Skip Header

1 - 25 of 82 results for author:"Scozzafava A." in Literature citations

Page of 4 | Next »

to top of page·  

Results Customize

› Repeat search in UniProtKB (32)

The generation of a 1-hydroxy-2-naphthoate 1,2-dioxygenase by single point mutations of salicylate 1,2-dioxygenase--rational design of mutants and the crystal structures of the A85H and W104Y variants.

Ferraroni M., Steimer L., Matera I., Burger S., Scozzafava A., Stolz A., Briganti F.

J. Struct. Biol. 180:563-571(2012) · UniProtKB (1)

Reaction intermediates and redox state changes in a blue laccase from Steccherinum ochraceum observed by crystallographic high/low X-ray dose experiments.

Ferraroni M., Matera I., Chernykh A., Kolomytseva M., Golovleva L.A., Scozzafava A., Briganti F.

J. Inorg. Biochem. 111:203-209(2012) · UniProtKB (1)

Dithiocarbamates strongly inhibit carbonic anhydrases and show antiglaucoma action in vivo.

Carta F., Aggarwal M., Maresca A., Scozzafava A., McKenna R., Masini E., Supuran C.T.

J. Med. Chem. 55:1721-1730(2012) · Mapped (1)

Dithiocarbamates: a new class of carbonic anhydrase inhibitors. Crystallographic and kinetic investigations.

Carta F., Aggarwal M., Maresca A., Scozzafava A., McKenna R., Supuran C.T.

Chem. Commun. (Camb.) 48:1868-1870(2012) · Mapped (1)

Dithiocarbamates are strong inhibitors of the beta-class fungal carbonic anhydrases from Cryptococcus neoformans, Candida albicans and Candida glabrata.

Monti S.M., Maresca A., Viparelli F., Carta F., De Simone G., Muhlschlegel F.A., Scozzafava A., Supuran C.T.

Bioorg. Med. Chem. Lett. 22:859-862(2012)

Crystal structures of salicylate 1,2-dioxygenase-substrates adducts: A step towards the comprehension of the structural basis for substrate selection in class III ring cleaving dioxygenases.

Ferraroni M., Matera I., Steimer L., Burger S., Scozzafava A., Stolz A., Briganti F.

J. Struct. Biol. 177:431-438(2012) · UniProtKB (1)

Conformational variability of different sulfonamide inhibitors with thienyl-acetamido moieties attributes to differential binding in the active site of cytosolic human carbonic anhydrase isoforms.

Biswas S., Aggarwal M., Guzel O., Scozzafava A., McKenna R., Supuran C.T.

Bioorg. Med. Chem. 19:3732-3738(2011) · Mapped (1)

Synthesis and crystallographic analysis of new sulfonamides incorporating NO-donating moieties with potent antiglaucoma action.

Mincione F., Benedini F., Biondi S., Cecchi A., Temperini C., Formicola G., Pacileo I., Scozzafava A., Masini E., Supuran C.T.

Bioorg. Med. Chem. Lett. 21:3216-3221(2011) · Mapped (1)

Sulfonamides incorporating 1,3,5-triazine moieties selectively and potently inhibit carbonic anhydrase transmembrane isoforms IX, XII and XIV over cytosolic isoforms I and II: Solution and X-ray crystallographic studies.

Carta F., Garaj V., Maresca A., Wagner J., Avvaru B.S., Robbins A.H., Scozzafava A., McKenna R., Supuran C.T.

Bioorg. Med. Chem. 19:3105-3119(2011) · Mapped (1)

Anticonvulsant 4-aminobenzenesulfonamide derivatives with branched-alkylamide moieties: X-ray crystallography and inhibition studies of human carbonic anhydrase isoforms I, II, VII, and XIV.

Hen N., Bialer M., Yagen B., Maresca A., Aggarwal M., Robbins A.H., McKenna R., Scozzafava A., Supuran C.T.

J. Med. Chem. 54:3977-3981(2011) · Mapped (1)

Selective hydrophobic pocket binding observed within the carbonic anhydrase II active site accommodate different 4-substituted-ureido-benzenesulfonamides and correlate to inhibitor potency.

Pacchiano F., Aggarwal M., Avvaru B.S., Robbins A.H., Scozzafava A., McKenna R., Supuran C.T.

Chem. Commun. (Camb.) 46:8371-8373(2010) · Mapped (1)

Characterization of the first beta-class carbonic anhydrase from an arthropod (Drosophila melanogaster) and phylogenetic analysis of beta-class carbonic anhydrases in invertebrates.

Syrjanen L., Tolvanen M., Hilvo M., Olatubosun A., Innocenti A., Scozzafava A., Leppiniemi J., Niederhauser B., Hytonen V.P., Gorr T.A. et al.

