{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,13]],"date-time":"2026-10-13T10:11:56Z","timestamp":1791886316816,"version":"4.3.4"},"reference-count":71,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/501100019003","name":"Enamine Ltd","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100019003","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":[[2026,1]]},"DOI":"10.1016\/j.ejmech.2025.118296","type":"journal-article","created":{"date-parts":[[2025,10,23]],"date-time":"2025-10-23T23:07:06Z","timestamp":1761260826000},"page":"118296","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":2,"special_numbering":"P1","title":["Expanding chemical space of N-acyl sulfonamides for carbonic anhydrase inhibitor discovery"],"prefix":"10.1016","volume":"302","author":[{"given":"Oleksii V.","family":"Gavrylenko","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bohdan V.","family":"Vashchenko","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vasyl","family":"Naumchyk","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Oleksii","family":"Chuk","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Olga","family":"Kuchuk","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alla","family":"Pogribna","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anzhelika I.","family":"Konovets","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Volodymyr S.","family":"Brovarets","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sergey A.","family":"Zozulya","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dmytro S.","family":"Radchenko","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6036-5859","authenticated-orcid":false,"given":"Oleksandr O.","family":"Grygorenko","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yurii S.","family":"Moroz","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"issue":"3594","key":"10.1016\/j.ejmech.2025.118296_bib1","first-page":"533","volume":"142","author":"Prontosil","year":"1938","journal-title":"Nature"},{"issue":"6","key":"10.1016\/j.ejmech.2025.118296_bib2","doi-asserted-by":"crossref","first-page":"775","DOI":"10.1007\/s10295-009-0553-8","article-title":"Different roads to discovery; prontosil (Hence sulfa drugs) and penicillin (Hence \u03b2-Lactams)","volume":"36","author":"Bentley","year":"2009","journal-title":"J. Ind. Microbiol. Biotechnol."},{"issue":"44","key":"10.1016\/j.ejmech.2025.118296_bib3","doi-asserted-by":"crossref","DOI":"10.1002\/chem.202401307","article-title":"Photocatalytic synthesis and functionalization of sulfones, sulfonamides and sulfoximines","volume":"30","author":"Garrido\u2010Gonz\u00e1lez","year":"2024","journal-title":"Chem. Eur J."},{"issue":"sup2","key":"10.1016\/j.ejmech.2025.118296_bib4","doi-asserted-by":"crossref","first-page":"180","DOI":"10.1080\/14756366.2016.1198900","article-title":"A class of sulfonamides as carbonic anhydrase I and II inhibitors","volume":"31","author":"Gokcen","year":"2016","journal-title":"J. Enzym. Inhib. Med. Chem."},{"issue":"1","key":"10.1016\/j.ejmech.2025.118296_bib5","doi-asserted-by":"crossref","first-page":"1051","DOI":"10.1080\/14756366.2019.1611801","article-title":"Fibrate-Based N -Acylsulphonamides targeting carbonic anhydrases: synthesis, biochemical evaluation, and docking studies","volume":"34","author":"Ammazzalorso","year":"2019","journal-title":"J. Enzym. Inhib. Med. Chem."},{"issue":"8","key":"10.1016\/j.ejmech.2025.118296_bib6","doi-asserted-by":"crossref","first-page":"3522","DOI":"10.1021\/jm500255y","article-title":"Cyclic secondary sulfonamides: unusually good inhibitors of cancer-related carbonic anhydrase enzymes","volume":"57","author":"Moeker","year":"2014","journal-title":"J. Med. Chem."