{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,11]],"date-time":"2026-10-11T16:07:13Z","timestamp":1791734833423,"version":"4.3.4"},"reference-count":53,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2017,5,1]],"date-time":"2017-05-01T00:00:00Z","timestamp":1493596800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["CA165284"],"award-info":[{"award-number":["CA165284"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["CA165284-03S1"],"award-info":[{"award-number":["CA165284-03S1"]}],"id":[{"id":"10.13039\/100000002","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":[[2017,5]]},"DOI":"10.1016\/j.ejmech.2017.03.026","type":"journal-article","created":{"date-parts":[[2017,3,19]],"date-time":"2017-03-19T06:15:33Z","timestamp":1489904133000},"page":"184-191","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":71,"special_numbering":"C","title":["Structure activity study of carbonic anhydrase IX: Selective inhibition with ureido-substituted benzenesulfonamides"],"prefix":"10.1016","volume":"132","author":[{"given":"Mam Y.","family":"Mboge","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Brian P.","family":"Mahon","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nicole","family":"Lamas","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lillien","family":"Socorro","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fabrizio","family":"Carta","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Claudiu T.","family":"Supuran","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Susan C.","family":"Frost","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2792-935X","authenticated-orcid":false,"given":"Robert","family":"McKenna","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.ejmech.2017.03.026_bib1a","doi-asserted-by":"crossref","first-page":"767","DOI":"10.1097\/GIM.0b013e31818b0d9b","article-title":"Is cancer a disease of abnormal cellular metabolism? New angles on an old idea","volume":"10","author":"DeBerardinis","year":"2008","journal-title":"Genet. Med."},{"key":"10.1016\/j.ejmech.2017.03.026_bib1b","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1016\/j.cmet.2007.10.002","article-title":"The biology of cancer: metabolic reprogramming fuels cell growth and proliferation","volume":"7","author":"DeBerardinis","year":"2008","journal-title":"Cell Metab."},{"key":"10.1016\/j.ejmech.2017.03.026_bib1c","doi-asserted-by":"crossref","first-page":"54","DOI":"10.1016\/j.gde.2008.02.003","article-title":"Brick by brick: metabolism and tumor cell growth","volume":"18","author":"Deberardinis","year":"2008","journal-title":"Curr. Opin. Genet. Dev."},{"key":"10.1016\/j.ejmech.2017.03.026_bib1d","doi-asserted-by":"crossref","first-page":"e0120958","DOI":"10.1371\/journal.pone.0120958","article-title":"Intermittent hypoxia selects for genotypes and phenotypes that increase survival, invasion, and therapy resistance","volume":"10","author":"Verduzco","year":"2015","journal-title":"PLoS One"},{"key":"10.1016\/j.ejmech.2017.03.026_bib2a","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.\u00a0Natl. Cancer Inst."},{"key":"10.1016\/j.ejmech.2017.03.026_bib2b","doi-asserted-by":"crossref","first-page":"320","DOI":"10.3390\/cancers5020320","article-title":"Hypoxia-inducible factors: mediators of cancer progression; prognostic and therapeutic targets in soft tissue sarcomas","volume":"5","author":"Sadri","year":"2013","journal-title":"Cancers (Basel)"},{"key":"10.1016\/j.ejmech.2017.03.026_bib2c","doi-asserted-by":"crossref","first-page":"1686","DOI":"10.1515\/bchm2.1967.348.1.1686","article-title":"On growth of cancer cells in media in which glucose is replaced by galactose","volume":"348","author":"Warburg","year":"1967","journal-title":"Hoppe Seylers Z Physiol. Chem."