Zobrazeno 1 - 10
of 50
pro vyhledávání: '"Claudia Temperini"'
Autor:
Claudiu T. Supuran, Francesca Benedini, Francesco Mincione, Alessandro Cecchi, Claudia Temperini, Ilaria Pacileo, Giuseppe Formicola, Andrea Scozzafava, Emanuela Masini, Stefano Biondi
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 21:3216-3221
Several aromatic/heterocyclic sulfonamide scaffolds have been used to synthesize compounds incorporating NO-donating moieties of the nitrate ester type, which have been investigated for the inhibition of five physiologically relevant human carbonic a
Autor:
Andrea Scozzafava, Claudia Temperini, Claudiu T. Supuran, Marc A. Ilies, Daniela Vullo, Khyati Dave
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 21:2764-2768
The 2,4,6-trimethylpyridinium derivative of histamine is an effective activator of the zinc enzyme carbonic anhydrase (CA, EC 4.2.1.1). However, unlike other CA activators, which bind at the entrance of the active site cavity, an X-ray crystal struct
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 20:474-478
Trithiocarbonate (CS32-) inhibits with low micromolar affinities several mammalian carbonic anhydrases, CAs, EC 4.2.1.1 [Innocenti et al., Bioorg. Med. Chem. Lett. 2009, 19, 1855]. Here we report the X-ray crystal structure of the hCA II-trithiocarbo
Autor:
Wesley K. M. Chong, Steele Rebecca, Francesca Benedini, Alessandro Cecchi, Ranjan Jagath Rajapakse, Stefano Biondi, Claudia Temperini, Daniela Miglietta, Claudiu T. Supuran, Laura Carzaniga, Valentina Borghi, Francesco Impagnatiello
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 19:6565-6570
Novel bi-functional compounds with a nitric oxide (NO)-releasing moiety bound to a dorzolamide scaffold were investigated. Several compounds were synthesized and their activity as selective carbonic anhydrase inhibitors (CAI) evaluated in vitro on re
Autor:
Claudiu T. Supuran, Rebecca A. Hall, Claudia Temperini, Alfonso Maresca, Fritz A. Mühlschlegel, Andrea Scozzafava, Letizia Crocetti
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 19:1371-1375
A sulfonamide derivative of the antihelmintic drug thiabendazole was prepared and investigated for inhibition of the zinc enzyme carbonic anhydrase CA (EC 4.2.1.1). Mammalian isoforms CA I–XIV and the nematode enzyme of Caenorhabditis elegans CAH-4
Non-Zinc Mediated Inhibition of Carbonic Anhydrases: Coumarins Are a New Class of Suicide Inhibitors
Autor:
Ngoc B. Pham, Alfonso Maresca, Claudia Temperini, Sally-Ann Poulsen, Ronald J. Quinn, Andrea Scozzafava, Claudiu T. Supuran, Hoan Vu
Publikováno v:
Journal of the American Chemical Society. 131:3057-3062
The X-ray crystal structure of the adduct between the zinc metalloenzyme carbonic anhydrase II (CA, EC 4.2.1.1) with the recently discovered natural product coumarin derivative 6-(1S-hydroxy-3-methylbutyl)-7-methoxy-2H-chromen-2-one showed the coumar
Publikováno v:
Bioorganic & Medicinal Chemistry. 16:8373-8378
An activation study of mammalian carbonic anhydrase (CA, EC 4.2.1.1) isoforms I–XIV with d - and l -tryptophan has been performed both by means of kinetic and X-ray crystallographic techniques. These compounds show a time dependent activity against
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 18:4282-4286
The new antitumor sulfamate EMD 486019 was investigated for its interaction with twelve catalytically active mammalian carbonic anhydrase (CA, EC 4.2.1.1) isozymes, hCA I – XIV. Similarly to 667-Coumate, a structurally related compound in phase II
Publikováno v:
Current Pharmaceutical Design. 14:708-715
The activation mechanism of Carbonic Anhydrase was recently explained using kinetic, spectroscopic and X-ray techniques. It has been demonstrated that the activators molecules (CAAs) bind at the entrance of the enzyme active-site facilitating the rat
Autor:
Alessandro Cecchi, Paul Wentworth, Claudiu T. Supuran, Claudia Temperini, G. Michael Blackburn, Nicholas A. Boyle, Andrea Scozzafava, Jaime Escribano Cabeza
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 18:999-1005
2-N,N-Dimethylamino-1,3,4-thiadiazole-5-methanesulfonamide was tested for its interaction with the 12 catalytically active mammalian carbonic anhydrase (CA, EC 4.2.1.1) isozymes, CA I–XIV. The compound is a potent inhibitor of CA IV, VII, IX, XII,