{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,2]],"date-time":"2026-09-02T10:32:37Z","timestamp":1788345157306,"version":"build-2803163510"},"reference-count":179,"publisher":"SAGE Publications","issue":"13","license":[{"start":{"date-parts":[[2021,10,11]],"date-time":"2021-10-11T00:00:00Z","timestamp":1633910400000},"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":[[2021,11]]},"abstract":"<jats:sec>\n                    <jats:title>Significance:<\/jats:title>\n                    <jats:p>Oxidative stress is a characteristic of many systemic diseases associated with thrombosis. Thiol isomerases are a family of oxidoreductases important in protein folding and are exquisitely sensitive to the redox environment. They are essential for thrombus formation and represent a previously unrecognized layer of control of the thrombotic process. Yet, the mechanisms by which thiol isomerases function in thrombus formation are unknown.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Recent Advances:<\/jats:title>\n                    <jats:p>\n                      The oxidoreductase activity of thiol isomerases in thrombus formation is controlled by the redox environment\n                      <jats:italic toggle=\"yes\">via<\/jats:italic>\n                      oxidative changes to active site cysteines. Specific alterations can now be detected owing to advances in the chemical biology of oxidative cysteine modifications.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Critical Issues:<\/jats:title>\n                    <jats:p>\n                      Understanding of the role of thiol isomerases in thrombus formation has focused largely on identifying single disulfide bond modifications in isolated proteins (\n                      <jats:italic toggle=\"yes\">e.g.<\/jats:italic>\n                      , \u03b1\n                      <jats:sub>IIb<\/jats:sub>\n                      \u03b2\n                      <jats:sub>3<\/jats:sub>\n                      , tissue factor, vitronectin, or glycoprotein Ib\u03b1 [GPIb\u03b1]). An alternative approach is to conceptualize thiol isomerases as effectors in redox signaling pathways that control thrombotic potential by modifying substrate networks.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Future Directions:<\/jats:title>\n                    <jats:p>Cysteine-based chemical biology will be employed to study thiol-dependent dynamics mediated by the redox state of thiol isomerases at the systems level. This approach could identify thiol isomerase-dependent modifications of the disulfide landscape that are prothrombotic.<\/jats:p>\n                  <\/jats:sec>","DOI":"10.1089\/ars.2021.0108","type":"journal-article","created":{"date-parts":[[2021,6,14]],"date-time":"2021-06-14T02:42:30Z","timestamp":1623638550000},"page":"1134-1155","update-policy":"https:\/\/doi.org\/10.1177\/sage-journals-update-policy","source":"Crossref","is-referenced-by-count":18,"title":["Oxidative Cysteine Modification of Thiol Isomerases in Thrombotic Disease: A Hypothesis"],"prefix":"10.1177","volume":"35","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-6340-457X","authenticated-orcid":false,"given":"Moua","family":"Yang","sequence":"first","affiliation":[{"name":"Division of Hemostasis and Thrombosis, Beth Israel Deaconess Medical Center and Harvard Medical School, Boston, Massachusetts, USA."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Robert","family":"Flaumenhaft","sequence":"additional","affiliation":[{"name":"Division of Hemostasis and Thrombosis, Beth Israel Deaconess Medical Center and Harvard Medical School, Boston, Massachusetts, USA."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"179","published-online":{"date-parts":[[2021,10,11]]},"reference":[{"key":"e_1_3_4_2_2","doi-asserted-by":"publisher","DOI":"10.1038\/s41589-018-0116-2"},{"key":"e_1_3_4_3_2","doi-asserted-by":"publisher","DOI":"10.1089\/ars.2006.8.283"},{"key":"e_1_3_4_4_2","doi-asserted-by":"publisher","DOI":"10.1002\/cbic.201900729"},{"key":"e_1_3_4_5_2","doi-asserted-by":"publisher","DOI":"10.1055\/s-0039-1681102"},{"key":"e_1_3_4_6_2","doi-asserted-by":"publisher","DOI":"10.1089\/ars.2007.1837"},{"key":"e_1_3_4_7_2","first-page":"850","article-title":"KDEL receptor 1 contributes to cell surface association of protein disulfide isomerases","volume":"52","author":"Bartels AK","year":"2019","unstructured":"Bartels AK, , G\u00f6ttert S, , Desel C, , Sch\u00e4fer M, , Krossa S, , Scheidig AJ, , Gr\u00f6tzinger J, , and Lorenzen I. 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