{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,23]],"date-time":"2026-07-23T04:08:10Z","timestamp":1784779690644,"version":"3.55.0"},"reference-count":60,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2018,12,1]],"date-time":"2018-12-01T00:00:00Z","timestamp":1543622400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2018,12,1]],"date-time":"2018-12-01T00:00:00Z","timestamp":1543622400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"funder":[{"DOI":"10.13039\/501100004481","name":"University of Tehran","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100004481","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003968","name":"Iran National Science Foundation","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100003968","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Center for International Scientific Studies and Collaborations"},{"DOI":"10.13039\/100005243","name":"UNESCO","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100005243","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["International Journal of Biological Macromolecules"],"published-print":{"date-parts":[[2018,12]]},"DOI":"10.1016\/j.ijbiomac.2018.08.186","type":"journal-article","created":{"date-parts":[[2018,8,31]],"date-time":"2018-08-31T09:16:13Z","timestamp":1535706973000},"page":"1198-1207","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":21,"special_numbering":"PA","title":["Mechanistic investigation of sulfonamide ligands as human carbonic anhydrase II inhibitors"],"prefix":"10.1016","volume":"120","author":[{"given":"Loghman","family":"Alaei","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Reza","family":"Khodarahmi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vahid","family":"Sheikh-Hasani","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nader","family":"Sheibani","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ali A.","family":"Moosavi-Movahedi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.ijbiomac.2018.08.186_bb0005","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.ijbiomac.2018.08.186_bb0010","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/S0163-7258(96)00198-2","article-title":"Structure and mechanism of carbonic anhydrase","volume":"74","author":"Lindskog","year":"1997","journal-title":"Pharmacol. Ther."},{"key":"10.1016\/j.ijbiomac.2018.08.186_bb0015","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1517\/13543776.12.2.217","article-title":"Applications of carbonic anhydrase inhibitors and activators in therapy","volume":"12","author":"Supuran","year":"2002","journal-title":"Expert Opin. Ther. Pat."},{"key":"10.1016\/j.ijbiomac.2018.08.186_bb0020","doi-asserted-by":"crossref","first-page":"575","DOI":"10.1517\/13543776.10.5.575","article-title":"Carbonic anhydrase inhibitors and their therapeutic potential","volume":"10","author":"Supuran","year":"2000","journal-title":"Expert Opin. Ther. Pat."},{"key":"10.1016\/j.ijbiomac.2018.08.186_bb0025","doi-asserted-by":"crossref","first-page":"767","DOI":"10.1002\/med.20068","article-title":"Therapeutic potential of sulfamides as enzyme inhibitors","volume":"26","author":"Winum","year":"2006","journal-title":"Med. Res. Rev."},{"key":"10.1016\/j.ijbiomac.2018.08.186_bb0030","doi-asserted-by":"crossref","first-page":"1101","DOI":"10.1006\/jmbi.1996.0699","article-title":"Characterizing the use of perdeuteration in NMR studies of large proteins: 13C, 15N and1H assignments of human carbonic anhydrase II","volume":"264","author":"Venters","year":"1996","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.ijbiomac.2018.08.186_bb0035","doi-asserted-by":"crossref","first-page":"301","DOI":"10.1006\/jmbi.1998.2077","article-title":"Crystal structure of carbonic anhydrase from Neisseria gonorrhoeae and its complex with the inhibitor acetazolamide1","volume":"283","author":"Huang","year":"1998","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.ijbiomac.2018.08.186_bb0040","doi-asserted-by":"crossref","first-page":"2908","DOI":"10.1021\/cg300098q","article-title":"Polymorphism of aromatic sulfonamides with fluorine groups","volume":"12","author":"Terada","year":"2012","journal-title":"Cryst. Growth Des."