{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,7]],"date-time":"2026-09-07T20:24:02Z","timestamp":1788812642929,"version":"build-2803163510"},"reference-count":173,"publisher":"MDPI AG","issue":"12","license":[{"start":{"date-parts":[[2021,6,18]],"date-time":"2021-06-18T00:00:00Z","timestamp":1623974400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100004663","name":"Ministry of Science and Technology, Taiwan","doi-asserted-by":"publisher","award":["MOST 108-2314-B-007-003-MY3"],"award-info":[{"award-number":["MOST 108-2314-B-007-003-MY3"]}],"id":[{"id":"10.13039\/501100004663","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100005057","name":"National Tsing Hua University","doi-asserted-by":"publisher","award":["110Q2705E1"],"award-info":[{"award-number":["110Q2705E1"]}],"id":[{"id":"10.13039\/501100005057","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100005057","name":"National Tsing Hua University","doi-asserted-by":"publisher","award":["110Q2729E1"],"award-info":[{"award-number":["110Q2729E1"]}],"id":[{"id":"10.13039\/501100005057","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Hydrogen Sulfide (H2S), an endogenously produced gasotransmitter, is involved in various important physiological and disease conditions, including vasodilation, stimulation of cellular bioenergetics, anti-inflammation, and pro-angiogenesis. In cancer, aberrant up-regulation of H2S-producing enzymes is frequently observed in different cancer types. The recognition that tumor-derived H2S plays various roles during cancer development reveals opportunities to target H2S-mediated signaling pathways in cancer therapy. In this review, we will focus on the mechanism of H2S-mediated protein persulfidation and the detailed information about the dysregulation of H2S-producing enzymes and metabolism in different cancer types. We will also provide an update on mechanisms of H2S-mediated cancer progression and summarize current options to modulate H2S production for cancer therapy.<\/jats:p>","DOI":"10.3390\/ijms22126562","type":"journal-article","created":{"date-parts":[[2021,6,18]],"date-time":"2021-06-18T11:19:20Z","timestamp":1624015160000},"page":"6562","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":79,"title":["The Hidden Role of Hydrogen Sulfide Metabolism in Cancer"],"prefix":"10.3390","volume":"22","author":[{"given":"Rong-Hsuan","family":"Wang","sequence":"first","affiliation":[{"name":"Institute of Biotechnology, College of Life Science, National Tsing Hua University, Hsinchu 300, Taiwan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yu-Hsin","family":"Chu","sequence":"additional","affiliation":[{"name":"Institute of Biotechnology, College of Life Science, National Tsing Hua University, Hsinchu 300, Taiwan"},{"name":"Department of Life Science, College of Life Science, National Tsing Hua University, Hsinchu 300, Taiwan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8656-5755","authenticated-orcid":false,"given":"Kai-Ti","family":"Lin","sequence":"additional","affiliation":[{"name":"Institute of Biotechnology, College of Life Science, National Tsing Hua University, Hsinchu 300, Taiwan"},{"name":"Department of Medical Science, College of Life Science, National Tsing Hua University, Hsinchu 300, Taiwan"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2021,6,18]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"1792","DOI":"10.1096\/fj.02-0211hyp","article-title":"Two\u2019s company, three\u2019s a crowd: Can H2S be the third endogenous gaseous transmitter?","volume":"16","author":"Wang","year":"2002","journal-title":"FASEB J."},{"key":"ref_2","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 gamma-lyase","volume":"322","author":"Yang","year":"2008","journal-title":"Science"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"1259","DOI":"10.1161\/CIRCRESAHA.111.240242","article-title":"Hydrogen sulfide as endothelium-derived hyperpolarizing factor sulfhydrates potassium channels","volume":"109","author":"Mustafa","year":"2011","journal-title":"Circ. Res."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"9161","DOI":"10.1073\/pnas.1202916109","article-title":"Hydrogen sulfide and nitric oxide are mutually dependent in the regulation of angiogenesis and endothelium-dependent vasorelaxation","volume":"109","author":"Coletta","year":"2012","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"289","DOI":"10.1016\/j.phrs.2010.06.002","article-title":"Hydrogen sulfide and ischemia-reperfusion injury","volume":"62","author":"Nicholson","year":"2010","journal-title":"Pharmacol. Res."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"2118","DOI":"10.1096\/fj.06-6270fje","article-title":"Hydrogen sulfide is an endogenous modulator of leukocyte-mediated inflammation","volume":"20","author":"Zanardo","year":"2006","journal-title":"FASEB J."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"623","DOI":"10.1093\/jb\/mvp111","article-title":"Vascular endothelium expresses 3-mercaptopyruvate sulfurtransferase and produces hydrogen sulfide","volume":"146","author":"Shibuya","year":"2009","journal-title":"J. Biochem."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"1380","DOI":"10.2105\/AJPH.91.9.1380","article-title":"De morbis artificum diatriba 1743","volume":"91","author":"Ramazzini","year":"2001","journal-title":"Am. J. Public Health"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"1","DOI":"10.2307\/4577000","article-title":"Hydrogen sulphide literature","volume":"39","author":"Mitchell","year":"1924","journal-title":"Public Health Rep."},{"key":"ref_10","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_11","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.niox.2017.09.011","article-title":"Environmental toxicology of hydrogen sulfide","volume":"71","author":"Rubright","year":"2017","journal-title":"Nitric Oxide Biol. Chem."