{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,11]],"date-time":"2026-05-11T20:12:09Z","timestamp":1778530329714,"version":"3.51.4"},"reference-count":83,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2021,10,1]],"date-time":"2021-10-01T00:00:00Z","timestamp":1633046400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2021,10,1]],"date-time":"2021-10-01T00:00:00Z","timestamp":1633046400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2021,10,1]],"date-time":"2021-10-01T00:00:00Z","timestamp":1633046400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2021,10,1]],"date-time":"2021-10-01T00:00:00Z","timestamp":1633046400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2021,10,1]],"date-time":"2021-10-01T00:00:00Z","timestamp":1633046400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2021,10,1]],"date-time":"2021-10-01T00:00:00Z","timestamp":1633046400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/501100002261","name":"Russian Foundation for Basic Research","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100002261","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100006769","name":"Russian Science Foundation","doi-asserted-by":"publisher","award":["21-73-20264"],"award-info":[{"award-number":["21-73-20264"]}],"id":[{"id":"10.13039\/501100006769","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["European Journal of Medicinal Chemistry"],"published-print":{"date-parts":[[2021,10]]},"DOI":"10.1016\/j.ejmech.2021.113589","type":"journal-article","created":{"date-parts":[[2021,6,10]],"date-time":"2021-06-10T01:47:05Z","timestamp":1623289625000},"page":"113589","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":20,"special_numbering":"C","title":["Investigation of 3-sulfamoyl coumarins against cancer-related IX and XII isoforms of human carbonic anhydrase as well as cancer cells leads to the discovery of 2-oxo-2H-benzo[h]chromene-3-sulfonamide \u2013 A new caspase-activating proapoptotic agent"],"prefix":"10.1016","volume":"222","author":[{"given":"Dmitry","family":"Dar'in","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Grigory","family":"Kantin","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Stanislav","family":"Kalinin","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Tatiana","family":"Sharonova","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6408-8329","authenticated-orcid":false,"given":"Alexander","family":"Bunev","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Gennady I.","family":"Ostapenko","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3342-702X","authenticated-orcid":false,"given":"Alessio","family":"Nocentini","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Vladimir","family":"Sharoyko","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4262-0323","authenticated-orcid":false,"given":"Claudiu T.","family":"Supuran","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mikhail","family":"Krasavin","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.ejmech.2021.113589_bib1","series-title":"Biochem. Cell Biol.","first-page":"930","article-title":"Why bicarbonate?","author":"Casey","year":"2006"},{"key":"10.1016\/j.ejmech.2021.113589_bib2","doi-asserted-by":"crossref","first-page":"2023","DOI":"10.1042\/BCJ20160115","article-title":"Structure and function of carbonic anhydrases","volume":"473","author":"Supuran","year":"2016","journal-title":"Biochem. J."},{"key":"10.1016\/j.ejmech.2021.113589_bib3","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1007\/978-94-007-7359-2_3","article-title":"Catalytic mechanism of \u03b1-class carbonic anhydrases: CO2 hydration and proton transfer","volume":"75","author":"Boone","year":"2014","journal-title":"Subcell. Biochem."