},{"key":"10.1016\/j.ijbiomac.2018.08.186_bb0045","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1016\/j.bpc.2015.05.009","article-title":"Intrinsic thermodynamics of 4-substituted-2,3,5,6-tetrafluorobenzenesulfonamide binding to carbonic anhydrases by isothermal titration calorimetry","volume":"205","author":"Zubrien\u0117","year":"2015","journal-title":"Biophys. Chem."},{"key":"10.1016\/j.ijbiomac.2018.08.186_bb0050","doi-asserted-by":"crossref","first-page":"2093","DOI":"10.1016\/j.bmc.2013.01.008","article-title":"4-Substituted-2,3,5,6-tetrafluorobenzenesulfonamides as inhibitors of carbonic anhydrases I, II, VII, XII, and XIII","volume":"21","author":"Dudutien\u0117","year":"2013","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.ijbiomac.2018.08.186_bb0055","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. Enzyme Inhib. Med. Chem."},{"key":"10.1016\/j.ijbiomac.2018.08.186_bb0060","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. Sect. F: Struct. Biol. Cryst. Commun."},{"key":"10.1016\/j.ijbiomac.2018.08.186_bb0065","doi-asserted-by":"crossref","first-page":"2315","DOI":"10.1016\/j.bmcl.2005.03.032","article-title":"Carbonic anhydrase inhibitors. Zonisamide is an effective inhibitor of the cytosolic isozyme II and mitochondrial isozyme V: solution and X-ray crystallographic studies","volume":"15","author":"De Simone","year":"2005","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/j.ijbiomac.2018.08.186_bb0070","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/0006-3002(61)90898-8","article-title":"Purification and properties of carbonic anhydrase from human erythrocytes","volume":"52","author":"Nyman","year":"1961","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.ijbiomac.2018.08.186_bb0075","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1021\/ed039p333","article-title":"The beer-lambert law","volume":"39","author":"Swinehart","year":"1962","journal-title":"J. Chem. Educ."},{"key":"10.1016\/j.ijbiomac.2018.08.186_bb0080","doi-asserted-by":"crossref","first-page":"668","DOI":"10.1021\/bi00855a005","article-title":"The catalytic versatility of erythrocyte carbonic anhydrase. III. Kinetic studies of the enzyme-catalyzed hydrolysis of p-nitrophenyl acetate","volume":"6","author":"Pocker","year":"1967","journal-title":"Biochemistry"},{"key":"10.1016\/j.ijbiomac.2018.08.186_bb0085","doi-asserted-by":"crossref","first-page":"6353","DOI":"10.1021\/bi00268a006","article-title":"Solvent deuterium isotope effects in the catalysis of oxygen-18 exchange by human carbonic anhydrase II","volume":"21","author":"Tu","year":"1982","journal-title":"Biochemistry"},{"key":"10.1016\/j.ijbiomac.2018.08.186_bb0090","doi-asserted-by":"crossref","first-page":"26233","DOI":"10.1016\/S0021-9258(19)74305-1","article-title":"A new class of carbonic anhydrase inhibitor","volume":"268","author":"Maren","year":"1993","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ijbiomac.2018.08.186_bb0095","series-title":"Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists","author":"Copeland","year":"2013"},{"key":"10.1016\/j.ijbiomac.2018.08.186_bb0100","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1002\/bmb.2002.494030050089","article-title":"Study of protein-ligand binding by fluorescence","volume":"30","author":"M\u00f6ller","year":"2002","journal-title":"Biochem. Mol. Biol. Educ."},{"key":"10.1016\/j.ijbiomac.2018.08.186_bb0105","series-title":"Methods in Enzymology","first-page":"400","article-title":"Measurement of ligand binding to proteins by fluorescence spectroscopy","year":"1985"},{"key":"10.1016\/j.ijbiomac.2018.08.186_bb0110","doi-asserted-by":"crossref","first-page":"526","DOI":"10.1126\/science.162.3853.526","article-title":"Fluorescence spectroscopy of proteins","volume":"162","author":"Stryer","year":"1968","journal-title":"Science"},{"key":"10.1016\/j.ijbiomac.2018.08.186_bb0115","doi-asserted-by":"crossref","first-page":"1721","DOI":"10.1016\/0006-2952(93)90576-I","article-title":"Study of interaction of carprofen and its enantiomers with human serum albumin\u2014I: mechanism of binding studied by dialysis and spectroscopic methods","volume":"46","author":"Rahman","year":"1993","journal-title":"Biochem. Pharmacol."