},{"key":"ref_12","first-page":"397","article-title":"Hydrogen sulphide production by bacteria","volume":"8","author":"Clarke","year":"1953","journal-title":"Microbiology"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"334","DOI":"10.1104\/pp.15.00009","article-title":"S-sulfhydration: A cysteine posttranslational modification in plant systems","volume":"168","author":"Aroca","year":"2015","journal-title":"Plant. Physiol."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"1369","DOI":"10.3389\/fpls.2018.01369","article-title":"Hydrogen sulfide signaling in plants: Emerging roles of protein persulfidation","volume":"9","author":"Aroca","year":"2018","journal-title":"Front. Plant Sci."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"243","DOI":"10.1007\/s00726-004-0072-x","article-title":"Endogenous production of hydrogen sulfide in mammals","volume":"26","author":"Kamoun","year":"2004","journal-title":"Amino Acids"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/ncomms2371","article-title":"A novel pathway for the production of hydrogen sulfide from D-cysteine in mammalian cells","volume":"4","author":"Shibuya","year":"2013","journal-title":"Nat. Commun."},{"key":"ref_17","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_18","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1038\/nrd.2015.1","article-title":"Gasotransmitters in cancer: From pathophysiology to experimental therapy","volume":"15","author":"Szabo","year":"2016","journal-title":"Nat. Rev. Drug Discov."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"re2","DOI":"10.1126\/scisignal.268re2","article-title":"Signaling by gasotransmitters","volume":"2","author":"Mustafa","year":"2009","journal-title":"Sci. Signal."},{"key":"ref_20","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_21","doi-asserted-by":"crossref","first-page":"4513","DOI":"10.1073\/pnas.0807974105","article-title":"Hydrogen sulfide as a mediator of human corpus cavernosum smooth-muscle relaxation","volume":"106","author":"Sorrentino","year":"2009","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"756","DOI":"10.1016\/j.bbrc.2004.04.094","article-title":"Endogenous hydrogen sulfide regulation of myocardial injury induced by isoproterenol","volume":"318","author":"Geng","year":"2004","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"15560","DOI":"10.1073\/pnas.0705891104","article-title":"Hydrogen sulfide attenuates myocardial ischemia-reperfusion injury by preservation of mitochondrial function","volume":"104","author":"Elrod","year":"2007","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"70","DOI":"10.1016\/j.ejphar.2014.01.009","article-title":"Hydrogen sulfide protected gastric epithelial cell from ischemia\/reperfusion injury by Keap1 s-sulfhydration, MAPK dependent anti-apoptosis and NF-\u03baB dependent anti-inflammation pathway","volume":"725","author":"Guo","year":"2014","journal-title":"Eur. J. Pharmacol."},{"key":"ref_25","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_26","doi-asserted-by":"crossref","first-page":"661","DOI":"10.1089\/ars.2006.8.661","article-title":"Hydrogen sulfide protects HT22 neuronal cells from oxidative stress","volume":"8","author":"Kimura","year":"2006","journal-title":"Antioxid. Redox Signal."},{"key":"ref_27","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_28","doi-asserted-by":"crossref","first-page":"1196","DOI":"10.1096\/fj.04-3583fje","article-title":"Hydrogen sulfide is a novel mediator of lipopolysaccharide-induced inflammation in the mouse","volume":"19","author":"Li","year":"2005","journal-title":"FASEB J."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1586\/ecp.10.134","article-title":"Hydrogen sulfide and inflammation: The good, the bad, the ugly and the promising","volume":"4","author":"Whiteman","year":"2011","journal-title":"Expert Rev. Clin. Pharmacol."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"21972","DOI":"10.1073\/pnas.0908047106","article-title":"Hydrogen sulfide is an endogenous stimulator of angiogenesis","volume":"106","author":"Papapetropoulos","year":"2009","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1016\/j.phrs.2016.08.026","article-title":"Regulation and role of endogenously produced hydrogen sulfide in angiogenesis","volume":"113","author":"Katsouda","year":"2016","journal-title":"Pharmacol. Res."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"ra86","DOI":"10.1126\/scisignal.2002329","article-title":"H2S-Induced sulfhydration of the phosphatase PTP1B and its role in the endoplasmic reticulum stress response","volume":"4","author":"Krishnan","year":"2011","journal-title":"Sci. Signal."},{"key":"ref_33","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_34","doi-asserted-by":"crossref","first-page":"1906","DOI":"10.1089\/ars.2012.4645","article-title":"Hydrogen sulfide protects against cellular senescence via S-sulfhydration of Keap1 and activation of Nrf2","volume":"18","author":"Yang","year":"2013","journal-title":"Antioxid. Redox Signal."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"66","DOI":"10.1016\/j.stem.2014.03.005","article-title":"Hydrogen sulfide maintains mesenchymal stem cell function and bone homeostasis via regulation of Ca2+ channel sulfhydration","volume":"15","author":"Liu","year":"2014","journal-title":"Cell Stem Cell"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"792","DOI":"10.1002\/embr.201338213","article-title":"S-sulfhydration of MEK 1 leads to PARP-1 activation and DNA damage repair","volume":"15","author":"Zhao","year":"2014","journal-title":"EMBO Rep."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"2293","DOI":"10.1016\/j.bbagen.2015.08.003","article-title":"H2S-induced S-sulfhydration of pyruvate carboxylase contributes to gluconeogenesis in liver cells","volume":"1850","author":"Ju","year":"2015","journal-title":"Biochim. Biophys. Acta Gen. Subj."},{"key":"ref_38","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_39","doi-asserted-by":"crossref","first-page":"742","DOI":"10.1089\/ars.2016.6826","article-title":"Cystathionine \u03b3-Lyase\u2013Hydrogen Sulfide Induces Runt-Related Transcription Factor 2 Sulfhydration, Thereby Increasing Osteoblast Activity to Promote Bone Fracture Healing","volume":"27","author":"Zheng","year":"2017","journal-title":"Antioxid. Redox Signal."