{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,24]],"date-time":"2026-09-24T04:32:07Z","timestamp":1790224327989,"version":"4.1.0"},"reference-count":254,"publisher":"MDPI AG","issue":"2","license":[{"start":{"date-parts":[[2020,2,18]],"date-time":"2020-02-18T00:00:00Z","timestamp":1581984000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100004442","name":"Narodowym Centrum Nauki","doi-asserted-by":"publisher","award":["UMO-2016\/22\/E\/NZ5\/00647."],"award-info":[{"award-number":["UMO-2016\/22\/E\/NZ5\/00647."]}],"id":[{"id":"10.13039\/501100004442","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biomolecules"],"abstract":"<jats:p>Hydrogen sulfide (H2S) is one of the important biological mediators involved in physiological and pathological processes in mammals. Recently developed H2S donors show promising effects against several pathological processes in preclinical and early clinical studies. For example, H2S donors have been found to be effective in the prevention of gastrointestinal ulcers during anti-inflammatory treatment. Notably, there are well-established medicines used for the treatment of a variety of diseases, whose chemical structure contains sulfur moieties and may release H2S. Hence, the therapeutic effect of these drugs may be partly the result of the release of H2S occurring during drug metabolism and\/or the effect of these drugs on the production of endogenous hydrogen sulfide. In this work, we review data regarding sulfur drugs commonly used in clinical practice that can support the hypothesis about H2S-dependent pharmacotherapeutic effects of these drugs.<\/jats:p>","DOI":"10.3390\/biom10020323","type":"journal-article","created":{"date-parts":[[2020,2,21]],"date-time":"2020-02-21T10:49:16Z","timestamp":1582282156000},"page":"323","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":120,"title":["Hydrogen Sulfide in Pharmacotherapy, Beyond the Hydrogen Sulfide-Donors"],"prefix":"10.3390","volume":"10","author":[{"given":"Ewelina","family":"Zaorska","sequence":"first","affiliation":[{"name":"Department of Experimental Physiology and Pathophysiology, Laboratory of Centre for Preclinical Research, Medical University of Warsaw, 02-091 Warsaw, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1943-0858","authenticated-orcid":false,"given":"Lenka","family":"Tomasova","sequence":"additional","affiliation":[{"name":"Institute of Clinical and Translational Research, Biomedical Research Center, Slovak Academy of Sciences, 84505 Bratislava, Slovakia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0968-3330","authenticated-orcid":false,"given":"Dominik","family":"Koszelewski","sequence":"additional","affiliation":[{"name":"Institute of Organic Chemistry, Polish Academy of Sciences Kasprzaka 44\/52, 01-224 Warsaw, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3032-196X","authenticated-orcid":false,"given":"Ryszard","family":"Ostaszewski","sequence":"additional","affiliation":[{"name":"Institute of Organic Chemistry, Polish Academy of Sciences Kasprzaka 44\/52, 01-224 Warsaw, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0088-8284","authenticated-orcid":false,"given":"Marcin","family":"Ufnal","sequence":"additional","affiliation":[{"name":"Department of Experimental Physiology and Pathophysiology, Laboratory of Centre for Preclinical Research, Medical University of Warsaw, 02-091 Warsaw, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2020,2,18]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"791","DOI":"10.1152\/physrev.00017.2011","article-title":"Physiological Implications of Hydrogen Sulfide: A Whiff Exploration That Blossomed","volume":"92","author":"Wang","year":"2012","journal-title":"Physiol. Rev."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"1066","DOI":"10.1523\/JNEUROSCI.16-03-01066.1996","article-title":"The possible role of hydrogen sulfide as an endogenous neuromodulator","volume":"16","author":"Abe","year":"1996","journal-title":"J. Neurosci."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"44","DOI":"10.3181\/00379727-179-42062","article-title":"Cyanide and sulfide interact with nitrogenous compounds to influence the relaxation of various smooth muscles","volume":"179","author":"Kruszyna","year":"1985","journal-title":"Proc. Soc. Exp. Biol. Med."},{"key":"ref_4","first-page":"587","article-title":"Effects of acute intoxication with hydrogen sulfide on central amino acid transmitter systems","volume":"9","author":"Kombian","year":"1988","journal-title":"Neurotoxicology"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"973","DOI":"10.1016\/0006-2952(89)90288-8","article-title":"Acute hydrogen sulfide poisoning. Demonstration of selective uptake of sulfide by the brainstem by measurement of brain sulfide levels","volume":"38","author":"Warenycia","year":"1989","journal-title":"Biochem. Pharm."},{"key":"ref_6","first-page":"93","article-title":"Stress-induced increases in brainstem amino acid levels are prevented by chronic sodium hydrosulfide treatment","volume":"11","author":"Warenycia","year":"1990","journal-title":"Neurotoxicology"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1152\/jn.1993.70.1.81","article-title":"The actions of hydrogen sulfide on dorsal raphe serotonergic neurons in vitro","volume":"70","author":"Kombian","year":"1993","journal-title":"J. Neurophysiol."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"5210","DOI":"10.1021\/cr040650b","article-title":"Use of Lawesson\u2019s Reagent in Organic Syntheses","volume":"107","author":"Ozturk","year":"2007","journal-title":"Chem. Rev."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"946","DOI":"10.1071\/CH09517","article-title":"Synthesis and Preliminary Pharmacological Evaluation of Aryl Dithiolethiones with Cyclooxygenase-2-Selective Inhibitory Activity and Hydrogen Sulfide-Releasing Properties","volume":"63","author":"Zanatta","year":"2010","journal-title":"Aust. J. Chem."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"1893","DOI":"10.1016\/j.bmcl.2008.02.007","article-title":"New sulfurated derivatives of. valproic acid with enhanced histone deacetylase inhibitory activity","volume":"18","author":"Perrino","year":"2008","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"4187","DOI":"10.1016\/j.bmc.2010.05.011","article-title":"New aryldithiolethione derivatives as potent histone deacetylase inhibitors","volume":"18","author":"Tazzari","year":"2010","journal-title":"Bioorg. Med. Chem."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"6359","DOI":"10.1021\/acs.jpcb.7b03683","article-title":"Computational Study of H2S Release in Reactions of Diallyl Polysulfides with Thiols","volume":"121","author":"Cai","year":"2017","journal-title":"J. Phys. Chem. B"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"904","DOI":"10.1021\/ml400239a","article-title":"Arylthioamides as H2S donors: L-cysteineactivated releasing properties and vascular effects in vitro and in vivo","volume":"4","author":"Martelli","year":"2013","journal-title":"ACS Med. Chem. Lett."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1016\/j.vph.2013.11.003","article-title":"Pharmacological characterization of the vascular effects of aryl isothiocyanates: Is hydrogen sulfide the real player?","volume":"60","author":"Martelli","year":"2014","journal-title":"Vascul. Pharmacol."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"10294","DOI":"10.1016\/j.bioorg.2019.102941","article-title":"Evaluation of thioamides, thiolactams and thioureas as hydrogen sulfide (H2S) donors for lowering blood pressure","volume":"88","author":"Zaorska","year":"2019","journal-title":"Bioorg. Chem."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"1346","DOI":"10.1016\/j.freeradbiomed.2009.09.018","article-title":"Making and working with hydrogen sulfide: The chemistry and generation of hydrogen sulfide in vitro and its measurement in vivo: A review","volume":"47","author":"Hughes","year":"2009","journal-title":"Free Radic. Biol. Med."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"16633","DOI":"10.1073\/pnas.0902952106","article-title":"No facilitator required for membrane transport of hydrogen sulfide","volume":"106","author":"Mathai","year":"2009","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"C941","DOI":"10.1152\/ajpcell.00178.2013","article-title":"Transport of H2S and HS\u2212 across the human red blood cell membrane: Rapid H2S diffusion and AE1-mediated Cl\u2212\/HS\u2212 exchange","volume":"305","author":"Jennings","year":"2013","journal-title":"Am. J. Physiol. Cell Physiol."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"494","DOI":"10.1038\/nature10881","article-title":"Identification and characterization of a bacterial hydrosulphide ion channel","volume":"483","author":"Czyzewski","year":"2012","journal-title":"Nature"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"504","DOI":"10.1038\/nrgastro.2012.85","article-title":"Contributions of the microbial hydrogen economy to colonic homeostasis","volume":"9","author":"Carbonero","year":"2012","journal-title":"Nat. Rev. Gastroenterol. Hepatol."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"310","DOI":"10.1002\/(SICI)1097-010X(19981015)282:3<310::AID-JEZ4>3.0.CO;2-P","article-title":"Sulfur reduction by human erythrocytes","volume":"282","author":"Searcy","year":"1998","journal-title":"J. Exp. Zool."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"22457","DOI":"10.1074\/jbc.M109.010868","article-title":"Relative contributions of cystathionine beta-synthase and gamma-cystathionase to H2S biogenesis via alternative trans-sulfuration reactions","volume":"284","author":"Singh","year":"2009","journal-title":"J. Biol. Chem."