{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,11]],"date-time":"2026-10-11T02:41:11Z","timestamp":1791686471093,"version":"4.3.4"},"reference-count":129,"publisher":"MDPI AG","issue":"3","license":[{"start":{"date-parts":[[2023,3,1]],"date-time":"2023-03-01T00:00:00Z","timestamp":1677628800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["R01-AG062469"],"award-info":[{"award-number":["R01-AG062469"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Center for Drug Design (CDD), University of Minnesota","award":["R01-AG062469"],"award-info":[{"award-number":["R01-AG062469"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Antioxidants"],"abstract":"<jats:p>3-mercaptopyruvate sulfurtransferase (3-MST) plays the important role of producing hydrogen sulfide. Conserved from bacteria to Mammalia, this enzyme is localized in mitochondria as well as the cytoplasm. 3-MST mediates the reaction of 3-mercaptopyruvate with dihydrolipoic acid and thioredoxin to produce hydrogen sulfide. Hydrogen sulfide is also produced through cystathionine beta-synthase and cystathionine gamma-lyase, along with 3-MST, and is known to alleviate a variety of illnesses such as cancer, heart disease, and neurological conditions. The importance of cystathionine beta-synthase and cystathionine gamma-lyase in hydrogen sulfide biogenesis is well-described, but documentation of the 3-MST pathway is limited. This account compiles the current state of knowledge about the role of 3-MST in physiology and pathology. Attempts at targeting the 3-MST pathway for therapeutic benefit are discussed, highlighting the potential of 3-MST as a therapeutic target.<\/jats:p>","DOI":"10.3390\/antiox12030603","type":"journal-article","created":{"date-parts":[[2023,3,1]],"date-time":"2023-03-01T03:03:48Z","timestamp":1677639828000},"page":"603","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":58,"title":["Role of 3-Mercaptopyruvate Sulfurtransferase (3-MST) in Physiology and Disease"],"prefix":"10.3390","volume":"12","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-4469-0827","authenticated-orcid":false,"given":"Swetha Pavani","family":"Rao","sequence":"first","affiliation":[{"name":"Center for Drug Design, College of Pharmacy, University of Minnesota, Minneapolis, MN 55455, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2381-6518","authenticated-orcid":false,"given":"Prakashkumar","family":"Dobariya","sequence":"additional","affiliation":[{"name":"Center for Drug Design, College of Pharmacy, University of Minnesota, Minneapolis, MN 55455, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Harshini","family":"Bellamkonda","sequence":"additional","affiliation":[{"name":"Center for Drug Design, College of Pharmacy, University of Minnesota, Minneapolis, MN 55455, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8733-2029","authenticated-orcid":false,"given":"Swati S.","family":"More","sequence":"additional","affiliation":[{"name":"Center for Drug Design, College of Pharmacy, University of Minnesota, Minneapolis, MN 55455, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2023,3,1]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"2621","DOI":"10.1089\/ars.2013.5448","article-title":"Hydrogen sulfide is an endogenous regulator of aging in Caenorhabditis elegans","volume":"20","author":"Qabazard","year":"2014","journal-title":"Antioxid. Redox Signal."},{"key":"ref_2","doi-asserted-by":"crossref","unstructured":"Randi, E.B., Casili, G., Jacquemai, S., and Szabo, C. (2021). Selenium-Binding Protein 1 (SELENBP1) Supports Hydrogen Sulfide Biosynthesis and Adipogenesis. Antioxidants, 10.","DOI":"10.3390\/antiox10030361"},{"key":"ref_3","doi-asserted-by":"crossref","unstructured":"Aroca, A., Gotor, C., Bassham, D.C., and Romero, L.C. (2020). Hydrogen Sulfide: From a Toxic Molecule to a Key Molecule of Cell Life. Antioxidants, 9.","DOI":"10.3390\/antiox9070621"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1016\/j.niox.2013.07.002","article-title":"Hydrogen sulfide chemical biology: Pathophysiological roles and detection","volume":"35","author":"Kolluru","year":"2013","journal-title":"Nitric Oxide"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"43464","DOI":"10.1074\/jbc.M112.414722","article-title":"Detection of reaction intermediates during human cystathionine beta-synthase-monitored turnover and H2S production","volume":"287","author":"Yadav","year":"2012","journal-title":"J. Biol. Chem."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"52082","DOI":"10.1074\/jbc.C400481200","article-title":"Production of the neuromodulator H2S by cystathionine beta-synthase via the condensation of cysteine and homocysteine","volume":"279","author":"Chen","year":"2004","journal-title":"J. Biol. Chem."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"13528","DOI":"10.1021\/bi0615644","article-title":"Human cystathionine beta-synthase is a target for sumoylation","volume":"45","author":"Kabil","year":"2006","journal-title":"Biochemistry"},{"key":"ref_8","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_9","doi-asserted-by":"crossref","first-page":"106","DOI":"10.1089\/ars.2011.4349","article-title":"Role of cystathionine gamma-lyase\/hydrogen sulfide pathway in cardiovascular disease: A novel therapeutic strategy?","volume":"17","author":"Pan","year":"2012","journal-title":"Antioxid. Redox Signal."