Design, synthesis and human carbonic anhydrase I, II, IX and XII inhibitory properties of 1,3-thiazole sulfonamides

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dc.authorid0000-0001-8611-9181en_US
dc.authorid0000-0003-4740-1138en_US
dc.contributor.authorErigür, Esra Caner
dc.contributor.authorAltuğ, Cevher
dc.contributor.authorAngeli, Andrea
dc.contributor.authorSupuran, Claudiu T.
dc.date.accessioned2024-02-08T13:34:21Z
dc.date.available2024-02-08T13:34:21Z
dc.date.issued2022en_US
dc.departmentBAİBÜ, Lisansüstü Eğitim Enstitüsü, Fen Bilimleri, Kimya Ana Bilim Dalıen_US
dc.descriptionWe are extremely grateful to Hayat Kimya San. A S and BAIBU BAP (Project No : 2021.03.03.1499) for financial support.en_US
dc.description.abstractCarbonic anhydrases (CAs, EC 4.2.1.1) are categorized as metalloenzymes and are widespread in both eukaryotes and prokaryotes. In mammals, 16 different isoforms of carbonic anhydrase were isolated and categorized as catalytic human isoform; cytosolic CAs (CA-I, II, III, VII and XIII), membrane-associated CAs (CA-IV, IX, XII, XIV and XV), mitochondrial CAs (CA-VA and VB), secreted CAs (CA-VI) and non- catalytic human isoform; inactive CA-related proteins (CA-VIII, X, and XI).1,2 Carbonic anhydrases, which are included in the enzyme family, help to the reversible conversion of carbon dioxide and water to bicarbonate anion and proton presence of Zn2+ ion at the catalytic site. They also provide transportation of carbon dioxide (CO2), keeps acid-base balance, regulation of pH, etc.3,4 By means of their critical participation in many regulatory physiologic processes, they play an active role in the treatment of many diseases such as glaucoma, epilepsy, obesity edema, cancer, neuropathic pain, etc.5en_US
dc.description.sponsorshipBAIBU BAP [2021.03.03.1499]; Hayat Kimya San. A Sen_US
dc.identifier.citationErigur, E. C., Altug, C., Angeli, A., & Supuran, C. T. (2022). Design, synthesis and human carbonic anhydrase I, II, IX and XII inhibitory properties of 1, 3-thiazole sulfonamides. Bioorganic & Medicinal Chemistry Letters, 59, 128581-128581.en_US
dc.identifier.doi10.1016/j.bmcl.2022.128581
dc.identifier.endpage4en_US
dc.identifier.issn0960-894X
dc.identifier.issn1464-3405
dc.identifier.pmid35066141en_US
dc.identifier.scopus2-s2.0-85123370879en_US
dc.identifier.scopusqualityQ2en_US
dc.identifier.startpage1en_US
dc.identifier.urihttp://dx.doi.org/10.1016/j.bmcl.2022.128581
dc.identifier.urihttps://hdl.handle.net/20.500.12491/11998
dc.identifier.volume59en_US
dc.identifier.wosWOS:000783550500008en_US
dc.identifier.wosqualityQ2en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.indekslendigikaynakPubMeden_US
dc.institutionauthorErigür, Esra Caner
dc.institutionauthorAltuğ, Cevher
dc.language.isoenen_US
dc.publisherPergamon-Elsevier Science Ltden_US
dc.relation.ispartofBioorganic & Medicinal Chemistry Lettersen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - İdari Personel ve Öğrencien_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectBiological Evaluationen_US
dc.subjectProtease Inhibitorsen_US
dc.subjectDerivativesen_US
dc.subjectAnticanceren_US
dc.subjectTargetsen_US
dc.subjectVIIen_US
dc.titleDesign, synthesis and human carbonic anhydrase I, II, IX and XII inhibitory properties of 1,3-thiazole sulfonamidesen_US
dc.typeArticleen_US

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