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"250","DOI":"10.1016\/j.redox.2018.08.008","article-title":"Amelioration of mitochondrial dysfunction in heart failure through S-sulfhydration of Ca2+\/calmodulin-dependent protein kinase II","volume":"19","author":"Wu","year":"2018","journal-title":"Redox Biol."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"1302","DOI":"10.1089\/ars.2019.7728","article-title":"S-Sulfhydration of SIRT3 by hydrogen sulfide attenuates mitochondrial dysfunction in cisplatin-induced acute kidney injury","volume":"31","author":"Yuan","year":"2019","journal-title":"Antioxid. Redox Signal."},{"key":"ref_42","unstructured":"Zhao, S., Song, T., Gu, Y., Zhang, Y., Cao, S., Miao, Q., Zhang, X., Chen, H., Gao, Y., and Zhang, L. (2020). Hydrogen sulfide alleviates liver injury via S-sulfhydrated-Keap1\/Nrf2\/LRP1 pathway. Hepatology."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"836","DOI":"10.1111\/bph.14601","article-title":"Hydrogen sulfide regulates muscle RING finger-1 protein S-sulfhydration at Cys44 to prevent cardiac structural damage in diabetic cardiomyopathy","volume":"177","author":"Sun","year":"2020","journal-title":"Br. J. Pharmacol."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"101813","DOI":"10.1016\/j.redox.2020.101813","article-title":"Polysulfide-mediated sulfhydration of SIRT1 prevents diabetic nephropathy by suppressing phosphorylation and acetylation of p65 NF-\u03baB and STAT3","volume":"38","author":"Sun","year":"2021","journal-title":"Redox Biol."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"e45986","DOI":"10.15252\/embr.201845986","article-title":"Dysregulation of cystathionine \u03b3-lyase promotes prostate cancer progression and metastasis","volume":"20","author":"Wang","year":"2019","journal-title":"EMBO Rep."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"ra72","DOI":"10.1126\/scisignal.2000464","article-title":"H2S signals through protein S-sulfhydration","volume":"2","author":"Mustafa","year":"2009","journal-title":"Sci. Signal."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"575","DOI":"10.1002\/anie.201305876","article-title":"Detection of protein S-sulfhydration by a tag-switch technique","volume":"53","author":"Zhang","year":"2014","journal-title":"Angew. Chem. Int. Ed."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"847","DOI":"10.1016\/j.bbagen.2013.05.040","article-title":"Sulfenic acid chemistry, detection and cellular lifetime","volume":"1840","author":"Gupta","year":"2014","journal-title":"Biochim. Biophys. Acta Gen. Subj."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"4411","DOI":"10.1074\/jbc.R111.285742","article-title":"Regulation by S-nitrosylation of protein post-translational modification","volume":"287","author":"Hess","year":"2012","journal-title":"J. Biol. Chem."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"146","DOI":"10.1016\/j.abb.2011.09.015","article-title":"The reaction of H2S with oxidized thiols: Generation of persulfides and implications to H2S biology","volume":"516","author":"Francoleon","year":"2011","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1016\/j.niox.2014.06.003","article-title":"Working with \u201cH2S\u201d: Facts and apparent artifacts","volume":"41","author":"Wedmann","year":"2014","journal-title":"Nitric Oxide"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"12061","DOI":"10.1002\/anie.201305669","article-title":"Generation of HNO and HSNO from nitrite by heme-iron-catalyzed metabolism with H2S","volume":"52","author":"Miljkovic","year":"2013","journal-title":"Angew. Chem. Int. Ed."},{"key":"ref_53","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_54","doi-asserted-by":"crossref","first-page":"7606","DOI":"10.1073\/pnas.1321232111","article-title":"Reactive cysteine persulfides and S-polythiolation regulate oxidative stress and redox signaling","volume":"111","author":"Ida","year":"2014","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_55","doi-asserted-by":"crossref","unstructured":"Hellmich, M.R., and Szabo, C. (2015). Hydrogen sulfide and cancer. Chem. Biochem. Pharmacol. Hydrog. Sulfide, 233\u2013241.","DOI":"10.1007\/978-3-319-18144-8_12"},{"key":"ref_56","first-page":"335","article-title":"Hydrogen sulfide metabolism and signaling in the tumor microenvironment","volume":"1219","author":"Fernandes","year":"2020","journal-title":"Tumor Microenviron."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"12474","DOI":"10.1073\/pnas.1306241110","article-title":"Tumor-derived hydrogen sulfide, produced by cystathionine-\u03b2-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_58","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_59","doi-asserted-by":"crossref","first-page":"228","DOI":"10.1016\/j.freeradbiomed.2015.05.024","article-title":"Role of cystathionine \u03b2-synthase in human breast Cancer","volume":"86","author":"Sen","year":"2015","journal-title":"Free Radic. Biol. Med."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"6085","DOI":"10.21873\/anticanres.12958","article-title":"Cystathione \u03b2-synthase is increased in thyroid malignancies","volume":"38","author":"Kilpatrick","year":"2018","journal-title":"Anticancer Res."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1097\/PAI.0000000000000705","article-title":"Clinical significance of CBS and CCL21 in gallbladder adenocarcinomas and squamous cell\/adenosquamous carcinomas","volume":"28","author":"Li","year":"2020","journal-title":"Appl. Immunohistochem. Mol. Morphol."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"1449","DOI":"10.3892\/or_00000373","article-title":"Expression of cystathionine \u03b2-synthase is downregulated in hepatocellular carcinoma and associated with poor prognosis","volume":"21","author":"Kim","year":"2009","journal-title":"Oncol. Rep."