Zobrazeno 1 - 10
of 27
pro vyhledávání: '"carbonic anhydrase VII"'
Autor:
Daria M. Monti, Giuseppina De Simone, Emma Langella, Claudiu T. Supuran, Anna Di Fiore, Simona M. Monti
Publikováno v:
Journal of Enzyme Inhibition and Medicinal Chemistry, Vol 32, Iss 1, Pp 5-12 (2017)
Carbonic anhydrases (CAs) III and VII are two cytosolic isoforms of the α-CA family which catalyze the physiological reaction of carbon dioxide hydration to bicarbonate and proton. Despite these two enzymes share a 49% sequence identity and present
Externí odkaz:
https://doaj.org/article/b0296123495643ca904d6b9b66899f58
Autor:
Alessio Nocentini, Elisabetta Orlandini, Elisa Nuti, Claudiu T. Supuran, Doretta Cuffaro, Susanna Nencetti, Lidia Ciccone, Armando Rossello
Publikováno v:
Journal of Enzyme Inhibition and Medicinal Chemistry, Vol 36, Iss 1, Pp 48-57 (2021)
Journal of Enzyme Inhibition and Medicinal Chemistry
article-version (VoR) Version of Record
Journal of Enzyme Inhibition and Medicinal Chemistry
article-version (VoR) Version of Record
The synthesis and carbonic anhydrase (CA; EC 4.2.1.1) activating effects of a series of oxime ether-based amino alcohols towards four human (h) CA isoforms expressed in human brain, hCA I, II, IV and VII, are described. Most investigated amino alcoho
Autor:
Katia D'Ambrosio, Fabrizio Carta, Simona Maria Monti, Andrea Angeli, Elena Lucarini, Giuseppina De Simone, Ozlem Akgul, Lorenzo Di Cesare Mannelli, Claudiu T. Supuran, Martina Buonanno, Carla Ghelardini
Publikováno v:
European Journal of Medicinal Chemistry. 227:113956
We report a series of compounds 1-17 derived from the antiepileptic drug Sulthiame (SLT) from which both the benzenesulfonamide and the sultam moiety were retained. All compounds were tested in vitro for their inhibition activity against the human (h
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Autor:
Emma Langella, Daria Maria Monti, Simona Maria Monti, Giuseppina De Simone, Claudiu T. Supuran, Anna Di Fiore
Publikováno v:
Journal of Enzyme Inhibition and Medicinal Chemistry, Vol 32, Iss 1, Pp 5-12 (2017)
Journal of Enzyme Inhibition and Medicinal Chemistry
Journal of Enzyme Inhibition and Medicinal Chemistry
Carbonic anhydrases (CAs) III and VII are two cytosolic isoforms of the α-CA family which catalyze the physiological reaction of carbon dioxide hydration to bicarbonate and proton. Despite these two enzymes share a 49% sequence identity and present
Autor:
Andrea Angeli, Giulio Poli, Claudiu T. Supuran, Tiziano Tuccinardi, Elena Lucarini, Lorenzo Di Cesare Mannelli, Carla Ghelardini, Murat Bozdag, Silvia Selleri, Fabrizio Carta, Jean-Yves Winum
Publikováno v:
Bioorganic Chemistry. 89:103033
Herein we report for the first time an efficient synthetic procedure for the preparation of N-aryl-N'-ureido-O-sulfamates (AUSs) as a new class of Carbonic Anhydrase Inhibitors (CAIs). The compounds were tested for the inhibition of several human (h)
Publikováno v:
Computational Biology and Chemistry. 35:50-56
The selectivity of a known arylsulfonamides inhibitor for two isozymes II and VII of human carbonic anhydrases (hCAs) was studied by homology modeling, molecular docking and molecular dynamics methods. The results show that the selectivity of the inh
Autor:
Stefano Agnello, Rosaria Gitto, Alba Chimirri, Stefania Ferro, Daniela Vullo, Claudiu T. Supuran
Publikováno v:
ChemMedChem. 5:823-826
Autor:
Claudiu T. Supuran, Catherine Michaux, Bernard Masereel, Johan Wouters, Anne Thiry, Jean-Michel Dogné
Publikováno v:
ChemMedChem. 2:1273-1280
Convulsions are common neurological disorders in clinical medicine and are triggered by several mechanisms. The enhancement of neuronal excitability can be related, among other factors, to GABAergic depolarization. Carbonic anhydrase (CA)VII contribu
Human carbonic anhydrase VII (hCA VII) is a cytosolic isoform belonging to the α-CA family that shows high carbon dioxide hydration activity. Recently, S -glutathionylation of two cysteine residues (i.e., Cys183 and Cys217) of this protein was obser
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5e731d7d0e0db77f161aba1b3d82bfab
https://doi.org/10.1016/b978-0-444-63258-6.00009-3
https://doi.org/10.1016/b978-0-444-63258-6.00009-3