},{"key":"10.1016\/j.ejmech.2017.03.026_bib2d","doi-asserted-by":"crossref","first-page":"1313","DOI":"10.1126\/science.6765631","article-title":"Warburg effect revisited","volume":"213","author":"Racker","year":"1981","journal-title":"Science"},{"key":"10.1016\/j.ejmech.2017.03.026_bib3a","first-page":"7075","article-title":"Hypoxia-inducible expression of tumor-associated carbonic anhydrases","volume":"60","author":"Wykoff","year":"2000","journal-title":"Cancer Res."},{"key":"10.1016\/j.ejmech.2017.03.026_bib3b","doi-asserted-by":"crossref","first-page":"6297","DOI":"10.1038\/sj.onc.1204012","article-title":"Identification of novel hypoxia dependent and independent target genes of the von Hippel-Lindau (VHL) tumour suppressor by mRNA differential expression profiling","volume":"19","author":"Wykoff","year":"2000","journal-title":"Oncogene"},{"key":"10.1016\/j.ejmech.2017.03.026_bib4a","doi-asserted-by":"crossref","first-page":"84","DOI":"10.18632\/oncotarget.422","article-title":"Recent developments in targeting carbonic anhydrase IX for cancer therapeutics","volume":"3","author":"McDonald","year":"2012","journal-title":"Oncotarget"},{"key":"10.1016\/j.ejmech.2017.03.026_bib4b","doi-asserted-by":"crossref","first-page":"358","DOI":"10.1158\/0008-5472.CAN-08-2470","article-title":"Hypoxia-inducible carbonic anhydrase IX and XII promote tumor cell growth by counteracting ccidosis through the regulation of the intracellular pH","volume":"69","author":"Chiche","year":"2009","journal-title":"Cancer Res."},{"key":"10.1016\/j.ejmech.2017.03.026_bib5","doi-asserted-by":"crossref","first-page":"771","DOI":"10.1111\/j.1582-4934.2009.00994.x","article-title":"Tumour hypoxia induces a metabolic shift causing acidosis: a common feature in cancer","volume":"14","author":"Chiche","year":"2010","journal-title":"J.\u00a0Cell Mol. Med."},{"key":"10.1016\/j.ejmech.2017.03.026_bib6a","doi-asserted-by":"crossref","first-page":"30","DOI":"10.1021\/ar00145a005","article-title":"The catalytic mechanism of carbonic anhydrase - implication of a rate limiting protolysis of water","volume":"21","author":"Silverman","year":"1988","journal-title":"Acc. Chem. Res."},{"key":"10.1016\/j.ejmech.2017.03.026_bib6b","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.2017.03.026_bib7a","doi-asserted-by":"crossref","first-page":"4757","DOI":"10.1200\/JCO.2007.12.1087","article-title":"Carbonic anhydrase IX is not an independent predictor of outcome for patients with clear cell renal cell carcinoma","volume":"25","author":"Leibovich","year":"2007","journal-title":"J.\u00a0Clin. Oncol."},{"key":"10.1016\/j.ejmech.2017.03.026_bib7b","doi-asserted-by":"crossref","first-page":"497","DOI":"10.1177\/002215549804600409","article-title":"Immunohistochemistry of carbonic anhydrase isozyme IX (MN\/CA IX) in human gut reveals polarized expression in the epithelial cells with the highest proliferative capacity","volume":"46","author":"Saarnio","year":"1998","journal-title":"J.\u00a0Histochem Cytochem"},{"key":"10.1016\/j.ejmech.2017.03.026_bib7c","doi-asserted-by":"crossref","first-page":"905","DOI":"10.1016\/S0002-9440(10)64038-2","article-title":"Expression of hypoxia-inducible cell-surface transmembrane carbonic anhydrases in human cancer","volume":"158","author":"Ivanov","year":"2001","journal-title":"Am. J. Pathol."