Výsledky vyhledávání - "Mosè Rossi b"

The alpha-carbonic anhydrase from the thermophilic bacterium Sulfurihydrogenibium yellowstonense YO3AOP1 is highly susceptible to inhibition by sulfonamides

Autor: Daniela Vullo a, Viviana De Luca b, Andrea Scozzafava a, Vincenzo Carginale b, Mosè Rossi b, c, Claudiu T. Supurana d, Clemente Capasso b

Publikováno v: Bioorganic & medicinal chemistry (Online) (2012). doi:10.1016/j.bmc.2012.07.024
info:cnr-pdr/source/autori:Daniela Vullo a, Viviana De Luca b, Andrea Scozzafava a, Vincenzo Carginale b, Mosè Rossi b, c, Claudiu T. Supurana d, Clemente Capasso b/titolo:The alpha-carbonic anhydrase from the thermophilic bacterium Sulfurihydrogenibium yellowstonense YO3AOP1 is highly susceptible to inhibition by sulfonamides/doi:10.1016%2Fj.bmc.2012.07.024/rivista:Bioorganic & medicinal chemistry (Online)/anno:2012/pagina_da:/pagina_a:/intervallo_pagine:/volume
Bioorganic & Medicinal Chemistry
Bioorganic & Medicinal Chemistry; Vol 21

The ?-carbonic anhydrase (CA, EC 4.2.1.1) from the newly discovered thermophilic bacterium Sulfurihydrogenibium yellowstonense YO3AOP1 (SspCA) was investigated for its inhibition with a large series of sulfonamides and a sulfamate, the classical inhi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::67bc49253c3dfaff5541a39d40228782
https://doi.org/10.1016/j.bmc.2012.07.024

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The first activation study of a bacterial carbonic anhydrase (CA). The thermostable α-CA from Sulfurihydrogenibium yellowstonense YO3AOP1 is highly activated by amino acids and amines

Autor: Daniela Vullo a, Viviana De Luca b, Andrea Scozzafava a, Vincenzo Carginale b, Mosè Rossi b, c, Claudiu T. Supuran a, d, Clemente Capasso b

Publikováno v: Bioorganic and medicinal chemistry letters (Online) 22 (2012): 6324–6327. doi:10.1016/j.bmcl.2012.08.088
info:cnr-pdr/source/autori:Daniela Vullo a, Viviana De Luca b, Andrea Scozzafava a, Vincenzo Carginale b, Mosè Rossi b, c, Claudiu T. Supuran a, d, Clemente Capasso b,/titolo:The first activation study of a bacterial carbonic anhydrase (CA). The thermostable ?-CA from Sulfurihydrogenibium yellowstonense YO3AOP1 is highly activated by amino acids and amines./doi:10.1016%2Fj.bmcl.2012.08.088/rivista:Bioorganic and medicinal chemistry letters (Online)/anno:2012/pagina_da:6324/pagina_a:6327/intervallo_pagine:6324–6327/volume:22
Bioorganic & Medicinal Chemistry Letters

The α-carbonic anhydrase (CA, EC 4.2.1.1) from the newly discovered thermophilic bacterium Sulfurihydrogenibium yellowstonense YO3AOP1 (SspCA) was investigated for its activation with a series of amino acids and amines. d -His, l -Phe, l -Tyr, l - a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::273ee0a438eae2ba92c133c74e9ff165
https://doi.org/10.1016/j.bmcl.2012.08.088

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Anion inhibition studies of the fastest carbonic anhydrase (CA) known, the extremo-CA from the bacterium Sulfurihydrogenibium azorense

Autor: Daniela Vullo a, Viviana De Luca b, Andrea Scozzafava a, Vincenzo Carginale b, Mosè Rossi b, c, Claudiu T. Supuran a, d, Clemente Capasso b

Publikováno v: Bioorganic and medicinal chemistry letters (Online) 22 (2012): 7142–7145. doi:10.1016/j.bmcl.2012.09.065.
info:cnr-pdr/source/autori:Daniela Vullo a, Viviana De Luca b, Andrea Scozzafava a, Vincenzo Carginale b, Mosè Rossi b, c, Claudiu T. Supuran a, d, Clemente Capasso b/titolo:Anion inhibition studies of the fastest carbonic anhydrase (CA) known, the extremo-CA from the bacterium Sulfurihydrogenibium azorense./doi:10.1016%2Fj.bmcl.2012.09.065./rivista:Bioorganic and medicinal chemistry letters (Online)/anno:2012/pagina_da:7142/pagina_a:7145/intervallo_pagine:7142–7145/volume:22

The ?-carbonic anhydrase (CA, EC 4.2.1.1) from the extremophilic bacterium Sulfurihydrogenibium azorense, SazCA, is the fastest CA known to date as a catalyst for CO2 hydration to bicarbonate and protons. We report an inhibition study of this enzyme

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=cnr_________::fb8e826a0aaa649a5022f0f752ef3c5e
http://www.sciencedirect.com/science/article/pii/S0960894X12012206

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