},{"issue":"15","key":"10.1016\/j.ejmech.2025.118296_bib7","doi-asserted-by":"crossref","first-page":"4834","DOI":"10.1021\/jm0501073","article-title":"Carbonic anhydrase inhibitors. Design of fluorescent sulfonamides as probes of tumor-associated carbonic anhydrase IX that inhibit isozyme IX-Mediated acidification of hypoxic tumors","volume":"48","author":"Cecchi","year":"2005","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.ejmech.2025.118296_bib8","doi-asserted-by":"crossref","DOI":"10.1016\/j.bmc.2023.117467","article-title":"Design and synthesis of sulfonamides incorporating a biotin moiety: carbonic anhydrase inhibitory effects, antiproliferative activity and molecular modeling studies","volume":"94","author":"Begines","year":"2023","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.ejmech.2025.118296_bib9","doi-asserted-by":"crossref","DOI":"10.1016\/j.molstruc.2022.133260","article-title":"Nitroimidazole-sulfonamides as carbonic anhydrase IX and XII inhibitors targeting tumor hypoxia: design, synthesis, molecular docking and molecular dynamics simulation","volume":"1264","author":"Almatary","year":"2022","journal-title":"J. Mol. Struct."},{"issue":"1","key":"10.1016\/j.ejmech.2025.118296_bib10","doi-asserted-by":"crossref","DOI":"10.1155\/2022\/5293349","article-title":"Carbonic anhydrase II\/IX\/XII inhibition, DFT, and molecular docking studies of hydrazide\u2010sulfonamide hybrids of 4\u2010Methylsalicyl\u2010 and acyl\u2010substituted hydrazide","volume":"2022","author":"Khushal","year":"2022","journal-title":"BioMed Res. Int."},{"issue":"11","key":"10.1016\/j.ejmech.2025.118296_bib11","doi-asserted-by":"crossref","first-page":"8767","DOI":"10.1039\/D3CP05846H","article-title":"Discovery of non-sulfonamide carbonic anhydrase IX inhibitors through structure-based virtual screening","volume":"26","author":"Cheng","year":"2024","journal-title":"Phys. Chem. Chem. Phys."},{"issue":"16","key":"10.1016\/j.ejmech.2025.118296_bib12","doi-asserted-by":"crossref","first-page":"8808","DOI":"10.3390\/ijms22168808","article-title":"Betulin sulfonamides as carbonic anhydrase inhibitors and anticancer agents in breast cancer cells","volume":"22","author":"G\u00fcttler","year":"2021","journal-title":"Int. J. Mol. Sci."},{"issue":"10","key":"10.1016\/j.ejmech.2025.118296_bib13","doi-asserted-by":"crossref","first-page":"5465","DOI":"10.1016\/j.bmc.2008.04.011","article-title":"Synthesis, in vitro antibacterial and carbonic anhydrase II inhibitory activities of N-Acylsulfonamides using silica sulfuric acid as an efficient catalyst under both solvent-free and heterogeneous conditions","volume":"16","author":"Massah","year":"2008","journal-title":"Bioorg. Med. Chem."},{"issue":"34","key":"10.1016\/j.ejmech.2025.118296_bib14","doi-asserted-by":"crossref","first-page":"36139","DOI":"10.18632\/oncotarget.5684","article-title":"Sulfonamide derivative targeting carbonic anhydrase IX as a nuclear imaging probe for colorectal cancer detection in vivo","volume":"6","author":"Guan","year":"2015","journal-title":"Oncotarget"},{"issue":"22","key":"10.1016\/j.ejmech.2025.118296_bib15","doi-asserted-by":"crossref","first-page":"7023","DOI":"10.3390\/molecules26227023","article-title":"Carbonic anhydrase inhibition with sulfonamides incorporating Pyrazole- and pyridazinecarboxamide moieties provides examples of isoform-selective inhibitors","volume":"26","author":"Angeli","year":"2021","journal-title":"Molecules"},{"issue":"6","key":"10.1016\/j.ejmech.2025.118296_bib16","doi-asserted-by":"crossref","first-page":"1094","DOI":"10.1111\/cbdd.13043","article-title":"N\u2010acylsulfonamides: synthetic routes and biological potential in medicinal chemistry","volume":"90","author":"Ammazzalorso","year":"2017","journal-title":"Chem. Biol. Drug Des."},{"key":"10.1016\/j.ejmech.2025.118296_bib17","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2021.113399","article-title":"Structure property relationships of N-Acylsulfonamides and related bioisosteres","volume":"218","author":"Francisco","year":"2021","journal-title":"Eur. J. Med. Chem."