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Author Notes:

To whom correspondence should be addressed. E-mail: dpjones@emory.edu.


Research Funding:

This work was supported, in whole or in part, by National Institutes of Health Grants ES009047, HL113451, and AG038746.

This is the seventh article in the Thematic Minireview Series on Redox-active Protein Modifications and Signaling.


  • Glutathione
  • Redox Regulation
  • Systems Biology
  • Thiol
  • Thioredoxin

The Redox Proteome


Journal Title:

Journal of Biological Chemistry


Volume 288, Number 37


, Pages 26512-26520

Type of Work:

Article | Final Publisher PDF


The redox proteome consists of reversible and irreversible covalent modifications that link redox metabolism to biologic structure and function. These modifications, especially of Cys, function at the molecular level in protein folding and maturation, catalytic activity, signaling, and macromolecular interactions and at the macroscopic level in control of secretion and cell shape. Interaction of the redox proteome with redox-active chemicals is central to macromolecular structure, regulation, and signaling during the life cycle and has a central role in the tolerance and adaptability to diet and environmental challenges.

Copyright information:

© 2013 by The American Society for Biochemistry and Molecular Biology, Inc.

This is an Open Access work distributed under the terms of the Creative Commons Attribution 3.0 Unported License (http://creativecommons.org/licenses/by/3.0/).

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