{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,19]],"date-time":"2026-09-19T13:58:22Z","timestamp":1789826302433,"version":"4.0.1"},"reference-count":198,"publisher":"SAGE Publications","issue":"18","license":[{"start":{"date-parts":[[2021,12,1]],"date-time":"2021-12-01T00:00:00Z","timestamp":1638316800000},"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":[[2021,12]]},"abstract":"<jats:sec>\n                    <jats:title>Significance:<\/jats:title>\n                    <jats:p>Changes in the oxidative balance can affect cellular physiology and adaptation through redox signaling. The endothelial cells that line blood vessels are particularly sensitive to reactive oxygen species, which can alter cell function by a number of mechanisms, including the oxidative post-translational modification (oxPTM) of proteins on critical cysteine thiols. Such modifications can act as redox-switches to alter the function of targeted proteins.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Recent Advances:<\/jats:title>\n                    <jats:p>\n                      Mapping the cysteine oxPTM proteome and characterizing the effects of individual oxPTMs to gain insight into consequences for cellular responses has proven challenging. A recent addition to the list of reversible oxPTMs that contributes to cellular redox homeostasis is persulfidation or\n                      <jats:italic toggle=\"yes\">S-<\/jats:italic>\n                      sulfhydration.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Critical Issues:<\/jats:title>\n                    <jats:p>\n                      It has been estimated that up to 25% of proteins are\n                      <jats:italic toggle=\"yes\">S<\/jats:italic>\n                      -sulfhydrated, making this modification almost as abundant as phosphorylation. In the endothelium, persulfides are generated by the trans-sulfuration pathway that catabolizes cysteine and cystathionine to generate hydrogen sulfide (H\n                      <jats:sub>2<\/jats:sub>\n                      S) and H\n                      <jats:sub>2<\/jats:sub>\n                      S-related sulfane sulfur compounds (H\n                      <jats:sub>2<\/jats:sub>\n                      S\n                      <jats:sub>n<\/jats:sub>\n                      ). This pathway is of particular importance for the vascular system, as the enzyme cystathionine \u03b3 lyase (CSE) in endothelial cells accounts for a significant portion of total vascular H\n                      <jats:sub>2<\/jats:sub>\n                      S\/H\n                      <jats:sub>2<\/jats:sub>\n                      S\n                      <jats:sub>n<\/jats:sub>\n                      production.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Future Directions:<\/jats:title>\n                    <jats:p>\n                      Impaired CSE activity in endothelial dysfunction has been linked with marked changes in the endothelial cell\n                      <jats:italic toggle=\"yes\">S<\/jats:italic>\n                      -sulfhydrome and can contribute to the development of atherosclerosis and hypertension. It will be interesting to determine how changes in the\n                      <jats:italic toggle=\"yes\">S<\/jats:italic>\n                      -sulfhydration of specific networks of proteins contribute to endothelial cell physiology and pathophysiology.\n                      <jats:italic toggle=\"yes\">Antioxid. Redox Signal<\/jats:italic>\n                      . 35, 1494\u20131514.\n                    <\/jats:p>\n                  <\/jats:sec>","DOI":"10.1089\/ars.2021.0162","type":"journal-article","created":{"date-parts":[[2021,8,4]],"date-time":"2021-08-04T05:06:48Z","timestamp":1628053608000},"page":"1494-1514","update-policy":"https:\/\/doi.org\/10.1177\/sage-journals-update-policy","source":"Crossref","is-referenced-by-count":32,"title":["Oxidative Post-Translational Modifications: A Focus on Cysteine\n                    <i>S-<\/i>\n                    Sulfhydration and the Regulation of Endothelial Fitness"],"prefix":"10.1177","volume":"35","author":[{"given":"Sofia-Iris","family":"Bibli","sequence":"first","affiliation":[{"name":"Institute for Vascular Signalling, Centre for Molecular Medicine, Goethe University, Frankfurt am Main, Germany."},{"name":"German Center of Cardiovascular Research (DZHK), Partner Site RheinMain, Frankfurt am Main, 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