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"20002","DOI":"10.1074\/jbc.M113.466177","article-title":"Structure and kinetic analysis of H2S production by human mercaptopyruvate sulfurtransferase","volume":"288","author":"Yadav","year":"2013","journal-title":"J. Biol. Chem."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"587","DOI":"10.1126\/science.1162667","article-title":"H2S as a physiologic vasorelaxant: Hypertension in mice with deletion of cystathionine \u03b3-lyase","volume":"322","author":"Yang","year":"2008","journal-title":"Science"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1006\/abbi.1997.0486","article-title":"Identification and tissue distribution of human cystathionine beta-synthase mRNA isoforms","volume":"350","author":"Bao","year":"1998","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"284","DOI":"10.1016\/0005-2744(74)90014-X","article-title":"Role of 3-mercaptopyruvate sulfurtransferase in the formation of the iron-sulfur chromophore of adrenal ferredoxin","volume":"364","author":"Taniguchi","year":"1974","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"8310","DOI":"10.1074\/jbc.M115.639831","article-title":"Sulfide oxidation by a noncanonical pathway in red blood cells generates thiosulfate and polysulfides","volume":"290","author":"Vitvitsky","year":"2015","journal-title":"J. Biol. Chem."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"363","DOI":"10.1089\/ars.2010.3781","article-title":"The quantitative significance of the transsulfuration enzymes for H2S production in murine tissues","volume":"15","author":"Kabil","year":"2011","journal-title":"Antioxid. Redox Signal."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"577","DOI":"10.1111\/j.1471-4159.2008.05502.x","article-title":"Production of the gaseous signal molecule hydrogen sulfide in mouse tissues","volume":"106","author":"Linden","year":"2008","journal-title":"J. Neurochem."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"G288","DOI":"10.1152\/ajpgi.00324.2005","article-title":"Sulfide-detoxifying enzymes in the human colon are decreased in cancer and upregulated in differentiation","volume":"291","author":"Ramasamy","year":"2006","journal-title":"Am. J. Physiol. Gastrointest Liver Physiol."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"4382","DOI":"10.1016\/S0021-9258(18)97073-0","article-title":"Transsulfuration in mammals. Microassays and tissue distributions of three enzymes of the pathway","volume":"240","author":"Mudd","year":"1965","journal-title":"J. Biol. Chem."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"12679","DOI":"10.1073\/pnas.1308487110","article-title":"Oxygen-sensitive mitochondrial accumulation of cystathionine beta-synthase mediated by Lon protease","volume":"110","author":"Teng","year":"2013","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"6804","DOI":"10.1021\/bi300778t","article-title":"Human sulfide: Quinone oxidoreductase catalyzes the first step in hydrogen sulfide metabolism and produces a sulfane sulfur metabolite","volume":"51","author":"Jackson","year":"2012","journal-title":"Biochemistry"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"703","DOI":"10.1089\/ars.2008.2253","article-title":"3-Mercaptopyruvate sulfurtransferase produces hydrogen sulfide and bound sulfane sulfur in the brain","volume":"11","author":"Shibuya","year":"2009","journal-title":"Antioxid. Redox Signal."},{"key":"ref_35","doi-asserted-by":"crossref","unstructured":"Agrawal, N., and Banerjee, R. (2008). Human polycomb 2 protein is a SUMO E3 ligase and alleviates substrate-induced inhibition of cystathionine beta-synthase sumoylation. PLoS ONE, 3.","DOI":"10.1371\/journal.pone.0004032"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"325","DOI":"10.1016\/j.redox.2017.02.021","article-title":"Catalase as a sulfide-sulfur oxido-reductase: An ancient (and modern?) regulator of reactive sulfur species (RSS)","volume":"12","author":"Olson","year":"2017","journal-title":"Redox Biol."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"4149","DOI":"10.1128\/AEM.71.7.4149-4152.2005","article-title":"Identification and functional analysis of Escherichia coli cysteine desulfhydrases","volume":"71","author":"Awano","year":"2005","journal-title":"Appl. Environ. Microbiol."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"304","DOI":"10.1016\/0014-5793(75)80831-3","article-title":"Crystallization and properties of cysteine desulfhydrase from Aerobacter aerogenes","volume":"52","author":"Kumagai","year":"1975","journal-title":"FEBS Lett."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"1610","DOI":"10.1016\/S0021-9258(19)42924-4","article-title":"Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. VI. The reaction of carbon monoxide with the Escherichia coli holoenzyme, the hemoprotein, and free siroheme","volume":"249","author":"Murphy","year":"1974","journal-title":"J. Biol. Chem."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"986","DOI":"10.1021\/acs.biochem.6b01093","article-title":"Use of Tissue Metabolite Analysis and Enzyme Kinetics To Discriminate between Alternate Pathways for Hydrogen Sulfide Metabolism","volume":"56","author":"Augustyn","year":"2017","journal-title":"Biochemistry"},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"180","DOI":"10.1016\/j.bbrc.2016.10.022","article-title":"Protein polysulfidation-dependent persulfide dioxygenase activity of ethylmalonic encephalopathy protein 1","volume":"480","author":"Jung","year":"2016","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1016\/0304-4165(68)90108-6","article-title":"Mechanism of formation of sulphhaemoglobin","volume":"156","author":"Nichol","year":"1968","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"20","DOI":"10.15171\/ijoem.2015.482","article-title":"Effects of long-term exposure to hydrogen sulfide on human red blood cells","volume":"6","author":"Saeedi","year":"2015","journal-title":"Int. J. Occup. Environ. Med."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"037011","DOI":"10.1088\/1752-7155\/2\/3\/037011","article-title":"A sensor system for monitoring the simple gases hydrogen, carbon monoxide, hydrogen sulfide, ammonia and ethanol in exhaled breath","volume":"2","author":"Costello","year":"2008","journal-title":"J. Breath Res."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"R1479","DOI":"10.1152\/ajpregu.90566.2008","article-title":"Whole tissue hydrogen sulfide concentrations are orders of magnitude lower than presently accepted values","volume":"295","author":"Furne","year":"2008","journal-title":"Am. J. Physiol. Regul. Integr. Comp. Physiol."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"1655","DOI":"10.1152\/japplphysiol.00907.2001","article-title":"Physiology of sulfide in the rat colon: Use of bismuth to assess colonic sulfide production","volume":"92","author":"Levitt","year":"2002","journal-title":"J. Appl. Physiol."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"488","DOI":"10.1093\/ajcn\/72.6.1488","article-title":"Contribution of dietary protein to sulfide production in the large intestine: An in vitro and a controlled feeding study in humans","volume":"72","author":"Magee","year":"2000","journal-title":"Am. J. Clin. Nutr."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"424","DOI":"10.1177\/153537020322800413","article-title":"Gastrointestinal and microbial responses to sulfate-supplemented drinking water in mice","volume":"228","author":"Deplancke","year":"2003","journal-title":"Exp. Biol. Med."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"255","DOI":"10.1016\/S0006-2952(01)00657-8","article-title":"Oxidation of hydrogen sulfide and methanethiol to thiosulfate by rat tissues: A specialized function of the colonic mucosa","volume":"62","author":"Furne","year":"2001","journal-title":"Biochem. Pharmacol."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"1107","DOI":"10.1172\/JCI7712","article-title":"Detoxification of hydrogen sulfide and methanethiol in the cecal mucosa","volume":"104","author":"Levitt","year":"1999","journal-title":"J. Clin. Investig."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1016\/j.freeradbiomed.2013.02.024","article-title":"Microbial regulation of host hydrogen sulfide bioavailability and metabolism","volume":"60","author":"Shen","year":"2013","journal-title":"Free Radic. Biol. Med."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"2140","DOI":"10.1002\/1873-3468.13090","article-title":"Biological hydropersulfides and related polysulfides\u2014A new concept and perspective in redox biology","volume":"592","author":"Fukuto","year":"2018","journal-title":"FEBS Lett."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"74","DOI":"10.1016\/j.redox.2017.11.009","article-title":"Metabolism of hydrogen sulfide (H2S) and Production of Reactive Sulfur Species (RSS) by superoxide dismutase","volume":"15","author":"Olson","year":"2018","journal-title":"Redox Biol."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"14774","DOI":"10.1038\/srep14774","article-title":"Identification of H2S3 and H2S produced by 3-mercaptopyruvate sulfurtransferase in the brain","volume":"5","author":"Kimura","year":"2015","journal-title":"Sci. Rep."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"10459","DOI":"10.1038\/s41598-017-11004-7","article-title":"3-Mercaptopyruvate sulfurtransferase produces potential redox regulators cysteine- and glutathione-persulfide (Cys-SSH and GSSH) together with signaling molecules H2S2, H2S3 and H2S","volume":"7","author":"Kimura","year":"2017","journal-title":"Sci. Rep."