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"87","DOI":"10.3389\/fendo.2013.00087","article-title":"Production of hydrogen sulfide from d-cysteine and its therapeutic potential","volume":"4","author":"Shibuya","year":"2013","journal-title":"Front. Endocrinol."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"362","DOI":"10.1016\/j.bbrc.2003.11.130","article-title":"H2S generated by heart in rat and its effects on cardiac function","volume":"313","author":"Geng","year":"2004","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_12","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_13","doi-asserted-by":"crossref","first-page":"848","DOI":"10.1139\/y03-077","article-title":"Modulation of endogenous production of H2S in rat tissues","volume":"81","author":"Zhao","year":"2003","journal-title":"Can. J. Physiol. Pharmacol."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1016\/j.bcp.2017.11.014","article-title":"A review of hydrogen sulfide (H(2)S) donors: Chemistry and potential therapeutic applications","volume":"149","author":"Powell","year":"2018","journal-title":"Biochem. Pharmacol."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"741","DOI":"10.1093\/embo-reports\/kvf150","article-title":"The rhodanese\/Cdc25 phosphatase superfamily. Sequence-structure-function relations","volume":"3","author":"Bordo","year":"2002","journal-title":"EMBO Rep."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"34543","DOI":"10.1074\/jbc.M114.605733","article-title":"Characterization and interaction studies of two isoforms of the dual localized 3-mercaptopyruvate sulfurtransferase TUM1 from humans","volume":"289","author":"Frasdorf","year":"2014","journal-title":"J. Biol. Chem."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"16230","DOI":"10.1074\/jbc.270.27.16230","article-title":"Cytosolic mercaptopyruvate sulfurtransferase is evolutionarily related to mitochondrial rhodanese. Striking similarity in active site amino acid sequence and the increase in the mercaptopyruvate sulfurtransferase activity of rhodanese by site-directed mutagenesis","volume":"270","author":"Nagahara","year":"1995","journal-title":"J. Biol. Chem."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"243","DOI":"10.1007\/s004180050286","article-title":"Tissue and subcellular distribution of mercaptopyruvate sulfurtransferase in the rat: Confocal laser fluorescence and immunoelectron microscopic studies combined with biochemical analysis","volume":"110","author":"Nagahara","year":"1998","journal-title":"Histochem. Cell Biol."},{"key":"ref_19","first-page":"1277","article-title":"Mercaptopyruvate sulfurtransferase as a defense against cyanide toxication: Molecular properties and mode of detoxification","volume":"14","author":"Nagahara","year":"1999","journal-title":"Histol. Histopathol."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"1986","DOI":"10.1038\/srep01986","article-title":"Antioxidant enzyme, 3-mercaptopyruvate sulfurtransferase-knockout mice exhibit increased anxiety-like behaviors: A model for human mercaptolactate-cysteine disulfiduria","volume":"3","author":"Nagahara","year":"2013","journal-title":"Sci. Rep."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"34569","DOI":"10.1074\/jbc.M505643200","article-title":"Post-translational regulation of mercaptopyruvate sulfurtransferase via a low redox potential cysteine-sulfenate in the maintenance of redox homeostasis","volume":"280","author":"Nagahara","year":"2005","journal-title":"J. Biol. Chem."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"1792","DOI":"10.1089\/ars.2012.5031","article-title":"Regulation of mercaptopyruvate sulfurtransferase activity via intrasubunit and intersubunit redox-sensing switches","volume":"19","author":"Nagahara","year":"2013","journal-title":"Antioxid. Redox Signal."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"1561","DOI":"10.1074\/jbc.M605931200","article-title":"Thioredoxin-dependent enzymatic activation of mercaptopyruvate sulfurtransferase. An intersubunit disulfide bond serves as a redox switch for activation","volume":"282","author":"Nagahara","year":"2007","journal-title":"J. Biol. Chem."},{"key":"ref_24","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_25","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1038\/s41419-019-1525-1","article-title":"Hydrogen sulfide: A gaseous signaling molecule modulates tissue homeostasis: Implications in ophthalmic diseases","volume":"10","author":"Han","year":"2019","journal-title":"Cell Death Dis."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"1386","DOI":"10.7150\/ijms.36516","article-title":"Potential for therapeutic use of hydrogen sulfide in oxidative stress-induced neurodegenerative diseases","volume":"16","author":"Tabassum","year":"2019","journal-title":"Int. J. Med. Sci."