{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,3]],"date-time":"2026-08-03T05:00:29Z","timestamp":1785733229848,"version":"3.56.0"},"reference-count":36,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2020,11,1]],"date-time":"2020-11-01T00:00:00Z","timestamp":1604188800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,11,1]],"date-time":"2020-11-01T00:00:00Z","timestamp":1604188800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2020,11,1]],"date-time":"2020-11-01T00:00:00Z","timestamp":1604188800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2020,11,1]],"date-time":"2020-11-01T00:00:00Z","timestamp":1604188800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2020,11,1]],"date-time":"2020-11-01T00:00:00Z","timestamp":1604188800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2020,11,1]],"date-time":"2020-11-01T00:00:00Z","timestamp":1604188800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2020,11,1]],"date-time":"2020-11-01T00:00:00Z","timestamp":1604188800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Bioorganic Chemistry"],"published-print":{"date-parts":[[2020,11]]},"DOI":"10.1016\/j.bioorg.2020.104272","type":"journal-article","created":{"date-parts":[[2020,9,8]],"date-time":"2020-09-08T11:14:50Z","timestamp":1599563690000},"page":"104272","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":43,"special_numbering":"C","title":["Synthesis and biological evaluation of some coumarin hybrids as selective carbonic anhydrase IX and XII inhibitors"],"prefix":"10.1016","volume":"104","author":[{"given":"Pavitra S.","family":"Thacker","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nerella","family":"Sridhar Goud","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Omkar S.","family":"Argulwar","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jyothsna","family":"Soman","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andrea","family":"Angeli","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mallika","family":"Alvala","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mohammed","family":"Arifuddin","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Claudiu T.","family":"Supuran","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.bioorg.2020.104272_b0005","doi-asserted-by":"crossref","first-page":"325","DOI":"10.3109\/14756366.2014.910202","article-title":"An overview of the alpha-, beta- and gamma-carbonic anhydrases from Bacteria: can bacterial carbonic anhydrases shed new light on evolution of bacteria?","volume":"30","author":"Capasso","year":"2015","journal-title":"J. Enzyme. Inhib. Med. Chem."},{"key":"10.1016\/j.bioorg.2020.104272_b0010","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1080\/14756366.2016.1225046","article-title":"Insights into the role of reactive sulfhydryl groups of Carbonic Anhydrase III and VII during oxidative damage","volume":"32","author":"Monti","year":"2017","journal-title":"J. Enzyme. Inhib. Med. Chem."},{"key":"10.1016\/j.bioorg.2020.104272_b0015","doi-asserted-by":"crossref","first-page":"485","DOI":"10.1080\/14756366.2018.1428572","article-title":"Carbon-versus sulphur-based zinc binding groups for carbonic anhydrase inhibitors?","volume":"33","author":"Supuran","year":"2018","journal-title":"J. Enzyme. Inhib. Med. Chem."},{"key":"10.1016\/j.bioorg.2020.104272_b0020","doi-asserted-by":"crossref","first-page":"4421","DOI":"10.1021\/cr200176r","article-title":"Multiple binding modes of inhibitors to carbonic anhydrases: how to design specific drugs targeting 15 different isoforms?","volume":"112","author":"Alterio","year":"2012","journal-title":"Chem. Rev."},{"key":"10.1016\/j.bioorg.2020.104272_b0025","first-page":"1","article-title":"Exploring the multiple binding modes of inhibitors to carbonic anhydrases for novel drug discovery [published online ahead of print, 2020 Mar 25]","author":"Supuran","year":"2020","journal-title":"Expert. Opin. Drug. Discov."