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"479","DOI":"10.1042\/BJ20110841","article-title":"Thioredoxin and dihydrolipoic acid are required for 3-mercaptopyruvate sulfurtransferase to produce hydrogen sulfide","volume":"439","author":"Mikami","year":"2011","journal-title":"Biochem. J."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1089\/ars.2008.2132","article-title":"A source of hydrogen sulfide and a mechanism of its release in the brain","volume":"11","author":"Ishigami","year":"2009","journal-title":"Antioxid. Redox Signal."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"ra72","DOI":"10.1126\/scisignal.2000464","article-title":"HS signals through protein S-Sulfhydration","volume":"2","author":"Mustafa","year":"2009","journal-title":"Sci. Signal."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"608","DOI":"10.3389\/fphar.2017.00608","article-title":"H2S-Induced Sulfhydration: Biological Function and Detection Methodology","volume":"8","author":"Zhang","year":"2017","journal-title":"Front. Pharmacol."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"1749","DOI":"10.1089\/ars.2012.5041","article-title":"Polysulfides link H2S to protein thiol oxidation","volume":"19","author":"Greiner","year":"2013","journal-title":"Antioxid. Redox Signal."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"1177","DOI":"10.1038\/s41467-017-01311-y","article-title":"Cysteinyl-tRNA synthetase governs cysteine polysulfidation and mitochondrial bioenergetics","volume":"8","author":"Akaike","year":"2017","journal-title":"Nat. Commun."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1089\/ars.2019.7878","article-title":"Hemeproteins as Targets for Sulfide Species","volume":"32","author":"Boubeta","year":"2020","journal-title":"Antioxid. Redox Signal."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"78","DOI":"10.1016\/j.jinorgbio.2014.01.013","article-title":"Hydrogen sulfide activation in hemeproteins: The sulfheme scenario","volume":"133","author":"Pietri","year":"2014","journal-title":"J. Inorg. Biochem."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"299","DOI":"10.1016\/0005-2728(77)90216-X","article-title":"The effect of inhibitors on the oxygen kinetics of cytochrome c oxidase","volume":"460","author":"Petersen","year":"1977","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"591","DOI":"10.1042\/bj2240591","article-title":"Interactions of sulphide and other ligands with cytochrome c oxidase. An electron-paramagnetic-resonance study","volume":"224","author":"Hill","year":"1984","journal-title":"Biochem. J."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"24","DOI":"10.1016\/0005-2728(75)90186-3","article-title":"The effect of sulphide on cytochrome aa3. Isosteric and allosteric shifts of the reduced alpha-peak","volume":"396","author":"Nicholls","year":"1975","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"188","DOI":"10.1016\/0005-2728(76)90132-8","article-title":"Ligand-induced spectral changes in cytochrome c oxidase and their possible significance","volume":"449","author":"Nicholls","year":"1976","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"1699","DOI":"10.1096\/fj.06-7407com","article-title":"Sulfide, the first inorganic substrate for human cells","volume":"21","author":"Goubern","year":"2007","journal-title":"FASEB J."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"601","DOI":"10.1096\/fj.12-216507","article-title":"Intramitochondrial hydrogen sulfide production by 3-mercaptopyruvate sulfurtransferase maintains mitochondrial electron flow and supports cellular bioenergetics","volume":"27","author":"Modis","year":"2013","journal-title":"FASEB J."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"ra87","DOI":"10.1126\/scisignal.2005478","article-title":"The coordination of S-sulfhydration, S-nitrosylation, and phosphorylation of endothelial nitric oxide synthase by hydrogen sulfide","volume":"7","author":"Altaany","year":"2014","journal-title":"Sci. Signal."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"3171","DOI":"10.2337\/db16-0020","article-title":"Hydrogen Sulfide Induces Keap1 S-sulfhydration and Suppresses Diabetes-Accelerated Atherosclerosis via Nrf2 Activation","volume":"65","author":"Xie","year":"2016","journal-title":"Diabetes"},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"438","DOI":"10.1016\/j.molcel.2017.12.019","article-title":"Evidence against Stable Protein S-Nitrosylation as a Widespread Mechanism of Post-translational Regulation","volume":"69","author":"Wolhuter","year":"2018","journal-title":"Mol. Cell."},{"key":"ref_73","first-page":"E4651","article-title":"Key bioactive reaction products of the NO\/H2S interaction are S\/N-hybrid species, polysulfides, and nitroxyl","volume":"112","author":"Kuhnle","year":"2015","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1007\/978-1-4939-9528-8_8","article-title":"In Vivo Measurement of H2S, Polysulfides, and \u201cSSNO(-) Mix\u201d-Mediated Vasoactive Responses and Evaluation of Ten Hemodynamic Parameters from Rat Arterial Pulse Waveform","volume":"2007","author":"Kristek","year":"2019","journal-title":"Methods Mol. Biol."},{"key":"ref_75","first-page":"527","article-title":"Nitroso-sulfide coupled signaling triggers specific vasoactive effects in the intrarenal arteries of patients with arterial hypertension","volume":"68","author":"Cacanyiova","year":"2017","journal-title":"J. Physiol. Pharmacol."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1016\/j.niox.2014.12.008","article-title":"The reaction products of sulfide and S-nitrosoglutathione are potent vasorelaxants","volume":"46","author":"Berenyiova","year":"2015","journal-title":"Nitric Oxide"},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"684","DOI":"10.1089\/ars.2017.7083","article-title":"The Reactive Species Interactome: Evolutionary Emergence, Biological Significance, and Opportunities for Redox Metabolomics and Personalized Medicine","volume":"27","author":"Koning","year":"2017","journal-title":"Antioxid. Redox Signal."},{"key":"ref_78","doi-asserted-by":"crossref","unstructured":"Kharma, A., Grman, M., Misak, A., Dominguez-Alvarez, E., Nasim, M.J., Ondrias, K., Chovanec, M., and Jacob, C. (2019). Inorganic Polysulfides and Related Reactive Sulfur-Selenium Species from the Perspective of Chemistry. Molecules, 24.","DOI":"10.3390\/molecules24071359"},{"key":"ref_79","doi-asserted-by":"crossref","unstructured":"Grman, M., Nasim, M.J., Leontiev, R., Misak, A., Jakusova, V., Ondrias, K., and Jacob, C. (2017). Inorganic Reactive Sulfur-Nitrogen Species: Intricate Release Mechanisms or Cacophony in Yellow, Blue and Red?. Antioxidants, 6.","DOI":"10.3390\/antiox6010014"},{"key":"ref_80","doi-asserted-by":"crossref","unstructured":"Misak, A., Kurakova, L., Goffa, E., Brezova, V., Grman, M., Ondriasova, E., Chovanec, M., and Ondrias, K. (2019). Sulfide (Na2S) and Polysulfide (Na2S2) Interacting with Doxycycline Produce\/Scavenge Superoxide and Hydroxyl Radicals and Induce\/Inhibit DNA Cleavage. Molecules, 24.","DOI":"10.3390\/molecules24061148"},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"136","DOI":"10.1016\/j.niox.2017.09.006","article-title":"Polysulfides and products of H2S\/S-nitrosoglutathione in comparison to H2S, glutathione and antioxidant Trolox are potent scavengers of superoxide anion radical and produce hydroxyl radical by decomposition of H2O2","volume":"76","author":"Misak","year":"2018","journal-title":"Nitric Oxide"},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"479","DOI":"10.33549\/physiolres.932772","article-title":"Captopril partially decreases the effect of H2S on rat blood pressure and inhibits H2S-induced nitric oxide release from S-nitrosoglutathione","volume":"64","author":"Drobna","year":"2015","journal-title":"Physiol. Res."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"50","DOI":"10.1016\/j.niox.2016.09.007","article-title":"Intracolonic hydrogen sulfide lowers blood pressure in rats","volume":"60","author":"Tomasova","year":"2016","journal-title":"Nitric Oxide"},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1016\/j.niox.2014.12.012","article-title":"Effects of AP39, a novel triphenylphosphonium derivatised anethole dithiolethione hydrogen sulfide donor, on rat haemodynamic parameters and chloride and calcium Cav3 and RyR2 channels","volume":"46","author":"Tomasova","year":"2015","journal-title":"Nitric Oxide"},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"6008","DOI":"10.1093\/emboj\/20.21.6008","article-title":"The vasorelaxant effect of H2S as a novel endogenous gaseous KATP channel opener","volume":"20","author":"Zhao","year":"2001","journal-title":"EMBO J."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"527","DOI":"10.1006\/bbrc.1997.6878","article-title":"The possible role of hydrogen sulfide as an endogenous smooth muscle relaxant in synergy with nitric oxide","volume":"237","author":"Hosoki","year":"1997","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"625","DOI":"10.1038\/sj.bjp.0706906","article-title":"Regulation of vascular nitric oxide in vitro and in vivo; a new role for endogenous hydrogen sulphide?","volume":"149","author":"Ali","year":"2006","journal-title":"Br. J. Pharmacol."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"751","DOI":"10.1016\/j.pharep.2014.04.004","article-title":"Exogenous hydrogen sulfide causes different hemodynamic effects in normotensive and hypertensive rats via neurogenic mechanisms","volume":"66","author":"Sikora","year":"2014","journal-title":"Pharm. Rep."