{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,4]],"date-time":"2026-10-04T03:16:33Z","timestamp":1791083793723,"version":"4.1.0"},"reference-count":75,"publisher":"MDPI AG","issue":"1","license":[{"start":{"date-parts":[[2025,1,16]],"date-time":"2025-01-16T00:00:00Z","timestamp":1736985600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001665","name":"Agence Nationale de la Recherche","doi-asserted-by":"publisher","award":["ANR-11-LABX-0002-01"],"award-info":[{"award-number":["ANR-11-LABX-0002-01"]}],"id":[{"id":"10.13039\/501100001665","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001665","name":"Agence Nationale de la Recherche","doi-asserted-by":"publisher","award":["ANR-15-IDEX-04-LUE"],"award-info":[{"award-number":["ANR-15-IDEX-04-LUE"]}],"id":[{"id":"10.13039\/501100001665","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001665","name":"Lorraine Universit\u00e9 d\u2019Excellence","doi-asserted-by":"publisher","award":["ANR-11-LABX-0002-01"],"award-info":[{"award-number":["ANR-11-LABX-0002-01"]}],"id":[{"id":"10.13039\/501100001665","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001665","name":"Lorraine Universit\u00e9 d\u2019Excellence","doi-asserted-by":"publisher","award":["ANR-15-IDEX-04-LUE"],"award-info":[{"award-number":["ANR-15-IDEX-04-LUE"]}],"id":[{"id":"10.13039\/501100001665","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Antioxidants"],"abstract":"<jats:p>The oxidative modification of specific cysteine residues to persulfides is thought to be the main way by which hydrogen sulfide (H2S) exerts its biological and signaling functions. Therefore, protein persulfidation represents an important thiol-switching mechanism as other reversible redox post-translational modifications. Considering their reductase activity but also their connections with proteins that generate H2S and its related molecules, the glutaredoxin (GRX) and thioredoxin (TRX)-reducing systems have potential dual roles in both protein persulfidation and depersulfidation. In this review, we will first focus on recent advances describing the physiological pathways leading to protein persulfidation before discussing the dual roles of the physiological TRX and glutathione\/GRX-reducing systems in protein persulfidation\/depersulfidation.<\/jats:p>","DOI":"10.3390\/antiox14010101","type":"journal-article","created":{"date-parts":[[2025,1,16]],"date-time":"2025-01-16T10:44:23Z","timestamp":1737024263000},"page":"101","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":12,"title":["Dual Roles of Reducing Systems in Protein Persulfidation and Depersulfidation"],"prefix":"10.3390","volume":"14","author":[{"given":"Zhichao","family":"Liu","sequence":"first","affiliation":[{"name":"Universit\u00e9 de Lorraine, INRAE, IAM, F-54000 Nancy, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2036-7884","authenticated-orcid":false,"given":"Nicolas","family":"Rouhier","sequence":"additional","affiliation":[{"name":"Universit\u00e9 de Lorraine, INRAE, IAM, F-54000 Nancy, France"},{"name":"Institut Universitaire de France, F-75000 Paris, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3127-2669","authenticated-orcid":false,"given":"J\u00e9r\u00e9my","family":"Couturier","sequence":"additional","affiliation":[{"name":"Universit\u00e9 de Lorraine, INRAE, IAM, F-54000 Nancy, France"},{"name":"Institut Universitaire de France, F-75000 Paris, France"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2025,1,16]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"741","DOI":"10.1093\/embo-reports\/kvf150","article-title":"The rhodanese\/Cdc25 phosphatase superfamily. 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