{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,29]],"date-time":"2026-04-29T03:40:48Z","timestamp":1777434048087,"version":"3.51.4"},"reference-count":160,"publisher":"SAGE Publications","issue":"13","license":[{"start":{"date-parts":[[2014,5,1]],"date-time":"2014-05-01T00:00:00Z","timestamp":1398902400000},"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":[[2014,5]]},"abstract":"<jats:p>\n                    <jats:bold>\n                      <jats:italic toggle=\"yes\">Significance:<\/jats:italic>\n                    <\/jats:bold>\n                    The regulation of platelet function is finely tuned by a balance between the vasculature's redox environment and the oxidative processes that occur in it. The activation of platelets at sites of vascular damage is essential for the maintenance of normal hemostasis. In the extracellular milieu, a normal redox environment is maintained by thiol\/disulfide redox couples, which include reduced and oxidized glutathione (GSH\/GSSG) and cysteine (Cys\/CySS). Oxidative changes in either of the plasma redox potentials are directly linked with risk factors for cardiovascular disease.\n                    <jats:bold>\n                      <jats:italic toggle=\"yes\">Recent Advances:<\/jats:italic>\n                    <\/jats:bold>\n                    Many proteins found on the surface of platelets contain cysteine residues that are targets for oxidation. These include platelet-specific integrins and thiol isomerase enzymes that respond to changes in the extracellular redox environment, thus influencing normal platelet responses.\n                    <jats:bold>\n                      <jats:italic toggle=\"yes\">Critical Issues:<\/jats:italic>\n                    <\/jats:bold>\n                    The post-translational modification of critical cysteine thiol groups is linked to alterations in redox potentials and occurs both intracellularly and extracellularly in normal platelet activation. Platelet integrins, in particular, are prime targets for redox modification due to their high cysteine content. Although the role of thiol\/disulfide bond exchange in platelet activation is established, the effects of a changing redox environment on platelet reactivity are unclear.\n                    <jats:bold>\n                      <jats:italic toggle=\"yes\">Future Directions:<\/jats:italic>\n                    <\/jats:bold>\n                    A thorough understanding of these mechanisms and how they interact with other platelet signaling events is of the utmost importance for the development of novel therapeutic targets so that we can protect against inappropriate thrombus formation.\n                    <jats:italic toggle=\"yes\">Antioxid. Redox Signal.<\/jats:italic>\n                    20, 2074\u20132089.\n                  <\/jats:p>","DOI":"10.1089\/ars.2013.5698","type":"journal-article","created":{"date-parts":[[2013,11,10]],"date-time":"2013-11-10T06:14:20Z","timestamp":1384064060000},"page":"2074-2089","update-policy":"https:\/\/doi.org\/10.1177\/sage-journals-update-policy","source":"Crossref","is-referenced-by-count":12,"title":["Regulation of Platelet Activity in a Changing Redox Environment"],"prefix":"10.1177","volume":"20","author":[{"given":"Desmond D.","family":"Murphy","sequence":"first","affiliation":[{"name":"Royal College of Surgeons in Ireland","place":["Ireland"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Emily C.","family":"Reddy","sequence":"additional","affiliation":[{"name":"Royal College of Surgeons in Ireland","place":["Ireland"]},{"name":"Dublin City University","place":["Ireland"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Niamh","family":"Moran","sequence":"additional","affiliation":[{"name":"Royal College of Surgeons in Ireland","place":["Ireland"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sarah","family":"O'Neill","sequence":"additional","affiliation":[{"name":"Royal College of Surgeons in Ireland","place":["Ireland"]}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"179","published-online":{"date-parts":[[2014,5,1]]},"reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M313320200"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.0606411103"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(18)43421-7"},{"key":"e_1_3_2_5_2","doi-asserted-by":"publisher","DOI":"10.1016\/S1357-2725(96)00122-7"},{"key":"e_1_3_2_6_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0891-5849(99)00175-6"},{"key":"e_1_3_2_7_2","doi-asserted-by":"publisher","DOI":"10.1002\/lsm.10044"},{"key":"e_1_3_2_8_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.jacc.2005.09.063"},{"key":"e_1_3_2_9_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi901180v"},{"key":"e_1_3_2_10_2","first-page":"201","article-title":"Cellular redox: a modulator of intestinal epithelial cell proliferation","volume":"18","author":"Aw TY","year":"2003","unstructured":"Aw TY. 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