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Journal Abstract Search
205 related items for PubMed ID: 19796939
1. Carbonic anhydrase II-induced selection of inhibitors from a dynamic combinatorial library of Schiff's bases. Nasr G, Petit E, Supuran CT, Winum JY, Barboiu M. Bioorg Med Chem Lett; 2009 Nov 01; 19(21):6014-7. PubMed ID: 19796939 [Abstract] [Full Text] [Related]
2. Carbonic anhydrase-encoded dynamic constitutional libraries: toward the discovery of isozyme-specific inhibitors. Nasr G, Petit E, Vullo D, Winum JY, Supuran CT, Barboiu M. J Med Chem; 2009 Aug 13; 52(15):4853-9. PubMed ID: 19580287 [Abstract] [Full Text] [Related]
3. Carbonic anhydrase inhibitors: inhibition of human cytosolic isozyme II and mitochondrial isozyme V with a series of benzene sulfonamide derivatives. Innocenti A, Antel J, Wurl M, Scozzafava A, Supuran CT. Bioorg Med Chem Lett; 2004 Nov 15; 14(22):5703-7. PubMed ID: 15482952 [Abstract] [Full Text] [Related]
4. Carbonic anhydrase inhibitors. Inhibition of human cytosolic isoforms I and II with (reduced) Schiff's bases incorporating sulfonamide, carboxylate and carboxymethyl moieties. Nasr G, Cristian A, Barboiu M, Vullo D, Winum JY, Supuran CT. Bioorg Med Chem; 2014 May 15; 22(10):2867-74. PubMed ID: 24746465 [Abstract] [Full Text] [Related]
5. Carbonic anhydrase inhibitors: Schiff's bases of aromatic and heterocyclic sulfonamides and their metal complexes. Mahmood-Ul-Hassan, Chohan ZH, Scozzafava A, Supuran CT. J Enzyme Inhib Med Chem; 2004 Jun 15; 19(3):263-7. PubMed ID: 15499998 [Abstract] [Full Text] [Related]
6. Fragment-based drug discovery of carbonic anhydrase II inhibitors by dynamic combinatorial chemistry utilizing alkene cross metathesis. Poulsen SA, Bornaghi LF. Bioorg Med Chem; 2006 May 15; 14(10):3275-84. PubMed ID: 16431113 [Abstract] [Full Text] [Related]
8. Inhibition of carbonic anhydrase isoforms I, II, IX and XII with Schiff's bases incorporating iminoureido moieties. Singasane N, Kharkar PS, Ceruso M, Supuran CT, Toraskar MP. J Enzyme Inhib Med Chem; 2015 Dec 15; 30(6):901-7. PubMed ID: 25744513 [Abstract] [Full Text] [Related]
9. Carbonic anhydrase inhibitors. Aromatic/heterocyclic sulfonamides incorporating phenacetyl, pyridylacetyl and thienylacetyl tails act as potent inhibitors of human mitochondrial isoforms VA and VB. Güzel O, Innocenti A, Scozzafava A, Salman A, Supuran CT. Bioorg Med Chem; 2009 Jul 15; 17(14):4894-9. PubMed ID: 19539481 [Abstract] [Full Text] [Related]
10. In situ click chemistry: enzyme-generated inhibitors of carbonic anhydrase II. Mocharla VP, Colasson B, Lee LV, Röper S, Sharpless KB, Wong CH, Kolb HC. Angew Chem Int Ed Engl; 2004 Dec 17; 44(1):116-20. PubMed ID: 15599912 [No Abstract] [Full Text] [Related]
11. 4-[N-(substituted 4-pyrimidinyl)amino]benzenesulfonamides as inhibitors of carbonic anhydrase isozymes I, II, VII, and XIII. Sūdžius J, Baranauskienė L, Golovenko D, Matulienė J, Michailovienė V, Torresan J, Jachno J, Sukackaitė R, Manakova E, Gražulis S, Tumkevičius S, Matulis D. Bioorg Med Chem; 2010 Nov 01; 18(21):7413-21. PubMed ID: 20889345 [Abstract] [Full Text] [Related]
13. Virtual screening-driven identification of human carbonic anhydrase inhibitors incorporating an original, new pharmacophore. Pala N, Dallocchio R, Dessì A, Brancale A, Carta F, Ihm S, Maresca A, Sechi M, Supuran CT. Bioorg Med Chem Lett; 2011 Apr 15; 21(8):2515-20. PubMed ID: 21420862 [Abstract] [Full Text] [Related]
15. QSAR study on para-substituted aromatic sulfonamides as carbonic anhydrase II inhibitors using topological information indices. Melagraki G, Afantitis A, Sarimveis H, Igglessi-Markopoulou O, Supuran CT. Bioorg Med Chem; 2006 Feb 15; 14(4):1108-14. PubMed ID: 16213737 [Abstract] [Full Text] [Related]
16. Carbonic anhydrase inhibitors. The X-ray crystal structure of human isoform II in adduct with an adamantyl analogue of acetazolamide resides in a less utilized binding pocket than most hydrophobic inhibitors. Avvaru BS, Wagner JM, Maresca A, Scozzafava A, Robbins AH, Supuran CT, McKenna R. Bioorg Med Chem Lett; 2010 Aug 01; 20(15):4376-81. PubMed ID: 20605094 [Abstract] [Full Text] [Related]