Literature DB >> 22147701

Regulation by S-nitrosylation of protein post-translational modification.

Douglas T Hess1, Jonathan S Stamler.   

Abstract

Protein post-translational modification by S-nitrosylation conveys a ubiquitous influence of nitric oxide on signal transduction in eukaryotic cells. The wide functional purview of S-nitrosylation reflects in part the regulation by S-nitrosylation of the principal protein post-translational modifications that play a role in cell signaling, including phosphorylation, acetylation, ubiquitylation and related modifications, palmitoylation, and alternative Cys-based redox modifications. In this minireview, we discuss the mechanisms through which S-nitrosylation exerts its broad pleiotropic influence on protein post-translational modification.

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Year:  2011        PMID: 22147701      PMCID: PMC3281651          DOI: 10.1074/jbc.R111.285742

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  78 in total

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4.  Fas-induced caspase denitrosylation.

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Review 7.  Protein S-nitrosylation: purview and parameters.

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  149 in total

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7.  Nitric oxide induces Ca2+-independent activity of the Ca2+/calmodulin-dependent protein kinase II (CaMKII).

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9.  Endothelial Nitric Oxide Synthase-Derived Nitric Oxide Prevents Dihydrofolate Reductase Degradation via Promoting S-Nitrosylation.

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Review 10.  Posttranslational Modifications of Chloroplast Proteins: An Emerging Field.

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