},{"issue":"8","key":"10.1016\/j.ejmech.2025.118296_bib18","doi-asserted-by":"crossref","first-page":"1567","DOI":"10.1039\/D3MD00229B","article-title":"N -Acylsulfonamide: a valuable moiety to design new sulfa drug analogues","volume":"14","author":"Amador","year":"2023","journal-title":"RSC Med. Chem."},{"issue":"3","key":"10.1016\/j.ejmech.2025.118296_bib19","doi-asserted-by":"crossref","first-page":"455","DOI":"10.1002\/cmdc.201402497","article-title":"Preclinical characterization of acyl sulfonimidamides: potential carboxylic acid bioisosteres with tunable properties","volume":"10","author":"Borhade","year":"2015","journal-title":"ChemMedChem"},{"issue":"10","key":"10.1016\/j.ejmech.2025.118296_bib20","doi-asserted-by":"crossref","first-page":"3733","DOI":"10.1021\/jo200031u","article-title":"Recognition properties of carboxylic acid bioisosteres: anion binding by tetrazoles, aryl sulfonamides, and acyl sulfonamides on a Calix[4]Arene scaffold","volume":"76","author":"Pinter","year":"2011","journal-title":"J. Org. Chem."},{"issue":"3","key":"10.1016\/j.ejmech.2025.118296_bib21","doi-asserted-by":"crossref","first-page":"567","DOI":"10.1021\/jm0101500","article-title":"Synthesis and evaluation of potent and selective \u03b2 3 adrenergic receptor agonists containing acylsulfonamide, sulfonylsulfonamide, and sulfonylurea carboxylic acid isosteres","volume":"45","author":"Uehling","year":"2002","journal-title":"J. Med. Chem."},{"issue":"6","key":"10.1016\/j.ejmech.2025.118296_bib22","doi-asserted-by":"crossref","first-page":"1926","DOI":"10.1016\/j.bmcl.2008.01.127","article-title":"Carboxylic acid bioisosteres acylsulfonamides, acylsulfamides, and sulfonylureas as novel antagonists of the CXCR2 receptor","volume":"18","author":"Winters","year":"2008","journal-title":"Bioorg. Med. Chem. Lett."},{"issue":"5","key":"10.1016\/j.ejmech.2025.118296_bib23","doi-asserted-by":"crossref","first-page":"2054","DOI":"10.1021\/acs.jmedchem.5b01660","article-title":"Discovery of 2-Indole-Acylsulfonamide myeloid cell leukemia 1 (Mcl-1) inhibitors using fragment-based methods","volume":"59","author":"Pelz","year":"2016","journal-title":"J. Med. Chem."},{"issue":"2","key":"10.1016\/j.ejmech.2025.118296_bib24","doi-asserted-by":"crossref","first-page":"390","DOI":"10.1016\/j.drudis.2018.10.016","article-title":"Evolution of commercially available compounds for HTS","volume":"24","author":"Volochnyuk","year":"2019","journal-title":"Drug Discov. Today"},{"issue":"2","key":"10.1016\/j.ejmech.2025.118296_bib25","doi-asserted-by":"crossref","first-page":"242","DOI":"10.1002\/cmdc.201200507","article-title":"A chemogenomic analysis of ionization constants\u2014implications for drug discovery","volume":"8","author":"Manallack","year":"2013","journal-title":"ChemMedChem"},{"issue":"9","key":"10.1016\/j.ejmech.2025.118296_bib26","doi-asserted-by":"crossref","first-page":"2437","DOI":"10.1021\/jm00171a018","article-title":"A novel series of selective leukotriene antagonists: exploration and optimization of the acidic region in 1,6-Disubstituted indoles and indazoles","volume":"33","author":"Yee","year":"1990","journal-title":"J. Med. Chem."},{"issue":"8","key":"10.1016\/j.ejmech.2025.118296_bib27","doi-asserted-by":"crossref","first-page":"538","DOI":"10.1021\/acsinfecdis.6b00021","article-title":"Carboxylate surrogates enhance the antimycobacterial activity of UDP-galactopyranose mutase probes","volume":"2","author":"Winton","year":"2016","journal-title":"ACS Infect. Dis."},{"issue":"5","key":"10.1016\/j.ejmech.2025.118296_bib28","doi-asserted-by":"crossref","first-page":"1708","DOI":"10.1021\/jm401840s","article-title":"Discovery and early clinical evaluation of BMS-605339, a potent and orally efficacious tripeptidic acylsulfonamide NS3 protease inhibitor for the treatment of hepatitis C virus infection","volume":"57","author":"Scola","year":"2014","journal-title":"J. Med. Chem."