536/DRO/DU:30038990

Document type: Journal Article
Collections: School of Life and Environmental Sciences
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Every reasonable effort has been made to ensure that permission has been obtained for items included in DRO. If you believe that your rights have been infringed by this repository, please contact drosupport@deakin.edu.au.