{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,14]],"date-time":"2026-10-14T15:06:31Z","timestamp":1791990391564,"version":"4.4.0"},"reference-count":67,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2018,8,1]],"date-time":"2018-08-01T00:00:00Z","timestamp":1533081600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"funder":[{"DOI":"10.13039\/501100004504","name":"Research Council of Lithuania","doi-asserted-by":"publisher","award":["S-MIP-17-87"],"award-info":[{"award-number":["S-MIP-17-87"]}],"id":[{"id":"10.13039\/501100004504","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":[[2018,8]]},"DOI":"10.1016\/j.ejmech.2018.06.059","type":"journal-article","created":{"date-parts":[[2018,6,27]],"date-time":"2018-06-27T18:56:55Z","timestamp":1530125815000},"page":"61-78","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":18,"special_numbering":"C","title":["Design of two-tail compounds with rotationally fixed benzenesulfonamide ring as inhibitors of carbonic anhydrases"],"prefix":"10.1016","volume":"156","author":[{"given":"Audrius","family":"Zak\u0161auskas","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Edita","family":"\u010capkauskait\u0117","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Linas","family":"Jezep\u010dikas","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vaida","family":"Linkuvien\u0117","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Migl\u0117","family":"Ki\u0161onait\u0117","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alexey","family":"Smirnov","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Elena","family":"Manakova","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Saulius","family":"Gra\u017eulis","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6178-6276","authenticated-orcid":false,"given":"Daumantas","family":"Matulis","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.ejmech.2018.06.059_bib1","doi-asserted-by":"crossref","first-page":"946","DOI":"10.1021\/cr050262p","article-title":"Carbonic anhydrase as a model for biophysical and physical-organic studies of proteins and Protein\u2212Ligand binding","volume":"108","author":"Krishnamurthy","year":"2008","journal-title":"Chem. Rev."},{"key":"10.1016\/j.ejmech.2018.06.059_bib2","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1038\/sj.ki.5002020","article-title":"The role of carbonic anhydrases in renal physiology","volume":"71","author":"Purkerson","year":"2007","journal-title":"Kidney Int."},{"key":"10.1016\/j.ejmech.2018.06.059_bib3","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. Pharmaceut. Des."},{"key":"10.1016\/j.ejmech.2018.06.059_bib4","doi-asserted-by":"crossref","first-page":"267","DOI":"10.3109\/14756366.2012.737323","article-title":"Structural annotation of human carbonic anhydrases","volume":"28","author":"Aggarwal","year":"2013","journal-title":"J.\u00a0Enzym. Inhib. Med. Chem."},{"key":"10.1016\/j.ejmech.2018.06.059_bib5","doi-asserted-by":"crossref","first-page":"903","DOI":"10.1517\/13543776.2012.707646","article-title":"Update on carbonic anhydrase inhibitors: a patent review (2008-2011)","volume":"22","author":"Aggarwal","year":"2012","journal-title":"Expert Opin. Ther. Pat."},{"key":"10.1016\/j.ejmech.2018.06.059_bib6","doi-asserted-by":"crossref","first-page":"4336","DOI":"10.1016\/j.bmc.2007.04.020","article-title":"Carbonic anhydrases as targets for medicinal chemistry","volume":"15","author":"Supuran","year":"2007","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.ejmech.2018.06.059_bib7","doi-asserted-by":"crossref","first-page":"3977","DOI":"10.1021\/jm200209n","article-title":"Anticonvulsant 4-aminobenzenesulfonamide derivatives with branched-alkylamide moieties: X-ray crystallography and inhibition studies of human carbonic anhydrase isoforms I, ii, vii, and XIV","volume":"54","author":"Hen","year":"2011","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.ejmech.2018.06.059_bib8","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1038\/nm1534","article-title":"Extracellular carbonic anhydrase mediates hemorrhagic retinal and cerebral vascular permeability through prekallikrein activation","volume":"13","author":"Gao","year":"2007","journal-title":"Nat. Med."