},{"key":"ref_27","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_28","first-page":"242","article-title":"Neuroprotective effects of hydrogen sulfide on sodium azide-induced oxidative stress in PC12 cells","volume":"41","author":"Gao","year":"2018","journal-title":"Int. J. Mol. Med."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"39379","DOI":"10.1074\/jbc.M111.298208","article-title":"Hydrogen sulfide protects the retina from light-induced degeneration by the modulation of Ca2+ influx","volume":"286","author":"Mikami","year":"2011","journal-title":"J. Biol. Chem."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"12939","DOI":"10.1039\/D1SC03828A","article-title":"Leveraging an enzyme\/artificial substrate system to enhance cellular persulfides and mitigate neuroinflammation","volume":"12","author":"Bora","year":"2021","journal-title":"Chem. Sci."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"30901","DOI":"10.1074\/jbc.M114.602664","article-title":"Organization of the human mitochondrial hydrogen sulfide oxidation pathway","volume":"289","author":"Libiad","year":"2014","journal-title":"J. Biol. Chem."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"457","DOI":"10.1038\/nchembio.1834","article-title":"Biogenesis of reactive sulfur species for signaling by hydrogen sulfide oxidation pathways","volume":"11","author":"Mishanina","year":"2015","journal-title":"Nat. Chem. Biol."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"27395","DOI":"10.1074\/jbc.271.44.27395","article-title":"Role of amino acid residues in the active site of rat liver mercaptopyruvate sulfurtransferase. CDNA cloning, overexpression, and site-directed mutagenesis","volume":"271","author":"Nagahara","year":"1996","journal-title":"J. Biol. Chem."},{"key":"ref_34","doi-asserted-by":"crossref","unstructured":"Ascencao, K., Dilek, N., Zuhra, K., Modis, K., Sato, T., and Szabo, C. (2022). Sequential Accumulation of \u2018Driver\u2019 Pathway Mutations Induces the Upregulation of Hydrogen-Sulfide-Producing Enzymes in Human Colonic Epithelial Cell Organoids. Antioxidants, 11.","DOI":"10.3390\/antiox11091823"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"102466","DOI":"10.1016\/j.redox.2022.102466","article-title":"Regulation of CyR61 expression and release by 3-mercaptopyruvate sulfurtransferase in colon cancer cells","volume":"56","author":"Ascencao","year":"2022","journal-title":"Redox Biol."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"105393","DOI":"10.1016\/j.phrs.2020.105393","article-title":"Pharmacological induction of mesenchymal-epithelial transition via inhibition of H2S biosynthesis and consequent suppression of ACLY activity in colon cancer cells","volume":"165","author":"Ascencao","year":"2021","journal-title":"Pharmacol. Res."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"174","DOI":"10.1016\/j.bcp.2017.10.007","article-title":"Drug resistance induces the upregulation of H(2)S-producing enzymes in HCT116 colon cancer cells","volume":"149","author":"Untereiner","year":"2018","journal-title":"Biochem. Pharmacol."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"113137","DOI":"10.1016\/j.biopha.2022.113137","article-title":"Endogenous and exogenous hydrogen sulfide modulates urothelial bladder carcinoma development in human cell lines","volume":"151","author":"Panza","year":"2022","journal-title":"Biomed. Pharmacother."},{"key":"ref_39","doi-asserted-by":"crossref","unstructured":"Augsburger, F., Randi, E.B., Jendly, M., Ascencao, K., Dilek, N., and Szabo, C. (2020). Role of 3-Mercaptopyruvate Sulfurtransferase in the Regulation of Proliferation, Migration, and Bioenergetics in Murine Colon Cancer Cells. Biomolecules, 10.","DOI":"10.3390\/biom10030447"},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"5109","DOI":"10.21873\/anticanres.12831","article-title":"Inhibition of Human Neuroblastoma Cell Proliferation by N-acetyl-L-cysteine as a Result of Increased Sulfane Sulfur Level","volume":"38","author":"Jurkowska","year":"2018","journal-title":"Anticancer Res."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"1855","DOI":"10.1007\/s00726-017-2484-4","article-title":"A possible mechanism of inhibition of U87MG and SH-SY5Y cancer cell proliferation by diallyl trisulfide and other aspects of its activity","volume":"49","author":"Jurkowska","year":"2017","journal-title":"Amino Acids"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1007\/s00726-010-0606-3","article-title":"The expression and activity of cystathionine-gamma-lyase and 3-mercaptopyruvate sulfurtransferase in human neoplastic cell lines","volume":"41","author":"Jurkowska","year":"2011","journal-title":"Amino Acids"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1016\/j.yexcr.2014.09.027","article-title":"Dedifferentiation of cancer cells following recovery from a potentially lethal damage is mediated by H2S-Nampt","volume":"330","author":"Ostrakhovitch","year":"2015","journal-title":"Exp. Cell Res."},{"key":"ref_44","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_45","doi-asserted-by":"crossref","first-page":"432","DOI":"10.1002\/jat.3734","article-title":"Hydrogen sulfide attenuates paraquat-induced epithelial-mesenchymal transition of human alveolar epithelial cells through regulating transforming growth factor-beta1\/Smad2\/3 signaling pathway","volume":"39","author":"Bai","year":"2019","journal-title":"J. Appl. Toxicol."