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For: Vullo D, Del Prete S, Di Fonzo P, Carginale V, Donald WA, Supuran CT, Capasso C. Comparison of the Sulfonamide Inhibition Profiles of the β- and γ-Carbonic Anhydrases from the Pathogenic Bacterium Burkholderia pseudomallei. Molecules 2017;22:E421. [PMID: 28272358 DOI: 10.3390/molecules22030421] [Cited by in Crossref: 18] [Cited by in F6Publishing: 20] [Article Influence: 3.6] [Reference Citation Analysis]
Number Citing Articles
1 Vincent J, Colin B, Lanneluc I, Sabot R, Sopéna V, Turcry P, Mahieux PY, Refait P, Jeannin M, Sablé S. New Biocalcifying Marine Bacterial Strains Isolated from Calcareous Deposits and Immediate Surroundings. Microorganisms 2021;10:76. [PMID: 35056526 DOI: 10.3390/microorganisms10010076] [Reference Citation Analysis]
2 Angeli A, Tanini D, Capperucci A, Supuran CT. First evaluation of organotellurium derivatives as carbonic anhydrase I, II, IV, VII and IX inhibitors. Bioorganic Chemistry 2018;76:268-72. [DOI: 10.1016/j.bioorg.2017.12.010] [Cited by in Crossref: 30] [Cited by in F6Publishing: 27] [Article Influence: 7.5] [Reference Citation Analysis]
3 Urbanski LJ, Bua S, Angeli A, Kuuslahti M, Hytönen VP, Supuran CT, Parkkila S. Sulphonamide inhibition profile of Staphylococcus aureus β-carbonic anhydrase. J Enzyme Inhib Med Chem 2020;35:1834-9. [PMID: 32972256 DOI: 10.1080/14756366.2020.1826942] [Cited by in F6Publishing: 2] [Reference Citation Analysis]
4 Del Prete S, De Luca V, Nocentini A, Scaloni A, Mastrolorenzo MD, Supuran CT, Capasso C. Anion Inhibition Studies of the Beta-Carbonic Anhydrase from Escherichia coli. Molecules 2020;25:E2564. [PMID: 32486444 DOI: 10.3390/molecules25112564] [Cited by in Crossref: 6] [Cited by in F6Publishing: 6] [Article Influence: 3.0] [Reference Citation Analysis]
5 Supuran CT, Capasso C. Biomedical applications of prokaryotic carbonic anhydrases. Expert Opin Ther Pat 2018;28:745-54. [PMID: 29973089 DOI: 10.1080/13543776.2018.1497161] [Cited by in Crossref: 38] [Cited by in F6Publishing: 46] [Article Influence: 9.5] [Reference Citation Analysis]
6 Angeli A, Alasmary FAS, Del Prete S, Osman SM, AlOthman Z, Donald WA, Capasso C, Supuran CT. The first activation study of a δ-carbonic anhydrase: TweCAδ from the diatom Thalassiosira weissflogii is effectively activated by amines and amino acids. J Enzyme Inhib Med Chem 2018;33:680-5. [PMID: 29536765 DOI: 10.1080/14756366.2018.1447570] [Cited by in Crossref: 12] [Cited by in F6Publishing: 13] [Article Influence: 3.0] [Reference Citation Analysis]
7 Del Prete S, Nocentini A, Supuran CT, Capasso C. Bacterial ι-carbonic anhydrase: a new active class of carbonic anhydrase identified in the genome of the Gram-negative bacterium Burkholderia territorii. J Enzyme Inhib Med Chem 2020;35:1060-8. [PMID: 32314608 DOI: 10.1080/14756366.2020.1755852] [Cited by in Crossref: 23] [Cited by in F6Publishing: 29] [Article Influence: 23.0] [Reference Citation Analysis]
8 Angeli A, Abbas G, Del Prete S, Carta F, Capasso C, Supuran CT. Acyl selenoureido benzensulfonamides show potent inhibitory activity against carbonic anhydrases from the pathogenic bacterium Vibrio cholerae. Bioorganic Chemistry 2017;75:170-2. [DOI: 10.1016/j.bioorg.2017.09.016] [Cited by in Crossref: 15] [Cited by in F6Publishing: 13] [Article Influence: 3.0] [Reference Citation Analysis]
9 Ali M, Angeli A, Bozdag M, Carta F, Capasso C, Farooq U, Supuran CT. Benzylaminoethylureido-Tailed Benzenesulfonamides Show Potent Inhibitory Activity against Bacterial Carbonic Anhydrases. ChemMedChem 2020;15:2444-7. [PMID: 32966693 DOI: 10.1002/cmdc.202000680] [Cited by in Crossref: 1] [Article Influence: 0.5] [Reference Citation Analysis]
10 Supuran CT, Capasso C. An Overview of the Bacterial Carbonic Anhydrases. Metabolites 2017;7:E56. [PMID: 29137134 DOI: 10.3390/metabo7040056] [Cited by in Crossref: 87] [Cited by in F6Publishing: 79] [Article Influence: 17.4] [Reference Citation Analysis]