},{"key":"10.1016\/j.ejmech.2018.06.059_bib9","doi-asserted-by":"crossref","first-page":"725","DOI":"10.1517\/13543776.2013.790957","article-title":"Antiobesity carbonic anhydrase inhibitors: a literature and patent review","volume":"23","author":"Scozzafava","year":"2013","journal-title":"Expert Opin. Ther. Pat."},{"key":"10.1016\/j.ejmech.2018.06.059_bib10","doi-asserted-by":"crossref","first-page":"655","DOI":"10.2174\/138161208783877820","article-title":"Are carbonic anhydrase inhibitors suitable for obtaining antiobesity drugs?","volume":"14","author":"De Simone","year":"2008","journal-title":"Curr. Pharmaceut. Des."},{"key":"10.1016\/j.ejmech.2018.06.059_bib11","doi-asserted-by":"crossref","first-page":"2719","DOI":"10.1074\/jbc.M308984200","article-title":"Characterization of CA XIII, a novel member of the carbonic anhydrase isozyme family","volume":"279","author":"Lehtonen","year":"2004","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.ejmech.2018.06.059_bib12","doi-asserted-by":"crossref","first-page":"1516","DOI":"10.2174\/092986710790979999","article-title":"Drug design studies of the novel antitumor targets carbonic anhydrase IX and XII","volume":"17","author":"Ozensoy Guler","year":"2010","journal-title":"Curr. Med. Chem."},{"key":"10.1016\/j.ejmech.2018.06.059_bib13","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.ejmech.2018.06.059_bib14","series-title":"Carbonic Anhydrase: its Inhibitors and Activators","author":"Supuran","year":"2004"},{"key":"10.1016\/j.ejmech.2018.06.059_bib15","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1080\/17460441.2017.1253677","article-title":"Advances in structure-based drug discovery of carbonic anhydrase inhibitors","volume":"12","author":"Supuran","year":"2017","journal-title":"Expet Opin. Drug Discov."},{"key":"10.1016\/j.ejmech.2018.06.059_bib16","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.2018.06.059_bib17","doi-asserted-by":"crossref","first-page":"146","DOI":"10.1002\/med.10025","article-title":"Carbonic anhydrase inhibitors","volume":"23","author":"Supuran","year":"2003","journal-title":"Med. Res. Rev."},{"key":"10.1016\/j.ejmech.2018.06.059_bib18","doi-asserted-by":"crossref","first-page":"2286","DOI":"10.1021\/jm00013a004","article-title":"Secondary interactions significantly removed from the sulfonamide binding pocket of carbonic anhydrase II influence inhibitor binding constants","volume":"38","author":"Boriack","year":"1995","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.ejmech.2018.06.059_bib19","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.2018.06.059_bib20","doi-asserted-by":"crossref","first-page":"30766","DOI":"10.1074\/jbc.M805353200","article-title":"Robert McKenna, Entrapment of carbon dioxide in the active site of carbonic anhydrase II","volume":"283","author":"Domsic","year":"2008","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.ejmech.2018.06.059_bib21","doi-asserted-by":"crossref","first-page":"3011","DOI":"10.1021\/ja057257n","article-title":"Ultrahigh resolution crystal structures of human carbonic anhydrases I and ii complexed with \u201cTwo-Prong\u201d inhibitors reveal the molecular basis of high affinity","volume":"128","author":"Jude","year":"2006","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.ejmech.2018.06.059_bib22","doi-asserted-by":"crossref","first-page":"1526","DOI":"10.1016\/j.bmc.2012.08.019","article-title":"Insights towards sulfonamide drug specificity in \u03b1-carbonic