{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,3]],"date-time":"2026-06-03T18:51:42Z","timestamp":1780512702903,"version":"3.54.1"},"reference-count":106,"publisher":"MDPI AG","issue":"3","license":[{"start":{"date-parts":[[2020,3,10]],"date-time":"2020-03-10T00:00:00Z","timestamp":1583798400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"NIIH\/NHLBI","award":["P01 HL128192"],"award-info":[{"award-number":["P01 HL128192"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Antioxidants"],"abstract":"<jats:p>Long considered vital to antioxidant defenses, thiol chemistry has more recently been recognized to be of fundamental importance to cell signaling. S-nitrosothiols\u2014such as S-nitrosoglutathione (GSNO)\u2014and hydrogen sulfide (H2S) are physiologic signaling thiols that are regulated enzymatically. Current evidence suggests that they modify target protein function primarily through post-translational modifications. GSNO is made by NOS and other metalloproteins; H2S by metabolism of cysteine, homocysteine and cystathionine precursors. GSNO generally acts independently of NO generation and has a variety of gene regulatory, immune modulator, vascular, respiratory and neuronal effects. Some of this physiology is shared with H2S, though the mechanisms differ. Recent evidence also suggests that molecules resulting from reactions between GSNO and H2S, such as thionitrous acid (HSNO), could also have a role in physiology. Taken together, these data suggest important new potential targets for thiol-based drug development.<\/jats:p>","DOI":"10.3390\/antiox9030225","type":"journal-article","created":{"date-parts":[[2020,3,10]],"date-time":"2020-03-10T11:59:36Z","timestamp":1583841576000},"page":"225","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":21,"title":["An Update on Thiol Signaling: S-Nitrosothiols, Hydrogen Sulfide and a Putative Role for Thionitrous Acid"],"prefix":"10.3390","volume":"9","author":[{"given":"Nadzeya","family":"Marozkina","sequence":"first","affiliation":[{"name":"Herman Wells Center for Pediatric Research, Riley Hospital for Children, School of Medicine, Indiana University, Indianapolis, IN 46202, USA"},{"name":"Indiana University, School of Medicine, 1044 W. Walnut Street, R4-474 Indianapolis, IN 46202, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Benjamin","family":"Gaston","sequence":"additional","affiliation":[{"name":"Herman Wells Center for Pediatric Research, Riley Hospital for Children, School of Medicine, Indiana University, Indianapolis, IN 46202, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2020,3,10]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"550","DOI":"10.4049\/jimmunol.138.2.550","article-title":"L-arginine is required for expression of the activated macrophage effector mechanism causing selective metabolic inhibition in target cells","volume":"138","author":"Hibbs","year":"1987","journal-title":"J. Immunol."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"25218","DOI":"10.1074\/jbc.274.36.25218","article-title":"L-arginine binding to nitric-oxide synthase. 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