},{"key":"10.1016\/j.ejmech.2017.03.026_bib8","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1186\/1471-2407-5-41","article-title":"Expression of a novel carbonic anhydrase, CA XIII, in normal and neoplastic colorectal mucosa","volume":"5","author":"Kummola","year":"2005","journal-title":"BMC Cancer"},{"key":"10.1016\/j.ejmech.2017.03.026_bib9a","doi-asserted-by":"crossref","first-page":"16233","DOI":"10.1073\/pnas.0908301106","article-title":"Crystal structure of the catalytic domain of the tumor-associated human carbonic anhydrase IX","volume":"106","author":"Alterio","year":"2009","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.ejmech.2017.03.026_bib9b","doi-asserted-by":"crossref","first-page":"404","DOI":"10.1016\/j.bbapap.2009.07.027","article-title":"Carbonic anhydrase IX: biochemical and crystallographic characterization of a novel antitumor target","volume":"1804","author":"De Simone","year":"2010","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.ejmech.2017.03.026_bib9c","doi-asserted-by":"crossref","first-page":"367","DOI":"10.1016\/j.radonc.2007.04.018","article-title":"Imaging the hypoxia surrogate marker CA IX requires expression and catalytic activity for binding fluorescent sulfonamide inhibitors","volume":"83","author":"Dubois","year":"2007","journal-title":"Radiother. Oncol."},{"key":"10.1016\/j.ejmech.2017.03.026_bib9d","doi-asserted-by":"crossref","first-page":"523","DOI":"10.1016\/j.radonc.2013.06.018","article-title":"Targeting carbonic anhydrase IX by nitroimidazole based sulfamides enhances the therapeutic effect of tumor irradiation: a new concept of dual targeting drugs","volume":"108","author":"Dubois","year":"2013","journal-title":"Radiother Oncol"},{"key":"10.1016\/j.ejmech.2017.03.026_bib9e","doi-asserted-by":"crossref","first-page":"168","DOI":"10.1038\/nrd2467","article-title":"Carbonic anhydrase: novel therapeutic applications for inhibitors and activators","volume":"7","author":"Supuran","year":"2008","journal-title":"Nat. Rev. Drug Discov."},{"key":"10.1016\/j.ejmech.2017.03.026_bib10a","doi-asserted-by":"crossref","first-page":"849","DOI":"10.1016\/j.bmc.2014.12.030","article-title":"Saccharin: a lead compound for structure-based drug design of carbonic anhydrase IX inhibitors","volume":"23","author":"Mahon","year":"2015","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.ejmech.2017.03.026_bib10b","doi-asserted-by":"crossref","first-page":"24856","DOI":"10.18632\/oncotarget.4498","article-title":"Evaluation of carbonic anhydrase IX as a therapeutic target for inhibition of breast cancer invasion and metastasis using a series of in\u00a0vitro breast cancer models","volume":"6","author":"Ward","year":"2015","journal-title":"Oncotarget"},{"key":"10.1016\/j.ejmech.2017.03.026_bib11a","doi-asserted-by":"crossref","first-page":"5210","DOI":"10.1038\/onc.2012.550","article-title":"Targeting carbonic anhydrase IX depletes breast cancer stem cells within the hypoxic niche","volume":"32","author":"Lock","year":"2013","journal-title":"Oncogene"},{"key":"10.1016\/j.ejmech.2017.03.026_bib11b","doi-asserted-by":"crossref","first-page":"3364","DOI":"10.1158\/0008-5472.CAN-10-4261","article-title":"Targeting tumor hypoxia: suppression of breast tumor growth and metastasis by novel carbonic anhydrase IX inhibitors","volume":"71","author":"Lou","year":"2011","journal-title":"Cancer Res."},{"key":"10.1016\/j.ejmech.2017.03.026_bib11c","doi-asserted-by":"crossref","first-page":"1896","DOI":"10.1021\/jm101541x","article-title":"Ureido-substituted benzenesulfonamides potently inhibit carbonic anhydrase IX and show antimetastatic activity in a model of breast cancer metastasis","volume":"54","author":"Pacchiano","year":"2011","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.ejmech.2017.03.026_bib11d","doi-asserted-by":"crossref","first-page":"591","DOI":"10.1517\/17460441.2015.1038235","article-title":"Designing carbonic anhydrase inhibitors for the treatment of breast cancer","volume":"10","author":"Supuran","year":"2015","journal-title":"Expert Opin. Drug Discov."},{"key":"10.1016\/j.ejmech.2017.03.026_bib11e","doi-asserted-by":"crossref","first-page":"1407","DOI":"10.4155\/fmc.15.71","article-title":"Carbonic anhydrase IX inhibitors in cancer therapy: an update","volume":"7","author":"Supuran","year":"2015","journal-title":"Future Med. Chem."