},{"key":"ref_63","doi-asserted-by":"crossref","unstructured":"Zhao, H., Li, Q., Wang, J., Su, X., Ng, K.M., Qiu, T., Shan, L., Ling, Y., Wang, L., and Cai, J. (2012). Frequent epigenetic silencing of the folate-metabolising gene cystathionine-beta-synthase in gastrointestinal cancer. PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0049683"},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"65677","DOI":"10.18632\/oncotarget.20057","article-title":"Cystathionine-\u03b3-lyase promotes process of breast cancer in association with STAT3 signaling pathway","volume":"8","author":"You","year":"2017","journal-title":"Oncotarget"},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"420","DOI":"10.1016\/j.taap.2011.09.026","article-title":"Hydrogen sulfide mediates the anti-survival effect of sulforaphane on human prostate cancer cells","volume":"257","author":"Pei","year":"2011","journal-title":"Toxicol. Appl. Pharmacol."},{"key":"ref_66","doi-asserted-by":"crossref","unstructured":"Zhang, L., Qi, Q., Yang, J., Sun, D., Li, C., Xue, Y., Jiang, Q., Tian, Y., Xu, C., and Wang, R. (2015). An anticancer role of hydrogen sulfide in human gastric cancer cells. Oxidative Med. Cell. Longev.","DOI":"10.1155\/2015\/636410"},{"key":"ref_67","doi-asserted-by":"crossref","unstructured":"Gai, J.-W., Qin, W., Liu, M., Wang, H.-F., Zhang, M., Li, M., Zhou, W.-H., Ma, Q.-T., Liu, G.-M., and Song, W.-H. (2016). Expression Profile of Hydrogen Sulfide and Its Synthases Correlates with Tumor Stage and Grade in Urothelial Cell Carcinoma of Bladder. Urologic Oncology: Seminars and Original Investigations, Elsevier.","DOI":"10.1016\/j.urolonc.2015.06.020"},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1016\/j.mrfmmm.2014.03.002","article-title":"Hydrogen sulfide (H2S)\/cystathionine \u03b3-lyase (CSE) pathway contributes to the proliferation of hepatoma cells","volume":"763","author":"Pan","year":"2014","journal-title":"Mutat. Res. Mol. Mech. Mutagen."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"2801","DOI":"10.1016\/j.cellsig.2014.08.023","article-title":"Wnt\/\u03b2-catenin signaling induces the transcription of cystathionine-\u03b3-lyase, a stimulator of tumor in colon cancer","volume":"26","author":"Fan","year":"2014","journal-title":"Cell. Signal."},{"key":"ref_70","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 H2S 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_71","doi-asserted-by":"crossref","first-page":"21350","DOI":"10.3390\/molecules191221350","article-title":"Is development of high-grade gliomas sulfur-dependent?","volume":"19","author":"Wrobel","year":"2014","journal-title":"Molecules"},{"key":"ref_72","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_73","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_74","doi-asserted-by":"crossref","first-page":"13098","DOI":"10.1096\/fj.201901304R","article-title":"Hydrogen sulfide signaling in mitochondria and disease","volume":"33","author":"Murphy","year":"2019","journal-title":"FASEB J."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"13528","DOI":"10.1021\/bi0615644","article-title":"Human cystathionine \u03b2-synthase is a target for sumoylation","volume":"45","author":"Kabil","year":"2006","journal-title":"Biochemistry"},{"key":"ref_76","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 \u03b2-synthase sumoylation. PLoS ONE, 3.","DOI":"10.1371\/journal.pone.0004032"},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"350","DOI":"10.1089\/ars.2014.5891","article-title":"S-glutathionylation enhances human cystathionine \u03b2-synthase activity under oxidative stress conditions","volume":"22","author":"Niu","year":"2015","journal-title":"Antioxid. Redox Signal."},{"key":"ref_78","doi-asserted-by":"crossref","unstructured":"Di Villa Bianca, R.d.E., Mitidieri, E., Esposito, D., Donnarumm, E., Russo, A., Fusco, F., Ianaro, A., Mirone, V., Cirino, G., and Russo, G. (2015). Human cystathionine-\u03b2-synthase phosphorylation on serine227 modulates hydrogen sulfide production in human urothelium. PLoS ONE, 10.","DOI":"10.1371\/journal.pone.0136859"},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"631","DOI":"10.1039\/B604182P","article-title":"Properties of an unusual heme cofactor in PLP-dependent cystathionine \u03b2-synthase","volume":"24","author":"Singh","year":"2007","journal-title":"Nat. Prod. Rep."},{"key":"ref_80","first-page":"351","article-title":"Correlation of methylation of CpG island in cystathionine beta synthase promoter and clinicopathological features in colorectal cancer","volume":"35","author":"Tu","year":"2013","journal-title":"Chin. J. Oncol."},{"key":"ref_81","first-page":"E3845","article-title":"Structural insight into the molecular mechanism of allosteric activation of human cystathionine \u03b2-synthase by S-adenosylmethionine","volume":"111","author":"Majtan","year":"2014","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"6489","DOI":"10.1073\/pnas.0509531103","article-title":"S-adenosylmethionine stabilizes cystathionine \u03b2-synthase and modulates redox capacity","volume":"103","author":"Prudova","year":"2006","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_83","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-\u03b2-synthase (CBS) on colorectal cancer cell proliferation and bioenergetics in vitro","volume":"41","author":"Coletta","year":"2014","journal-title":"Nitric Oxide"},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"2523","DOI":"10.1074\/jbc.RA117.000103","article-title":"Allosteric control of human cystathionine \u03b2-synthase activity by a redox active disulfide bond","volume":"293","author":"Niu","year":"2018","journal-title":"J. Biol. Chem."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"1398","DOI":"10.1158\/1541-7786.MCR-14-0184","article-title":"Decreased expression of cystathionine \u03b2-synthase promotes glioma tumorigenesis","volume":"12","author":"Takano","year":"2014","journal-title":"Mol. Cancer Res."