BMC Biochem. 11:28-28(2010) · Mapped (3)

Carbonic anhydrase inhibitors. The X-ray crystal structure of human isoform II in adduct with an adamantyl analogue of acetazolamide resides in a less utilized binding pocket than most hydrophobic inhibitors.

Avvaru B.S., Wagner J.M., Maresca A., Scozzafava A., Robbins A.H., Supuran C.T., McKenna R.

Bioorg. Med. Chem. Lett. 20:4376-4381(2010) · Mapped (1)

Coumarinyl-substituted sulfonamides strongly inhibit several human carbonic anhydrase isoforms: solution and crystallographic investigations.

Wagner J., Avvaru B.S., Robbins A.H., Scozzafava A., Supuran C.T., McKenna R.

Bioorg. Med. Chem. 18:4873-4878(2010) · Mapped (1)

Polyamines inhibit carbonic anhydrases by anchoring to the zinc-coordinated water molecule.

Carta F., Temperini C., Innocenti A., Scozzafava A., Kaila K., Supuran C.T.

J. Med. Chem. 53:5511-5522(2010) · Mapped (1)

Carbonic anhydrase inhibitors. The beta-carbonic anhydrases from the fungal pathogens Cryptococcus neoformans and Candida albicans are strongly inhibited by substituted-phenyl-1H-indole-5-sulfonamides.

Guzel O., Maresca A., Hall R.A., Scozzafava A., Mastrolorenzo A., Muhlschlegel F.A., Supuran C.T.

Bioorg. Med. Chem. Lett. 20:2508-2511(2010)

Catechol 1,2-dioxygenase from the Gram-positive Rhodococcus opacus 1CP: quantitative structure/activity relationship and the crystal structures of native enzyme and catechols adducts.

Matera I., Ferraroni M., Kolomytseva M., Golovleva L., Scozzafava A., Briganti F.

J. Struct. Biol. 170:548-564(2010) · Mapped (1)

The coumarin-binding site in carbonic anhydrase accommodates structurally diverse inhibitors: the antiepileptic lacosamide as an example and lead molecule for novel classes of carbonic anhydrase inhibitors.

Temperini C., Innocenti A., Scozzafava A., Parkkila S., Supuran C.T.

J. Med. Chem. 53:850-854(2010) · Mapped (1)

Carbonic anhydrase inhibitors. X-ray crystal studies of the carbonic anhydrase II-trithiocarbonate adduct--an inhibitor mimicking the sulfonamide and urea binding to the enzyme.

Temperini C., Scozzafava A., Supuran C.T.

Bioorg. Med. Chem. Lett. 20:474-478(2010) · Mapped (1)

Crystal structure of the catalytic domain of the tumor-associated human carbonic anhydrase IX.

Alterio V., Hilvo M., Di Fiore A., Supuran C.T., Pan P., Parkkila S., Scaloni A., Pastorek J., Pastorekova S., Pedone C. et al.

Proc. Natl. Acad. Sci. U.S.A. 106:16233-16238(2009) · UniProtKB (1) · Mapped (1)

Carbonic anhydrase inhibitors. Inhibition and homology modeling studies of the fungal beta-carbonic anhydrase from Candida albicans with sulfonamides.

Innocenti A., Hall R.A., Schlicker C., Scozzafava A., Steegborn C., Muhlschlegel F.A., Supuran C.T.

Bioorg. Med. Chem. 17:4503-4509(2009)

Discovery of low nanomolar and subnanomolar inhibitors of the mycobacterial beta-carbonic anhydrases Rv1284 and Rv3273.

Guzel O., Maresca A., Scozzafava A., Salman A., Balaban A.T., Supuran C.T.

J. Med. Chem. 52:4063-4067(2009) · UniProtKB (2)

Carbonic anhydrase inhibitors. Cloning, characterization, and inhibition studies of a new beta-carbonic anhydrase from Mycobacterium tuberculosis.

Nishimori I., Minakuchi T., Vullo D., Scozzafava A., Innocenti A., Supuran C.T.

J. Med. Chem. 52:3116-3120(2009)

Molecular cloning, characterization, and inhibition studies of the Rv1284 beta-carbonic anhydrase from Mycobacterium tuberculosis with sulfonamides and a sulfamate.

Minakuchi T., Nishimori I., Vullo D., Scozzafava A., Supuran C.T.

J. Med. Chem. 52:2226-2232(2009) · UniProtKB (2)

Carbonic anhydrase activators: activation of the beta-carbonic anhydrase Nce103 from the yeast Saccharomyces cerevisiae with amines and amino acids.

Isik S., Kockar F., Aydin M., Arslan O., Guler O.O., Innocenti A., Scozzafava A., Supuran C.T.

Bioorg. Med. Chem. Lett. 19:1662-1665(2009) · Mapped (1)

to top of page·

Page of 4 | Next »