},{"key":"10.1016\/j.ejmech.2017.03.026_bib11f","doi-asserted-by":"crossref","first-page":"598","DOI":"10.1016\/j.ejcb.2010.03.004","article-title":"Carbonic anhydrase XII promotes invasion and migration ability of MDA MB231 breast cancer through the p38 MAPK signaling pathway","volume":"89","author":"Hsieh","year":"2010","journal-title":"Eur. J. Cell Biol."},{"key":"10.1016\/j.ejmech.2017.03.026_bib12a","doi-asserted-by":"crossref","first-page":"855","DOI":"10.2174\/156802607780636726","article-title":"Carbonic anhydrase inhibitors as anticonvulsant agents","volume":"7","author":"Thiry","year":"2007","journal-title":"Curr. Top. Med. Chem."},{"key":"10.1016\/j.ejmech.2017.03.026_bib12b","doi-asserted-by":"crossref","first-page":"603","DOI":"10.2174\/138161208783877884","article-title":"Carbonic anhydrases\u2013an overview","volume":"14","author":"Supuran","year":"2008","journal-title":"Curr. Pharm. Des."},{"key":"10.1016\/j.ejmech.2017.03.026_bib12c","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.\u00a0Enzyme Inhib. Med. Chem."},{"key":"10.1016\/j.ejmech.2017.03.026_bib13","doi-asserted-by":"crossref","first-page":"2930","DOI":"10.1021\/bi062066y","article-title":"Atomic crystal and molecular dynamics simulation structures of human carbonic anhydrase II: insights into the proton transfer mechanism","volume":"46","author":"Fisher","year":"2007","journal-title":"Biochemistry"},{"key":"10.1016\/j.ejmech.2017.03.026_bib14a","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.2017.03.026_bib14b","doi-asserted-by":"crossref","first-page":"1526","DOI":"10.1016\/j.bmc.2012.08.019","article-title":"Insights towards sulfonamide drug specificity in alpha-carbonic anhydrases","volume":"21","author":"Aggarwal","year":"2013","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.ejmech.2017.03.026_bib15","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.\u00a0Enzyme Inhib. Med. Chem."},{"key":"10.1016\/j.ejmech.2017.03.026_bib16","doi-asserted-by":"crossref","first-page":"8635","DOI":"10.1021\/jm5012935","article-title":"Structural insights into carbonic anhydrase IX isoform specificity of carbohydrate-based sulfamates","volume":"57","author":"Moeker","year":"2014","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.ejmech.2017.03.026_bib17","doi-asserted-by":"crossref","first-page":"8371","DOI":"10.1039\/c0cc02707c","article-title":"Selective hydrophobic pocket binding observed within the carbonic anhydrase II active site accommodate different 4-substituted-ureido-benzenesulfonamides and correlate to inhibitor potency","volume":"46","author":"Pacchiano","year":"2010","journal-title":"Chem. Commun. (Camb)"},{"key":"10.1016\/j.ejmech.2017.03.026_bib18a","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1021\/bi301099k","article-title":"Water networks in fast proton transfer during catalysis by human carbonic anhydrase II","volume":"52","author":"Mikulski","year":"2013","journal-title":"Biochemistry"},{"key":"10.1016\/j.ejmech.2017.03.026_bib18b","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1021\/bi902007b","article-title":"A\u00a0short, strong hydrogen bond in the active site of human carbonic anhydrase II","volume":"49","author":"Avvaru","year":"2010","journal-title":"Biochemistry"},{"key":"10.1016\/j.ejmech.2017.03.026_bib19","doi-asserted-by":"crossref","first-page":"992","DOI":"10.1107\/S1744309109036665","article-title":"High-resolution structure of human carbonic anhydrase II complexed with acetazolamide reveals insights into inhibitor drug design","volume":"65","author":"Sippel","year":"2009","journal-title":"Acta Crystallogr. F."