},{"key":"ref_86","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_87","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1007\/s00726-010-0606-3","article-title":"The expression and activity of cystathionine-\u03b3-lyase and 3-mercaptopyruvate sulfurtransferase in human neoplastic cell lines","volume":"41","author":"Jurkowska","year":"2011","journal-title":"Amino Acids"},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"583","DOI":"10.1111\/bph.14446","article-title":"Regulators of the transsulfuration pathway","volume":"176","author":"Sbodio","year":"2019","journal-title":"Br. J. Pharmacol"},{"key":"ref_89","doi-asserted-by":"crossref","unstructured":"He, F., Ru, X., and Wen, T. (2020). NRF2, a transcription factor for stress response and beyond. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21134777"},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"465","DOI":"10.1089\/ars.2012.4944","article-title":"The gasotransmitter hydrogen sulfide induces nrf2-target genes by inactivating the keap1 ubiquitin ligase substrate adaptor through formation of a disulfide bond between cys-226 and cys-613","volume":"19","author":"Hourihan","year":"2013","journal-title":"Antioxid. Redox Signal."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"26450","DOI":"10.1074\/jbc.M111.266643","article-title":"Specificity protein-1 as a critical regulator of human cystathionine \u03b3-lyase in smooth muscle cells","volume":"286","author":"Yang","year":"2011","journal-title":"J. Biol. Chem."},{"key":"ref_92","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_93","doi-asserted-by":"crossref","first-page":"577","DOI":"10.1111\/bph.14100","article-title":"Multiple role of 3-mercaptopyruvate sulfurtransferase: Antioxidative function, H2S and polysulfide production and possible SOx production","volume":"175","author":"Nagahara","year":"2018","journal-title":"Br. J. Pharmacol."},{"key":"ref_94","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_95","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_96","doi-asserted-by":"crossref","first-page":"266","DOI":"10.1093\/jnci\/93.4.266","article-title":"Tumor hypoxia: Definitions and current clinical, biologic, and molecular aspects","volume":"93","author":"Hockel","year":"2001","journal-title":"J. Natl. Cancer Inst."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"385","DOI":"10.3389\/fphar.2016.00385","article-title":"The role of hydrogen sulfide in renal system","volume":"7","author":"Cao","year":"2016","journal-title":"Front. Pharmacol."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1007\/s10528-013-9624-7","article-title":"Regulation of cystathionine \u03b3-lyase in mammalian cells by hypoxia","volume":"52","author":"Wang","year":"2014","journal-title":"Biochem. Genet."},{"key":"ref_99","doi-asserted-by":"crossref","unstructured":"Malagrin\u00f2, F., Zuhra, K., Mascolo, L., Mastronicola, D., Vicente, J.B., Forte, E., and Giuffr\u00e8, A. (2019). Hydrogen sulfide oxidation: Adaptive changes in mitochondria of SW480 colorectal cancer cells upon exposure to hypoxia. Oxidative Med. Cell. Longev.","DOI":"10.1155\/2019\/8102936"},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"C305","DOI":"10.1152\/ajpcell.00230.2015","article-title":"Hydrogen sulfide promotes angiogenesis by downregulating miR-640 via the VEGFR2\/mTOR pathway","volume":"310","author":"Zhou","year":"2016","journal-title":"Am. J. Physiol. Cell Physiol."},{"key":"ref_101","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_102","doi-asserted-by":"crossref","first-page":"853","DOI":"10.1111\/j.1476-5381.2010.01191.x","article-title":"Hydrogen sulphide and angiogenesis: Mechanisms and applications","volume":"164","author":"Papapetropoulos","year":"2011","journal-title":"Br. J. Pharmacol."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1186\/1756-9966-30-87","article-title":"Apoptosis in cancer: From pathogenesis to treatment","volume":"30","author":"Wong","year":"2011","journal-title":"J. Exp. Clin. Cancer Res."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"646","DOI":"10.1016\/j.cell.2011.02.013","article-title":"Hallmarks of cancer: The next generation","volume":"144","author":"Hanahan","year":"2011","journal-title":"Cell"},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"H1237","DOI":"10.1152\/ajpheart.00004.2019","article-title":"Hydrogen sulfide-mediated regulation of cell death signaling ameliorates adverse cardiac remodeling and diabetic cardiomyopathy","volume":"316","author":"Kar","year":"2019","journal-title":"Am. J. Physiol. Heart Circ. Physiol."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"H801","DOI":"10.1152\/ajpheart.00377.2008","article-title":"Hydrogen sulfide attenuates hepatic ischemia-reperfusion injury: Role of antioxidant and antiapoptotic signaling","volume":"295","author":"Jha","year":"2008","journal-title":"Am. J. Physiol. Heart Circ. Physiol."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"3990","DOI":"10.3748\/wjg.v11.i26.3990","article-title":"Hydrogen sulfide protects colon cancer cells from chemopreventative agent beta-phenylethyl isothiocyanate induced apoptosis","volume":"11","author":"Rose","year":"2005","journal-title":"World J. Gastroenterol."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"1909","DOI":"10.3892\/or.2016.5014","article-title":"Exogenous hydrogen sulfide exerts proliferation, anti-apoptosis, migration effects and accelerates cell cycle progression in multiple myeloma cells via activating the Akt pathway","volume":"36","author":"Zheng","year":"2016","journal-title":"Oncol. Rep."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"2194","DOI":"10.3892\/ijo.2015.2914","article-title":"Exogenous hydrogen sulfide exerts proliferation\/anti-apoptosis\/angiogenesis\/migration effects via amplifying the activation of NF-kappaB pathway in PLC\/PRF\/5 hepatoma cells","volume":"46","author":"Zhen","year":"2015","journal-title":"Int. J. Oncol."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"467","DOI":"10.1111\/j.1476-5381.2010.00887.x","article-title":"Protective effect of hydrogen sulphide against 6-OHDA-induced cell injury in SH-SY5Y cells involves PKC\/PI3K\/Akt pathway","volume":"161","author":"Tiong","year":"2010","journal-title":"Br. J. Pharmacol."