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"36125","DOI":"10.1038\/srep36125","article-title":"Inhibition of hydrogen sulfide biosynthesis sensitizes lung adenocarcinoma to chemotherapeutic drugs by inhibiting mitochondrial DNA repair and suppressing cellular bioenergetics","volume":"6","author":"Szczesny","year":"2016","journal-title":"Sci. Rep."},{"key":"ref_47","doi-asserted-by":"crossref","unstructured":"Breza, J., Soltysova, A., Hudecova, S., Penesova, A., Szadvari, I., Babula, P., Chovancova, B., Lencesova, L., Pos, O., and Breza, J. (2018). Endogenous H(2)S producing enzymes are involved in apoptosis induction in clear cell renal cell carcinoma. BMC Cancer, 18.","DOI":"10.1186\/s12885-018-4508-1"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"166.e15","DOI":"10.1016\/j.urolonc.2015.06.020","article-title":"Expression profile of hydrogen sulfide and its synthases correlates with tumor stage and grade in urothelial cell carcinoma of bladder","volume":"34","author":"Gai","year":"2016","journal-title":"Urol. Oncol."},{"key":"ref_49","first-page":"8484","article-title":"Increased H(2)S and its synthases in urothelial cell carcinoma of the bladder, and enhanced cisplatin-induced apoptosis following H(2)S inhibition in EJ cells","volume":"15","author":"Wahafu","year":"2018","journal-title":"Oncol. Lett."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"113775","DOI":"10.1016\/j.bcp.2019.113775","article-title":"Hydrogen sulfide modulates epithelial-mesenchymal transition and angiogenesis in non-small cell lung cancer via HIF-1alpha activation","volume":"172","author":"Wang","year":"2020","journal-title":"Biochem. Pharmacol."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"6221","DOI":"10.1021\/acs.jmedchem.1c00260","article-title":"Novel Aryl-Substituted Pyrimidones as Inhibitors of 3-Mercaptopyruvate Sulfurtransferase with Antiproliferative Efficacy in Colon Cancer","volume":"64","author":"Bantzi","year":"2021","journal-title":"J. Med. Chem."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"186","DOI":"10.1016\/j.bcp.2017.10.011","article-title":"Role of endogenous and exogenous nitric oxide, carbon monoxide and hydrogen sulfide in HCT116 colon cancer cell proliferation","volume":"149","author":"Olah","year":"2018","journal-title":"Biochem. Pharmacol."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"1692","DOI":"10.1111\/liv.14188","article-title":"miR-26b-5p helps in EpCAM+cancer stem cells maintenance via HSC71\/HSPA8 and augments malignant features in HCC","volume":"39","author":"Khosla","year":"2019","journal-title":"Liver Int."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"1173","DOI":"10.1111\/liv.15228","article-title":"3-Mercaptopyruvate sulfurtransferase represses tumour progression and predicts prognosis in hepatocellular carcinoma","volume":"42","author":"Li","year":"2022","journal-title":"Liver Int."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"913","DOI":"10.1038\/s41419-022-05358-8","article-title":"Glioblastoma cell motility depends on enhanced oxidative stress coupled with mobilization of a sulfurtransferase","volume":"13","author":"Daubon","year":"2022","journal-title":"Cell Death Dis."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"2775","DOI":"10.21873\/invivo.12102","article-title":"Patterns of Expression of H(2)S-Producing Enzyme in Human Renal Cell Carcinoma Specimens: Potential Avenue for Future Therapeutics","volume":"34","author":"Sogutdelen","year":"2020","journal-title":"In Vivo"},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"585","DOI":"10.1159\/000492464","article-title":"Hydrogen Sulfide and Hydrogen Sulfide-Synthesizing Enzymes Are Altered in a Case of Oral Adenoid Cystic Carcinoma","volume":"11","author":"Dongsoo","year":"2018","journal-title":"Case Rep. Oncol."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"682","DOI":"10.1159\/000493008","article-title":"Hydrogen Sulfide-Synthesizing Enzymes Are Altered in a Case of Oral Cavity Mucoepidermoid Carcinoma","volume":"11","author":"Kim","year":"2018","journal-title":"Case Rep. Oncol."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"3843","DOI":"10.21873\/anticanres.12668","article-title":"Hydrogen Sulfide Is Increased in Oral Squamous Cell Carcinoma Compared to Adjacent Benign Oral Mucosae","volume":"38","author":"Meram","year":"2018","journal-title":"Anticancer Res."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1111\/pcmr.12312","article-title":"Role of the cystathionine gamma lyase\/hydrogen sulfide pathway in human melanoma progression","volume":"28","author":"Panza","year":"2015","journal-title":"Pigment Cell Melanoma Res."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"866","DOI":"10.1111\/bph.14574","article-title":"3-Mercaptopyruvate sulfurtransferase supports endothelial cell angiogenesis and bioenergetics","volume":"177","author":"Toro","year":"2020","journal-title":"Br. J. Pharmacol."