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CARBONIC ANHYDRASE INHIBITORS: STACKING WITH PHE131 DETERMINES ACTIVE SITE BINDING REGION OF INHIBITORS AS EXEMPLIFIED BY THE X-RAY CRYSTAL STRUCTURE OF A MEMBRANE-IMPERMEANT ANTITUMOR SULFONAMIDE COM

Autor: V. MENCHISE, G. DE SIMONE, V. ALTERIO, A. DI FIORE, A. SCOZZAFAVA, C. T. SUPURAN, PEDONE, CARLO

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od______3730::b339256c088bc8a05bf91064f8c161b1
http://hdl.handle.net/11588/10647

Carbonic anhydrase inhibitors: stacking with Phe131 determines active site binding region of inhibitors as exemplified by the X-ray crystal structure of a membrane-impermeant antitumor sulfonamide complexed with isozyme II

Autor: V. Menchise, and Andrea Scozzafava, Claudiu T. Supuran, Anna Di Fiore, Giuseppina De Simone, Carlo Pedone, V. Alterio

Publikováno v: Journal of medicinal chemistry 48 (2005): 5721–5727. doi:10.1021/jm050333c
info:cnr-pdr/source/autori:Menchise V; De Simone G; Alterio V; Di Fiore A; Pedone C; Scozzafava A; Supuran CT./titolo:Carbonic anhydrase inhibitors: stacking with Phe131 determines active site binding region of inhibitors as exemplified by the X-ray crystal structure of a membrane-impermeant antitumor sulfonamide complexed with isozyme II./doi:10.1021%2Fjm050333c/rivista:Journal of medicinal chemistry/anno:2005/pagina_da:5721/pagina_a:5727/intervallo_pagine:5721–5727/volume:48

Structure for the adduct of carbonic anhydrase II with 1-N-(4-sulfamoylphenyl-ethyl)-2,4,6-trimethylpyridinium perchlorate, a membrane-impermeant antitumor sulfonamide, is reported. The phenylethyl moiety fills the active site, making van der Waals i

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9e25a78972d8de7cf84127c9b489a261
https://publications.cnr.it/doc/180101

Crystal structure of the W35A mutant thioredoxin h from Chlamydomonas reinhardtii: the substitution of the conserved active site Trp leads to modifications in the environment of the two catalytic cysteines

Autor: V, Menchise, C, Corbier, C, Didierjean, J P, Jacquot, E, Benedetti, M, Saviano, A, Aubry

Publikováno v: Biopolymers. 56(1)

The conformational analysis of W35A thioredoxin h from the eukaryotic green alga Chlamydomonas reinhardtii in the solid state has been carried out by x-ray diffraction, with the aim to clarify the role of Trp in the catalysis. Comparative analysis of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::ee7da9c9146925869aacc81b261e140f
https://pubmed.ncbi.nlm.nih.gov/11582571

Conformational restriction through C alpha i--C alpha i cyclization: Ac12c, the largest cycloaliphatic C alpha,alpha- disubstituted glycine known

Autor: M, Saviano, R, Iacovino, V, Menchise, E, Benedetti, G M, Bonora, M, Gatos, L, Graci, F, Formaggio, M, Crisma, C, Toniolo

Publikováno v: Biopolymers. 53(2)

Two complete series of N-protected, monodispersed oligopeptide esters to the pentamer level from 1-aminocyclododecane-1-carboxylic acid (Ac(12)c), an alpha-amino acid conformationally constrained through C(alpha)(i)--C(alpha)(i) cyclization, and eith

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::4d39665b108c44dde6efe74f676caffb
https://pubmed.ncbi.nlm.nih.gov/10679624