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"86","DOI":"10.1186\/1476-4598-12-86","article-title":"The complexity of NF-kappaB signaling in inflammation and cancer","volume":"12","author":"Hoesel","year":"2013","journal-title":"Mol. Cancer"},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1016\/j.ccell.2018.03.022","article-title":"NRF2 and the Hallmarks of Cancer","volume":"34","author":"Chapman","year":"2018","journal-title":"Cancer Cell"},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"621","DOI":"10.1080\/15216540600957438","article-title":"ERK1\/2 MAP kinases in cell survival and apoptosis","volume":"58","author":"Lu","year":"2006","journal-title":"IUBMB Life"},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"610","DOI":"10.1038\/nrm.2017.53","article-title":"The multifaceted roles of PARP1 in DNA repair and chromatin remodelling","volume":"18","author":"Nussenzweig","year":"2017","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1158\/2159-8290.CD-16-0860","article-title":"Targeting DNA Repair in Cancer: Beyond PARP Inhibitors","volume":"7","author":"Brown","year":"2017","journal-title":"Cancer Discov."},{"key":"ref_116","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_117","doi-asserted-by":"crossref","unstructured":"Li, M., Liu, Y., Deng, Y., Pan, L., Fu, H., Han, X., Li, Y., Shi, H., and Wang, T. (2021). Therapeutic potential of endogenous hydrogen sulfide inhibition in breast cancer (Review). Oncol. Rep., 45.","DOI":"10.3892\/or.2021.8019"},{"key":"ref_118","doi-asserted-by":"crossref","unstructured":"Szabo, C. (2021). Hydrogen Sulfide, an Endogenous Stimulator of Mitochondrial Function in Cancer Cells. Cells, 10.","DOI":"10.3390\/cells10020220"},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"101772","DOI":"10.1016\/j.redox.2020.101772","article-title":"Effects of hydrogen sulfide on mitochondrial function and cellular bioenergetics","volume":"38","author":"Paul","year":"2021","journal-title":"Redox Biol."},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"116","DOI":"10.1016\/j.phrs.2016.08.023","article-title":"S-Sulfhydration of ATP synthase by hydrogen sulfide stimulates mitochondrial bioenergetics","volume":"113 Pt A","author":"Modis","year":"2016","journal-title":"Pharmacol. Res."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1016\/j.cmet.2015.12.006","article-title":"The Emerging Hallmarks of Cancer Metabolism","volume":"23","author":"Pavlova","year":"2016","journal-title":"Cell Metab."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"519","DOI":"10.1085\/jgp.8.6.519","article-title":"The Metabolism of Tumors in the Body","volume":"8","author":"Warburg","year":"1927","journal-title":"J. Gen. Physiol."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"904","DOI":"10.1002\/iub.1216","article-title":"Lactate dehydrogenase A in cancer: A promising target for diagnosis and therapy","volume":"65","author":"Miao","year":"2013","journal-title":"IUBMB Life"},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"86","DOI":"10.1016\/j.bcp.2017.03.025","article-title":"H2S-induced S-sulfhydration of lactate dehydrogenase a (LDHA) stimulates cellular bioenergetics in HCT116 colon cancer cells","volume":"136","author":"Untereiner","year":"2017","journal-title":"Biochem. Pharmacol."},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"395","DOI":"10.1146\/annurev-pathol-020117-043854","article-title":"Epithelial Mesenchymal Transition in Tumor Metastasis","volume":"13","author":"Mittal","year":"2018","journal-title":"Annu. Rev. Pathol."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"5741","DOI":"10.1158\/0008-5472.CAN-16-3480","article-title":"Upregulation of Cystathionine-beta-Synthase in Colonic Epithelia Reprograms Metabolism and Promotes Carcinogenesis","volume":"77","author":"Phillips","year":"2017","journal-title":"Cancer Res."},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1038\/nrd2115","article-title":"Angiogenesis: An organizing principle for drug discovery?","volume":"6","author":"Folkman","year":"2007","journal-title":"Nat. Rev. Drug Discov."},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"3500","DOI":"10.4049\/jimmunol.1202769","article-title":"The role of IL-1beta in the early tumor cell-induced angiogenic response","volume":"190","author":"Carmi","year":"2013","journal-title":"J. Immunol."},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"73","DOI":"10.7150\/ijbs.47850","article-title":"Role of hydrogen sulfide donors in cancer development and progression","volume":"17","author":"Ngowi","year":"2021","journal-title":"Int. J. Biol. Sci."},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"4322","DOI":"10.1111\/bph.12773","article-title":"Utilizing hydrogen sulfide as a novel anti-cancer agent by targeting cancer glycolysis and pH imbalance","volume":"171","author":"Lee","year":"2014","journal-title":"Br. J. Pharmacol."},{"key":"ref_131","doi-asserted-by":"crossref","unstructured":"Lee, Z.W., Zhou, J., Chen, C.-S., Zhao, Y., Tan, C.-H., Li, L., Moore, P.K., and Deng, L.-W. (2011). The slow-releasing hydrogen sulfide donor, GYY4137, exhibits novel anti-cancer effects in vitro and in vivo. PLoS ONE, 6.","DOI":"10.1371\/journal.pone.0021077"},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1016\/j.yexcr.2013.10.023","article-title":"Differential susceptibility to hydrogen sulfide-induced apoptosis between PHLDA1-overexpressing oral cancer cell lines and oral keratinocytes: Role of PHLDA1 as an apoptosis suppressor","volume":"320","author":"Murata","year":"2014","journal-title":"Exp. Cell Res."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"1259","DOI":"10.3892\/ijo.2014.2305","article-title":"GYY4137, a hydrogen sulfide (H2S) donor, shows potent anti-hepatocellular carcinoma activity through blocking the STAT3 pathway","volume":"44","author":"Lu","year":"2014","journal-title":"Int. J. Oncol."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1111\/pcmr.12312","article-title":"Role of the cystathionine \u03b3 lyase\/hydrogen sulfide pathway in human melanoma progression","volume":"28","author":"Panza","year":"2015","journal-title":"Pigment. Cell Melanoma Res."