},{"key":"10.1016\/j.ejmech.2021.113589_bib4","doi-asserted-by":"crossref","first-page":"56","DOI":"10.3390\/metabo7040056","article-title":"An overview of the bacterial carbonic anhydrases","volume":"7","author":"Supuran","year":"2017","journal-title":"Metabolites"},{"key":"10.1016\/j.ejmech.2021.113589_bib5","doi-asserted-by":"crossref","first-page":"644","DOI":"10.1080\/14756366.2019.1571273","article-title":"Inhibition of \u03b1-, \u03b2-, \u03b3-, \u03b4-, \u03b6- and \u03b7-class carbonic anhydrases from bacteria, fungi, algae, diatoms and protozoans with famotidine","volume":"34","author":"Angeli","year":"2019","journal-title":"J.\u00a0Enzym. Inhib. Med. Chem."},{"key":"10.1016\/j.ejmech.2021.113589_bib6","doi-asserted-by":"crossref","first-page":"1194","DOI":"10.1080\/14756366.2018.1490733","article-title":"Inhibition of \u03b1-, \u03b2-, \u03b3-, and \u03b4-carbonic anhydrases from bacteria and diatoms with N\u2032 -aryl- N -hydroxy-ureas","volume":"33","author":"Berrino","year":"2018","journal-title":"J.\u00a0Enzym. Inhib. Med. Chem."},{"key":"10.1016\/j.ejmech.2021.113589_bib7","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3390\/ijms22020571","article-title":"Effect of sulfonamides and their structurally related derivatives on the activity of \u03b9-carbonic anhydrase from burkholderia territorii","volume":"22","author":"De Luca","year":"2021","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.ejmech.2021.113589_bib8","doi-asserted-by":"crossref","first-page":"54","DOI":"10.1080\/14756366.2016.1217856","article-title":"Cloning, expression and purification of the complete domain of the \u03b7-carbonic anhydrase from Plasmodium falciparum","volume":"31","author":"Del Prete","year":"2016","journal-title":"J.\u00a0Enzym. Inhib. Med. Chem."},{"key":"10.1016\/j.ejmech.2021.113589_bib9","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1007\/978-94-007-7359-2_15","article-title":"Carbonic anhydrase inhibitors drug design","volume":"75","author":"McKenna","year":"2014","journal-title":"Subcell. Biochem."},{"key":"10.1016\/j.ejmech.2021.113589_bib10","doi-asserted-by":"crossref","first-page":"759","DOI":"10.3109\/14756366.2012.672983","article-title":"Structure-based drug discovery of carbonic anhydrase inhibitors","volume":"27","author":"Supuran","year":"2012","journal-title":"J.\u00a0Enzym. Inhib. Med. Chem."},{"key":"10.1016\/j.ejmech.2021.113589_bib11","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1016\/j.cbpa.2010.06.161","article-title":"Perspectives on carbonic anhydrase","volume":"157","author":"Gilmour","year":"2010","journal-title":"Comp. Biochem. Physiol. Mol. Integr. Physiol."},{"key":"10.1016\/j.ejmech.2021.113589_bib12","doi-asserted-by":"crossref","first-page":"1854","DOI":"10.1016\/j.bbapap.2011.07.007","article-title":"Molecular evolution and selection pressure in alpha-class carbonic anhydrase family members","volume":"1814","author":"McDevitt","year":"2011","journal-title":"Biochim. Biophys. Acta Protein Proteonomics"},{"key":"10.1016\/j.ejmech.2021.113589_bib13","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1007\/s10555-019-09799-0","article-title":"The role of carbonic anhydrase IX in cancer development: links to hypoxia, acidosis, and beyond","volume":"38","author":"Pastorekova","year":"2019","journal-title":"Canc. Metastasis Rev."},{"key":"10.1016\/j.ejmech.2021.113589_bib14","doi-asserted-by":"crossref","first-page":"509","DOI":"10.1080\/13543776.2019.1629419","article-title":"Carbonic anhydrases as disease markers","volume":"29","author":"Zamanova","year":"2019","journal-title":"Expert Opin. Ther. Pat."},{"key":"10.1016\/j.ejmech.2021.113589_bib15","doi-asserted-by":"crossref","first-page":"825","DOI":"10.2174\/156802607780636690","article-title":"Carbonic anhydrases as drug targets - an overview","volume":"7","author":"Supuran","year":"2007","journal-title":"Curr. Top. Med. Chem."