2013
DOI: 10.1074/jbc.r113.460261
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Regulation of Protein Function and Signaling by Reversible Cysteine S-Nitrosylation

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-nitrosy… Show more

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Cited by 264 publications
(192 citation statements)
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“…This nomenclature could also accommodate chemical species not currently identified in vivo or in vitro, such as reaction products of cysteine sulfur with nitrogen oxide (for review of cysteine S-nitrosylation, see [8]). Figure 1 indicates the domain structure of HMGB1 and its family members; we expect HMGB2 to undergo the same posttranslational modification as HMGB1, although so far these modifications have not been identified or even been sought after.…”
mentioning
confidence: 99%
“…This nomenclature could also accommodate chemical species not currently identified in vivo or in vitro, such as reaction products of cysteine sulfur with nitrogen oxide (for review of cysteine S-nitrosylation, see [8]). Figure 1 indicates the domain structure of HMGB1 and its family members; we expect HMGB2 to undergo the same posttranslational modification as HMGB1, although so far these modifications have not been identified or even been sought after.…”
mentioning
confidence: 99%
“…Although the physiological relevance of S-nitrosylation has been shown in several proteins [79], there has been an active debate on its role in the nervous system among NO researchers [50]. One possible function of S-nitrosylation may be neuroprotection via the elimination of excess NO which would otherwise promote oxidative stress [80].…”
Section: Downstream Targets Of No In the Pcmentioning
confidence: 99%
“…One putative S-nitrosylation site has been identified. S-nitrosylation reactions signal a broad spectrum of cellular activities including transcriptional and posttranscriptional regulation of protein expression as well as regulation of membrane, cytosolic, mitochondrial, nuclear, and extracellular protein functions (Gould et al, 2013). All these PTMs suggest various cellular functions and processes including cell cycle regulation; DNA repair; chromosomal maintenance; modification of cytoplasmic signal transduction, nuclear import, and subnuclear compartmentalization; DNA repair; transcription regulation; and stress response.…”
Section: Posttranslational Modificationsmentioning
confidence: 99%