11 Haapanen S, Bua S, Kuuslahti M, Parkkila S, Supuran CT. Cloning, Characterization and Anion Inhibition Studies of a β-Carbonic Anhydrase from the Pathogenic Protozoan Entamoeba histolytica. Molecules 2018;23:E3112. [PMID: 30486513 DOI: 10.3390/molecules23123112] [Cited by in Crossref: 4] [Cited by in F6Publishing: 5] [Article Influence: 1.0] [Reference Citation Analysis]
12 Supuran CT, Capasso C. Antibacterial carbonic anhydrase inhibitors: an update on the recent literature. Expert Opin Ther Pat 2020;30:963-82. [PMID: 32806966 DOI: 10.1080/13543776.2020.1811853] [Cited by in Crossref: 9] [Cited by in F6Publishing: 12] [Article Influence: 4.5] [Reference Citation Analysis]
13 Bua S, Haapanen S, Kuuslahti M, Parkkila S, Supuran CT. Sulfonamide Inhibition Studies of a New β-Carbonic Anhydrase from the Pathogenic Protozoan Entamoeba histolytica. Int J Mol Sci 2018;19:E3946. [PMID: 30544802 DOI: 10.3390/ijms19123946] [Cited by in Crossref: 4] [Cited by in F6Publishing: 4] [Article Influence: 1.0] [Reference Citation Analysis]
14 Urbański LJ, Di Fiore A, Azizi L, Hytönen VP, Kuuslahti M, Buonanno M, Monti SM, Angeli A, Zolfaghari Emameh R, Supuran CT, De Simone G, Parkkila S. Biochemical and structural characterisation of a protozoan beta-carbonic anhydrase from Trichomonas vaginalis. J Enzyme Inhib Med Chem 2020;35:1292-9. [PMID: 32515610 DOI: 10.1080/14756366.2020.1774572] [Cited by in Crossref: 2] [Cited by in F6Publishing: 7] [Article Influence: 2.0] [Reference Citation Analysis]
15 Peperidou A, Bua S, Bozdag M, Hadjipavlou-Litina D, Supuran CT. Novel 6- and 7-Substituted Coumarins with Inhibitory Action against Lipoxygenase and Tumor-Associated Carbonic Anhydrase IX. Molecules 2018;23:E153. [PMID: 29329232 DOI: 10.3390/molecules23010153] [Cited by in Crossref: 14] [Cited by in F6Publishing: 12] [Article Influence: 3.5] [Reference Citation Analysis]
16 Rasti B, Mazraedoost S, Panahi H, Falahati M, Attar F. New insights into the selective inhibition of the β-carbonic anhydrases of pathogenic bacteria Burkholderia pseudomallei and Francisella tularensis: a proteochemometrics study. Mol Divers 2019;23:263-73. [PMID: 30120657 DOI: 10.1007/s11030-018-9869-5] [Cited by in Crossref: 2] [Article Influence: 0.5] [Reference Citation Analysis]
17 Angeli A, Ferraroni M, Pinteala M, Maier SS, Simionescu BC, Carta F, Del Prete S, Capasso C, Supuran CT. Crystal Structure of a Tetrameric Type II β-Carbonic Anhydrase from the Pathogenic Bacterium Burkholderia pseudomallei. Molecules 2020;25:E2269. [PMID: 32408533 DOI: 10.3390/molecules25102269] [Cited by in Crossref: 2] [Cited by in F6Publishing: 5] [Article Influence: 1.0] [Reference Citation Analysis]
18 Angeli A, Del Prete S, Pinteala M, Maier SS, Donald WA, Simionescu BC, Capasso C, Supuran CT. The first activation study of the β-carbonic anhydrases from the pathogenic bacteria Brucella suis and Francisella tularensis with amines and amino acids. J Enzyme Inhib Med Chem 2019;34:1178-85. [PMID: 31282230 DOI: 10.1080/14756366.2019.1630617] [Cited by in Crossref: 2] [Cited by in F6Publishing: 4] [Article Influence: 0.7] [Reference Citation Analysis]
19 Vullo D, Del Prete S, Osman SM, Alasmary FAS, AlOthman Z, Donald WA, Capasso C, Supuran CT. Comparison of the amine/amino acid activation profiles of the β- and γ-carbonic anhydrases from the pathogenic bacterium Burkholderia pseudomallei. J Enzyme Inhib Med Chem 2018;33:25-30. [PMID: 29098887 DOI: 10.1080/14756366.2017.1387544] [Cited by in Crossref: 7] [Cited by in F6Publishing: 13] [Article Influence: 1.4] [Reference Citation Analysis]
20 Akdemir A, Angeli A, Göktaş F, Eraslan Elma P, Karalı N, Supuran CT. Novel 2-indolinones containing a sulfonamide moiety as selective inhibitors of candida β-carbonic anhydrase enzyme. J Enzyme Inhib Med Chem 2019;34:528-31. [PMID: 30724625 DOI: 10.1080/14756366.2018.1564045] [Cited by in Crossref: 7] [Cited by in F6Publishing: 7] [Article Influence: 2.3] [Reference Citation Analysis]
21 Supuran CT. Special Issue: Sulfonamides. Molecules 2017;22:E1642. [PMID: 28961201 DOI: 10.3390/molecules22101642] [Cited by in Crossref: 33] [Cited by in F6Publishing: 28] [Article Influence: 6.6] [Reference Citation Analysis]