},{"issue":"2","key":"10.1016\/j.ejmech.2025.118296_bib29","doi-asserted-by":"crossref","first-page":"714","DOI":"10.1016\/j.bmc.2011.12.008","article-title":"A new class of non-thiazolidinedione, non-carboxylic-acid-based highly selective peroxisome proliferator-activated receptor (PPAR) \u03b3 agonists: design and synthesis of benzylpyrazole acylsulfonamides","volume":"20","author":"Rikimaru","year":"2012","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.ejmech.2025.118296_bib30","doi-asserted-by":"crossref","DOI":"10.1016\/j.bmc.2024.117653","article-title":"Bioisoteres for carboxylic acids: from ionized isosteres to novel unionized replacements","volume":"104","author":"Hall","year":"2024","journal-title":"Bioorg. Med. Chem."},{"issue":"3","key":"10.1016\/j.ejmech.2025.118296_bib31","doi-asserted-by":"crossref","first-page":"541","DOI":"10.1111\/j.1742-4658.2010.07976.x","article-title":"Functional and structural analyses of N\u2010 acylsulfonamide\u2010linked dinucleoside inhibitors of RNase A","volume":"278","author":"Thiyagarajan","year":"2011","journal-title":"FEBS J."},{"issue":"38","key":"10.1016\/j.ejmech.2025.118296_bib32","doi-asserted-by":"crossref","first-page":"7582","DOI":"10.1039\/D2OB01569B","article-title":"Facile access to 4\u2032-(N -Acylsulfonamide) modified nucleosides and evaluation of their inhibitory activity against SARS-CoV-2 RNA cap N 7-Guanine-Methyltransferase Nsp14","volume":"20","author":"Amador","year":"2022","journal-title":"Org. Biomol. Chem."},{"issue":"20","key":"10.1016\/j.ejmech.2025.118296_bib33","doi-asserted-by":"crossref","first-page":"6408","DOI":"10.1002\/slct.201901024","article-title":"A unified approach to access N \u2010acyl sulfonamide tethered peptide conjugates","volume":"4","author":"Sagar","year":"2019","journal-title":"ChemistrySelect"},{"issue":"2","key":"10.1016\/j.ejmech.2025.118296_bib34","doi-asserted-by":"crossref","first-page":"988","DOI":"10.1128\/AAC.04227-14","article-title":"In vitro and in vivo antiviral activity and resistance profile of the hepatitis C virus NS3\/4A protease inhibitor ABT-450","volume":"59","author":"Pilot-Matias","year":"2015","journal-title":"Antimicrob. Agents Chemother."},{"issue":"6","key":"10.1016\/j.ejmech.2025.118296_bib35","doi-asserted-by":"crossref","first-page":"2443","DOI":"10.1021\/jm9015526","article-title":"Discovery of vaniprevir (MK-7009), a macrocyclic hepatitis C virus NS3\/4a protease inhibitor","volume":"53","author":"McCauley","year":"2010","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.ejmech.2025.118296_bib36","article-title":"New treatments for genotype 1 chronic hepatitis C & ndash; focus on simeprevir","volume":"387","author":"Kanda","year":"2014","journal-title":"Therapeut. Clin. Risk Manag."},{"key":"10.1016\/j.ejmech.2025.118296_bib37","article-title":"Simeprevir for the treatment of hepatitis C virus infection","volume":"241","author":"Brochot","year":"2014","journal-title":"Pharmgenomics. Pers. Med."},{"issue":"12","key":"10.1016\/j.ejmech.2025.118296_bib38","doi-asserted-by":"crossref","first-page":"6716","DOI":"10.3390\/v7122968","article-title":"Mechanisms of hepatitis C viral resistance to direct acting antivirals","volume":"7","author":"Ahmed","year":"2015","journal-title":"Viruses"},{"issue":"5","key":"10.1016\/j.ejmech.2025.118296_bib39","doi-asserted-by":"crossref","first-page":"719","DOI":"10.1517\/13543784.2014.902049","article-title":"MK-5172: a second-generation protease inhibitor for the treatment of hepatitis C virus infection","volume":"23","author":"Gentile","year":"2014","journal-title":"Expet Opin. Invest. Drugs"},{"issue":"8","key":"10.1016\/j.ejmech.2025.118296_bib40","doi-asserted-by":"crossref","first-page":"4161","DOI":"10.1128\/AAC.00324-12","article-title":"MK-5172, a selective inhibitor of hepatitis C virus NS3\/4a protease with broad activity across genotypes and resistant variants","volume":"56","author":"Summa","year":"2012","journal-title":"Antimicrob. Agents Chemother."