},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"e02244","DOI":"10.1016\/j.heliyon.2019.e02244","article-title":"Hydrogen sulfide donor GYY4137 suppresses proliferation of human colorectal cancer Caco-2 cells by inducing both cell cycle arrest and cell death","volume":"5","author":"Sakuma","year":"2019","journal-title":"Heliyon"},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s41419-020-2222-9","article-title":"ADT-OH, a hydrogen sulfide-releasing donor, induces apoptosis and inhibits the development of melanoma in vivo by upregulating FADD","volume":"11","author":"Cai","year":"2020","journal-title":"Cell Death Dis."},{"key":"ref_137","doi-asserted-by":"crossref","unstructured":"Kaium, M., Liu, Y., Zhu, Q., Liu, C.-h., Duan, J.-L., Tan, B.K., and Zhu, Y.Z. (2011). H2S donor, S-propargyl-cysteine, increases CSE in SGC-7901 and cancer-induced mice: Evidence for a novel anti-cancer effect of endogenous H2S?. PLoS ONE, 6.","DOI":"10.1371\/journal.pone.0020525"},{"key":"ref_138","doi-asserted-by":"crossref","unstructured":"Wu, Y.C., Wang, X.J., Yu, L., Chan, F.K., Cheng, A.S., Yu, J., Sung, J.J., Wu, W.K., and Cho, C.H. (2012). Hydrogen sulfide lowers proliferation and induces protective autophagy in colon epithelial cells. PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0037572"},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"424","DOI":"10.1089\/ars.2014.5933","article-title":"The therapeutic potential of cystathionine \u03b2-synthetase\/hydrogen sulfide inhibition in cancer","volume":"22","author":"Hellmich","year":"2015","journal-title":"Antioxid. Redox Signal."},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"11788","DOI":"10.1039\/C4CC00968A","article-title":"Hydrogen sulfide (H2S) releasing agents: Chemistry and biological applications","volume":"50","author":"Zhao","year":"2014","journal-title":"Chem. Commun."},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"367","DOI":"10.1016\/j.apsb.2015.06.004","article-title":"Hydrogen sulfide prodrugs\u2014A review","volume":"5","author":"Zheng","year":"2015","journal-title":"Acta Pharm. Sin. B"},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"18","DOI":"10.1007\/s11684-015-0427-6","article-title":"Therapeutic application of hydrogen sulfide donors: The potential and challenges","volume":"10","author":"Wu","year":"2016","journal-title":"Front. Med."},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"96","DOI":"10.1089\/ars.2019.7841","article-title":"Activatable small-molecule hydrogen sulfide donors","volume":"32","author":"Levinn","year":"2020","journal-title":"Antioxid. Redox Signal."},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"664","DOI":"10.3389\/fphar.2017.00664","article-title":"Recent development of hydrogen sulfide releasing\/stimulating reagents and their potential applications in cancer and glycometabolic disorders","volume":"8","author":"Yang","year":"2017","journal-title":"Front. Pharmacol."},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"1154","DOI":"10.1002\/ptr.6586","article-title":"Diallyl trisulfide, a H2S donor, inhibits cell growth of human papillary thyroid carcinoma KTC-1 cells through a positive feedback loop between H2S and cystathionine-gamma-lyase","volume":"34","author":"Xu","year":"2020","journal-title":"Phytother. Res."},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"110464","DOI":"10.1016\/j.ecoenv.2020.110464","article-title":"Exogenous hydrogen sulfide donor NaHS alleviates nickel-induced epithelial-mesenchymal transition and the migration of A549 cells by regulating TGF-\u03b21\/Smad2\/Smad3 signaling","volume":"195","author":"Ye","year":"2020","journal-title":"Ecotoxicol. Environ. Saf."},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"101564","DOI":"10.1016\/j.redox.2020.101564","article-title":"Hydrogen sulfide and its donors: Novel antitumor and antimetastatic therapies for triple-negative breast cancer","volume":"34","author":"Li","year":"2020","journal-title":"Redox Biol."},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"677","DOI":"10.1016\/0006-291X(75)90452-0","article-title":"Active site-directed inactivation of cystathionine \u03b3-synthetase and glutamic pyruvic transaminase by propargylglycine","volume":"62","author":"Marcotte","year":"1975","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"922","DOI":"10.1111\/bph.12171","article-title":"Selectivity of commonly used pharmacological inhibitors for cystathionine \u03b2 synthase (CBS) and cystathionine \u03b3 lyase (CSE)","volume":"169","author":"Asimakopoulou","year":"2013","journal-title":"Br. J. Pharmacol."},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"378","DOI":"10.1016\/j.eururo.2008.05.014","article-title":"Hydrogen sulphide is involved in testosterone vascular effect","volume":"56","author":"Bucci","year":"2009","journal-title":"Eur. Urol."},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"1998","DOI":"10.1161\/ATVBAHA.110.209783","article-title":"Hydrogen sulfide is an endogenous inhibitor of phosphodiesterase activity","volume":"30","author":"Bucci","year":"2010","journal-title":"Arter. Thromb. Vasc. Biol."},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1042\/BJ20131434","article-title":"The cystathionine \u03b3-lyase\/hydrogen sulfide system maintains cellular glutathione status","volume":"460","author":"Lee","year":"2014","journal-title":"Biochemical. J."},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"917","DOI":"10.1038\/nrd2425","article-title":"Hydrogen sulphide and its therapeutic potential","volume":"6","year":"2007","journal-title":"Nat. Rev. Drug Discov."},{"key":"ref_154","doi-asserted-by":"crossref","first-page":"1301","DOI":"10.1016\/0006-291X(76)90338-7","article-title":"Irreversible inactivation of aspartate aminotransferases during transamination with L-propargylglycine","volume":"68","author":"Tanase","year":"1976","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"3487","DOI":"10.1016\/S0021-9258(19)85725-3","article-title":"Mechanism-based inactivation of pig heart L-alanine transaminase by L-propargylglycine. Half-site reactivity","volume":"255","author":"Burnett","year":"1980","journal-title":"J. Biol. Chem."