},{"key":"10.1016\/j.ejmech.2021.113589_bib16","doi-asserted-by":"crossref","DOI":"10.1016\/j.bmc.2019.115086","article-title":"Highly hydrophilic 1,3-oxazol-5-yl benzenesulfonamide inhibitors of carbonic anhydrase II for reduction of glaucoma-related intraocular pressure","volume":"27","author":"Kalinin","year":"2019","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.ejmech.2021.113589_bib17","series-title":"Carbon. Anhydrases Biochem. Pharmacol. An Evergr. Pharm. Target","first-page":"367","article-title":"Carbonic anhydrase inhibitors for the treatment of neuropathic pain and arthritis","author":"Nocentini","year":"2019"},{"key":"10.1016\/j.ejmech.2021.113589_bib18","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1517\/14728214.2012.664132","article-title":"Carbonic anhydrase inhibitors as emerging drugs for the treatment of obesity","volume":"17","author":"Supuran","year":"2012","journal-title":"Expet Opin. Emerg. Drugs"},{"key":"10.1016\/j.ejmech.2021.113589_bib19","doi-asserted-by":"crossref","first-page":"349","DOI":"10.1007\/978-94-007-7359-2_17","article-title":"Glaucoma and the applications of carbonic anhydrase inhibitors","volume":"75","author":"Scozzafava","year":"2014","journal-title":"Subcell. Biochem."},{"key":"10.1016\/j.ejmech.2021.113589_bib20","doi-asserted-by":"crossref","first-page":"168","DOI":"10.1038\/nrd2467","article-title":"Carbonic anhydrases: novel therapeutic applications for inhibitors and activators","volume":"7","author":"Supuran","year":"2008","journal-title":"Nat. Rev. Drug Discov."},{"key":"10.1016\/j.ejmech.2021.113589_bib21","doi-asserted-by":"crossref","first-page":"603","DOI":"10.2147\/JEP.S265620","article-title":"p>Experimental carbonic anhydrase inhibitors for the treatment of hypoxic tumors<\/p>","volume":"12","author":"Supuran","year":"2020","journal-title":"J.\u00a0Exp. Pharmacol."},{"key":"10.1016\/j.ejmech.2021.113589_bib22","doi-asserted-by":"crossref","first-page":"108","DOI":"10.2174\/1573399812666161214122351","article-title":"The role of carbonic anhydrase in hepatic glucose production","volume":"14","author":"Ismail","year":"2018","journal-title":"Curr. Diabetes Rev."},{"key":"10.1016\/j.ejmech.2021.113589_bib23","doi-asserted-by":"crossref","first-page":"1206","DOI":"10.1080\/14756366.2020.1766455","article-title":"Carbonic anhydrase modulation of emotional memory. Implications for the treatment of cognitive disorders","volume":"35","author":"Blandina","year":"2020","journal-title":"J.\u00a0Enzym. Inhib. Med. Chem."},{"key":"10.1016\/j.ejmech.2021.113589_bib24","doi-asserted-by":"crossref","first-page":"412","DOI":"10.3390\/metabo10100412","article-title":"Carbonic anhydrase inhibitors targeting metabolism and tumor microenvironment","volume":"10","author":"Angeli","year":"2020","journal-title":"Metabolites"},{"key":"10.1016\/j.ejmech.2021.113589_bib25","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3390\/ijms22063171","article-title":"Proton transport in cancer cells: the role of carbonic anhydrases","volume":"22","author":"Becker","year":"2021","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.ejmech.2021.113589_bib26","article-title":"Carbonic anhydrase XII inhibition overcomes P-glycoprotein-mediated drug resistance: a potential new combination therapy in cancer","volume":"4","author":"Tonissen","year":"2021","journal-title":"Cancer Drug Resist"},{"key":"10.1016\/j.ejmech.2021.113589_bib27","doi-asserted-by":"crossref","DOI":"10.3390\/metabo8010019","article-title":"Carbonic anhydrases: role in pH control and cancer","volume":"8","author":"Mboge","year":"2018","journal-title":"Metabolites"},{"key":"10.1016\/j.ejmech.2021.113589_bib28","series-title":"Top. Anti-cancer Res.","first-page":"3","article-title":"Advances in anti-cancer drug development targeting carbonic anhydrase IX and XII","author":"Mboge","year":"2016"},{"key":"10.1016\/j.ejmech.2021.113589_bib29","doi-asserted-by":"crossref","first-page":"963","DOI":"10.1080\/13543784.2018.1548608","article-title":"Carbonic anhydrase inhibitors as emerging agents for the treatment and imaging of hypoxic