},{"key":"10.1016\/j.bioorg.2020.104272_b0030","doi-asserted-by":"crossref","first-page":"297","DOI":"10.1080\/17425255.2020.1743679","article-title":"An update on drug interaction considerations in the therapeutic use of carbonic anhydrase inhibitors","volume":"16","author":"Supuran","year":"2020","journal-title":"Expert. Opin. Drug. Metab. Toxicol."},{"key":"10.1016\/j.bioorg.2020.104272_b0035","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1080\/14756366.2018.1532419","article-title":"The carbonic anhydrase IX inhibitor SLC-0111 sensitises cancer cells to conventional chemotherapy","volume":"34","author":"Andreucci","year":"2019","journal-title":"J. Enzyme. Inhib. Med. Chem."},{"key":"10.1016\/j.bioorg.2020.104272_b0040","doi-asserted-by":"crossref","first-page":"255","DOI":"10.1080\/14756366.2019.1697251","article-title":"Carbonic anhydrase IX as a novel candidate in liquid biopsy","volume":"35","author":"OzensoyGuler","year":"2020","journal-title":"J. Enzyme. Inhib. Med. Chem."},{"key":"10.1016\/j.bioorg.2020.104272_b0045","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.bioorg.2020.104272_b0050","doi-asserted-by":"crossref","first-page":"1150","DOI":"10.3390\/ijms17071150","article-title":"Non-classical inhibition of carbonic anhydrase","volume":"17","author":"Lomelino","year":"2016","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.bioorg.2020.104272_b0055","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. Enzyme. Inhib. Med. Chem."},{"key":"10.1016\/j.bioorg.2020.104272_b0060","doi-asserted-by":"crossref","DOI":"10.1016\/j.bioorg.2020.103739","article-title":"Design, synthesis and biological evaluation of coumarin linked 1,2,4-oxadiazoles as selective carbonic anhydrase IX and XII inhibitors","volume":"98","author":"Thacker","year":"2020","journal-title":"Bioorg. Chem."},{"key":"10.1016\/j.bioorg.2020.104272_b0065","doi-asserted-by":"crossref","first-page":"386","DOI":"10.1016\/j.bioorg.2019.02.004","article-title":"Design, synthesis and biological evaluation of coumarin-3-carboxamides as selective carbonic anhydrase IX and XII inhibitors","volume":"86","author":"Thacker","year":"2019","journal-title":"Bioorg. Chem."},{"key":"10.1016\/j.bioorg.2020.104272_b0070","doi-asserted-by":"crossref","first-page":"765","DOI":"10.1016\/j.bioorg.2019.04.004","article-title":"Synthesis and biological evaluation of coumarin-1,3,4-oxadiazole hybrids as selective carbonic anhydrase IX and XII inhibitors","volume":"87","author":"Narella","year":"2019","journal-title":"Bioorg. Chem."},{"key":"10.1016\/j.bioorg.2020.104272_b0075","doi-asserted-by":"crossref","first-page":"276","DOI":"10.1016\/j.ejmech.2017.11.061","article-title":"Inhibitory effects and structural insights for a novel series of coumarin-based compounds that selectively target human CA IX and CA XII carbonic anhydrases","volume":"143","author":"De Luca","year":"2018","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.bioorg.2020.104272_b0080","doi-asserted-by":"crossref","first-page":"170","DOI":"10.1016\/j.ejmech.2016.04.077","article-title":"The therapeutic voyage of pyrazole and its analogs: a review","volume":"120","author":"Khan","year":"2016","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.bioorg.2020.104272_h0085","doi-asserted-by":"crossref","first-page":"583","DOI":"10.1016\/j.ejmech.2015.09.021","article-title":"Isatin-pyrazolebenzenesulfonamide hybrids potently inhibit tumor-associated carbonic anhydrase isoforms IX and XII","volume":"103","author":"Ibrahim","year":"2015","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.bioorg.2020.104272_h0090","doi-asserted-by":"crossref","first-page":"4649","DOI":"10.1016\/j.bmc.2015.05.052","article-title":"5-Aryl-1H-pyrazole-3-carboxylic acids as selective inhibitors of human carbonic anhydrases IX and