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"35","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_63","doi-asserted-by":"crossref","first-page":"e13829","DOI":"10.1111\/eci.13829","article-title":"Exercise restores endogenous H(2) S synthesis and mitochondrial function in the heart of old rats","volume":"52","author":"Strutynska","year":"2022","journal-title":"Eur. J. Clin. Invest."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"113833","DOI":"10.1016\/j.bcp.2020.113833","article-title":"Cardiovascular phenotype of mice lacking 3-mercaptopyruvate sulfurtransferase","volume":"176","author":"Peleli","year":"2020","journal-title":"Biochem. Pharmacol."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"222","DOI":"10.1161\/CIRCRESAHA.121.319817","article-title":"Mitochondrial H(2)S Regulates BCAA Catabolism in Heart Failure","volume":"131","author":"Li","year":"2022","journal-title":"Circ. Res."},{"key":"ref_66","first-page":"798","article-title":"Hydrogen Sulfide Ameliorates Myocardial Injury Caused by Sepsis Through Suppressing ROS-Mediated Endoplasmic Reticulum Stress","volume":"53","author":"Zhao","year":"2022","journal-title":"Sichuan Da Xue Xue Bao Yi Xue Ban"},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"6492469","DOI":"10.1155\/2016\/6492469","article-title":"The H2S Donor NaHS Changes the Expression Pattern of H2S-Producing Enzymes after Myocardial Infarction","volume":"2016","author":"Li","year":"2016","journal-title":"Oxidative Med. Cell. Longev."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"H71","DOI":"10.1152\/ajpheart.00574.2014","article-title":"MPST but not CSE is the primary regulator of hydrogen sulfide production and function in the coronary artery","volume":"310","author":"Kuo","year":"2016","journal-title":"Am. J. Physiol. Heart Circ. Physiol."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"690371","DOI":"10.3389\/fphar.2021.690371","article-title":"Hydrogen Sulfide Ameliorates Angiotensin II-Induced Atrial Fibrosis Progression to Atrial Fibrillation through Inhibition of the Warburg Effect and Endoplasmic Reticulum Stress","volume":"12","author":"Hu","year":"2021","journal-title":"Front. Pharmacol."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"130","DOI":"10.1016\/j.biochi.2022.04.013","article-title":"Heart and kidney H(2)S production is reduced in hypertensive and older rats","volume":"199","author":"Szlezak","year":"2022","journal-title":"Biochimie"},{"key":"ref_71","doi-asserted-by":"crossref","unstructured":"Szlezak, D., Bronowicka-Adamska, P., Hutsch, T., Ufnal, M., and Wrobel, M. (2021). Hypertension and Aging Affect Liver Sulfur Metabolism in Rats. Cells, 10.","DOI":"10.3390\/cells10051238"},{"key":"ref_72","first-page":"3693","article-title":"Erythrocytic or serum hydrogen sulfide association with hypertension development in untreated essential hypertension","volume":"124","author":"Zheng","year":"2011","journal-title":"Chin. Med. J."},{"key":"ref_73","doi-asserted-by":"crossref","unstructured":"Panagaki, T., Randi, E.B., and Szabo, C. (2020). Role of 3-Mercaptopyruvate Sulfurtransferase in the Regulation of Proliferation and Cellular Bioenergetics in Human Down Syndrome Fibroblasts. Biomolecules, 10.","DOI":"10.3390\/biom10040653"},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"53","DOI":"10.3389\/fpsyg.2019.00053","article-title":"Inhibited Endogenous H(2)S Generation and Excessive Autophagy in Hippocampus Contribute to Sleep Deprivation-Induced Cognitive Impairment","volume":"10","author":"Yang","year":"2019","journal-title":"Front. Psychol."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"106210","DOI":"10.1016\/j.phrs.2022.106210","article-title":"An integrated multi-omics approach revealed the regulation of melatonin on age-dependent mitochondrial function impair and lipid dyshomeostasis in mice hippocampus","volume":"179","author":"Jiang","year":"2022","journal-title":"Pharmacol. Res."},{"key":"ref_76","doi-asserted-by":"crossref","unstructured":"Jiang, Z., Li, C., Manuel, M.L., Yuan, S., Kevil, C.G., McCarter, K.D., Lu, W., and Sun, H. (2015). Role of hydrogen sulfide in early blood-brain barrier disruption following transient focal cerebral ischemia. PLoS ONE, 10.","DOI":"10.1371\/journal.pone.0117982"},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"C720","DOI":"10.1152\/ajpcell.00014.2020","article-title":"3-Mercaptopyruvate sulfurtransferase\/hydrogen sulfide protects cerebral endothelial cells against oxygen-glucose deprivation\/reoxygenation-induced injury via mitoprotection and inhibition of the RhoA\/ROCK pathway","volume":"319","author":"Zhang","year":"2020","journal-title":"Am. J. Physiol. Cell Physiol."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"444","DOI":"10.1152\/jn.00400.2021","article-title":"Betaine protects rats against ischemia\/reperfusion injury-induced brain damage","volume":"127","author":"Li","year":"2022","journal-title":"J. Neurophysiol."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1007\/s10571-016-0369-9","article-title":"Upregulation of 3-MST Relates to Neuronal Autophagy After Traumatic Brain Injury in Mice","volume":"37","author":"Zhang","year":"2017","journal-title":"Cell Mol. Neurobiol."