tumors","volume":"27","author":"Supuran","year":"2018","journal-title":"Expet Opin. Invest. Drugs"},{"key":"10.1016\/j.ejmech.2021.113589_bib30","doi-asserted-by":"crossref","DOI":"10.7150\/thno.21848","article-title":"Past, present, and future: development of theranostic agents targeting carbonic anhydrase IX","volume":"7","author":"Lau","year":"2017","journal-title":"Theranostics"},{"key":"10.1016\/j.ejmech.2021.113589_bib31","article-title":"Radiotracers for positron emission tomography (PET) targeting tumour-associated carbonic anhydrase isoforms","author":"Burianova","year":"2020","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ejmech.2021.113589_bib32","doi-asserted-by":"crossref","first-page":"453543","DOI":"10.1155\/2015\/453543","article-title":"Probing the surface of human carbonic anhydrase for clues towards the design of isoform specific inhibitors","volume":"2015","author":"Pinard","year":"2015","journal-title":"BioMed Res. Int."},{"key":"10.1016\/j.ejmech.2021.113589_bib33","doi-asserted-by":"crossref","first-page":"345","DOI":"10.3109\/14756366.2015.1122001","article-title":"How many carbonic anhydrase inhibition mechanisms exist?","volume":"31","author":"Supuran","year":"2016","journal-title":"J.\u00a0Enzym. Inhib. Med. Chem."},{"key":"10.1016\/j.ejmech.2021.113589_bib34","doi-asserted-by":"crossref","first-page":"334","DOI":"10.1016\/j.bmc.2013.11.016","article-title":"Combining the tail and the ring approaches for obtaining potent and isoform-selective carbonic anhydrase inhibitors: solution and X-ray crystallographic studies","volume":"22","author":"Bozdag","year":"2014","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.ejmech.2021.113589_bib35","doi-asserted-by":"crossref","first-page":"7422","DOI":"10.1021\/acs.jmedchem.0c00733","article-title":"Sulfonamide inhibitors of human carbonic anhydrases designed through a three-tails approach: improving ligand\/isoform matching and selectivity of action","volume":"63","author":"Bonardi","year":"2020","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.ejmech.2021.113589_bib36","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1002\/cbic.201600513","article-title":"Structure\u2013activity relationships of benzenesulfonamide-based inhibitors towards carbonic anhydrase isoform specificity","volume":"18","author":"Bhatt","year":"2017","journal-title":"Chembiochem"},{"key":"10.1016\/j.ejmech.2021.113589_bib37","doi-asserted-by":"crossref","first-page":"335","DOI":"10.1021\/jm901287j","article-title":"Deciphering the mechanism of carbonic anhydrase inhibition with coumarins and thiocoumarins","volume":"53","author":"Maresca","year":"2010","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.ejmech.2021.113589_bib38","doi-asserted-by":"crossref","first-page":"793","DOI":"10.1517\/17460441.2013.795145","article-title":"Exploiting the hydrophobic and hydrophilic binding sites for designing carbonic anhydrase inhibitors","volume":"8","author":"De Simone","year":"2013","journal-title":"Expet Opin. Drug Discov."},{"key":"10.1016\/j.ejmech.2021.113589_bib39","doi-asserted-by":"crossref","first-page":"685","DOI":"10.1080\/14756366.2021.1887171","article-title":"Selective inhibition of carbonic anhydrase IX and XII by coumarin and psoralen derivatives","volume":"36","author":"Meleddu","year":"2021","journal-title":"J.\u00a0Enzym. Inhib. Med. Chem."},{"key":"10.1016\/j.ejmech.2021.113589_bib40","doi-asserted-by":"crossref","first-page":"506","DOI":"10.1080\/14756366.2020.1712596","article-title":"Sulfocoumarins as dual inhibitors of human carbonic anhydrase isoforms IX\/XII and of human thioredoxin reductase","volume":"35","author":"Krasavin","year":"2020","journal-title":"J.\u00a0Enzym. Inhib. Med. Chem."