XII","volume":"23","author":"Cvijetic","year":"2015","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.bioorg.2020.104272_h0095","doi-asserted-by":"crossref","first-page":"284","DOI":"10.1016\/j.ejmech.2014.02.023","article-title":"4-Functionalized 1,3-diarylpyrazoles bearing benzenesulfonamide moiety as selective potent inhibitors of the tumor associated carbonic anhydrase isoforms IX and XII","volume":"76","author":"Khloya","year":"2014","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.bioorg.2020.104272_h0100","doi-asserted-by":"crossref","unstructured":"C. Yamali, H. I. Gul, A. Ece, S. Bua S, A. Angeli A, H. Sakagami H, E. Sahin, C. T. Supuran, Synthesis, biological evaluation and in silico modelling studies of 1,3,5-trisubstituted pyrazoles carrying benzenesulfonamide as potential anticancer agents and selective cancer-associated hCA IX isoenzyme inhibitors,Bioorg. Chem. 92 (2019) 103222.","DOI":"10.1016\/j.bioorg.2019.103222"},{"key":"10.1016\/j.bioorg.2020.104272_b0095","doi-asserted-by":"crossref","unstructured":"A. C. Tripathi, S. J. Gupta, G. N. Fatima P. K. Sonar, A. Verma, S. K. Saraf, 4-Thiazolidinones: the advances continue,Eur. J. Med. Chem. 72 (2014) 52\u201377.","DOI":"10.1016\/j.ejmech.2013.11.017"},{"key":"10.1016\/j.bioorg.2020.104272_h0110","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1016\/j.bioorg.2018.01.031","article-title":"Synthesis, biological evaluation and computational studies of novel iminothiazolidinonebenzenesulfonamides as potent carbonic anhydrase II and IX inhibitors","volume":"77","author":"Mahmood","year":"2018","journal-title":"Bioorg. Chem."},{"key":"10.1016\/j.bioorg.2020.104272_h0115","doi-asserted-by":"crossref","first-page":"1299","DOI":"10.1080\/14756366.2018.1499628","article-title":"Novel thiazolidinone-containing compounds, without the well-known sulphonamide zinc-binding group acting as human carbonic anhydrase IX inhibitors","volume":"33","author":"Guzel-Akdemir","year":"2018","journal-title":"J. Enzyme. Inhib. Med. Chem."},{"key":"10.1016\/j.bioorg.2020.104272_h0120","doi-asserted-by":"crossref","unstructured":"Z. P. Zhang, Z. F. Yin, J. Y. Li, Z. P. Wang, Q. J. Wu, J. Wang, Y. Liu Y, M. S. Cheng, Synthesis, Molecular Docking Analysis, and Carbonic Anhydrase Inhibitory Evaluations of Benzenesulfonamide Derivatives Containing Thiazolidinone,Molecules.24 (2019) 2418.","DOI":"10.3390\/molecules24132418"},{"key":"10.1016\/j.bioorg.2020.104272_b0105","doi-asserted-by":"crossref","first-page":"30","DOI":"10.1016\/j.bioorg.2017.01.010","article-title":"Medicinal attributes of 1,2,3-triazoles: Current developments","volume":"71","author":"Dheer","year":"2017","journal-title":"Bioorg. Chem."},{"key":"10.1016\/j.bioorg.2020.104272_h0130","doi-asserted-by":"crossref","unstructured":"P. Singh, B. Swain, P. S. Thacker, D. K. Sigalapalli, P. Y. Purnachander, A. Angeli A, C. T. Supuran, M. Arifuddin, Synthesis and carbonic anhydrase inhibition studies of sulfonamide based indole-1,2,3-triazole chalcone hybrids,Bioorg. Chem. 99 (2020)103839.","DOI":"10.1016\/j.bioorg.2020.103839"},{"key":"10.1016\/j.bioorg.2020.104272_h0135","doi-asserted-by":"crossref","first-page":"1256","DOI":"10.1016\/j.bmcl.2014.01.076","article-title":"6-Triazolyl-substituted sulfocoumarins are potent, selective inhibitors of the tumor-associated carbonic anhydrases IX and XII","volume":"24","author":"Grandane","year":"2014","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/j.bioorg.2020.104272_h0140","doi-asserted-by":"crossref","first-page":"5130","DOI":"10.1016\/j.bmc.2013.06.041","article-title":"5-Substituted-(1,2,3-triazol-4-yl)thiophene-2-sulfonamides strongly inhibit human carbonic anhydrases I, II, IX and XII: solution and X-ray crystallographic studies","volume":"21","author":"Leitans","year":"2013","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.bioorg.2020.104272_b0115","doi-asserted-by":"crossref","unstructured":"D. Srikrishna P. K. Dubey, Synthesis of novel substituted 3-(4-((1H-benzo[d]imidazol-2-ylthio)methyl)-1-phenyl-1H-pyrazol-3-yl)-2H-chromen-2-ones: various approaches,Res. Chem. Intermed.44 (2018) 4455\u20134468.","DOI":"10.1007\/s11164-018-3397-x"},{"key":"10.1016\/j.bioorg.2020.104272_b0120","doi-asserted-by":"crossref","first-page":"2463","DOI":"10.1016\/j.tetlet.2014.03.007","article-title":"Silica gel promoted environment friendly synthesis of 2,3-disubstituted 4-thiazolidinones","volume":"55","author":"Thakare","year":"2014","journal-title":"Tetrahydron. Lett."