},{"key":"ref_80","doi-asserted-by":"crossref","unstructured":"Lazarevic, M., Battaglia, G., Jevtic, B., Dedovic, N., Bruno, V., Cavalli, E., Miljkovic, D., Nicoletti, F., Momcilovic, M., and Fagone, P. (2020). Upregulation of Tolerogenic Pathways by the Hydrogen Sulfide Donor GYY4137 and Impaired Expression of H(2)S-Producing Enzymes in Multiple Sclerosis. Antioxidants, 9.","DOI":"10.3390\/antiox9070608"},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"109722","DOI":"10.1016\/j.biopha.2019.109722","article-title":"Evaluation of H(2)S-producing enzymes in cerebrospinal fluid and its relationship with interleukin-6 and neurologic deficits in subarachnoid hemorrhage","volume":"123","author":"Han","year":"2020","journal-title":"Biomed. Pharmacother."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"102484","DOI":"10.1016\/j.redox.2022.102484","article-title":"Sulfanegen stimulates 3-mercaptopyruvate sulfurtransferase activity and ameliorates Alzheimer\u2019s disease pathology and oxidative stress in vivo","volume":"57","author":"Rao","year":"2022","journal-title":"Redox Biol."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1016\/j.pbb.2016.11.002","article-title":"Hydrogen sulfide ameliorates learning memory impairment in APP\/PS1 transgenic mice: A novel mechanism mediated by the activation of Nrf2","volume":"150\u2013151","author":"Liu","year":"2016","journal-title":"Pharmacol. Biochem. Behav."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1002\/jbt.21514","article-title":"Dose and time-dependent effects of cyanide on thiosulfate sulfurtransferase, 3-mercaptopyruvate sulfurtransferase, and cystathionine lambda-lyase activities","volume":"27","author":"Singh","year":"2013","journal-title":"J. Biochem. Mol. Toxicol."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1080\/15376520490434683","article-title":"Sulfurtransferases and cyanide detoxification in mouse liver, kidney, and brain","volume":"14","author":"Wrobel","year":"2004","journal-title":"Toxicol. Mech. Methods"},{"key":"ref_86","first-page":"212","article-title":"Allyl disulfide as donor and cyanide as acceptor of sulfane sulfur in the mouse tissues","volume":"57","author":"Iciek","year":"2005","journal-title":"Pharmacol. Rep."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1002\/jbt.2570070203","article-title":"Modifiers of mercaptopyruvate sulfurtransferase catalyzed conversion of cyanide to thiocyanate in vitro","volume":"7","author":"Wing","year":"1992","journal-title":"J. Biochem. Toxicol."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"597","DOI":"10.1016\/0887-2333(92)90073-Z","article-title":"The effect of picrylsulphonic acid on In vitro conversion of cyanide to thiocyanate by 3-mercaptopyruvate sulphurtransferase and rhodanese","volume":"6","author":"Wing","year":"1992","journal-title":"Toxicol. In Vitro"},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"1601","DOI":"10.1177\/0960327110394225","article-title":"The effect of uremic toxin cyanate (OCN-) on anaerobic sulfur metabolism and prooxidative processes in the rat kidney: A protective role of lipoate","volume":"30","author":"Iciek","year":"2011","journal-title":"Hum. Exp. Toxicol."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"202","DOI":"10.1111\/nyas.13114","article-title":"Development of sulfanegen for mass cyanide casualties","volume":"1374","author":"Patterson","year":"2016","journal-title":"Ann. N. Y. Acad. Sci."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"1346","DOI":"10.1021\/jm301633x","article-title":"Cyanide antidotes for mass casualties: Water-soluble salts of the dithiane (sulfanegen) from 3-mercaptopyruvate for intramuscular administration","volume":"56","author":"Patterson","year":"2013","journal-title":"J. Med. Chem."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1016\/j.taap.2010.08.002","article-title":"Sulfanegen sodium treatment in a rabbit model of sub-lethal cyanide toxicity","volume":"248","author":"Brenner","year":"2010","journal-title":"Toxicol. Appl. Pharmacol."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"9501792","DOI":"10.1155\/2017\/9501792","article-title":"Hydrogen Sulfide Inhibits High Glucose-Induced sFlt-1 Production via Decreasing ADAM17 Expression in 3T3-L1 Adipocytes","volume":"2017","author":"Hu","year":"2017","journal-title":"Int. J. Endocrinol."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"2271","DOI":"10.1007\/s11357-022-00600-9","article-title":"Inhibition of the 3-mercaptopyruvate sulfurtransferase-hydrogen sulfide system promotes cellular lipid accumulation","volume":"44","author":"Casili","year":"2022","journal-title":"Geroscience"},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"319","DOI":"10.1089\/ars.2020.8206","article-title":"Activation of Endogenous H(2)S Biosynthesis or Supplementation with Exogenous H(2)S Enhances Adipose Tissue Adipogenesis and Preserves Adipocyte Physiology in Humans","volume":"35","author":"Comas","year":"2021","journal-title":"Antioxid. Redox Signal."