Results 11 to 20 of about 2,875,268 (275)

Multivalent Carbonic Anhydrases Inhibitors [PDF]

open access: yesInternational Journal of Molecular Sciences, 2019
Biomolecular recognition using a multivalent strategy has been successfully applied, this last decade on several biological targets, especially carbohydrate-processing enzymes, proteases, and phosphorylases.
F. Carta, P. Dumy, C. Supuran, J. Winum
semanticscholar   +4 more sources

Acipimox inhibits human carbonic anhydrases [PDF]

open access: yesJournal of Enzyme Inhibition and Medicinal Chemistry, 2022
Acipimox, a nicotinic acid derivative in clinical use for the treatment of hyperlipidaemia, incorporates a free carboxylic acid and an N-oxide moiety, functionalities known to interact with the metalloenzyme carbonic anhydrase (CA, EC 4.2.1.1) and ...
Mattia Mori, Claudiu T. Supuran
doaj   +2 more sources

1,2,3-Benzoxathiazine-2,2-dioxides – effective inhibitors of human carbonic anhydrases [PDF]

open access: yesJournal of Enzyme Inhibition and Medicinal Chemistry, 2023
A series of 1,2,3-benzoxathiazine-2,2-dioxides possessing various substituents in the 5, 7, or 8 position was obtained from corresponding 2-hydroxybenzaldehydes in their reaction with sulfamoyl chloride.
Jekaterina Ivanova   +4 more
doaj   +2 more sources

Activation of β- and γ-carbonic anhydrases from pathogenic bacteria with tripeptides

open access: yesJournal of Enzyme Inhibition and Medicinal Chemistry, 2018
Six tripeptides incorporating acidic amino acid residues were prepared for investigation as activators of β- and γ-carbonic anhydrases (CAs, EC 4.2.1.1) from the pathogenic bacteria Vibrio cholerae, Mycobacterium tuberculosis, and Burkholderia ...
Azzurra Stefanucci   +8 more
doaj   +2 more sources

Polyamines and α-Carbonic Anhydrases [PDF]

open access: yesMolecules, 2016
Natural products represent a straightforward source for molecular structures bearing a vast array of chemical features and potentially useful for biomedical purposes.
Andrea Scozzafava   +2 more
doaj   +3 more sources

Carbonic Anhydrases: Different Active Sites, Same Metal Selectivity Rules [PDF]

open access: yesMolecules
Carbonic anhydrases are mononuclear metalloenzymes catalyzing the reversible hydration of carbon dioxide in organisms belonging to all three domains of life.
Nikoleta Kircheva   +2 more
doaj   +2 more sources

Coral Carbonic Anhydrases: Regulation by Ocean Acidification

open access: yesMarine Drugs, 2016
Global change is a major threat to the oceans, as it implies temperature increase and acidification. Ocean acidification (OA) involving decreasing pH and changes in seawater carbonate chemistry challenges the capacity of corals to form their skeletons ...
Didier Zoccola   +5 more
doaj   +2 more sources

Inhibition of pathogenic bacterial carbonic anhydrases by monothiocarbamates [PDF]

open access: yesJournal of Enzyme Inhibition and Medicinal Chemistry, 2023
Carbonic anhydrases (CAs) from the pathogenic bacteria Nesseria gonorrhoeae and vancomycin-resistant enterococci (VRE) have recently been validated as antibacterial drug targets. Here we explored the inhibition of the α-CA from N.
Simone Giovannuzzi   +9 more
doaj   +2 more sources

Investigation on N-Aryl-2-(4-sulfamoylphenyl)hydrazine-1-carbothioamide as Human Carbonic Anhydrases Inhibitors [PDF]

open access: yesPharmaceuticals
Background: Among the 15 human (h) carbonic anhydrase (CA; EC 4.2.1.1) isoforms, hCA IX and XII are particularly important due to their roles in tumor cell growth and survival, identifying them as promising targets for anticancer therapy.
Morteza Abdoli   +7 more
doaj   +2 more sources

Thermostable Carbonic Anhydrases in Biotechnological Applications

open access: yesInternational Journal of Molecular Sciences, 2015
Carbonic anhydrases are ubiquitous metallo-enzymes which catalyze the reversible hydration of carbon dioxide in bicarbonate ions and protons. Recent years have seen an increasing interest in the utilization of these enzymes in CO2 capture and storage ...
Simona Maria Monti   +2 more
exaly   +2 more sources

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