anhydrases","volume":"21","author":"Aggarwal","year":"2013","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.ejmech.2018.06.059_bib23","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.2018.06.059_bib24","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.2018.06.059_bib25","doi-asserted-by":"crossref","first-page":"3307","DOI":"10.1016\/j.bmc.2010.03.014","article-title":"Thioether benzenesulfonamide inhibitors of carbonic anhydrases II and IV: structure-based drug design, synthesis, and biological evaluation","volume":"18","author":"Vernier","year":"2010","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.ejmech.2018.06.059_bib26","doi-asserted-by":"crossref","first-page":"1776","DOI":"10.1016\/j.bmcl.2014.02.030","article-title":"Synthesis and carbonic anhydrase I, II, IX and XII inhibition studies of 4-N,N-disubstituted sulfanilamides incorporating 4,4,4-trifluoro-3-oxo-but-1-enyl, phenacylthiourea and imidazole-2(3H)-one\/thione moieties","volume":"24","author":"Congiu","year":"2014","journal-title":"Bioorg. Med. Chem. Lett"},{"key":"10.1016\/j.ejmech.2018.06.059_bib27","doi-asserted-by":"crossref","first-page":"1494","DOI":"10.1021\/jm501798g","article-title":"Carbonic anhydrase inhibitors with dual-tail moieties to match the hydrophobic and hydrophilic halves of the carbonic anhydrase active site","volume":"58","author":"Tanpure","year":"2015","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.ejmech.2018.06.059_bib28","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1016\/j.bioorg.2017.08.017","article-title":"N-Sulfamoylphenyl- and N-sulfamoylphenyl-N-thiazolyl-\u03b2-alanines and their derivatives as inhibitors of human carbonic anhydrases","volume":"75","author":"Va\u0161kevi\u010dien\u0117","year":"2017","journal-title":"Bioorg. Chem."},{"key":"10.1016\/j.ejmech.2018.06.059_bib29","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.ejmech.2017.03.023","article-title":"Dual-tail approach to discovery of novel carbonic anhydrase IX inhibitors by simultaneously matching the hydrophobic and hydrophilic halves of the active site","volume":"132","author":"Hou","year":"2017","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ejmech.2018.06.059_bib30","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1080\/14756366.2016.1178248","article-title":"Isoform-selective inhibitory profile of 2-imidazoline-substituted benzene sulfonamides against a panel of human carbonic anhydrases","volume":"31","author":"Supuran","year":"2016","journal-title":"J.\u00a0Enzym. Inhib. Med. Chem."},{"key":"10.1016\/j.ejmech.2018.06.059_bib31","doi-asserted-by":"crossref","first-page":"9435","DOI":"10.1021\/jm501003k","article-title":"Discovery and characterization of novel selective inhibitors of carbonic anhydrase IX","volume":"57","author":"Dudutien\u0117","year":"2014","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.ejmech.2018.06.059_bib32","doi-asserted-by":"crossref","first-page":"1985","DOI":"10.1002\/cmdc.200900386","article-title":"Thermodynamic optimisation in drug discovery: a case study using carbonic anhydrase inhibitors","volume":"4","author":"Scott","year":"2009","journal-title":"ChemMedChem"},{"key":"10.1016\/j.ejmech.2018.06.059_bib33","first-page":"5360","article-title":"Combinatorial design of isoform-selective N-Alkylated benzimidazole-based inhibitors of carbonic anhydrases","volume":"2","author":"\u010capkauskait\u0117","year":"2017","journal-title":"Chemistry"},{"key":"10.1016\/j.ejmech.2018.06.059_bib34","doi-asserted-by":"crossref","first-page":"6937","DOI":"10.1016\/j.bmc.2013.09.029","article-title":"Benzenesulfonamides with pyrimidine moiety as inhibitors of human carbonic anhydrases I, II, VI, VII, XII, and XIII","volume":"21","author":"\u010capkauskait\u0117","year":"2013","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.ejmech.2018.06.059_bib35","doi-asserted-by":"crossref","first-page":"7357","DOI":"10.1016\/j.bmc.2010.09.016","article-title":"Indapamide-like benzenesulfonamides as inhibitors of carbonic anhydrases I, II, VII, and XIII","volume":"18","author":"\u010capkauskait\u0117","year":"2010","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.ejmech.2018.06.059_bib36","doi-asserted-by":"crossref","first-page":"1619","DOI":"10.1039\/jr9350001619","article-title":"385. Derivatives of 6-bromo- and 4: 6-dibromo-m-toluidine","author":"Parkes","year":"1935","journal-title":"J.