},{"key":"10.1016\/j.ejmech.2017.03.026_bib20","doi-asserted-by":"crossref","first-page":"774","DOI":"10.1016\/j.jmb.2007.05.022","article-title":"Inference of macromolecular assemblies from crystalline state","volume":"372","author":"Krissinel","year":"2007","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.ejmech.2017.03.026_bib21","doi-asserted-by":"crossref","first-page":"6630","DOI":"10.1021\/acs.jmedchem.5b00845","article-title":"Mapping selective inhibition of the cancer-related carbonic anhydrase IX using structure-activity relationships of glucosyl-based sulfamates","volume":"58","author":"Mahon","year":"2015","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.ejmech.2017.03.026_bib22","doi-asserted-by":"crossref","first-page":"279","DOI":"10.1016\/S0002-9440(10)65569-1","article-title":"Immunohistochemical study of colorectal tumors for expression of a novel transmembrane carbonic anhydrase, MN\/CA IX, with potential value as a marker of cell proliferation","volume":"153","author":"Saarnio","year":"1998","journal-title":"Am. J. Pathol."},{"key":"10.1016\/j.ejmech.2017.03.026_bib23a","doi-asserted-by":"crossref","first-page":"1322","DOI":"10.1021\/bi802035f","article-title":"Design of a carbonic anhydrase IX active-site mimic to screen inhibitors for possible anticancer properties","volume":"48","author":"Genis","year":"2009","journal-title":"Biochemistry"},{"key":"10.1016\/j.ejmech.2017.03.026_bib23b","doi-asserted-by":"crossref","first-page":"7210","DOI":"10.1016\/j.bmc.2013.08.033","article-title":"Structural study of interaction between brinzolamide and dorzolamide inhibition of human carbonic anhydrases","volume":"21","author":"Pinard","year":"2013","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.ejmech.2017.03.026_bib24","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1016\/S0076-6879(97)76066-X","article-title":"Processing of X-ray diffraction data collected in oscillation mode","volume":"276","author":"Otwinowski","year":"1997","journal-title":"Method Enzymol."},{"key":"10.1016\/j.ejmech.2017.03.026_bib25","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1107\/S0907444909052925","article-title":"PHENIX: a comprehensive Python-based system for macromolecular structure solution","volume":"66","author":"Adams","year":"2010","journal-title":"Acta Crystallogr. D. Biol. Crystallogr."},{"key":"10.1016\/j.ejmech.2017.03.026_bib26","doi-asserted-by":"crossref","first-page":"2126","DOI":"10.1107\/S0907444904019158","article-title":"Coot: model-building tools for molecular graphics","volume":"60","author":"Emsley","year":"2004","journal-title":"Acta Crystallogr. D. Biol. Crystallogr."},{"key":"10.1016\/j.ejmech.2017.03.026_bib27","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1107\/S0907444912000200","article-title":"Handling ligands with coot","volume":"68","author":"Debreczeni","year":"2012","journal-title":"Acta Crystallogr. D. Biol. Crystallogr."}],"container-title":["European Journal of Medicinal Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0223523417301836?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0223523417301836?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2020,2,24]],"date-time":"2020-02-24T11:33:44Z","timestamp":1582544024000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0223523417301836"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2017,5]]},"references-count":53,"alternative-id":["S0223523417301836"],"URL":"https:\/\/doi.org\/10.1016\/j.ejmech.2017.03.026","relation":{},"ISSN":["0223-5234"],"issn-type":[{"value":"0223-5234","type":"print"}],"subject":[],"published":{"date-parts":[[2017,5]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Structure activity study of carbonic anhydrase IX: Selective inhibition with ureido-substituted benzenesulfonamides","name":"articletitle","label":"Article Title"},{"value":"European Journal of Medicinal Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.ejmech.2017.03.026","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2017 Elsevier Masson SAS. All rights reserved.","name":"copyright","label":"Copyright"}]}}