},{"issue":"10","key":"10.1016\/j.ejmech.2025.118296_bib41","doi-asserted-by":"crossref","first-page":"1043","DOI":"10.1007\/s40265-017-0753-x","article-title":"Resistance mechanisms in hepatitis C virus: implications for direct-acting antiviral use","volume":"77","author":"Bagaglio","year":"2017","journal-title":"Drugs"},{"issue":"9973","key":"10.1016\/j.ejmech.2025.118296_bib42","doi-asserted-by":"crossref","first-page":"1075","DOI":"10.1016\/S0140-6736(14)61795-5","article-title":"Efficacy and safety of 12 weeks versus 18 weeks of treatment with Grazoprevir (MK-5172) and Elbasvir (MK-8742) with or without ribavirin for hepatitis C virus genotype 1 infection in previously untreated patients with cirrhosis and patients with previous","volume":"385","author":"Lawitz","year":"2015","journal-title":"Lancet"},{"issue":"4","key":"10.1016\/j.ejmech.2025.118296_bib43","doi-asserted-by":"crossref","first-page":"332","DOI":"10.1021\/ml300017p","article-title":"Discovery of MK-5172, a macrocyclic hepatitis C virus NS3\/4a protease inhibitor","volume":"3","author":"Harper","year":"2012","journal-title":"ACS Med. Chem. Lett."},{"issue":"9","key":"10.1016\/j.ejmech.2025.118296_bib44","doi-asserted-by":"crossref","first-page":"2222","DOI":"10.1016\/j.bmcl.2014.02.054","article-title":"Design and synthesis of triazolopyrimidine acylsulfonamides as novel anti-mycobacterial leads acting through inhibition of Acetohydroxyacid synthase","volume":"24","author":"Patil","year":"2014","journal-title":"Bioorg. Med. Chem. Lett."},{"issue":"2","key":"10.1016\/j.ejmech.2025.118296_bib45","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1016\/j.bbapap.2003.11.006","article-title":"Biochemical characterization of an inhibitor of Escherichia Coli UDP-N-Acetylmuramyl-l-Alanine ligase","volume":"1698","author":"Ehmann","year":"2004","journal-title":"Biochim. Biophys. Acta, Proteins Proteomics"},{"issue":"9","key":"10.1016\/j.ejmech.2025.118296_bib46","doi-asserted-by":"crossref","first-page":"981","DOI":"10.1002\/jps.2600700903","article-title":"Pharmacokinetics of sulfisoxazole compared in humans and two monogastric animal species","volume":"70","author":"Suber","year":"1981","journal-title":"J. Pharmacol. Sci."},{"issue":"1","key":"10.1016\/j.ejmech.2025.118296_bib47","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1586\/17476348.2016.1121103","article-title":"Selexipag for the treatment of pulmonary arterial hypertension","volume":"10","author":"Sharma","year":"2016","journal-title":"Expet Rev. Respir. Med."},{"issue":"11","key":"10.1016\/j.ejmech.2025.118296_bib48","doi-asserted-by":"crossref","first-page":"2168","DOI":"10.1158\/1535-7163.MCT-11-0323","article-title":"Tasisulam sodium, an antitumor agent that inhibits mitotic progression and induces vascular normalization","volume":"10","author":"Meier","year":"2011","journal-title":"Mol. Cancer Therapeut."},{"issue":"7042","key":"10.1016\/j.ejmech.2025.118296_bib49","doi-asserted-by":"crossref","first-page":"677","DOI":"10.1038\/nature03579","article-title":"An inhibitor of Bcl-2 family proteins induces regression of solid tumours","volume":"435","author":"Oltersdorf","year":"2005","journal-title":"Nature"},{"issue":"2","key":"10.1016\/j.ejmech.2025.118296_bib50","doi-asserted-by":"crossref","first-page":"202","DOI":"10.1038\/nm.3048","article-title":"ABT-199, a potent and selective BCL-2 inhibitor, achieves antitumor activity while sparing platelets","volume":"19","author":"Souers","year":"2013","journal-title":"Nat. Med."