},{"key":"10.1016\/j.ijbiomac.2018.08.186_bb0120","series-title":"Formation and Stability of Inorganic Complexes in Solution","author":"Job","year":"1928"},{"key":"10.1016\/j.ijbiomac.2018.08.186_bb0125","doi-asserted-by":"crossref","first-page":"435","DOI":"10.2116\/analsci.22.435","article-title":"Study of the interaction of carbamazepine with bovine serum albumin by fluorescence quenching method","volume":"22","author":"Wang","year":"2006","journal-title":"Anal. Sci."},{"key":"10.1016\/j.ijbiomac.2018.08.186_bb0130","doi-asserted-by":"crossref","first-page":"1223","DOI":"10.1016\/S0039-9140(98)00198-2","article-title":"Investigation of the interaction between acridine orange and bovine serum albumin","volume":"47","author":"Feng","year":"1998","journal-title":"Talanta"},{"key":"10.1016\/j.ijbiomac.2018.08.186_bb0135","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.ijbiomac.2018.08.186_bb0140","doi-asserted-by":"crossref","first-page":"2638","DOI":"10.1021\/bi00815a012","article-title":"Kinetics of complex formation between human carbonic anhydrases and aromatic sulfonamides","volume":"9","author":"Taylor","year":"1970","journal-title":"Biochemistry"},{"key":"10.1016\/j.ijbiomac.2018.08.186_bb0145","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.ijbiomac.2018.08.186_bb0150","doi-asserted-by":"crossref","first-page":"699","DOI":"10.1016\/j.jpba.2007.10.016","article-title":"Probing the binding of morin to human serum albumin by optical spectroscopy","volume":"46","author":"Zhang","year":"2008","journal-title":"J. Pharm. Biomed. Anal."},{"key":"10.1016\/j.ijbiomac.2018.08.186_bb0155","doi-asserted-by":"crossref","first-page":"134","DOI":"10.1016\/j.jpba.2007.12.029","article-title":"Studies on interaction between vitamin B12 and human serum albumin","volume":"47","author":"Hou","year":"2008","journal-title":"J. Pharm. Biomed. Anal."},{"key":"10.1016\/j.ijbiomac.2018.08.186_bb0160","first-page":"79","article-title":"Applications of circular dichroism and optical rotatory dispersion in molecular biology","author":"Lu","year":"1987","journal-title":"Science"},{"key":"10.1016\/j.ijbiomac.2018.08.186_bb0165","doi-asserted-by":"crossref","first-page":"392","DOI":"10.1002\/bip.20853","article-title":"Protein secondary structure analyses from circular dichroism spectroscopy: methods and reference databases","volume":"89","author":"Whitmore","year":"2008","journal-title":"Biopolymers"},{"key":"10.1016\/j.ijbiomac.2018.08.186_bb0170","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1016\/j.bbapap.2005.06.005","article-title":"How to study proteins by circular dichroism","volume":"1751","author":"Kelly","year":"2005","journal-title":"Biochim. Biophys. Acta, Proteins Proteomics"},{"key":"10.1016\/j.ijbiomac.2018.08.186_bb0175","doi-asserted-by":"crossref","first-page":"1701","DOI":"10.1002\/jcc.20291","article-title":"GROMACS: fast, flexible, and free","volume":"26","author":"Van Der Spoel","year":"2005","journal-title":"J. Comput. Chem."},{"key":"10.1016\/j.ijbiomac.2018.08.186_bb0180","doi-asserted-by":"crossref","first-page":"392","DOI":"10.1126\/science.1107996","article-title":"Atomic-scale visualization of inertial dynamics","volume":"308","author":"Lindenberg","year":"2005","journal-title":"Science"},{"key":"10.1016\/j.ijbiomac.2018.08.186_bb0185","doi-asserted-by":"crossref","first-page":"435","DOI":"10.1021\/ct700301q","article-title":"GROMACS 4: algorithms for highly efficient, load-balanced, and scalable molecular simulation","volume":"4","author":"Hess","year":"2008","journal-title":"J. Chem. Theory Comput."