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"971","DOI":"10.1016\/j.pharep.2017.03.021","article-title":"Na2S, a fast-releasing H2S donor, given as suppository lowers blood pressure in rats","volume":"69","author":"Tomasova","year":"2017","journal-title":"Pharm. Rep."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"561","DOI":"10.18388\/abp.2017_1569","article-title":"Parenteral Na2S, a fast-releasing H2S donor, but not GYY4137, a slow-releasing H2S donor, lowers blood pressure in rats","volume":"64","author":"Drapala","year":"2017","journal-title":"Acta Biochim. Pol."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"2351","DOI":"10.1161\/CIRCULATIONAHA.107.753467","article-title":"Characterization of a novel, water-soluble hydrogen sulfide-releasing molecule (GYY4137): New insights into the biology of hydrogen sulfide","volume":"117","author":"Li","year":"2008","journal-title":"Circulation"},{"key":"ref_92","first-page":"501","article-title":"The adaptive role of nitric oxide and hydrogen sulphide in vasoactive responses of thoracic aorta is triggered already in young spontaneously hypertensive rats","volume":"67","author":"Cacanyiova","year":"2016","journal-title":"J. Physiol. Pharmacol."},{"key":"ref_93","first-page":"102","article-title":"Endogenous H2S is involved in the development of spontaneous hypertension","volume":"35","author":"Du","year":"2003","journal-title":"Beijing Da Xue Xue Bao Yi Xue Ban"},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"670","DOI":"10.1111\/j.1745-7254.2008.00796.x","article-title":"Hydrogen sulfide regulates lung tissue-oxidized glutathione and total antioxidant capacity in hypoxic pulmonary hypertensive rats","volume":"29","author":"Wei","year":"2008","journal-title":"Acta Pharmacol. Sin."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"243","DOI":"10.1016\/j.preghy.2014.04.013","article-title":"Molecular mechanisms and therapeutic implications of the carbon monoxide\/hmox1 and the hydrogen sulfide\/CSE pathways in the prevention of pre-eclampsia and fetal growth restriction","volume":"4","author":"Ahmed","year":"2014","journal-title":"Pregnancy Hypertens."},{"key":"ref_96","doi-asserted-by":"crossref","unstructured":"Tomasova, L., Konopelski, P., and Ufnal, M. (2016). Gut bacteria and hydrogen sulfide: The new old players in circulatory system homeostasis. Molecules, 21.","DOI":"10.3390\/molecules21111558"},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"172675","DOI":"10.1016\/j.ejphar.2019.172675","article-title":"L-cysteine\/hydrogen sulfide pathway induces cGMP-dependent relaxation of corpus cavernosum and penile arteries from patients with erectile dysfunction and improves arterial vasodilation induced by PDE5 inhibition","volume":"863","author":"Fernandez","year":"2019","journal-title":"Eur. J. Pharm."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"e12885","DOI":"10.1111\/and.12885","article-title":"Do penile haemodynamics change in the presence of hydrogen sulphide (H2S) donor in metabolic syndrome-induced erectile dysfunction?","volume":"50","author":"Dayar","year":"2018","journal-title":"Andrologia"},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"38","DOI":"10.1016\/j.phrs.2016.08.015","article-title":"Hydrogen sulfide compensates nitric oxide deficiency in murine corpus cavernosum","volume":"113","author":"Dikmen","year":"2016","journal-title":"Pharmacol. Res."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"1522","DOI":"10.1111\/j.1464-410X.2009.08415.x","article-title":"Effect of hydrogen sulphide-donating sildenafil (ACS6) on erectile function and oxidative stress in rabbit isolated corpus cavernosum and in hypertensive rats","volume":"103","author":"Shukla","year":"2009","journal-title":"BJU Int."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"H2088","DOI":"10.1152\/ajpheart.01290.2010","article-title":"Hydrogen sulfide dilates cerebral arterioles by activating smooth muscle cell plasma membrane KATP channels","volume":"300","author":"Liang","year":"2011","journal-title":"Am. J. Physiol. Heart Circ. Physiol."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"1167","DOI":"10.1089\/ars.2009.2894","article-title":"Molecular mechanism for H2S-induced activation of K ATP channels","volume":"12","author":"Jiang","year":"2010","journal-title":"Antioxid. Redox Signal."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"4579140","DOI":"10.1155\/2018\/4579140","article-title":"An Update on Hydrogen Sulfide and Nitric Oxide Interactions in the Cardiovascular System","volume":"2018","author":"Wu","year":"2018","journal-title":"Oxid. Med. Cell. Longev."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"1344","DOI":"10.1161\/HYPERTENSIONAHA.114.04281","article-title":"Protein kinase G I\u03b1 oxidation paradoxically underlies blood pressure lowering by the reductant hydrogen sulfde","volume":"64","author":"Stubbert","year":"2014","journal-title":"Hypertenstion"},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"C537","DOI":"10.1152\/ajpcell.00329.2016","article-title":"Vascular biology of hydrogen sulfide. American journal of physiology","volume":"312","author":"Kanagy","year":"2017","journal-title":"Cell Physiol."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"1","DOI":"10.2119\/molmed.2015.00035","article-title":"Regulation of Vascular Tone, Angiogenesis and Cellular Bioenergetics by the 3-Mercaptopyruvate Sulfurtransferase\/H2S Pathway: Functional Impairment by Hyperglycemia and Restoration by DL-alpha-Lipoic Acid","volume":"21","author":"Coletta","year":"2015","journal-title":"Mol. Med."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"448","DOI":"10.1089\/ars.2012.4565","article-title":"VEGFR2 functions as an H2S-targeting receptor protein kinase with its novel Cys1045-Cys1024 disulfide bond serving as a specific molecular switch for hydrogen sulfide actions in vascular endothelial cells","volume":"19","author":"Tao","year":"2013","journal-title":"Antioxid. Redox Signal."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"441","DOI":"10.1096\/fj.15-278648","article-title":"Cystathionine beta-synthase regulates endothelial function via protein S-sulfhydration","volume":"30","author":"Saha","year":"2016","journal-title":"FASEB J."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1016\/j.biochi.2015.03.009","article-title":"Hydrogen sulphide induces HIF-1alpha and Nrf2 in THP-1 macrophages","volume":"112","author":"Lohninger","year":"2015","journal-title":"Biochimie"},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"78","DOI":"10.1016\/j.atherosclerosis.2017.08.012","article-title":"Hydrogen sulfide attenuates calcification of vascular smooth muscle cells via KEAP1\/NRF2\/NQO1 activation","volume":"265","author":"Aghagolzadeh","year":"2017","journal-title":"Atherosclerosis"},{"key":"ref_111","doi-asserted-by":"crossref","unstructured":"Corsello, T., Komaravelli, N., and Casola, A. (2018). Role of Hydrogen Sulfide in NRF2- and Sirtuin-Dependent Maintenance of Cellular Redox Balance. Antioxidants, 7.","DOI":"10.3390\/antiox7100129"},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"105636","DOI":"10.1016\/j.biocel.2019.105636","article-title":"Protective Effects of Hydrogen Sulfide on a Cell Culture Model of Traumatic Scratch Injury involving Suppression of Oxidative Stress and Upregulation of Nrf-2","volume":"117","author":"Zhang","year":"2019","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"105746","DOI":"10.1016\/j.intimp.2019.105746","article-title":"Nrf2\/HO-1 signaling pathway participated in the protection of hydrogen sulfide on neuropathic pain in rats","volume":"75","author":"Chen","year":"2019","journal-title":"Int. Immunopharmacol."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"475","DOI":"10.1007\/s12017-018-8505-y","article-title":"Neuroprotective Effect of Hydrogen Sulfide in Hyperhomocysteinemia Is Mediated Through Antioxidant Action Involving Nrf2","volume":"20","author":"Kumar","year":"2018","journal-title":"Neuromol. Med."},{"key":"ref_115","first-page":"1299","article-title":"Protective effect of a hydrogen sulfide donor on balloon injury-induced restenosis via the Nrf2\/HIF-1alpha signaling pathway","volume":"43","author":"Ling","year":"2019","journal-title":"Int. J. Mol. Med."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1016\/j.molcel.2011.10.021","article-title":"Hydrogen Sulfide-Linked Sulfhydration of NF-\u03baB Mediates Its Antiapoptotic Actions","volume":"45","author":"Sen","year":"2012","journal-title":"Mol. Cell."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1146\/annurev.pa.32.040192.000545","article-title":"Toxicology of hydrogen sulfide","volume":"32","author":"Reiffenstein","year":"1992","journal-title":"Annu. Rev. Pharmacol. Toxicol."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"118","DOI":"10.1016\/j.neuint.2019.01.027","article-title":"Signaling by hydrogen sulfide (H2S) and polysulfides (H2Sn) in the central nervous system","volume":"126","author":"Kimura","year":"2019","journal-title":"Neurochem. Int."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"24","DOI":"10.1186\/s12990-015-0023-4","article-title":"Polysulfide evokes acute pain through the activation of nociceptive TRPA1 in mouse sensory neurons","volume":"11","author":"Hatakeyama","year":"2015","journal-title":"Mol. Pain"},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"10143","DOI":"10.1523\/JNEUROSCI.5779-12.2013","article-title":"TRPA1 channels are regulators of astrocyte basal calcium levels and long-term potentiation via constitutive D-serine release","volume":"33","author":"Shigetomi","year":"2013","journal-title":"J. Neurosci."