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Mol Cell. 2018 Feb 1;69(3):351-353. doi: 10.1016/j.molcel.2018.01.022.

Protein S-Nitrosylation: Enzymatically Controlled, but Intrinsically Unstable, Post-translational Modification.

Author information

1
Department of Biochemistry and Molecular Pharmacology, New York University School of Medicine, New York, NY 10016, USA.
2
Department of Biochemistry and Molecular Pharmacology, New York University School of Medicine, New York, NY 10016, USA; Howard Hughes Medical Institute, New York University School of Medicine, New York, NY 10016, USA. Electronic address: evgeny.nudler@nyumc.org.

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.

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