},{"key":"10.1016\/j.ijbiomac.2018.08.186_bb0190","series-title":"Intermolecular Forces","first-page":"331","article-title":"Interaction models for water in relation to protein hydration","author":"Berendsen","year":"1981"},{"key":"10.1016\/j.ijbiomac.2018.08.186_bb0195","doi-asserted-by":"crossref","first-page":"8345","DOI":"10.1063\/1.465608","article-title":"The effect of long-range electrostatic interactions in simulations of macromolecular crystals: a comparison of the Ewald and truncated list methods","volume":"99","author":"York","year":"1993","journal-title":"J. Chem. Phys."},{"key":"10.1016\/j.ijbiomac.2018.08.186_bb0200","doi-asserted-by":"crossref","first-page":"450","DOI":"10.1063\/1.469422","article-title":"Effect of the treatment of long-range forces on the dynamics of ions in aqueous solutions","volume":"102","author":"Perera","year":"1995","journal-title":"J. Chem. Phys."},{"key":"10.1016\/j.ijbiomac.2018.08.186_bb0205","doi-asserted-by":"crossref","DOI":"10.1103\/PhysRevLett.90.075503","article-title":"Predicting crystal structures: the Parrinello-Rahman method revisited","volume":"90","author":"Marto\u0148\u00e1k","year":"2003","journal-title":"Phys. Rev. Lett."},{"key":"10.1016\/j.ijbiomac.2018.08.186_bb0210","doi-asserted-by":"crossref","first-page":"1657","DOI":"10.1021\/ja00214a001","article-title":"The OPLS [optimized potentials for liquid simulations] potential functions for proteins, energy minimizations for crystals of cyclic peptides and crambin","volume":"110","author":"Jorgensen","year":"1988","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.ijbiomac.2018.08.186_bb0215","doi-asserted-by":"crossref","first-page":"1355","DOI":"10.1107\/S0907444904011679","article-title":"PRODRG: a tool for high-throughput crystallography of protein\u2013ligand complexes","volume":"60","author":"Schu\u00c8ttelkopf","year":"2004","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.ijbiomac.2018.08.186_bb0220","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1107\/S0907444909042073","article-title":"MolProbity: all-atom structure validation for macromolecular crystallography","volume":"66","author":"Chen","year":"2010","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.ijbiomac.2018.08.186_bb0225","doi-asserted-by":"crossref","first-page":"3099","DOI":"10.1016\/0006-2952(73)90196-2","article-title":"Relationship between the inhibition constant (Ki) and the concentration of inhibitor which causes 50 per cent inhibition (I50) of an enzymatic reaction","volume":"22","author":"Yung-Chi","year":"1973","journal-title":"Biochem. Pharmacol."},{"key":"10.1016\/j.ijbiomac.2018.08.186_bb0230","series-title":"Enzymes: Biochemistry, Biotechnology, Clinical Chemistry","author":"Palmer","year":"2007"},{"key":"10.1016\/j.ijbiomac.2018.08.186_bb0235","series-title":"Physical Biochemistry: Applications to Biochemistry and Molecular Biology","author":"Freifelder","year":"1982"},{"key":"10.1016\/j.ijbiomac.2018.08.186_bb0240","doi-asserted-by":"crossref","first-page":"974","DOI":"10.1007\/s12010-014-1341-0","article-title":"Probing of the interaction between \u03b2-lactoglobulin and the anticancer drug oxaliplatin","volume":"175","author":"Ghalandari","year":"2015","journal-title":"Appl. Biochem. Biotechnol."},{"key":"10.1016\/j.ijbiomac.2018.08.186_bb0245","doi-asserted-by":"crossref","first-page":"391","DOI":"10.1016\/j.jlumin.2015.07.016","article-title":"Biophysical study on the interaction between two palladium (II) complexes and human serum albumin by multispectroscopic methods","volume":"167","author":"Saeidifar","year":"2015","journal-title":"J. Lumin."},{"key":"10.1016\/j.ijbiomac.2018.08.186_bb0250","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1016\/j.molstruc.2007.06.035","article-title":"Spectroscopic investigation of the interaction between riboflavin and bovine serum albumin","volume":"931","author":"Guo","year":"2009","journal-title":"J. Mol. Struct."