\u00a0Chem. Soc."},{"key":"10.1016\/j.ejmech.2018.06.059_bib37","doi-asserted-by":"crossref","first-page":"4092","DOI":"10.1248\/cpb.30.4092","article-title":"Studies on benzenesulfonamide derivatives with alpha- and beta-adrenergic antagonistic and antihypertensive activities","volume":"30","author":"Fujikura","year":"1982","journal-title":"Chem Pharm Bull Tokyo"},{"key":"10.1016\/j.ejmech.2018.06.059_bib38","series-title":"Cycloalkylated Benzothiadiazines, a Process for Their Preparation and Pharmaceutical Compostions Containing Them","author":"Francotte","year":"2010"},{"key":"10.1016\/j.ejmech.2018.06.059_bib39","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1007\/s00249-017-1256-0","article-title":"Intrinsic thermodynamics of high affinity inhibitor binding to recombinant human carbonic anhydrase IV","volume":"47","author":"Mickevi\u010di\u016bt\u0117","year":"2018","journal-title":"Eur. Biophys. J."},{"key":"10.1016\/j.ejmech.2018.06.059_bib40","first-page":"328","article-title":"Zur Chemie des Furosemids, I. Synthesen von 5-Sulfamoyl-anthranils\u00e4ure-Derivaten","volume":"99","author":"Sturm","year":"1966","journal-title":"Eur. J. Inorg. Chem."},{"key":"10.1016\/j.ejmech.2018.06.059_bib41","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1016\/S0301-4622(01)00207-1","article-title":"Thermodynamics of the hydrophobic effect. I. Coupling of aggregation and pKa shifts in solutions of aliphatic amines","volume":"93","author":"Matulis","year":"2001","journal-title":"Biophys. Chem."},{"key":"10.1016\/j.ejmech.2018.06.059_bib42","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1016\/S0301-4622(01)00208-3","article-title":"Thermodynamics of the hydrophobic effect. II. Calorimetric measurement of enthalpy, entropy, and heat capacity of aggregation of alkylamines and long aliphatic chains","volume":"93","author":"Matulis","year":"2001","journal-title":"Biophys. Chem."},{"key":"10.1016\/j.ejmech.2018.06.059_bib43","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1016\/S0301-4622(01)00209-5","article-title":"Thermodynamics of the hydrophobic effect. III. Condensation and aggregation of alkanes, alcohols, and alkylamines","volume":"93","author":"Matulis","year":"2001","journal-title":"Biophys. Chem."},{"key":"10.1016\/j.ejmech.2018.06.059_bib44","doi-asserted-by":"crossref","first-page":"1","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.2018.06.059_bib45","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1016\/j.ejmech.2012.02.050","article-title":"Design of [(2-pyrimidinylthio)acetyl]benzenesulfonamides as inhibitors of human carbonic anhydrases","volume":"51","author":"\u010capkauskait\u0117","year":"2012","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ejmech.2018.06.059_bib46","doi-asserted-by":"crossref","first-page":"322","DOI":"10.1021\/jm801386n","article-title":"Carbonic anhydrase inhibitors. Comparison of chlorthalidone and indapamide X-ray crystal structures in adducts with isozyme II: when three water molecules and the keto-enol tautomerism make the difference","volume":"52","author":"Temperini","year":"2009","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.ejmech.2018.06.059_bib47","series-title":"Process for the Preparation of 2-chloro and 2,6-dichloroanilines","author":"Mckendry","year":"1991"},{"key":"10.1016\/j.ejmech.2018.06.059_bib48","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1021\/jo00941a005","article-title":"Stereochemistry of sulfur compounds. IV. New ring system of carbon, nitrogen, and chiral sulfur","volume":"38","author":"Williams","year":"1973","journal-title":"J.