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"1485","DOI":"10.1016\/S0006-291X(02)00422-9","article-title":"Brain hydrogen sulfide is severely decreased in Alzheimer\u2019s disease","volume":"293","author":"Eto","year":"2002","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"1984","DOI":"10.1007\/s11064-009-0006-9","article-title":"Hydrogen sulfide attenuates neuronal injury induced by vascular dementia via inhibiting apoptosis in rats","volume":"34","author":"Zhang","year":"2009","journal-title":"Neurochem. Res."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1111\/j.1474-9726.2009.00543.x","article-title":"Neuroprotective effects of hydrogen sulfide on Parkinson\u2019s disease rat models","volume":"9","author":"Hu","year":"2010","journal-title":"Aging Cell"},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"96","DOI":"10.1038\/nature13136","article-title":"Cystathionine gamma-lyase deficiency mediates neurodegeneration in Huntington\u2019s disease","volume":"509","author":"Paul","year":"2014","journal-title":"Nature"},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"200","DOI":"10.1038\/nm.1907","article-title":"Loss of ETHE1, a mitochondrial dioxygenase, causes fatal sulfide toxicity in ethylmalonic encephalopathy","volume":"15","author":"Tiranti","year":"2009","journal-title":"Nat. Med."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"1165","DOI":"10.1096\/fj.04-1815fje","article-title":"Hydrogen sulfide protects neurons from oxidative stress","volume":"18","author":"Kimura","year":"2004","journal-title":"FASEB J."},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1089\/ars.2008.2282","article-title":"Hydrogen sulfide increases glutathione production and suppresses oxidative stress in mitochondria","volume":"12","author":"Kimura","year":"2010","journal-title":"Antioxid. Redox Signal."},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"1626","DOI":"10.1038\/ncomms2623","article-title":"Sulfhydration mediates neuroprotective actions of parkin","volume":"4","author":"Vandiver","year":"2013","journal-title":"Nat. Commun."},{"key":"ref_129","unstructured":"Coavoy-Sanchez, S.A., Costa, S.K.P., and Muscara, M.N. (2019). Hydrogen sulfide and dermatological diseases. Br. J. Pharmacol., 1\u20139."},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"2223","DOI":"10.1007\/s10620-017-4681-0","article-title":"Gaseous Mediators in Gastrointestinal Mucosal Defense and Injury","volume":"62","author":"Wallace","year":"2017","journal-title":"Dig. Dis. Sci."},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"S26","DOI":"10.1016\/j.niox.2015.02.062","article-title":"PP32\u2014Antipsoriatic activity of GYY4137 (a slow-releasing hydrogen sulphide donor) microemulsion system using a mouse skin model of psoriasis","volume":"47","author":"Schmidt","year":"2015","journal-title":"Nitric Oxide"},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.coph.2015.08.005","article-title":"Gaseous mediator-based anti-inflammatory drugs","volume":"25","author":"Sulaieva","year":"2015","journal-title":"Curr. Opin. Pharm."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"447","DOI":"10.1124\/jpet.106.106435","article-title":"5-Amino-2-hydroxybenzoic acid 4-(5-thioxo-5H-[1,2]dithiol-3yl)-phenyl ester (ATB-429), a hydrogen sulfide-releasing derivative of mesalamine, exerts antinociceptive effects in a model of postinflammatory hypersensitivity","volume":"319","author":"Distrutti","year":"2006","journal-title":"J. Pharm. Exp."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"1463","DOI":"10.1111\/j.1476-5381.2010.00640.x","article-title":"Differing effects of exogenous and endogenous hydrogen sulphide in carrageenan-induced knee joint synovitis in the rat","volume":"159","author":"Santos","year":"2010","journal-title":"Br. J. Pharmacol."},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"325","DOI":"10.1124\/jpet.105.091595","article-title":"Evidence that hydrogen sulfide exerts antinociceptive effects in the gastrointestinal tract by activating KATP channels","volume":"316","author":"Distrutti","year":"2006","journal-title":"J. Pharmacol. Exp. Ther."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"12474","DOI":"10.1073\/pnas.1306241110","article-title":"Tumor-derived hydrogen sulfide, produced by cystathionine-beta-synthase, stimulates bioenergetics, cell proliferation, and angiogenesis in colon cancer","volume":"110","author":"Szabo","year":"2013","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"1500","DOI":"10.1016\/j.bbabio.2010.04.004","article-title":"Oxidation of hydrogen sulfide remains a priority in mammalian cells and causes reverse electron transfer in colonocytes","volume":"1797","author":"Lagoutte","year":"2010","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"146","DOI":"10.1016\/j.niox.2014.03.001","article-title":"Effect of S-adenosyl-L-methionine (SAM), an allosteric activator of cystathionine-beta-synthase (CBS) on colorectal cancer cell proliferation and bioenergetics in vitro","volume":"41","author":"Modis","year":"2014","journal-title":"Nitric Oxide"},{"key":"ref_139","doi-asserted-by":"crossref","unstructured":"Bhattacharyya, S., Saha, S., Giri, K., Lanza, I.R., Nair, K.S., Jennings, N.B., Rodriguez-Aguayo, C., Lopez-Berestein, G., Basal, E., and Weaver, A.L. (2013). Cystathionine beta-synthase (CBS) contributes to advanced ovarian cancer progression and drug resistance. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0079167"},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"233","DOI":"10.1007\/978-3-319-18144-8_12","article-title":"Hydrogen Sulfide and Cancer","volume":"230","author":"Hellmich","year":"2015","journal-title":"Handb. Exp. Pharmacol."},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"301","DOI":"10.1111\/j.1464-5491.2005.01415.x","article-title":"Reduced plasma total homocysteine concentrations in Type 1 diabetes mellitus is determined by increased renal clearance","volume":"22","author":"Veldman","year":"2005","journal-title":"Diabet. Med."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"519","DOI":"10.1113\/jphysiol.2005.097642","article-title":"Activation of KATP channels by H2S in rat insulin-secreting cells and the underlying mechanisms","volume":"569","author":"Yang","year":"2005","journal-title":"J. Physiol."},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1038\/labinvest.2008.109","article-title":"Pancreatic islet overproduction of H2S and suppressed insulin release in Zucker diabetic rats","volume":"89","author":"Wu","year":"2009","journal-title":"Lab. Investig."},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.niox.2019.02.011","article-title":"Sodium\/calcium exchanger is involved in apoptosis induced by H2S in tumor cells through decreased levels of intracellular pH","volume":"87","author":"Szadvari","year":"2019","journal-title":"Nitric Oxide"},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"1329","DOI":"10.1007\/s00424-013-1366-1","article-title":"Sodium\/calcium exchanger is upregulated by sulfide signaling, forms complex with the beta1 and beta3 but not beta2 adrenergic receptors, and induces apoptosis","volume":"466","author":"Markova","year":"2014","journal-title":"Pflug. Arch."},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"350","DOI":"10.1111\/apha.12105","article-title":"Sulphide signalling potentiates apoptosis through the up-regulation of IP3 receptor types 1 and 2","volume":"208","author":"Lencesova","year":"2013","journal-title":"Acta Physiol."},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1089\/ars.2017.7058","article-title":"A Review of Hydrogen Sulfide Synthesis, Metabolism, and Measurement: Is Modulation of Hydrogen Sulfide a Novel Therapeutic for Cancer?","volume":"31","author":"Cao","year":"2019","journal-title":"Antioxid. Redox Signal."},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"9764","DOI":"10.1021\/jm501105n","article-title":"Beyond C, H, O, and N! Analysis of the elemental composition of U.S. FDA approved drug architectures","volume":"57","author":"Smith","year":"2014","journal-title":"J. Med. Chem."},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"2633","DOI":"10.1055\/s-0035-1560638","article-title":"Natural Products Containing Hydrogen Sulfide Releasing Moieties","volume":"26","author":"Pluth","year":"2015","journal-title":"Synlett"},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"6633","DOI":"10.1021\/es049514e","article-title":"Equilibrium Distribution of Polysulfide Ions in Aqueous Solutions at 25 \u00b0C: A New Approach for the Study of Polysulfides\u2019 Equilibria","volume":"38","author":"Kamyshny","year":"2014","journal-title":"Environ. Sci. Technol."},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"1200","DOI":"10.1016\/S0891-5849(03)00144-8","article-title":"Comparative effects of mono-, di-, tri-, and tetrasulfides derived from plants of the Allium family: Redox cycling in vitro and hemolytic activity and Phase 2 enzyme induction in vivo","volume":"34","author":"Munday","year":"2003","journal-title":"Free Radic. Biol. Med."},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"3905","DOI":"10.1021\/cr010127m","article-title":"The Chemistry of Organic Polysulfanes R\u2212Sn\u2212R (n> 2)","volume":"102","author":"Steudel","year":"2002","journal-title":"Chem. Rev."},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"1505","DOI":"10.1039\/B703832A","article-title":"Polysulfides as biologically active ingredients of garlic","volume":"5","author":"Anwar","year":"2007","journal-title":"Org. Biomol. Chem."