Works by Capasso, Clemente
Results: 146
Effect of a recombinant manganese superoxide dismutase on prevention of contrast-induced acute kidney injury.
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- Clinical & Experimental Nephrology, 2014, v. 18, n. 3, p. 424, doi. 10.1007/s10157-013-0828-2
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Susceptibility to Heavy Metals and Cadmium Accumulation in Aerobic and Anaerobic Thermophilic Microorganisms Isolated from Deep-Sea Hydrothermal Vents.
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- Current Microbiology, 2000, v. 41, n. 3, p. 201, doi. 10.1007/s00284431056
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A comprehensive investigation of the anion inhibition profile of a β-carbonic anhydrase from Acinetobacter baumannii for crafting innovative antimicrobial treatments.
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- Journal of Enzyme Inhibition & Medicinal Chemistry, 2024, v. 39, n. 1, p. 1, doi. 10.1080/14756366.2024.2372731
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Cloning, expression, and purification of an α-carbonic anhydrase from Toxoplasma gondii to unveil its kinetic parameters and anion inhibition profile.
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- Journal of Enzyme Inhibition & Medicinal Chemistry, 2024, v. 39, n. 1, p. 1, doi. 10.1080/14756366.2024.2346523
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Benzenesulfonamide derivatives as Vibrio cholerae carbonic anhydrases inhibitors: a computational-aided insight in the structural rigidity-activity relationships.
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- Journal of Enzyme Inhibition & Medicinal Chemistry, 2023, v. 38, n. 1, p. 1, doi. 10.1080/14756366.2023.2201402
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Inhibition studies with simple and complex (in)organic anions of the γ-carbonic anhydrase from Mammaliicoccus (Staphylococcus) sciuri, MscCAγ.
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- Journal of Enzyme Inhibition & Medicinal Chemistry, 2023, v. 38, n. 1, p. 1, doi. 10.1080/14756366.2023.2173748
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Novel thiazolone-benzenesulphonamide inhibitors of human and bacterial carbonic anhydrases.
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- Journal of Enzyme Inhibition & Medicinal Chemistry, 2023, v. 38, n. 1, p. 1, doi. 10.1080/14756366.2022.2163243
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The gram-negative bacterium Escherichia coli as a model for testing the effect of carbonic anhydrase inhibition on bacterial growth.
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- Journal of Enzyme Inhibition & Medicinal Chemistry, 2022, v. 37, n. 1, p. 2092, doi. 10.1080/14756366.2022.2101644
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Inhibition studies of bacterial α-carbonic anhydrases with phenols.
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- Journal of Enzyme Inhibition & Medicinal Chemistry, 2022, v. 37, n. 1, p. 666, doi. 10.1080/14756366.2022.2038592
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Heterologous expression and biochemical characterisation of the recombinant β-carbonic anhydrase (MpaCA) from the warm-blooded vertebrate pathogen malassezia pachydermatis.
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- Journal of Enzyme Inhibition & Medicinal Chemistry, 2022, v. 37, n. 1, p. 62, doi. 10.1080/14756366.2021.1994559
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Coumarins inhibit η-class carbonic anhydrase from Plasmodium falciparum.
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- Journal of Enzyme Inhibition & Medicinal Chemistry, 2022, v. 37, n. 1, p. 680, doi. 10.1080/14756366.2022.2036986
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Coumarins effectively inhibit bacterial a-carbonic anhydrases.
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- Journal of Enzyme Inhibition & Medicinal Chemistry, 2022, v. 37, n. 1, p. 333, doi. 10.1080/14756366.2021.2012174
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Activation studies with amino acids and amines of a β-carbonic anhydrase from Mammaliicoccus (Staphylococcus) sciuri previously annotated as Staphylococcus aureus (SauBCA) carbonic anhydrase.
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- Journal of Enzyme Inhibition & Medicinal Chemistry, 2022, v. 37, n. 1, p. 2786, doi. 10.1080/14756366.2022.2131780
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A comparative study of carbonic anhydrase activity in lymphocytes from colorectal cancer tissues and adjacent healthy counterparts.
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- Journal of Enzyme Inhibition & Medicinal Chemistry, 2022, v. 37, n. 1, p. 1651, doi. 10.1080/14756366.2022.2085694
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An overview on the recently discovered iota-carbonic anhydrases.
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- Journal of Enzyme Inhibition & Medicinal Chemistry, 2021, v. 36, n. 1, p. 1988, doi. 10.1080/14756366.2021.1972995
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Is carbonic anhydrase inhibition useful as a complementary therapy of Covid-19 infection?
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- Journal of Enzyme Inhibition & Medicinal Chemistry, 2021, v. 36, n. 1, p. 1230, doi. 10.1080/14756366.2021.1924165
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Effect of amino acids and amines on the activity of the recombinant ι-carbonic anhydrase from the Gram-negative bacterium Burkholderia territorii.
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- Journal of Enzyme Inhibition & Medicinal Chemistry, 2021, v. 36, n. 1, p. 1000, doi. 10.1080/14756366.2021.1919891
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Reconsidering anion inhibitors in the general context of drug design studies of modulators of activity of the classical enzyme carbonic anhydrase.
