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Lookup NU author(s): Dr Elizabeth Veal
This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).
H2O2 signals trigger adaptive responses affecting cell division, differentiation, migration and survival. These signals are transduced by selective oxidation of cysteines on specific target proteins, with redox-sensitive cysteines now identified in many proteins, including both kinases and phosphatases. Assessing the contribution of these oxidation events to cell signaling, presents several challenges, including understanding how and when the selective oxidation of specific proteins takes place in vivo. In recent years, a combination of biochemical, structural, genetic and computational approaches in fungi, plants and animals have revealed different ways in which thiol peroxidases(peroxiredoxins) are bypassed or utilized in relaying these signals. Together these mechanisms provide a conceptual framework for selectively oxidizing signaling proteins that will further advance understanding of how redox modifications contribute to health and disease.
Author(s): Veal EA, Kritsiligkou P
Publication type: Article
Publication status: Published
Journal: Current Opinion in Chemical Biology
Year: 2024
Volume: 81
Print publication date: 01/08/2024
Online publication date: 02/07/2024
Acceptance date: 09/06/2024
Date deposited: 15/07/2024
ISSN (print): 1367-5931
ISSN (electronic): 1879-0402
Publisher: Elsevier Ltd.
URL: https://doi.org/10.1016/j.cbpa.2024.102496
DOI: 10.1016/j.cbpa.2024.102496
Data Access Statement: No data was used for the research described in the article.
Notes: This review comes from a themed issue on Chemical Genetics and Epigenetics 2024; Edited by Yimon Aye and Christine Winterbourn
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