},{"key":"ref_154","doi-asserted-by":"crossref","first-page":"17977","DOI":"10.1073\/pnas.0705710104","article-title":"Hydrogen sulfide mediates the vasoactivity of garlic","volume":"104","author":"Benavides","year":"2007","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1080\/10942910601113327","article-title":"Allicin and Other Functional Active Components in Garlic: Health Benefits and Bioavailability","volume":"10","author":"Rahman","year":"2007","journal-title":"Int. J. Food Prop."},{"key":"ref_156","doi-asserted-by":"crossref","first-page":"60","DOI":"10.1017\/S0954422410000338","article-title":"Garlic in health and disease","volume":"24","author":"Rana","year":"2011","journal-title":"Nutr. Res. Rev."},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"538","DOI":"10.1080\/10408390802145344","article-title":"Garlic: Nature\u2019s protection against physiological threats","volume":"49","author":"Butt","year":"2009","journal-title":"Crit. Rev. Food Sci. Nutr."},{"key":"ref_158","doi-asserted-by":"crossref","first-page":"1284","DOI":"10.1038\/aps.2013.127","article-title":"Hydrogen sulfide and translational medicine","volume":"34","author":"Guo","year":"2013","journal-title":"Acta Pharm. Sin."},{"key":"ref_159","doi-asserted-by":"crossref","first-page":"610","DOI":"10.1055\/s-0034-1368591","article-title":"Hydrogen Sulfide Releasing Capacity of Natural Isothiocyanates: Is It a Reliable Explanation for the Multiple Biological Effects of Brassicaceae?","volume":"80","author":"Citi","year":"2014","journal-title":"Planta Med."},{"key":"ref_160","doi-asserted-by":"crossref","first-page":"420","DOI":"10.1016\/j.taap.2011.09.026","article-title":"Hydrogen sulfide mediates the antisurvival effect of sulforaphane on human prostate cancer cells","volume":"257","author":"Pei","year":"2011","journal-title":"Toxicol. Appl. Pharm."},{"key":"ref_161","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1055\/s-0031-1278362","article-title":"Antihypertensive effects of dietary protein and its mechanism","volume":"19","author":"Vasdev","year":"2010","journal-title":"Int. J. Angiol."},{"key":"ref_162","doi-asserted-by":"crossref","first-page":"1636S","DOI":"10.1093\/jn\/136.6.1636S","article-title":"The Sulfur-Containing Amino Acids: An Overview","volume":"136","author":"Brosnan","year":"2006","journal-title":"J. Nutr."},{"key":"ref_163","doi-asserted-by":"crossref","first-page":"2675","DOI":"10.1016\/j.bmc.2012.02.028","article-title":"Thioglycine and l-thiovaline: Biologically active H2S-donors","volume":"20","author":"Zhou","year":"2012","journal-title":"Bioorg. Med. Chem."},{"key":"ref_164","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1055\/s-0031-1278316","article-title":"The antihypertensive effect of cysteine","volume":"18","author":"Vasdev","year":"2009","journal-title":"Int. J. Angiol."},{"key":"ref_165","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1016\/S0140-6736(95)90165-5","article-title":"Homocysteine metabolism in pregnancies complicated by neural-tube defects","volume":"345","author":"Mills","year":"1995","journal-title":"Lancet"},{"key":"ref_166","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1146\/annurev.med.49.1.31","article-title":"Homocysteine and cardiovascular disease","volume":"49","author":"Refsum","year":"1998","journal-title":"Annu. Rev. Med."},{"key":"ref_167","doi-asserted-by":"crossref","first-page":"1296","DOI":"10.1016\/j.yexcr.2010.02.032","article-title":"Selenoproteins-What unique properties can arise with selenocysteine in place of cysteine?","volume":"316","author":"Arner","year":"2010","journal-title":"Exp. Cell Res."},{"key":"ref_168","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1016\/S1872-0854(10)04006-3","article-title":"Redox Chemistry of Biological Thiols","volume":"4","author":"Nagy","year":"2010","journal-title":"Adv. Mol. Toxicol."},{"key":"ref_169","doi-asserted-by":"crossref","first-page":"244","DOI":"10.1016\/j.freeradbiomed.2013.05.050","article-title":"The thiol pool in human plasma: The central contribution of albumin to redox processes","volume":"65","author":"Turell","year":"2013","journal-title":"Free Radic. Biol. Med."},{"key":"ref_170","first-page":"11","article-title":"Review on Various Uses of N-Acetyl Cysteine","volume":"19","author":"Mokhtari","year":"2017","journal-title":"Cell J."},{"key":"ref_171","doi-asserted-by":"crossref","first-page":"225","DOI":"10.4062\/biomolther.2017.251","article-title":"Effects and Mechanisms of Taurine as a Therapeutic Agent","volume":"26","author":"Schaffer","year":"2018","journal-title":"Biomol. Ther."},{"key":"ref_172","first-page":"625","article-title":"Constitutive expression of the taurine transporter in a human colon carcinoma cell line","volume":"263","author":"Tiruppathi","year":"1992","journal-title":"Am. J. Physiol."},{"key":"ref_173","doi-asserted-by":"crossref","first-page":"349","DOI":"10.1113\/jphysiol.2002.026500","article-title":"Structure, function and immunolocalization of a proton-coupled amino acid transporter (hPAT1) in the human intestinal cell line Caco-2","volume":"546","author":"Chen","year":"2003","journal-title":"J. Physiol."},{"key":"ref_174","doi-asserted-by":"crossref","first-page":"448","DOI":"10.3389\/fphys.2012.00448","article-title":"Microbial pathways in colonic sulfur metabolism and links with health and disease","volume":"3","author":"Carbonero","year":"2012","journal-title":"Front. Physiol."},{"key":"ref_175","doi-asserted-by":"crossref","first-page":"653","DOI":"10.1097\/00004872-199406000-00005","article-title":"Taurine amplifies renal kallikrein and prevents salt-induced hypertension in Dahl rats","volume":"12","author":"Ideishi","year":"1994","journal-title":"J. Hypertens."},{"key":"ref_176","doi-asserted-by":"crossref","first-page":"643","DOI":"10.1007\/s007260070014","article-title":"Effects of high salt diets and taurine on the development of hypertension in the stroke-prone spontaneously hypertensive rat","volume":"19","author":"Dawson","year":"2000","journal-title":"Amino Acids"},{"key":"ref_177","doi-asserted-by":"crossref","first-page":"132","DOI":"10.1007\/s00380-003-0757-1","article-title":"Oral taurine supplementation prevents fructose-induced hypertension in rats","volume":"19","author":"Harada","year":"2004","journal-title":"Heart Vessels"},{"key":"ref_178","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1111\/j.1440-1681.2006.04345.x","article-title":"Taurine attenuates hypertension and renal dysfunction induced by cyclosporine A in rats","volume":"33","author":"Hagar","year":"2006","journal-title":"Clin. Exp. Pharm. Physiol."},{"key":"ref_179","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1007\/978-0-387-75681-3_8","article-title":"Antihypertensive effect of taurine in rat","volume":"643","author":"Hu","year":"2009","journal-title":"Adv. Exp. Med. Biol."},{"key":"ref_180","doi-asserted-by":"crossref","first-page":"581","DOI":"10.1007\/978-3-319-15126-7_47","article-title":"Role of ROS Production and Turnover in the Antioxidant Activity of Taurine","volume":"803","author":"Shimada","year":"2015","journal-title":"Adv. Exp. Med. Biol."},{"key":"ref_181","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1038\/sj.ki.5001503","article-title":"Accelerated NaCl-induced hypertension in taurine-deficient rat: Role of renal function","volume":"70","author":"Mozaffari","year":"2006","journal-title":"Kidney Int."},{"key":"ref_182","doi-asserted-by":"crossref","first-page":"541","DOI":"10.1161\/HYPERTENSIONAHA.115.06624","article-title":"Taurine supplementation lowers blood pressure and improves vascular function in prehypertension: Randomized, double-blind, placebo controlled study","volume":"67","author":"Sun","year":"2016","journal-title":"Hypertension"},{"key":"ref_183","doi-asserted-by":"crossref","first-page":"S9","DOI":"10.1097\/01.hjh.0000165623.72310.dd","article-title":"The cardiovscular continuum and renin-angiotensin-aldosterone system blockade","volume":"13","author":"Dzau","year":"2005","journal-title":"J. Hypertens."},{"key":"ref_184","doi-asserted-by":"crossref","first-page":"274","DOI":"10.1007\/s11892-006-0060-5","article-title":"Inhibition of the renin angiotensin system: Implications for the endothelium","volume":"6","author":"Savoia","year":"2006","journal-title":"Curr. Diab. Rep."},{"key":"ref_185","doi-asserted-by":"crossref","first-page":"441","DOI":"10.1126\/science.191908","article-title":"Design of specific inhibitors of angiotensin-converting enzyme: New class of orally active antihypertensive agents","volume":"196","author":"Ondetti","year":"1977","journal-title":"Science"},{"key":"ref_186","doi-asserted-by":"crossref","first-page":"437","DOI":"10.1007\/BF00054194","article-title":"Attenuation of myocardial reperfusion injury by sulphydryl-containing angiotensin converting enzyme inhibitors","volume":"6","author":"Liu","year":"1992","journal-title":"Cardiovasc. Drugs"},{"key":"ref_187","doi-asserted-by":"crossref","first-page":"836","DOI":"10.1016\/S0140-6736(79)92186-X","article-title":"Captopril in the treatment of clinical hypertension and cardiac failure","volume":"2","author":"Atkinson","year":"1979","journal-title":"Lancet"},{"key":"ref_188","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1161\/JAHA.116.003531","article-title":"Zofenopril Protects against Myocardial Ischemia-Reperfusion Injury by Increasing Nitric Oxide and Hydrogen Sulfide Bioavailability","volume":"5","author":"Donnarumma","year":"2016","journal-title":"J. Am. Heart Assoc."},{"key":"ref_189","doi-asserted-by":"crossref","first-page":"2961","DOI":"10.1111\/bph.13101","article-title":"Characterization of zofenoprilat as an inducer of functional angiogenesis through increased H2S availability","volume":"172","author":"Terzuoli","year":"2015","journal-title":"Br. J. Pharmacol."