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"108054","DOI":"10.1016\/j.abb.2019.07.019","article-title":"Hydrogen sulfide regulates circadian-clock genes in C(2)C(12) myotubes and the muscle of high-fat-diet-fed mice","volume":"672","author":"Parsanathan","year":"2019","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"138","DOI":"10.1016\/j.niox.2014.03.002","article-title":"Effect of feeding a high fat diet on hydrogen sulfide (H2S) metabolism in the mouse","volume":"41","author":"Peh","year":"2014","journal-title":"Nitric Oxide"},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"20211894","DOI":"10.1084\/jem.20211894","article-title":"MPST sulfurtransferase maintains mitochondrial protein import and cellular bioenergetics to attenuate obesity","volume":"219","author":"Katsouda","year":"2022","journal-title":"J. Exp. Med."},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"190","DOI":"10.1016\/j.phrs.2017.09.023","article-title":"Reduced adipose tissue H(2)S in obesity","volume":"128","author":"Katsouda","year":"2018","journal-title":"Pharmacol. Res."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"2121","DOI":"10.1113\/JP270054","article-title":"Evidence for a functional vasodilatatory role for hydrogen sulphide in the human cutaneous microvasculature","volume":"593","author":"Kutz","year":"2015","journal-title":"J. Physiol."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"411","DOI":"10.1152\/japplphysiol.01049.2011","article-title":"Precursors and inhibitors of hydrogen sulfide synthesis affect acute hypoxic pulmonary vasoconstriction in the intact lung","volume":"112","author":"Madden","year":"2012","journal-title":"J. Appl. Physiol."},{"key":"ref_102","first-page":"737","article-title":"Vasomotor effects of hydrogen sulfide in human umbilical vessels","volume":"68","author":"Mohammed","year":"2017","journal-title":"J. Physiol. Pharmacol."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"350","DOI":"10.1016\/j.jsxm.2016.01.002","article-title":"Decreased Endogenous Hydrogen Sulfide Generation in Penile Tissues of Diabetic Rats with Erectile Dysfunction","volume":"13","author":"Zhang","year":"2016","journal-title":"J. Sex. Med."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"692","DOI":"10.1038\/aja.2013.32","article-title":"Further evidence of endogenous hydrogen sulphide as a mediator of relaxation in human and rat bladder","volume":"15","author":"Gai","year":"2013","journal-title":"Asian J. Androl."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"1902","DOI":"10.1111\/bph.12084","article-title":"Hydrogen sulphide-induced relaxation of porcine peripheral bronchioles","volume":"168","author":"Rashid","year":"2013","journal-title":"Br. J. Pharmacol."},{"key":"ref_106","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_107","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1186\/s13075-020-02147-6","article-title":"The protective role of the 3-mercaptopyruvate sulfurtransferase (3-MST)-hydrogen sulfide (H(2)S) pathway against experimental osteoarthritis","volume":"22","author":"Nasi","year":"2020","journal-title":"Arthritis Res. Ther."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"262","DOI":"10.1016\/j.ijom.2017.07.021","article-title":"The expression of endogenous hydrogen sulfide signal during distraction osteogenesis in a rabbit model","volume":"47","author":"Jiang","year":"2018","journal-title":"Int. J. Oral. Maxillofac. Surg."},{"key":"ref_109","first-page":"611","article-title":"Hydrogen sulfide formation in experimental model of acute pancreatitis","volume":"66","author":"Hutsch","year":"2019","journal-title":"Acta Biochim. Pol."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"577","DOI":"10.1111\/bph.14100","article-title":"Multiple role of 3-mercaptopyruvate sulfurtransferase: Antioxidative function, H(2) S and polysulfide production and possible SO(x) production","volume":"175","author":"Nagahara","year":"2018","journal-title":"Br. J. Pharmacol."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1016\/j.phrs.2016.11.001","article-title":"Interaction between endogenous carbon monoxide and hydrogen sulfide in the mechanism of gastroprotection against acute aspirin-induced gastric damage","volume":"114","author":"Magierowski","year":"2016","journal-title":"Pharmacol. Res."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"3176","DOI":"10.1007\/s10620-016-4280-5","article-title":"Hydrogen Sulfide and Carbon Monoxide Protect Gastric Mucosa Compromised by Mild Stress Against Alendronate Injury","volume":"61","author":"Magierowski","year":"2016","journal-title":"Dig. Dis. Sci."},{"key":"ref_113","doi-asserted-by":"crossref","unstructured":"Bronowicka-Adamska, P., Wrobel, M., Magierowski, M., Magierowska, K., Kwiecien, S., and Brzozowski, T. (2017). Hydrogen Sulphide Production in Healthy and Ulcerated Gastric Mucosa of Rats. Molecules, 22.","DOI":"10.3390\/molecules22040530"},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"102469","DOI":"10.1016\/j.redox.2022.102469","article-title":"MPST deficiency promotes intestinal epithelial cell apoptosis and aggravates inflammatory bowel disease via AKT","volume":"56","author":"Zhang","year":"2022","journal-title":"Redox Biol."