},{"issue":"1","key":"10.1016\/j.ejmech.2025.118296_bib51","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1186\/s13045-015-0224-3","article-title":"ABT-199 (Venetoclax) and BCL-2 inhibitors in clinical development","volume":"8","author":"Cang","year":"2015","journal-title":"J. Hematol. Oncol."},{"issue":"4","key":"10.1016\/j.ejmech.2025.118296_bib52","doi-asserted-by":"crossref","first-page":"484","DOI":"10.1002\/jcph.821","article-title":"Pharmacokinetics of venetoclax, a novel BCL\u20102 inhibitor, in patients with relapsed or refractory chronic lymphocytic leukemia or non\u2010hodgkin lymphoma","volume":"57","author":"Salem","year":"2017","journal-title":"J. Clin. Pharmacol."},{"issue":"11","key":"10.1016\/j.ejmech.2025.118296_bib53","doi-asserted-by":"crossref","first-page":"1335","DOI":"10.1002\/jcph.730","article-title":"Evaluation of Rifampin's transporter inhibitory and CYP3A inductive effects on the pharmacokinetics of venetoclax, a BCL\u20102 inhibitor: results of a single\u2010 and multiple\u2010dose study","volume":"56","author":"Agarwal","year":"2016","journal-title":"J. Clin. Pharmacol."},{"issue":"2","key":"10.1016\/j.ejmech.2025.118296_bib54","doi-asserted-by":"crossref","first-page":"908","DOI":"10.1021\/acs.jmedchem.8b01621","article-title":"Identification of selective acyl sulfonamide\u2013cycloalkylether inhibitors of the voltage-gated sodium channel (Na V) 1.7 with potent analgesic activity","volume":"62","author":"Sun","year":"2019","journal-title":"J. Med. Chem."},{"issue":"17","key":"10.1016\/j.ejmech.2025.118296_bib55","doi-asserted-by":"crossref","first-page":"1612","DOI":"10.1056\/NEJMoa1807120","article-title":"VX-445\u2013Tezacaftor\u2013Ivacaftor in patients with cystic fibrosis and one or two Phe508del alleles","volume":"379","author":"Keating","year":"2018","journal-title":"N. Engl. J. Med."},{"issue":"17","key":"10.1016\/j.ejmech.2025.118296_bib56","doi-asserted-by":"crossref","first-page":"1599","DOI":"10.1056\/NEJMoa1807119","article-title":"VX-659\u2013Tezacaftor\u2013Ivacaftor in patients with cystic fibrosis and one or two Phe508del alleles","volume":"379","author":"Davies","year":"2018","journal-title":"N. Engl. J. Med."},{"issue":"2","key":"10.1016\/j.ejmech.2025.118296_bib57","doi-asserted-by":"crossref","first-page":"82","DOI":"10.1183\/23120541.00082-2019","article-title":"Clinical development of triple-combination CFTR modulators for cystic fibrosis patients with one or two F508del alleles","volume":"5","author":"Taylor-Cousar","year":"2019","journal-title":"ERJ Open Res"},{"issue":"5","key":"10.1016\/j.ejmech.2025.118296_bib58","first-page":"23","article-title":"Keep them breathing","volume":"30","author":"Brown","year":"2017","journal-title":"J. Am. Acad. Physician Assistants"},{"issue":"D1","key":"10.1016\/j.ejmech.2025.118296_bib59","doi-asserted-by":"crossref","first-page":"D1388","DOI":"10.1093\/nar\/gkaa971","article-title":"PubChem in 2021: new data content and improved web interfaces","volume":"49","author":"Kim","year":"2021","journal-title":"Nucleic Acids Res."},{"issue":"D1","key":"10.1016\/j.ejmech.2025.118296_bib60","doi-asserted-by":"crossref","first-page":"D1100","DOI":"10.1093\/nar\/gkr777","article-title":"ChEMBL: a large-scale bioactivity database for drug discovery","volume":"40","author":"Gaulton","year":"2012","journal-title":"Nucleic Acids Res."},{"issue":"11","key":"10.1016\/j.ejmech.2025.118296_bib61","doi-asserted-by":"crossref","DOI":"10.1016\/j.isci.2020.101681","article-title":"Generating multibillion chemical space of readily accessible screening compounds","volume":"23","author":"Grygorenko","year":"2020","journal-title":"iScience"},{"issue":"5","key":"10.1016\/j.ejmech.2025.118296_bib62","doi-asserted-by":"crossref","first-page":"3161","DOI":"10.1021\/acs.joc.3c02636","article-title":"SNAr or sulfonylation? Chemoselective amination of Halo(Het)Arene sulfonyl halides for synthetic applications and ultralarge compound library design","volume":"89","author":"Naumchyk","year":"2024","journal-title":"J. Org. Chem."