},{"key":"ref_190","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1016\/j.phrs.2013.08.003","article-title":"The sulphydryl containing ACE inhibitor Zofenoprilat protects coronary endothelium from Doxorubicin-induced apoptosis","volume":"76","author":"Monti","year":"2013","journal-title":"Pharmacol. Res."},{"key":"ref_191","doi-asserted-by":"crossref","first-page":"426","DOI":"10.1016\/j.phrs.2016.09.017","article-title":"H2S dependent and independent anti-inflammatory activity of zofenoprilat in cells of the vascular wall","volume":"113","author":"Monti","year":"2016","journal-title":"Pharmacol. Res."},{"key":"ref_192","doi-asserted-by":"crossref","first-page":"138","DOI":"10.1093\/cvr\/cvu026","article-title":"Hydrogen sulfide accounts for the peripheral vascular effects of zofenopril independently of ACE inhibition","volume":"102","author":"Bucci","year":"2014","journal-title":"Cardiovasc. Res."},{"key":"ref_193","doi-asserted-by":"crossref","first-page":"383","DOI":"10.1007\/BF00316478","article-title":"Pharmacokinetics of temocapril, an ACE inhibitor with preferential biliary excretion, in patients with impaired liver function","volume":"44","author":"Furuta","year":"1993","journal-title":"Eur. J. Clin. Pharm."},{"key":"ref_194","doi-asserted-by":"crossref","first-page":"920","DOI":"10.1161\/01.CIR.0000029801.86489.50","article-title":"Comparison of Omapatrilat and Enalapril in Patients With Chronic Heart Failure: The Omapatrilat Versus Enalapril Randomized Trial of Utility in Reducing Events (OVERTURE)","volume":"106","author":"Packer","year":"2002","journal-title":"Circulation"},{"key":"ref_195","doi-asserted-by":"crossref","first-page":"347","DOI":"10.1097\/00005344-199503000-00001","article-title":"Responses to an Orally Active Renin Inhibitor, Remikiren (Ro 42\u20135892), After Controlled Salt Depletion in Humans","volume":"25","author":"MacFadyen","year":"1995","journal-title":"J. Cardiovasc. Pharmacol."},{"key":"ref_196","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1161\/01.HYP.22.1.9","article-title":"Comparative effects of three different potent renin inhibitors in primates","volume":"22","author":"Clozel","year":"1993","journal-title":"Hypertension"},{"key":"ref_197","first-page":"A6445","article-title":"Optimization of tissue targeting properties of macitentan, a new dual endothelin receptor antagonist, improves its efficacy in a rat model of pulmonary fibrosis associated with pulmonary arterial hypertension","volume":"183","author":"Iglarz","year":"2011","journal-title":"Am. J. Respir. Crit. Care Med."},{"key":"ref_198","doi-asserted-by":"crossref","first-page":"325","DOI":"10.1023\/A:1011460426786","article-title":"Hemodynamic effects of bosentan in patients with chronic heart failure","volume":"6","author":"Kiowski","year":"2001","journal-title":"Heart Fail. Rev."},{"key":"ref_199","doi-asserted-by":"crossref","first-page":"654","DOI":"10.1124\/jpet.105.092544","article-title":"Differential effects of the phosphodiesterase type 5 inhibitors sildenafil, vardenafil, and tadalafil in rat aorta","volume":"316","author":"Teixeira","year":"2006","journal-title":"J. Pharmacol. Exp. Ther."},{"key":"ref_200","doi-asserted-by":"crossref","first-page":"998","DOI":"10.1016\/j.urology.2004.07.038","article-title":"Simultaneous administration of vardenafil and tamsulosin does not induce clinically significant hypotension in patients with benign prostatic hyperplasia","volume":"64","author":"Auerbach","year":"2004","journal-title":"Urology"},{"key":"ref_201","doi-asserted-by":"crossref","first-page":"2249","DOI":"10.1016\/S0024-3205(01)01308-X","article-title":"Inhibition of cyclic GMP hydrolysis in human corpus cavernosum smooth muscle cells by vardenafil, a novel, selective phosphodiesterase type 5 inhibitor","volume":"69","author":"Kim","year":"2001","journal-title":"Life Sci."},{"key":"ref_202","doi-asserted-by":"crossref","first-page":"282","DOI":"10.1038\/sj.ijir.3900726","article-title":"The phosphodiesterase inhibitory selectivity and the in vitro and in vivo potency of the new PDE5 inhibitor vardenafil","volume":"13","author":"Angulo","year":"2001","journal-title":"Int. J. Impot. Res."},{"key":"ref_203","first-page":"47","article-title":"Sildenafil: An orally active type 5 cyclic GMP-specific phosphodiesterase inhibitor for the treatment of penile erectile dysfunction","volume":"8","author":"Boolell","year":"1996","journal-title":"Int. J. Impot. Res."},{"key":"ref_204","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1016\/S0735-1097(98)00656-1","article-title":"ACC\/AHA expert consensus document. Use of sildenafil (Viagra) in patients with cardiovascular disease","volume":"1","author":"Cheitlin","year":"1999","journal-title":"J. Am. Coll. Cardiol."},{"key":"ref_205","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1111\/j.1472-8206.1999.tb00333.x","article-title":"The pharmacological basis and pathophysiological significance of the heart rate-lowering property of diltiazem","volume":"13","author":"Grosset","year":"1999","journal-title":"Fundam. Clin. Pharmacol."},{"key":"ref_206","doi-asserted-by":"crossref","first-page":"405","DOI":"10.1089\/ars.2010.3517","article-title":"Hydrogen sulfide: Neurophysiology and neuropathology","volume":"15","author":"Hu","year":"2011","journal-title":"Antioxid. Redox Signal."},{"key":"ref_207","doi-asserted-by":"crossref","unstructured":"Perez-Torres, I., Guarner-Lans, V., and Rubio-Ruiz, M.E. (2017). Reductive stress in inflammation-associated diseases and the pro-oxidant effect of antioxidant agents. Int. J. Mol. Sci., 18.","DOI":"10.3390\/ijms18102098"},{"key":"ref_208","first-page":"1","article-title":"Excess hydrogen sulfide and polysulfides production underlies a schizophrenia pathophysiology","volume":"e10695","author":"Ide","year":"2019","journal-title":"EMBO Mol. Med."},{"key":"ref_209","doi-asserted-by":"crossref","first-page":"412","DOI":"10.1046\/j.1440-1681.2002.03677.x","article-title":"Age-related changes in dopamine D2 receptors in rat heart and coronary vessels","volume":"29","author":"Cavallotti","year":"2002","journal-title":"Clin. Exp. Pharmacol. Physiol."},{"key":"ref_210","doi-asserted-by":"crossref","first-page":"14","DOI":"10.1016\/0169-328X(94)90206-2","article-title":"Differential influence of haloperidol and sulpiride on dopamine receptors and peptide mRNA levels in the rat striatum and pituitary","volume":"23","author":"Jaber","year":"1994","journal-title":"Brain Res. Mol. Brain Res."},{"key":"ref_211","doi-asserted-by":"crossref","first-page":"412","DOI":"10.1093\/nar\/30.1.412","article-title":"TTD: Therapeutic Target Database","volume":"30","author":"Chen","year":"2002","journal-title":"Nucleic Acids Res."},{"key":"ref_212","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1016\/j.parkreldis.2004.07.008","article-title":"Plasma homocysteine levels in Parkinson\u2019s disease: Role of antiparkinsonian medications","volume":"11","author":"Zoccolella","year":"2005","journal-title":"Parkinsonism Relat. Disord."},{"key":"ref_213","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1016\/bs.mie.2014.11.015","article-title":"Neuroprotective effects of hydrogen sulfide in Parkinson\u2019s disease animal models: Methods and protocols","volume":"554","author":"Xue","year":"2015","journal-title":"Methods Enzym."},{"key":"ref_214","doi-asserted-by":"crossref","first-page":"343","DOI":"10.1089\/ars.2010.3671","article-title":"Inhaled Hydrogen Sulfide Prevents Neurodegeneration and Movement Disorder in a Mouse Model of Parkinson\u2019s Disease","volume":"15","author":"Kida","year":"2011","journal-title":"Antioxid. Redox Signal."},{"key":"ref_215","doi-asserted-by":"crossref","first-page":"17318","DOI":"10.1074\/jbc.M110.115261","article-title":"Effects of Hydrogen Sulfide-releasing l-DOPA Derivatives on Glial Activation","volume":"285","author":"Lee","year":"2010","journal-title":"J. Biol. Chem."},{"key":"ref_216","doi-asserted-by":"crossref","first-page":"1888","DOI":"10.1056\/NEJM199906173402407","article-title":"Gastrointestinal toxicity of nonsteroidal anti-inflammatory drugs","volume":"340","author":"Wolfe","year":"1999","journal-title":"N. Engl. J. Med."},{"key":"ref_217","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1586\/ecp.10.122","article-title":"Therapeutic potential of new hydrogen sulfide-releasing hybrids","volume":"4","author":"Sparatore","year":"2011","journal-title":"Expert Rev. Clin. Pharm."},{"key":"ref_218","doi-asserted-by":"crossref","first-page":"G467","DOI":"10.1152\/ajpgi.00169.2013","article-title":"Hydrogen sulfide-based therapeutics and gastrointestinal diseases: Translating physiology to treatments","volume":"305","author":"Chan","year":"2013","journal-title":"Am. J. Physiol. Gastrointest Liver. Physiol."},{"key":"ref_219","doi-asserted-by":"crossref","first-page":"586","DOI":"10.1016\/j.freeradbiomed.2008.11.013","article-title":"Pharmacological profile of a novel H2S-releasing aspirin","volume":"46","author":"Perrino","year":"2009","journal-title":"Free Radic. Biol. Med."},{"key":"ref_220","doi-asserted-by":"crossref","first-page":"706","DOI":"10.1016\/j.freeradbiomed.2006.12.011","article-title":"Anti-inflammatory and gastrointestinal effects of a novel diclofenac derivative","volume":"42","author":"Li","year":"2007","journal-title":"Free Radic. Biol. Med."},{"key":"ref_221","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1053\/j.gastro.2006.11.042","article-title":"Gastrointestinal safety and antiinflammatory effects of a hydrogen sulfide-releasing diclofenac derivative in the rat","volume":"132","author":"Wallace","year":"2007","journal-title":"Gastroenterology"},{"key":"ref_222","doi-asserted-by":"crossref","first-page":"996","DOI":"10.1038\/sj.bjp.0707193","article-title":"Enhanced activity of a hydrogen sulphide releasing derivative of mesalamine (ATB-429) in a mouse model of colitis","volume":"150","author":"Fiorucci","year":"2007","journal-title":"Br. J. Pharm."