},{"key":"10.1016\/j.ijbiomac.2018.08.186_bb0255","series-title":"Biochemical Applications","author":"Lakowicz","year":"1992"},{"key":"10.1016\/j.ijbiomac.2018.08.186_bb0260","doi-asserted-by":"crossref","first-page":"324","DOI":"10.1016\/j.saa.2012.05.030","article-title":"Study of the interaction between bovine serum albumin and analogs of biphenyldicarboxylate by spectrofluorimetry","volume":"96","author":"Wang","year":"2012","journal-title":"Spectrochim. Acta A Mol. Biomol. Spectrosc."},{"key":"10.1016\/j.ijbiomac.2018.08.186_bb0265","doi-asserted-by":"crossref","first-page":"675","DOI":"10.1016\/j.bmc.2017.12.035","article-title":"Benzimidazole design, synthesis, and docking to build selective carbonic anhydrase VA inhibitors","volume":"26","author":"\u010capkauskait\u0117","year":"2018","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.ijbiomac.2018.08.186_bb0270","series-title":"Carbonic Anhydrase","first-page":"13","article-title":"Carbonic anhydrases: catalytic and inhibition mechanisms, distribution and physiological roles","author":"Supuran","year":"2004"},{"key":"10.1016\/j.ijbiomac.2018.08.186_bb0275","doi-asserted-by":"crossref","first-page":"3096","DOI":"10.1021\/bi00514a017","article-title":"Thermodynamics of protein association reactions: forces contributing to stability","volume":"20","author":"Ross","year":"1981","journal-title":"Biochemistry"},{"key":"10.1016\/j.ijbiomac.2018.08.186_bb0280","first-page":"511","article-title":"Thermodynamics of protein interactions","author":"Timaseff","year":"1972","journal-title":"Protides Biol. Fluids"},{"key":"10.1016\/j.ijbiomac.2018.08.186_bb0285","doi-asserted-by":"crossref","first-page":"371","DOI":"10.1007\/s10930-007-9073-4","article-title":"Competitive inhibitory effects of acetazolamide upon interactions with bovine carbonic anhydrase II","volume":"26","author":"Safarian","year":"2007","journal-title":"Protein J."},{"key":"10.1016\/j.ijbiomac.2018.08.186_bb0290","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1016\/j.jphotochem.2006.06.015","article-title":"Binding of trazodone hydrochloride with human serum albumin: a spectroscopic study","volume":"185","author":"Kandagal","year":"2007","journal-title":"J. Photochem. Photobiol. A Chem."},{"key":"10.1016\/j.ijbiomac.2018.08.186_bb0295","doi-asserted-by":"crossref","first-page":"12125","DOI":"10.1021\/ja002627n","article-title":"Contribution of fluorine to protein\u2212ligand affinity in the binding of fluoroaromatic inhibitors to carbonic anhydrase II","volume":"122","author":"Kim","year":"2000","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.ijbiomac.2018.08.186_bb0300","doi-asserted-by":"crossref","first-page":"885","DOI":"10.2174\/156802607780636717","article-title":"Dual carbonic anhydrase-cyclooxygenase-2 inhibitors","volume":"7","author":"Dogne","year":"2007","journal-title":"Curr. Top. Med. Chem."}],"container-title":["International Journal of Biological Macromolecules"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0141813018342338?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0141813018342338?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,26]],"date-time":"2025-09-26T07:22:36Z","timestamp":1758871356000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0141813018342338"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2018,12]]},"references-count":60,"alternative-id":["S0141813018342338"],"URL":"https:\/\/doi.org\/10.1016\/j.ijbiomac.2018.08.186","relation":{},"ISSN":["0141-8130"],"issn-type":[{"value":"0141-8130","type":"print"}],"subject":[],"published":{"date-parts":[[2018,12]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Mechanistic investigation of sulfonamide ligands as human carbonic anhydrase II inhibitors","name":"articletitle","label":"Article Title"},{"value":"International Journal of Biological Macromolecules","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.ijbiomac.2018.08.186","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2018 Elsevier B.V. All rights reserved.","name":"copyright","label":"Copyright"}]}}