},{"key":"10.1016\/j.ejmech.2021.113589_bib41","doi-asserted-by":"crossref","first-page":"8271","DOI":"10.1021\/jm200983e","article-title":"Glycosyl coumarin carbonic anhydrase IX and XII inhibitors strongly attenuate the growth of primary breast tumors","volume":"54","author":"Touisni","year":"2011","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.ejmech.2021.113589_bib42","doi-asserted-by":"crossref","first-page":"2743","DOI":"10.1021\/jm0600287","article-title":"Indanesulfonamides as carbonic anhydrase inhibitors. Toward structure-based design of selective inhibitors of the tumor-associated isozyme CA IX","volume":"49","author":"Thiry","year":"2006","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.ejmech.2021.113589_bib43","doi-asserted-by":"crossref","first-page":"2882","DOI":"10.1016\/j.bmc.2016.04.052","article-title":"Novel sulfonamide bearing coumarin scaffolds as selective inhibitors of tumor associated carbonic anhydrase isoforms IX and XII","volume":"24","author":"Chandak","year":"2016","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.ejmech.2021.113589_bib44","doi-asserted-by":"crossref","first-page":"4873","DOI":"10.1016\/j.bmc.2010.06.028","article-title":"Coumarinyl-substituted sulfonamides strongly inhibit several human carbonic anhydrase isoforms: solution and crystallographic investigations","volume":"18","author":"Wagner","year":"2010","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.ejmech.2021.113589_bib45","doi-asserted-by":"crossref","first-page":"112897","DOI":"10.1016\/j.ejmech.2020.112897","article-title":"Novel 3-substituted coumarins as selective human carbonic anhydrase IX and XII inhibitors: synthesis, biological and molecular dynamics analysis","volume":"209","author":"Abdelrahman","year":"2021","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ejmech.2021.113589_bib46","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.ejmech.2013.04.035","article-title":"Sulfonamides containing coumarin moieties selectively and potently inhibit carbonic anhydrases II and IX: design, synthesis, inhibitory activity and 3D-QSAR analysis","volume":"66","author":"Wang","year":"2013","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ejmech.2021.113589_bib47","doi-asserted-by":"crossref","first-page":"991","DOI":"10.3109\/14756366.2015.1077823","article-title":"Synthesis, antioxidant and carbonic anhydrase I and II inhibitory activities of novel sulphonamide-substituted coumarylthiazole derivatives","volume":"31","author":"Kurt","year":"2016","journal-title":"J.\u00a0Enzym. Inhib. Med. Chem."},{"key":"10.1016\/j.ejmech.2021.113589_bib48","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1515\/hc-2020-0008","article-title":"Coumarin sulfonamide derivatives: an emerging class of therapeutic agents","volume":"26","author":"Irfan","year":"2020","journal-title":"Heterocycl. Commun."},{"key":"10.1016\/j.ejmech.2021.113589_bib49","doi-asserted-by":"crossref","first-page":"3463","DOI":"10.2174\/1568026618666180118153502","article-title":"ADME and safety aspects of non-cleavable linkers in drug discovery and development","volume":"17","author":"Walles","year":"2018","journal-title":"Curr. Top. Med. Chem."},{"key":"10.1016\/j.ejmech.2021.113589_bib50","series-title":"Pract. Med. Chem","first-page":"251","article-title":"Identical and non-identical twin drugs","author":"Contreras","year":"2003"},{"key":"10.1016\/j.ejmech.2021.113589_bib51","doi-asserted-by":"crossref","first-page":"4496","DOI":"10.1002\/cber.19040370442","article-title":"Condensationen von Salicylaldehyd mit Cyanessigester, Benzoylessigester und Acetylaceton","volume":"37","author":"Knoevenagel","year":"1904","journal-title":"Berichte Der Dtsch. Chem. Gesellschaft."},{"key":"10.1016\/j.ejmech.2021.113589_bib52","doi-asserted-by":"crossref","first-page":"3767","DOI":"10.1002\/ejoc.200600335","article-title":"Ionic liquid as catalyst and reaction medium \u2013 a simple, efficient and green procedure for Knoevenagel condensation of aliphatic and aromatic carbonyl compounds using a task-specific basic ionic liquid","author":"Ranu","year":"2006","journal-title":"Eur. J. Org Chem."