\u00a0Org. Chem."},{"key":"10.1016\/j.ejmech.2018.06.059_bib49","doi-asserted-by":"crossref","first-page":"3222","DOI":"10.1529\/biophysj.108.134973","article-title":"A\u00a0quantitative model of thermal stabilization and destabilization of proteins by ligands","volume":"95","author":"Cimmperman","year":"2008","journal-title":"Biophys. J."},{"key":"10.1016\/j.ejmech.2018.06.059_bib50","doi-asserted-by":"crossref","first-page":"7413","DOI":"10.1016\/j.bmc.2010.09.011","article-title":"4-[N-(Substituted 4-pyrimidinyl)amino]benzenesulfonamides as inhibitors of carbonic anhydrase isozymes I, II, VII, and XIII","volume":"18","author":"S\u016bd\u017eius","year":"2010","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.ejmech.2018.06.059_bib51","doi-asserted-by":"crossref","first-page":"1431","DOI":"10.1016\/j.bmc.2012.10.016","article-title":"Characterization of human carbonic anhydrase XII stability and inhibitor binding","volume":"21","author":"Jogait\u0117","year":"2013","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.ejmech.2018.06.059_bib52","doi-asserted-by":"crossref","first-page":"863","DOI":"10.3109\/14756360903571685","article-title":"Inhibition and binding studies of carbonic anhydrase isozymes I, II and IX with benzimidazo[1,2-c][1,2,3]thiadiazole-7-sulphonamides","volume":"25","author":"Baranauskien\u0117","year":"2010","journal-title":"J.\u00a0Enzym. Inhib. Med. Chem."},{"key":"10.1016\/j.ejmech.2018.06.059_bib53","doi-asserted-by":"crossref","first-page":"204","DOI":"10.3109\/14756366.2014.908291","article-title":"Intrinsic thermodynamics of sulfonamide inhibitor binding to human carbonic anhydrases I and II","volume":"30","author":"Mork\u016bnait\u0117","year":"2015","journal-title":"J.\u00a0Enzym. Inhib. Med. Chem."},{"key":"10.1016\/j.ejmech.2018.06.059_bib54","doi-asserted-by":"crossref","first-page":"2191","DOI":"10.1007\/s10973-015-5073-3","article-title":"Thermodynamic characterization of human carbonic anhydrase VB stability and intrinsic binding of compounds","volume":"123","author":"Kasiliauskait\u0117","year":"2016","journal-title":"J.\u00a0Therm. Anal. Calorim."},{"key":"10.1016\/j.ejmech.2018.06.059_bib55","doi-asserted-by":"crossref","first-page":"972","DOI":"10.1111\/febs.13196","article-title":"Intrinsic binding of 4-substituted-2,3,5,6-tetrafluorobenezenesulfonamides to native and recombinant human carbonic anhydrase VI","volume":"282","author":"Kazokait\u0117","year":"2015","journal-title":"FEBS J."},{"key":"10.1016\/j.ejmech.2018.06.059_bib56","doi-asserted-by":"crossref","first-page":"166","DOI":"10.1002\/jmr.2404","article-title":"Intrinsic thermodynamics of trifluoromethanesulfonamide and ethoxzolamide binding to human carbonic anhydrase VII: thermodynamics of TFS and EZA binding to CA VII","volume":"28","author":"Pilipuityt\u0117","year":"2015","journal-title":"J.\u00a0Mol. Recogn."},{"key":"10.1016\/j.ejmech.2018.06.059_bib57","doi-asserted-by":"crossref","first-page":"708","DOI":"10.1016\/j.bbagen.2016.01.007","article-title":"Intrinsic thermodynamics of inhibitor binding to human carbonic anhydrase IX","volume":"1860","author":"Linkuvien\u0117","year":"2016","journal-title":"Biochim. Biophys. Acta BBA - Gen. Subj"},{"key":"10.1016\/j.ejmech.2018.06.059_bib58","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1186\/2046-1682-5-12","article-title":"Intrinsic thermodynamics of ethoxzolamide inhibitor binding to human carbonic anhydrase XIII","volume":"5","author":"Baranauskien\u0117","year":"2012","journal-title":"BMC Biophys."