},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"6717212","DOI":"10.1155\/2018\/6717212","article-title":"Hydrogen Sulfide Attenuates LPS-Induced Acute Kidney Injury by Inhibiting Inflammation and Oxidative Stress","volume":"2018","author":"Chen","year":"2018","journal-title":"Oxidative Med. Cell. Longev."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"2169","DOI":"10.1136\/gutjnl-2017-313778","article-title":"Fatty acids promote fatty liver disease via the dysregulation of 3-mercaptopyruvate sulfurtransferase\/hydrogen sulfide pathway","volume":"67","author":"Li","year":"2018","journal-title":"Gut"},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"667","DOI":"10.1139\/cjpp-2016-0611","article-title":"Exercise restores bioavailability of hydrogen sulfide and promotes autophagy influx in livers of mice fed with high-fat diet","volume":"95","author":"Wang","year":"2017","journal-title":"Can. J. Physiol. Pharmacol."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1186\/s12934-020-01444-8","article-title":"MsrR is a thiol-based oxidation-sensing regulator of the XRE family that modulates C. glutamicum oxidative stress resistance","volume":"19","author":"Si","year":"2020","journal-title":"Microb Cell Fact."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"986","DOI":"10.1126\/science.1209855","article-title":"H2S: A universal defense against antibiotics in bacteria","volume":"334","author":"Shatalin","year":"2011","journal-title":"Science"},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"1012","DOI":"10.1073\/pnas.0409042102","article-title":"Characterization of potential selenium-binding proteins in the selenophosphate synthetase system","volume":"102","author":"Ogasawara","year":"2005","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"194","DOI":"10.1007\/s12011-016-0752-x","article-title":"Role of Hydrogen Sulfide on Autophagy in Liver Injuries Induced by Selenium Deficiency in Chickens","volume":"175","author":"Wenzhong","year":"2017","journal-title":"Biol. Trace Elem. Res."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1007\/s12011-018-1292-3","article-title":"Endogenous Hydrogen Sulfide Promotes Apoptosis via Mitochondrial Pathways in the Livers of Broilers with Selenium Deficiency Exudative Diathesis Disease","volume":"186","author":"Zheng","year":"2018","journal-title":"Biol. Trace Elem. Res."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"C41","DOI":"10.1152\/ajpcell.00398.2011","article-title":"Increased endogenous H2S generation by CBS, CSE, and 3MST gene therapy improves ex vivo renovascular relaxation in hyperhomocysteinemia","volume":"303","author":"Sen","year":"2012","journal-title":"Am. J. Physiol. Cell Physiol."},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"40227","DOI":"10.1038\/srep40227","article-title":"Discovery and Mechanistic Characterization of Selective Inhibitors of H(2)S-producing Enzyme: 3-Mercaptopyruvate Sulfurtransferase (3MST) Targeting Active-site Cysteine Persulfide","volume":"7","author":"Hanaoka","year":"2017","journal-title":"Sci. Rep."},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"102331","DOI":"10.1016\/j.redox.2022.102331","article-title":"Emerging roles of cystathionine beta-synthase in various forms of cancer","volume":"53","author":"Ascencao","year":"2022","journal-title":"Redox Biol."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1016\/j.niox.2017.04.010","article-title":"Hydrogen sulfide attenuates cardiac injury in takotsubo cardiomyopathy by alleviating oxidative stress","volume":"67","author":"Zhang","year":"2017","journal-title":"Nitric Oxide"},{"key":"ref_127","doi-asserted-by":"crossref","unstructured":"Zhao, H., Chan, S.J., Ng, Y.K., and Wong, P.T. (2013). Brain 3-Mercaptopyruvate Sulfurtransferase (3MST): Cellular Localization and Downregulation after Acute Stroke. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0067322"},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"e10695","DOI":"10.15252\/emmm.201910695","article-title":"Excess hydrogen sulfide and polysulfides production underlies a schizophrenia pathophysiology","volume":"11","author":"Ide","year":"2019","journal-title":"EMBO Mol. Med."},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1016\/j.toxlet.2006.02.002","article-title":"Evidence for a functional genetic polymorphism of the human mercaptopyruvate sulfurtransferase (MPST), a cyanide detoxification enzyme","volume":"165","author":"Rat","year":"2006","journal-title":"Toxicol. Lett."}],"container-title":["Antioxidants"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2076-3921\/12\/3\/603\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T18:44:55Z","timestamp":1760121895000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2076-3921\/12\/3\/603"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,3,1]]},"references-count":129,"journal-issue":{"issue":"3","published-online":{"date-parts":[[2023,3]]}},"alternative-id":["antiox12030603"],"URL":"https:\/\/doi.org\/10.3390\/antiox12030603","relation":{},"ISSN":["2076-3921"],"issn-type":[{"value":"2076-3921","type":"electronic"}],"subject":[],"published":{"date-parts":[[2023,3,1]]}}}