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- W2138840509 abstract "Protein S -nitrosation is deemed as a prototype of posttranslational modifications governing cell signaling. It takes place on specific cysteine residues that covalently incorporate a nitric oxide (NO) moiety to form S -nitrosothiol derivatives and depends on the ratio between NO produced by NO synthases and nitrosothiol removal catalyzed by denitrosating enzymes. A large number of cysteine-containing proteins are found to undergo S -nitrosation and, among them, the enzymes catalyzing ubiquitination, mainly the class of ubiquitin E3 ligases and the 20S component of the proteasome, have been reported to be redox modulated in their activity. In this review we will outline the processes regulating S -nitrosation and try to debate whether and how it affects protein ubiquitination and degradation via the proteasome. In particular, since muscle and neuronal health largely depends on the balance between protein synthesis and breakdown, here we will discuss the impact of S -nitrosation in the efficiency of protein quality control system, providing lines of evidence and speculating about its involvement in the onset and maintenance of neuromuscular dysfunctions." @default.
- W2138840509 created "2016-06-24" @default.
- W2138840509 creator A5000293981 @default.
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- W2138840509 creator A5036813695 @default.
- W2138840509 creator A5061051393 @default.
- W2138840509 creator A5087896955 @default.
- W2138840509 date "2014-01-01" @default.
- W2138840509 modified "2023-10-12" @default.
- W2138840509 title "<i>S</i>-Nitrosation and Ubiquitin-Proteasome System Interplay in Neuromuscular Disorders" @default.
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