},{"key":"10.1016\/j.ejmech.2018.06.059_bib59","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1016\/j.jbiotec.2016.10.018","article-title":"Purification, enzymatic activity and inhibitor discovery for recombinant human carbonic anhydrase XIV","volume":"240","author":"Juozapaitien\u0117","year":"2016","journal-title":"J.\u00a0Biotechnol."},{"key":"10.1016\/j.ejmech.2018.06.059_bib60","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1107\/S0907444909047337","article-title":"XDS","volume":"D66","author":"Kabsch","year":"2010","journal-title":"Acta Crystallogr. D"},{"key":"10.1016\/j.ejmech.2018.06.059_bib61","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1107\/S0907444910048675","article-title":"iMOSFLM: a new graphical interface for diffraction-image processing with MOSFLM","volume":"67","author":"Battye","year":"2011","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.ejmech.2018.06.059_bib62","doi-asserted-by":"crossref","first-page":"1022","DOI":"10.1107\/S0021889897006766","article-title":"MOLREP: an automated program for molecular replacement","volume":"30","author":"Vagin","year":"1997","journal-title":"J.\u00a0Appl. Crystallogr."},{"key":"10.1016\/j.ejmech.2018.06.059_bib63","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1186\/1758-2946-4-17","article-title":"Avogadro: an advanced semantic chemical editor, visualization, and analysis platform","volume":"4","author":"Hanwell","year":"2012","journal-title":"J.\u00a0Cheminf."},{"key":"10.1016\/j.ejmech.2018.06.059_bib64","doi-asserted-by":"crossref","first-page":"2184","DOI":"10.1107\/S0907444904023510","article-title":"REFMAC5 dictionary: organization of prior chemical knowledge and guidelines for its use","volume":"60","author":"Vagin","year":"2004","journal-title":"Acta Crystallogr Biol Crystallogr"},{"key":"10.1016\/j.ejmech.2018.06.059_bib65","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1107\/S0907444910045749","article-title":"Overview of the CCP4 suite and current developments","volume":"67","author":"Winn","year":"2011","journal-title":"Acta Crystallogr. D Biol. Crystallogr"},{"key":"10.1016\/j.ejmech.2018.06.059_bib66","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1107\/S0907444910007493","article-title":"Features and development of \u0131t coot","volume":"66","author":"Emsley","year":"2010","journal-title":"Acta Crystallogr. D"},{"key":"10.1016\/j.ejmech.2018.06.059_bib67","doi-asserted-by":"crossref","first-page":"240","DOI":"10.1107\/S0907444996012255","article-title":"Refinement of macromolecular structures by the maximum-likelihood method","volume":"53","author":"Murshudov","year":"1997","journal-title":"Acta Crystallogr Biol Crystallogr."}],"container-title":["European Journal of Medicinal Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0223523418305506?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0223523418305506?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2019,9,22]],"date-time":"2019-09-22T12:45:52Z","timestamp":1569156352000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0223523418305506"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2018,8]]},"references-count":67,"alternative-id":["S0223523418305506"],"URL":"https:\/\/doi.org\/10.1016\/j.ejmech.2018.06.059","relation":{},"ISSN":["0223-5234"],"issn-type":[{"value":"0223-5234","type":"print"}],"subject":[],"published":{"date-parts":[[2018,8]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Design of two-tail compounds with rotationally fixed benzenesulfonamide ring as inhibitors of carbonic anhydrases","name":"articletitle","label":"Article Title"},{"value":"European Journal of Medicinal Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.ejmech.2018.06.059","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2018 Elsevier Masson SAS. All rights reserved.","name":"copyright","label":"Copyright"}]}}