},{"key":"ref_156","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1016\/j.fob.2013.01.010","article-title":"Irreversible inactivation of snake venom l-amino acid oxidase by covalent modification during catalysis of l-propargylglycine","volume":"3","author":"Mitra","year":"2013","journal-title":"FEBS Open Bio"},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"497","DOI":"10.1124\/pr.117.014050","article-title":"International union of basic and clinical pharmacology. CII: Pharmacological modulation of H2S levels: H2S donors and H2S biosynthesis inhibitors","volume":"69","author":"Szabo","year":"2017","journal-title":"Pharmacol. Rev."},{"key":"ref_158","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_159","doi-asserted-by":"crossref","first-page":"194","DOI":"10.1038\/s42003-019-0431-5","article-title":"Non-enzymatic hydrogen sulfide production from cysteine in blood is catalyzed by iron and vitamin B6","volume":"2","author":"Yang","year":"2019","journal-title":"Commun. Biol."},{"key":"ref_160","doi-asserted-by":"crossref","unstructured":"Zuhra, K., Augsburger, F., Majtan, T., and Szabo, C. (2020). Cystathionine-beta-Synthase: Molecular Regulation and Pharmacological Inhibition. Biomolecules, 10.","DOI":"10.3390\/biom10050697"},{"key":"ref_161","doi-asserted-by":"crossref","first-page":"242","DOI":"10.1021\/acscentsci.6b00019","article-title":"\u201cZipped synthesis\u201d by cross-metathesis provides a cystathionine \u03b2-synthase inhibitor that attenuates cellular H2S levels and reduces neuronal infarction in a rat ischemic stroke model","volume":"2","author":"McCune","year":"2016","journal-title":"ACS Cent. Sci."},{"key":"ref_162","doi-asserted-by":"crossref","first-page":"18","DOI":"10.1016\/j.phrs.2016.08.016","article-title":"Screening of a composite library of clinically used drugs and well-characterized pharmacological compounds for cystathionine \u03b2-synthase inhibition identifies benserazide as a drug potentially suitable for repurposing for the experimental therapy of colon cancer","volume":"113","author":"Druzhyna","year":"2016","journal-title":"Pharmacol. Res."},{"key":"ref_163","doi-asserted-by":"crossref","first-page":"198","DOI":"10.1039\/C6MD00493H","article-title":"Discovery of selective cystathionine \u03b2-synthase inhibitors by high-throughput screening with a fluorescent thiol probe","volume":"8","author":"Niu","year":"2017","journal-title":"MedChemComm"},{"key":"ref_164","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1039\/C7MD00484B","article-title":"Antitumor effect of sikokianin C, a selective cystathionine \u03b2-synthase inhibitor, against human colon cancer in vitro and in vivo","volume":"9","author":"Niu","year":"2018","journal-title":"MedChemComm"},{"key":"ref_165","doi-asserted-by":"crossref","first-page":"1556","DOI":"10.1111\/bph.13459","article-title":"d-Penicillamine modulates hydrogen sulfide (H2S) pathway through selective inhibition of cystathionine-\u03b3-lyase","volume":"173","author":"Brancaleone","year":"2016","journal-title":"Br. J. Pharmacol."},{"key":"ref_166","doi-asserted-by":"crossref","first-page":"34398","DOI":"10.1038\/srep34398","article-title":"Fragment-based de novo design of a cystathionine \u03b3-lyase selective inhibitor blocking hydrogen sulfide production","volume":"6","author":"Corvino","year":"2016","journal-title":"Sci. Rep."},{"key":"ref_167","doi-asserted-by":"crossref","first-page":"1241","DOI":"10.1021\/acsmedchemlett.7b00313","article-title":"2-Arylidene hydrazinecarbodithioates as potent, selective inhibitors of cystathionine \u03b3-lyase (CSE)","volume":"8","author":"Bhattacharjee","year":"2017","journal-title":"ACS Med. Chem. Lett."},{"key":"ref_168","doi-asserted-by":"crossref","first-page":"1677","DOI":"10.1021\/acs.jmedchem.8b01720","article-title":"Discovery of a Bioactive Inhibitor with a New Scaffold for Cystathionine \u03b3-Lyase","volume":"62","author":"Hu","year":"2018","journal-title":"J. Med. Chem."},{"key":"ref_169","first-page":"427","article-title":"I157172, a novel inhibitor of cystathionine \u03b3-lyase, inhibits growth and migration of breast cancer cells via SIRT1-mediated deacetylation of STAT3","volume":"41","author":"Wang","year":"2019","journal-title":"Oncol. Rep."},{"key":"ref_170","doi-asserted-by":"crossref","first-page":"40227","DOI":"10.1038\/srep40227","article-title":"Discovery and mechanistic characterization of selective inhibitors of H2S-producing enzyme: 3-mercaptopyruvate sulfurtransferase (3MST) targeting active-site cysteine persulfide","volume":"7","author":"Hanaoka","year":"2017","journal-title":"Sci. Rep."},{"key":"ref_171","doi-asserted-by":"crossref","first-page":"669","DOI":"10.1089\/ars.2017.7070","article-title":"Fluorescent probes and selective inhibitors for biological studies of hydrogen sulfide-and polysulfide-mediated signaling","volume":"27","author":"Takano","year":"2017","journal-title":"Antioxidants Redox Signal."},{"key":"ref_172","doi-asserted-by":"crossref","first-page":"18003","DOI":"10.1021\/ja207851s","article-title":"Development of a highly selective fluorescence probe for hydrogen sulfide","volume":"133","author":"Sasakura","year":"2011","journal-title":"J. Am. Chem. Soc."},{"key":"ref_173","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."}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/22\/12\/6562\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T06:18:31Z","timestamp":1760163511000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/22\/12\/6562"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,6,18]]},"references-count":173,"journal-issue":{"issue":"12","published-online":{"date-parts":[[2021,6]]}},"alternative-id":["ijms22126562"],"URL":"https:\/\/doi.org\/10.3390\/ijms22126562","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2021,6,18]]}}}