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- Journal of Enzyme Inhibition & Medicinal Chemistry, 2021, v. 36, n. 1, p. 561, doi. 10.1080/14756366.2021.1882453
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Evaluating the efficiency of enzyme accelerated CO<sub>2</sub> capture: chemical kinetics modelling for interpreting measurement results.
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- Journal of Enzyme Inhibition & Medicinal Chemistry, 2021, v. 36, n. 1, p. 393, doi. 10.1080/14756366.2020.1864631
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Anion inhibition studies of the Zn(II)-bound ι-carbonic anhydrase from the Gram-negative bacterium Burkholderia territorii.
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- Journal of Enzyme Inhibition & Medicinal Chemistry, 2021, v. 36, n. 1, p. 372, doi. 10.1080/14756366.2020.1867122
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Toxicity evaluation of sulfamides and coumarins that efficiently inhibit human carbonic anhydrases.
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- Journal of Enzyme Inhibition & Medicinal Chemistry, 2020, v. 35, n. 1, p. 1765, doi. 10.1080/14756366.2020.1822829
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Escherichia coliγ-carbonic anhydrase: characterisation and effects of simple aromatic/heterocyclic sulphonamide inhibitors.
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- Journal of Enzyme Inhibition & Medicinal Chemistry, 2020, v. 35, n. 1, p. 1545, doi. 10.1080/14756366.2020.1800670
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Synthesis, computational studies and assessment of in vitro inhibitory activity of umbelliferon-based compounds against tumour-associated carbonic anhydrase isoforms IX and XII.
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- Journal of Enzyme Inhibition & Medicinal Chemistry, 2020, v. 35, n. 1, p. 1442, doi. 10.1080/14756366.2020.1786821
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Activation studies of the β-carbonic anhydrases from Escherichia coli with amino acids and amines.
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- Journal of Enzyme Inhibition & Medicinal Chemistry, 2020, v. 35, n. 1, p. 1379, doi. 10.1080/14756366.2020.1781845
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Carbonic anhydrase modulation of emotional memory. Implications for the treatment of cognitive disorders.
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- Journal of Enzyme Inhibition & Medicinal Chemistry, 2020, v. 35, n. 1, p. 1206, doi. 10.1080/14756366.2020.1766455
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Bacterial ι-carbonic anhydrase: a new active class of carbonic anhydrase identified in the genome of the Gram-negative bacterium Burkholderia territorii.
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- Journal of Enzyme Inhibition & Medicinal Chemistry, 2020, v. 35, n. 1, p. 1060, doi. 10.1080/14756366.2020.1755852
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Use of an immobilised thermostable α-CA (SspCA) for enhancing the metabolic efficiency of the freshwater green microalga Chlorella sorokiniana.
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- Journal of Enzyme Inhibition & Medicinal Chemistry, 2020, v. 35, n. 1, p. 913, doi. 10.1080/14756366.2020.1746785
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Activation studies of the β-carbonic anhydrases from Malassezia restricta with amines and amino acids.
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- Journal of Enzyme Inhibition & Medicinal Chemistry, 2020, v. 35, n. 1, p. 824, doi. 10.1080/14756366.2020.1743284
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Inhibition survey with phenolic compounds against the δ- and η-class carbonic anhydrases from the marine diatom thalassiosira weissflogii and protozoan Plasmodium falciparum.
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- Journal of Enzyme Inhibition & Medicinal Chemistry, 2020, v. 35, n. 1, p. 377, doi. 10.1080/14756366.2019.1706089
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Carbonic anhydrase IX as a novel candidate in liquid biopsy.
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- Journal of Enzyme Inhibition & Medicinal Chemistry, 2020, v. 35, n. 1, p. 255, doi. 10.1080/14756366.2019.1697251
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Plasmatic exosomes from prostate cancer patients show increased carbonic anhydrase IX expression and activity and low pH.
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- Journal of Enzyme Inhibition & Medicinal Chemistry, 2020, v. 35, n. 1, p. 280, doi. 10.1080/14756366.2019.1697249
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Phosphonamidates are the first phosphorus-based zinc binding motif to show inhibition of β-class carbonic anhydrases from bacteria, fungi, and protozoa.
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- Journal of Enzyme Inhibition & Medicinal Chemistry, 2020, v. 35, n. 1, p. 59, doi. 10.1080/14756366.2019.1681987
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Exploring new structural features of the 4-[(3-methyl-4-aryl-2,3-dihydro-1,3-thiazol-2-ylidene)amino]benzenesulphonamide scaffold for the inhibition of human carbonic anhydrases.
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- Journal of Enzyme Inhibition & Medicinal Chemistry, 2019, v. 34, n. 1, p. 1526, doi. 10.1080/14756366.2019.1654470
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The first activation study of the β-carbonic anhydrases from the pathogenic bacteria Brucella suis and Francisella tularensis with amines and amino acids.