},{"key":"10.1016\/j.ejmech.2021.113589_bib53","doi-asserted-by":"crossref","first-page":"763","DOI":"10.1021\/jo00154a001","article-title":"Direct synthesis of trisubstituted isothiazole 1,1-dioxides. Regioselective substitution reactions at C-3 and C-4","volume":"48","author":"Britcher","year":"1983","journal-title":"J.\u00a0Org. Chem."},{"key":"10.1016\/j.ejmech.2021.113589_bib54","doi-asserted-by":"crossref","first-page":"2561","DOI":"10.1016\/S0021-9258(18)62326-9","article-title":"The carbon dioxide hydration activity of carbonic anhydrase","volume":"246","author":"Khalifah","year":"1971","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.ejmech.2021.113589_bib55","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1080\/14756360410001689540","article-title":"Carbonic anhydrases: current state of the art, therapeutic applications and future prospects","volume":"19","author":"Pastorekova","year":"2004","journal-title":"J.\u00a0Enzym. Inhib. Med. Chem."},{"key":"10.1016\/j.ejmech.2021.113589_bib56","first-page":"773","article-title":"Differential regulation and prognostic significance of endogenous hypoxic markers in endometrial carcinomas","volume":"39","author":"Dong Soo","year":"2018","journal-title":"Eur. J. Gynaecol. Oncol."},{"key":"10.1016\/j.ejmech.2021.113589_bib57","doi-asserted-by":"crossref","first-page":"355","DOI":"10.2217\/14750708.4.3.355","article-title":"Therapeutic applications of the carbonic anhydrase inhibitors","volume":"4","author":"Supuran","year":"2007","journal-title":"Therapy"},{"key":"10.1016\/j.ejmech.2021.113589_bib58","doi-asserted-by":"crossref","DOI":"10.1155\/2015\/453543","article-title":"Probing the surface of human carbonic anhydrase for clues towards the design of isoform specific inhibitors","volume":"2015","author":"Pinard","year":"2015","journal-title":"BioMed Res. Int."},{"key":"10.1016\/j.ejmech.2021.113589_bib59","doi-asserted-by":"crossref","first-page":"1799","DOI":"10.1002\/med.21497","article-title":"Inhibition of carbonic anhydrase IX targets primary tumors, metastases, and cancer stem cells: three for the price of one","volume":"38","author":"Supuran","year":"2018","journal-title":"Med. Res. Rev."},{"key":"10.1016\/j.ejmech.2021.113589_bib60","doi-asserted-by":"crossref","DOI":"10.1186\/s12964-020-0530-4","article-title":"Tumor microenvironment complexity and therapeutic implications at a glance","volume":"18","author":"Baghban","year":"2020","journal-title":"Cell Commun. Signal."},{"key":"10.1016\/j.ejmech.2021.113589_bib61","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1080\/14756360902784425","article-title":"Taking advantage of tumor cell adaptations to hypoxia for developing new tumor markers and treatment strategies","volume":"24","author":"Ebbesen","year":"2009","journal-title":"J.\u00a0Enzym. Inhib. Med. Chem."},{"key":"10.1016\/j.ejmech.2021.113589_bib62","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1016\/j.gene.2017.04.027","article-title":"Carbonic anhydrase XII functions in health and disease","volume":"623","author":"Waheed","year":"2017","journal-title":"Gene"},{"key":"10.1016\/j.ejmech.2021.113589_bib63","doi-asserted-by":"crossref","first-page":"1569","DOI":"10.2174\/09298673113209990227","article-title":"Histopathological determinants of tumor resistance: a special look to the immunohistochemical expression of carbonic anhydrase IX in human cancers","volume":"21","author":"Ilardi","year":"2014","journal-title":"Curr. Med. Chem."},{"key":"10.1016\/j.ejmech.2021.113589_bib67","doi-asserted-by":"crossref","first-page":"1555","DOI":"10.1080\/14756366.2020.1801674","article-title":"Inhibitory activity against carbonic anhydrase IX and XII as a candidate selection criterion in the development of new anticancer agents","volume":"35","author":"Krasavin","year":"2020","journal-title":"J.\u00a0Enzym. Inhib. Med. Chem."