Protein S-Nitrosylation: Enzymatically Controlled, but Intrinsically Unstable, Post-translational Modification
- PMID: 29395059
- DOI: 10.1016/j.molcel.2018.01.022
Protein S-Nitrosylation: Enzymatically Controlled, but Intrinsically Unstable, Post-translational Modification
Abstract
Reports by Seth et al. (2018) and Wolhuter et al. (2018) in this issue of Molecular Cell highlight the enzymatic synthesis, functionality, and propagation of S-nitrosylation-based signaling and address its low stability due to the elevated reactivity toward other cellular thiols.
Copyright © 2018. Published by Elsevier Inc.
Comment on
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Evidence against Stable Protein S-Nitrosylation as a Widespread Mechanism of Post-translational Regulation.Mol Cell. 2018 Feb 1;69(3):438-450.e5. doi: 10.1016/j.molcel.2017.12.019. Epub 2018 Jan 18. Mol Cell. 2018. PMID: 29358077 Free PMC article.
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A Multiplex Enzymatic Machinery for Cellular Protein S-nitrosylation.Mol Cell. 2018 Feb 1;69(3):451-464.e6. doi: 10.1016/j.molcel.2017.12.025. Epub 2018 Jan 18. Mol Cell. 2018. PMID: 29358078 Free PMC article.
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