},{"issue":"6","key":"10.1016\/j.ejmech.2025.118296_bib63","doi-asserted-by":"crossref","first-page":"955","DOI":"10.3109\/14756366.2014.1001754","article-title":"Esterase activity of carbonic anhydrases serves as surrogate for selecting antibodies blocking hydratase activity","volume":"30","author":"Uda","year":"2015","journal-title":"J. Enzym. Inhib. Med. Chem."},{"issue":"6","key":"10.1016\/j.ejmech.2025.118296_bib64","doi-asserted-by":"crossref","first-page":"1009","DOI":"10.3390\/molecules22061009","article-title":"Mechanistic explanation of the weak carbonic anhydrase's esterase activity","volume":"22","author":"Piazzetta","year":"2017","journal-title":"Mol"},{"issue":"23","key":"10.1016\/j.ejmech.2025.118296_bib65","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."},{"issue":"5","key":"10.1016\/j.ejmech.2025.118296_bib66","doi-asserted-by":"crossref","first-page":"616","DOI":"10.1107\/S0907444910006554","article-title":"Atomic resolution studies of carbonic anhydrase II","volume":"66","author":"Behnke","year":"2010","journal-title":"Acta Crystallogr. Sect. D Biol. Crystallogr."},{"issue":"42","key":"10.1016\/j.ejmech.2025.118296_bib67","doi-asserted-by":"crossref","first-page":"26800","DOI":"10.18632\/oncotarget.25508","article-title":"Novel fluorinated carbonic anhydrase IX inhibitors reduce hypoxia-induced acidification and clonogenic survival of cancer cells","volume":"9","author":"Kazokait\u0117","year":"2018","journal-title":"Oncotarget"},{"key":"10.1016\/j.ejmech.2025.118296_bib68","unstructured":"https:\/\/www.molsoft.com."},{"key":"10.1016\/j.ejmech.2025.118296_bib69","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1016\/j.softx.2015.06.001","article-title":"GROMACS: high performance molecular simulations through multi-level parallelism from laptops to supercomputers","volume":"1\u20132","author":"Abraham","year":"2015","journal-title":"SoftwareX"},{"issue":"10","key":"10.1016\/j.ejmech.2025.118296_bib70","doi-asserted-by":"crossref","first-page":"6281","DOI":"10.1021\/acs.jctc.1c00645","article-title":"Gmx_MMPBSA: a new tool to perform end-state free energy calculations with GROMACS","volume":"17","author":"Vald\u00e9s-Tresanco","year":"2021","journal-title":"J. Chem. Theor. Comput."},{"key":"10.1016\/j.ejmech.2025.118296_bib71","series-title":"Purification of Laboratory Chemicals","author":"Armarego","year":"2003"}],"container-title":["European Journal of Medicinal Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S022352342501061X?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S022352342501061X?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,3,12]],"date-time":"2026-03-12T06:01:37Z","timestamp":1773295297000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S022352342501061X"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,1]]},"references-count":71,"alternative-id":["S022352342501061X"],"URL":"https:\/\/doi.org\/10.1016\/j.ejmech.2025.118296","relation":{"has-preprint":[{"id-type":"doi","id":"10.26434\/chemrxiv-2025-c4rw4-v2","asserted-by":"object"},{"id-type":"doi","id":"10.26434\/chemrxiv-2025-c4rw4","asserted-by":"object"}]},"ISSN":["0223-5234"],"issn-type":[{"value":"0223-5234","type":"print"}],"subject":[],"published":{"date-parts":[[2026,1]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Expanding chemical space of N-acyl sulfonamides for carbonic anhydrase inhibitor discovery","name":"articletitle","label":"Article Title"},{"value":"European Journal of Medicinal Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.ejmech.2025.118296","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2025 Elsevier Masson SAS. All rights are reserved, including those for text and data mining, AI training, and similar technologies.","name":"copyright","label":"Copyright"}],"article-number":"118296"}}