},{"key":"10.1016\/j.ejmech.2021.113589_bib68","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1007\/s10555-019-09799-0","article-title":"The role of carbonic anhydrase IX in cancer development: links to hypoxia, acidosis, and beyond","volume":"38","author":"Pastorekova","year":"2019","journal-title":"Canc. Metastasis Rev."},{"key":"10.1016\/j.ejmech.2021.113589_bib69","doi-asserted-by":"crossref","first-page":"271","DOI":"10.3892\/ijo.2015.3253","article-title":"CA IX is upregulated in CoCl2-induced hypoxia and associated with cell invasive potential and a poor prognosis of breast cancer","volume":"48","author":"Chu","year":"2016","journal-title":"Int. J. Oncol."},{"key":"10.1016\/j.ejmech.2021.113589_bib70","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1016\/j.ejmech.2012.02.038","article-title":"Novel isoxazole polycyclic aromatic hydrocarbons as DNA-intercalating agents","volume":"51","author":"Rescifina","year":"2012","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ejmech.2021.113589_bib71","doi-asserted-by":"crossref","first-page":"45","DOI":"10.3892\/ol.2011.436","article-title":"Polycyclic aromatic compounds as anticancer agents: evaluation of synthesis and in\u00a0vitro cytotoxicity","volume":"3","author":"Bandyopadhyay","year":"2012","journal-title":"Oncol. Lett."},{"key":"10.1016\/j.ejmech.2021.113589_bib72","doi-asserted-by":"crossref","first-page":"55","DOI":"10.3389\/fchem.2014.00055","article-title":"Polycyclic aromatic compounds as anticancer agents: synthesis and biological evaluation of methoxy dibenzofluorene derivatives","volume":"2","author":"Becker","year":"2014","journal-title":"Front. Chem."},{"key":"10.1016\/j.ejmech.2021.113589_bib73","doi-asserted-by":"crossref","first-page":"15","DOI":"10.2174\/1381612826666201118113311","article-title":"A\u00a0comprehensive review on fused heterocyclic as DNA intercalators: promising anticancer agents","volume":"27","author":"Sharma","year":"2021","journal-title":"Curr. Pharmaceut. Des."},{"key":"10.1016\/j.ejmech.2021.113589_bib74","doi-asserted-by":"crossref","first-page":"200","DOI":"10.1016\/j.critrevonc.2013.12.012","article-title":"Cancer therapeutics: targeting the apoptotic pathway","volume":"90","author":"Khan","year":"2014","journal-title":"Crit. Rev. Oncol. Hematol."},{"key":"10.1016\/j.ejmech.2021.113589_bib75","doi-asserted-by":"crossref","first-page":"1002","DOI":"10.1016\/S1470-2045(08)70209-2","article-title":"Targeted manipulation of apoptosis in cancer treatment","volume":"9","author":"Call","year":"2008","journal-title":"Lancet Oncol."},{"key":"10.1016\/j.ejmech.2021.113589_bib76","doi-asserted-by":"crossref","first-page":"710","DOI":"10.1124\/jpet.110.167270","article-title":"Selective inhibition of carbonic anhydrase IX decreases cell proliferation and induces ceramide-mediated apoptosis in human cancer cells","volume":"334","author":"Cianchi","year":"2010","journal-title":"J.\u00a0Pharmacol. Exp. Therapeut."},{"key":"10.1016\/j.ejmech.2021.113589_bib77","doi-asserted-by":"crossref","first-page":"1137","DOI":"10.1080\/14756366.2018.1481403","article-title":"Selective inhibition of carbonic anhydrase-IX by sulphonamide derivatives induces pH and reactive oxygen species-mediated apoptosis in cervical cancer HeLa cells","volume":"33","author":"Koyuncu","year":"2018","journal-title":"J.\u00a0Enzym. Inhib. Med. Chem."},{"key":"10.1016\/j.ejmech.2021.113589_bib78","doi-asserted-by":"crossref","first-page":"1095","DOI":"10.1080\/14756366.2018.1477137","article-title":"Novel coumarin-6-sulfonamides as apoptotic anti-proliferative agents: synthesis, in\u00a0vitro biological evaluation, and QSAR studies","volume":"33","author":"Sabt","year":"2018","journal-title":"J.\u00a0Enzym. Inhib. Med. Chem."