},{"key":"10.1016\/j.bioorg.2020.104272_b0125","doi-asserted-by":"crossref","DOI":"10.1016\/j.bioorg.2020.103663","article-title":"Synthesis, 18F-radiolabeling and apoptosis inducing studies of novel 4, 7-disubstituted coumarins","volume":"97","author":"Goud","year":"2020","journal-title":"Bioorg. Chem."},{"key":"10.1016\/j.bioorg.2020.104272_b0130","doi-asserted-by":"crossref","unstructured":"R. G. Khalifah, The carbon dioxide hydration activity of carbonic anhydrase. I. Stop-flow kinetic studies on the native human isoenzymes B and C, J. Biol. Chem. 246 (1971) 2561-2573.","DOI":"10.1016\/S0021-9258(18)62326-9"},{"key":"10.1016\/j.bioorg.2020.104272_b0135","doi-asserted-by":"crossref","first-page":"1172","DOI":"10.1080\/14756366.2019.1626376","article-title":"Synthesis and biological evaluation of novel 8-substituted quinoline-2-carboxamides as carbonic anhydrase inhibitors","volume":"34","author":"Thacker","year":"2019","journal-title":"J. Enzyme. Inhib. Med. Chem."},{"key":"10.1016\/j.bioorg.2020.104272_b0140","doi-asserted-by":"crossref","first-page":"521","DOI":"10.1016\/j.ejmech.2017.01.017","article-title":"Novel indolin-2-one-based sulfonamides as carbonic anhydrase inhibitors: Synthesis, in vitro biological evaluation against carbonic anhydrases isoforms I, II, IV and VII and molecular docking studies","volume":"127","author":"Eldehna","year":"2017","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.bioorg.2020.104272_b0145","doi-asserted-by":"crossref","first-page":"10692","DOI":"10.1021\/acs.jmedchem.6b01389","article-title":"Benzenesulfonamides incorporating flexible triazole moieties are highly effective carbonic anhydrase inhibitors: synthesis and kinetic, crystallographic, computational, and intraocular pressure lowering investigations","volume":"59","author":"Nocentini","year":"2016","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.bioorg.2020.104272_b0150","doi-asserted-by":"crossref","DOI":"10.1016\/j.bioorg.2019.103544","article-title":"Benzimidazole derivatives as potent and isoform selective tumor-associated carbonic anhydrase IX\/XII inhibitors","volume":"95","author":"Uslu","year":"2020","journal-title":"Bioorg. Chem."}],"container-title":["Bioorganic Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0045206820315704?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0045206820315704?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,11,19]],"date-time":"2025-11-19T15:42:23Z","timestamp":1763566943000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0045206820315704"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,11]]},"references-count":36,"alternative-id":["S0045206820315704"],"URL":"https:\/\/doi.org\/10.1016\/j.bioorg.2020.104272","relation":{},"ISSN":["0045-2068"],"issn-type":[{"value":"0045-2068","type":"print"}],"subject":[],"published":{"date-parts":[[2020,11]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Synthesis and biological evaluation of some coumarin hybrids as selective carbonic anhydrase IX and XII inhibitors","name":"articletitle","label":"Article Title"},{"value":"Bioorganic Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bioorg.2020.104272","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2020 Elsevier Inc. All rights reserved.","name":"copyright","label":"Copyright"}],"article-number":"104272"}}