{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,19]],"date-time":"2026-10-19T01:42:27Z","timestamp":1792374147967,"version":"4.4.0"},"reference-count":209,"publisher":"SAGE Publications","issue":"10","license":[{"start":{"date-parts":[[2019,4,1]],"date-time":"2019-04-01T00:00:00Z","timestamp":1554076800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.sagepub.com\/page\/policies\/text-and-data-mining-license"}],"content-domain":{"domain":["journals.sagepub.com"],"crossmark-restriction":true},"short-container-title":["Antioxidants &amp; Redox Signaling"],"published-print":{"date-parts":[[2019,4]]},"abstract":"<jats:sec>\n                    <jats:title>Significance:<\/jats:title>\n                    <jats:p>Protein S-nitrosylation, the oxidative modification of cysteine by nitric oxide (NO) to form protein S-nitrosothiols (SNOs), mediates redox-based signaling that conveys, in large part, the ubiquitous influence of NO on cellular function. S-nitrosylation regulates protein activity, stability, localization, and protein\u2013protein interactions across myriad physiological processes, and aberrant S-nitrosylation is associated with diverse pathophysiologies.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Recent Advances:<\/jats:title>\n                    <jats:p>It is recently recognized that S-nitrosylation endows S-nitroso-protein (SNO-proteins) with S-nitrosylase activity, that is, the potential to trans-S-nitrosylate additional proteins, thereby propagating SNO-based signals, analogous to kinase-mediated signaling cascades. In addition, it is increasingly appreciated that cellular S-nitrosylation is governed by dynamically coupled equilibria between SNO-proteins and low-molecular-weight SNOs, which are controlled by a growing set of enzymatic denitrosylases comprising two main classes (high and low molecular weight). S-nitrosylases and denitrosylases, which together control steady-state SNO levels, may be identified with distinct physiology and pathophysiology ranging from cardiovascular and respiratory disorders to neurodegeneration and cancer.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Critical Issues:<\/jats:title>\n                    <jats:p>The target specificity of protein S-nitrosylation and the stability and reactivity of protein SNOs are determined substantially by enzymatic machinery comprising highly conserved transnitrosylases and denitrosylases. Understanding the differential functionality of SNO-regulatory enzymes is essential, and is amenable to genetic and pharmacological analyses, read out as perturbation of specific equilibria within the SNO circuitry.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Future Directions:<\/jats:title>\n                    <jats:p>The emerging picture of NO biology entails equilibria among potentially thousands of different SNOs, governed by denitrosylases and nitrosylases. Thus, to elucidate the operation and consequences of S-nitrosylation in cellular contexts, studies should consider the roles of SNO-proteins as both targets and transducers of S-nitrosylation, functioning according to enzymatically governed equilibria.<\/jats:p>\n                  <\/jats:sec>","DOI":"10.1089\/ars.2017.7403","type":"journal-article","created":{"date-parts":[[2017,11,13]],"date-time":"2017-11-13T02:07:44Z","timestamp":1510538864000},"page":"1331-1351","update-policy":"https:\/\/doi.org\/10.1177\/sage-journals-update-policy","source":"Crossref","is-referenced-by-count":277,"title":["Protein S-Nitrosylation: Determinants of Specificity and Enzymatic Regulation of S-Nitrosothiol-Based Signaling"],"prefix":"10.1177","volume":"30","author":[{"given":"Colin T.","family":"Stomberski","sequence":"first","affiliation":[{"name":"Institute for Transformative Molecular Medicine, Case Western Reserve University, Cleveland, Ohio."},{"name":"Department of Biochemistry, Case Western Reserve University, Cleveland, Ohio."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Douglas T.","family":"Hess","sequence":"additional","affiliation":[{"name":"Institute for Transformative Molecular Medicine, Case Western Reserve University, Cleveland, Ohio."},{"name":"Department of Medicine, Case Western Reserve University, Cleveland, Ohio."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jonathan S.","family":"Stamler","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Case Western Reserve University, Cleveland, Ohio."},{"name":"Department of Medicine, Case Western Reserve University, Cleveland, Ohio."},{"name":"Harrington Discovery Institute, University Hospitals Cleveland Medical Center, Cleveland, 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