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- Journal of Enzyme Inhibition & Medicinal Chemistry, 2019, v. 34, n. 1, p. 1178, doi. 10.1080/14756366.2019.1630617
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Seeking new approach for therapeutic treatment of cholera disease via inhibition of bacterial carbonic anhydrases: experimental and theoretical studies for sixteen benzenesulfonamide derivatives.
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- Journal of Enzyme Inhibition & Medicinal Chemistry, 2019, v. 34, n. 1, p. 1186, doi. 10.1080/14756366.2019.1618292
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Thermostability enhancement of the α-carbonic anhydrase from Sulfurihydrogenibium yellowstonense by using the anchoring-and-self-labelling-protein-tag system (ASL<sup>tag</sup>).
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- Journal of Enzyme Inhibition & Medicinal Chemistry, 2019, v. 34, n. 1, p. 946, doi. 10.1080/14756366.2019.1605991
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Inhibition of α-, β-, γ-, δ-, ζ- and η-class carbonic anhydrases from bacteria, fungi, algae, diatoms and protozoans with famotidine.
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- Journal of Enzyme Inhibition & Medicinal Chemistry, 2019, v. 34, n. 1, p. 644, doi. 10.1080/14756366.2019.1571273
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Phaeodactylum tricornutum as a model organism for testing the membrane penetrability of sulphonamide carbonic anhydrase inhibitors.
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- Journal of Enzyme Inhibition & Medicinal Chemistry, 2019, v. 34, n. 1, p. 510, doi. 10.1080/14756366.2018.1559840
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An AGT-based protein-tag system for the labelling and surface immobilization of enzymes on E. coli outer membrane.
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- Journal of Enzyme Inhibition & Medicinal Chemistry, 2019, v. 34, n. 1, p. 490, doi. 10.1080/14756366.2018.1559161
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Inhibition of bacterial α-, β- and γ-class carbonic anhydrases with selenazoles incorporating benzenesulfonamide moieties.
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- Journal of Enzyme Inhibition & Medicinal Chemistry, 2019, v. 34, n. 1, p. 244, doi. 10.1080/14756366.2018.1547287
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Prostate cancer cells and exosomes in acidic condition show increased carbonic anhydrase IX expression and activity.
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- Journal of Enzyme Inhibition & Medicinal Chemistry, 2019, v. 34, n. 1, p. 272, doi. 10.1080/14756366.2018.1538980
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Identification and characterization of the α-CA in the outer membrane vesicles produced by Helicobacter pylori.
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- Journal of Enzyme Inhibition & Medicinal Chemistry, 2019, v. 34, n. 1, p. 189, doi. 10.1080/14756366.2018.1539716
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Discovering a new class of antifungal agents that selectively inhibits microbial carbonic anhydrases.
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- Journal of Enzyme Inhibition & Medicinal Chemistry, 2018, v. 33, n. 1, p. 1537, doi. 10.1080/14756366.2018.1516652
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Inhibition of α-, β-, γ-, and δ-carbonic anhydrases from bacteria and diatoms with N′-aryl-N-hydroxy-ureas.
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- Journal of Enzyme Inhibition & Medicinal Chemistry, 2018, v. 33, n. 1, p. 1194, doi. 10.1080/14756366.2018.1490733
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Activation of β- and γ-carbonic anhydrases from pathogenic bacteria with tripeptides.
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- Journal of Enzyme Inhibition & Medicinal Chemistry, 2018, v. 33, n. 1, p. 945, doi. 10.1080/14756366.2018.1468530
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Synthesis of novel benzenesulfamide derivatives with inhibitory activity against human cytosolic carbonic anhydrase I and II and Vibrio cholerae α- and β-class enzymes.
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- Journal of Enzyme Inhibition & Medicinal Chemistry, 2018, v. 33, n. 1, p. 1125, doi. 10.1080/14756366.2018.1467901
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Mono- and di-thiocarbamate inhibition studies of the δ-carbonic anhydrase TweCAδ from the marine diatom Thalassiosira weissflogii.
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- Journal of Enzyme Inhibition & Medicinal Chemistry, 2018, v. 33, n. 1, p. 707, doi. 10.1080/14756366.2018.1450400
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The first activation study of a δ-carbonic anhydrase: TweCAδ from the diatom Thalassiosira weissflogii is effectively activated by amines and amino acids.
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- Journal of Enzyme Inhibition & Medicinal Chemistry, 2018, v. 33, n. 1, p. 680, doi. 10.1080/14756366.2018.1447570
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Activation studies with amines and amino acids of the β-carbonic anhydrase encoded by the Rv3273 gene from the pathogenic bacterium Mycobacterium tuberculosis.
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- Journal of Enzyme Inhibition & Medicinal Chemistry, 2018, v. 33, n. 1, p. 364, doi. 10.1080/14756366.2017.1422250
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Activation studies of the α- and β-carbonic anhydrases from the pathogenic bacterium Vibrio cholerae with amines and amino acids.
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- Journal of Enzyme Inhibition & Medicinal Chemistry, 2018, v. 33, n. 1, p. 227, doi. 10.1080/14756366.2017.1412316
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