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- W2000038034 endingPage "26479" @default.
- W2000038034 startingPage "26473" @default.
- W2000038034 abstract "NO is a versatile free radical that mediates numerous biological functions within every major organ system. A molecular pathway by which NO accomplishes functional diversity is the selective modification of protein cysteine residues to form S-nitrosocysteine. This post-translational modification, S-nitrosylation, impacts protein function, stability, and location. Despite considerable advances with individual proteins, the in vivo biological chemistry, the structural elements that govern the selective S-nitrosylation of cysteine residues, and the potential overlap with other redox modifications are unknown. In this minireview, we explore the functional features of S-nitrosylation at the proteome level and the structural diversity of endogenously modified residues, and we discuss the potential overlap and complementation that may exist with other cysteine modifications." @default.
- W2000038034 created "2016-06-24" @default.
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- W2000038034 date "2013-09-01" @default.
- W2000038034 modified "2023-10-16" @default.
- W2000038034 title "Regulation of Protein Function and Signaling by Reversible Cysteine S-Nitrosylation" @default.
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- W2000038034 doi "https://doi.org/10.1074/jbc.r113.460261" @default.
- W2000038034 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3772194" @default.
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