},{"key":"ref_223","doi-asserted-by":"crossref","first-page":"1236","DOI":"10.1111\/j.1476-5381.2009.00611.x","article-title":"Markedly reduced toxicity of a hydrogen sulphide-releasing derivative of naproxen (ATB-346)","volume":"159","author":"Wallace","year":"2010","journal-title":"Br. J. Pharm."},{"key":"ref_224","doi-asserted-by":"crossref","first-page":"715","DOI":"10.1016\/j.bcp.2011.12.018","article-title":"Hydrogen sulfide-releasing NSAIDs inhibit the growth of human cancer cells: A general property and evidence of a tissue type-independent effect","volume":"83","author":"Chattopadhyay","year":"2012","journal-title":"Biochem. Pharm."},{"key":"ref_225","doi-asserted-by":"crossref","first-page":"879","DOI":"10.1038\/nrd1225","article-title":"COX-2 and beyond: Approaches to prostaglandin inhibition in human disease","volume":"2","author":"FitzGerald","year":"2003","journal-title":"Nat. Rev. Drug Discov."},{"key":"ref_226","doi-asserted-by":"crossref","first-page":"433","DOI":"10.1056\/NEJM200108093450607","article-title":"The coxibs, selective inhibitors of cyclooxygenase-2","volume":"345","author":"FitzGerald","year":"2001","journal-title":"N. Engl. J. Med."},{"key":"ref_227","doi-asserted-by":"crossref","first-page":"1773","DOI":"10.1016\/S0960-894X(99)00288-7","article-title":"The discovery of rofecoxib, [MK 966, VIOXX, 4-(4\u2032-methylsulfonylphenyl)-3-phenyl- 2(5H)-furanone], an orally active cyclooxygenase-2 inhibitor","volume":"9","author":"Prasit","year":"1999","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"ref_228","first-page":"346","article-title":"Etoricoxib. Analgesic drug, antiarthritic, cyclooxygenase-2 inhibitor","volume":"26","author":"Sorbera","year":"2001","journal-title":"Drugs Future"},{"key":"ref_229","doi-asserted-by":"crossref","first-page":"775","DOI":"10.1021\/jm990577v","article-title":"4-[5-Methyl-3-phenylisoxazol-4- yl]- benzenesulfonamide, Valdecoxib: A potent and selective inhibitor of COX-2","volume":"43","author":"Talley","year":"2000","journal-title":"J. Med. Chem."},{"key":"ref_230","doi-asserted-by":"crossref","first-page":"255","DOI":"10.1016\/j.amjmed.2005.09.054","article-title":"Celecoxib Versus Naproxen and Diclofenac in Osteoarthritis Patients: SUCCESS-I Study","volume":"119","author":"Singh","year":"2006","journal-title":"Am. J. Med."},{"key":"ref_231","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1177\/0300060516673707","article-title":"Efficacy of celecoxib versus ibuprofen for the treatment of patients with osteoarthritis of the knee: A randomized double-blind, non-inferiority trial","volume":"45","author":"Gordo","year":"2017","journal-title":"J. Int. Med. Res."},{"key":"ref_232","doi-asserted-by":"crossref","first-page":"142","DOI":"10.1021\/jm070821f","article-title":"New Celecoxib Derivatives as Anti-Inflammatory Agents","volume":"51","author":"Fischer","year":"2008","journal-title":"J. Med. Chem."},{"key":"ref_233","doi-asserted-by":"crossref","first-page":"953","DOI":"10.2165\/00003495-199345060-00007","article-title":"Cyclosporin. A review of its pharmacodynamic and pharmacokinetic properties, and therapeutic use in immunoregulatory disorders","volume":"45","author":"Faulds","year":"1993","journal-title":"Drugs"},{"key":"ref_234","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1016\/j.toxlet.2017.09.002","article-title":"Perinatal ciclosporin A exposure elicits sex-related cardiac dysfunction and inflammation in the rat progeny","volume":"281","author":"Awan","year":"2017","journal-title":"Toxicol. Lett."},{"key":"ref_235","doi-asserted-by":"crossref","first-page":"F572","DOI":"10.1152\/ajprenal.00275.2017","article-title":"Molecular basis of the counteraction by calcium channel blockers of Cyclosporine nephrotoxicity","volume":"315","author":"Hammoud","year":"2018","journal-title":"Am. J. Physiol. Ren. Physiol."},{"key":"ref_236","doi-asserted-by":"crossref","first-page":"287","DOI":"10.1007\/s12012-016-9383-x","article-title":"H2S prevents cyclosporine A-induced vasomotor alteration in rats","volume":"17","author":"Ping","year":"2017","journal-title":"Cardiovasc. Toxicol."},{"key":"ref_237","doi-asserted-by":"crossref","first-page":"419","DOI":"10.1016\/j.jss.2015.02.061","article-title":"Hydrogen sulphide as a novel therapy to ameliorate cyclosporine nephrotoxicity","volume":"197","author":"Lee","year":"2015","journal-title":"J. Surg. Res."},{"key":"ref_238","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.prostaglandins.2019.01.001","article-title":"Upregulation of cystathionine-\u03b3-lyase\/hydrogen sulfide pathway underlies the celecoxib counteraction of cyclosporine-induced hypertension and renal insult in rats","volume":"141","author":"Helmy","year":"2019","journal-title":"Prostaglandins Lipid Mediat."},{"key":"ref_239","doi-asserted-by":"crossref","first-page":"513","DOI":"10.1089\/thy.1999.9.513","article-title":"Methimazole and Propylthiouracil Increase Cellular Thyroid Peroxidase Activity and Thyroid Peroxidase mRNA in Cultured Porcine Thyroid Follicles","volume":"9","author":"Sugawara","year":"1999","journal-title":"Thyroid"},{"key":"ref_240","doi-asserted-by":"crossref","first-page":"1041","DOI":"10.1089\/thy.2006.16.1041","article-title":"Differential evolution of thyroid peroxidase and thyrotropin receptor antibodies in Graves\u2019 disease: Thyroid peroxidase antibody activity reverts to pretreatment level after carbimazole withdrawal","volume":"16","author":"Guilhem","year":"2006","journal-title":"Thyroid"},{"key":"ref_241","doi-asserted-by":"crossref","first-page":"2706","DOI":"10.1021\/ar4001229","article-title":"Antithyroid Drugs and Their Analogues: Synthesis, Structure, and Mechanism of Action","volume":"46","author":"Manna","year":"2013","journal-title":"Acc. Chem. Res."},{"key":"ref_242","doi-asserted-by":"crossref","first-page":"1320","DOI":"10.1016\/j.cmet.2017.05.003","article-title":"Hypothalamic-pituitary axis regulates hydrogen sulfide production","volume":"25","author":"Hine","year":"2017","journal-title":"Cell Metab."},{"key":"ref_243","doi-asserted-by":"crossref","first-page":"665","DOI":"10.1078\/0944-7113-00277","article-title":"The combined effects of Trigonella and Allium extracts in the regulation of hyperthyroidism in rats","volume":"10","author":"Tahiliani","year":"2003","journal-title":"Phytomedicine"},{"key":"ref_244","first-page":"5","article-title":"Comparison of the effectiveness of pentobarbital and thiopental in patients with refractory intracranial hypertension. Preliminary report of 20 patients","volume":"16","author":"Barcelo","year":"2005","journal-title":"Neurocirugia"},{"key":"ref_245","doi-asserted-by":"crossref","first-page":"474","DOI":"10.1097\/00000542-198106000-00006","article-title":"Pharmacokinetics and plasma binding of thiopental. II: Studies at cesarean section","volume":"54","author":"Morgan","year":"1981","journal-title":"Anesthesiology"},{"key":"ref_246","first-page":"301","article-title":"Surgical anesthesia in turkeys with thialbarbital sodium","volume":"36","author":"Bercovitz","year":"1975","journal-title":"Am. J. Vet. Res."},{"key":"ref_247","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1080\/AC.67.4.2170696","article-title":"Intractable hypotension and myocardial ischaemia induced by co-ingestion of ethanol and disulfiram","volume":"67","author":"Moreels","year":"2012","journal-title":"Acta Cardiol."},{"key":"ref_248","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1097\/00000441-200701000-00007","article-title":"Refractive Hypotension in a Patient with Disulfiram-Ethanol Reaction","volume":"333","author":"Ho","year":"2007","journal-title":"Am. J. Med. Sci."},{"key":"ref_249","doi-asserted-by":"crossref","first-page":"152","DOI":"10.1007\/BF01965129","article-title":"Peripheral hypotensive and central hypertensive effects of cimetidine","volume":"12","author":"Paakkari","year":"1982","journal-title":"Agents Actions"},{"key":"ref_250","doi-asserted-by":"crossref","first-page":"20824","DOI":"10.1074\/jbc.M114.559518","article-title":"Hydrogen Sulfide Represses Androgen Receptor Transactivation by Targeting at the Second Zinc Finger Module","volume":"289","author":"Zhao","year":"2014","journal-title":"J. Biol. Chem."},{"key":"ref_251","doi-asserted-by":"crossref","first-page":"437","DOI":"10.3892\/ol.2014.2700","article-title":"Sulfur inhibits the growth of androgen-independent prostate cancer in vivo","volume":"9","author":"Duan","year":"2014","journal-title":"Oncol. Lett."},{"key":"ref_252","doi-asserted-by":"crossref","first-page":"1629","DOI":"10.1158\/1535-7163.MCT-13-0027","article-title":"NF- B2\/p52 Induces Resistance to Enzalutamide in Prostate Cancer: Role of Androgen Receptor and Its Variants","volume":"12","author":"Nadiminty","year":"2013","journal-title":"Mol. Cancer"},{"key":"ref_253","doi-asserted-by":"crossref","first-page":"1057","DOI":"10.1007\/s40262-015-0283-1","article-title":"Pharmacokinetic Drug Interaction Studies with Enzalutamide","volume":"54","author":"Gibbons","year":"2015","journal-title":"Clin. Pharm."},{"key":"ref_254","doi-asserted-by":"crossref","first-page":"823","DOI":"10.1080\/14737140.2018.1503954","article-title":"Apalutamide for the treatment of prostate cancer","volume":"18","author":"Rathkopf","year":"2018","journal-title":"Expert Rev. 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