},{"key":"10.1016\/j.ejmech.2021.113589_bib79","article-title":"Coumarin sulfonamides and amides derivatives: design, synthesis, and antitumor activity in\u00a0vitro","volume":"26","author":"Zhang","year":"2021","journal-title":"Molecules"},{"key":"10.1016\/j.ejmech.2021.113589_bib80","doi-asserted-by":"crossref","first-page":"395","DOI":"10.1038\/s41571-020-0341-y","article-title":"Targeting apoptosis in cancer therapy","volume":"17","author":"Carneiro","year":"2020","journal-title":"Nat. Rev. Clin. Oncol."},{"key":"10.1016\/j.ejmech.2021.113589_bib81","doi-asserted-by":"crossref","first-page":"4363","DOI":"10.1021\/ol701950d","article-title":"\u03b4-Sultone formation through Rh-catalyzed C-H insertion","volume":"9","author":"Wolckenhauer","year":"2007","journal-title":"Org. Lett."},{"key":"10.1016\/j.ejmech.2021.113589_bib82","doi-asserted-by":"crossref","first-page":"3467","DOI":"10.1002\/adsc.201100473","article-title":"Metal-free, radical addition to alkenes via desulfitative chlorine atom transfer","volume":"353","author":"Cao","year":"2011","journal-title":"Adv. Synth. Catal."},{"key":"10.1016\/j.ejmech.2021.113589_bib83","doi-asserted-by":"crossref","first-page":"6539","DOI":"10.1021\/jm060967z","article-title":"A\u00a0novel class of carbonic anhydrase inhibitors: glycoconjugate benzene sulfonamides prepared by \u201cclick-tailing","volume":"49","author":"Wilkinson","year":"2006","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.ejmech.2021.113589_bib84","doi-asserted-by":"crossref","first-page":"3277","DOI":"10.2174\/138161210793429869","article-title":"Carbonic anhydrase inhibitors developed through 'click tailing","volume":"16","author":"Lopez","year":"2010","journal-title":"Curr. Pharmaceut. Des."},{"key":"10.1016\/j.ejmech.2021.113589_bib85","doi-asserted-by":"crossref","first-page":"1651","DOI":"10.1021\/jm061320h","article-title":"Carbonic anhydrase inhibitors: inhibition of isozymes I, II, and IX with triazole-linked O-glycosides of benzene sulfonamides","volume":"50","author":"Wilkinson","year":"2007","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.ejmech.2021.113589_bib86","doi-asserted-by":"crossref","first-page":"927","DOI":"10.1021\/ml500196t","article-title":"Carbonic anhydrase inhibition with benzenesulfonamides and tetrafluorobenzenesulfonamides obtained via click chemistry","volume":"5","author":"Pala","year":"2014","journal-title":"ACS Med. Chem. Lett."}],"updated-by":[{"DOI":"10.1016\/j.ejmech.2021.113788","type":"erratum","label":"Erratum","source":"publisher","updated":{"date-parts":[[2021,12,5]],"date-time":"2021-12-05T00:00:00Z","timestamp":1638662400000}}],"container-title":["European Journal of Medicinal Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0223523421004384?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0223523421004384?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2023,1,14]],"date-time":"2023-01-14T06:15:33Z","timestamp":1673676933000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0223523421004384"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,10]]},"references-count":83,"alternative-id":["S0223523421004384"],"URL":"https:\/\/doi.org\/10.1016\/j.ejmech.2021.113589","relation":{"erratum":[{"id-type":"doi","id":"10.1016\/j.ejmech.2021.113788","asserted-by":"object"}]},"ISSN":["0223-5234"],"issn-type":[{"value":"0223-5234","type":"print"}],"subject":[],"published":{"date-parts":[[2021,10]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Investigation of 3-sulfamoyl coumarins against cancer-related IX and XII isoforms of human carbonic anhydrase as well as cancer cells leads to the discovery of 2-oxo-2H-benzo[h]chromene-3-sulfonamide \u2013 A new caspase-activating proapoptotic agent","name":"articletitle","label":"Article Title"},{"value":"European Journal of Medicinal Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.ejmech.2021.113589","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2021 Elsevier Masson SAS. All rights reserved.","name":"copyright","label":"Copyright"}],"article-number":"113589"}}