Zobrazeno 1 - 10
of 188
pro vyhledávání: '"M. Lo Bello"'
Publikováno v:
Journal of the neurological sciences (2015).
info:cnr-pdr/source/autori:V. La Bellaa,?, M. Lo Belloa, F. Di Finia, F.L. Confortib, R. Spataroa./titolo:Expression and subcellular localization of FUS protein in fibroblasts of preclinical FUS P525L mutation carriers and patients with sporadic ALS/doi:/rivista:Journal of the neurological sciences/anno:2015/pagina_da:/pagina_a:/intervallo_pagine:/volume
info:cnr-pdr/source/autori:V. La Bellaa,?, M. Lo Belloa, F. Di Finia, F.L. Confortib, R. Spataroa./titolo:Expression and subcellular localization of FUS protein in fibroblasts of preclinical FUS P525L mutation carriers and patients with sporadic ALS/doi:/rivista:Journal of the neurological sciences/anno:2015/pagina_da:/pagina_a:/intervallo_pagine:/volume
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::35929de8ea2fd2bdf94d4d0fdda9df07
https://publications.cnr.it/doc/337950
https://publications.cnr.it/doc/337950
Autor:
M. Lo Bello, Aaron J. Oakley, A.P. Mazzetti, A.M. Caccuri, Jamie Rossjohn, Michael W. Parker, Marzia Nuccetelli, Giorgio Ricci, William J. McKinstry, Giorgio Federici, Chiara Micaloni, Giovanni Antonini
Publikováno v:
Biochemistry. 39:15961-15970
We have probed the electrophilic binding site (H-site) of human glutathione transferase P1-1 through mutagenesis of two valines, Val 10 and Val 35, into glycine and alanine, respectively. These two residues were previously shown to be the only confor
Publikováno v:
Journal of Molecular Biology. 291:913-926
Glutathione S -transferases (GSTs) play a pivotal role in the detoxification of foreign chemicals and toxic metabolites. They were originally termed ligandins because of their ability to bind large molecules (molecular masses >400 Da), possibly for s
Autor:
Marzia Nuccetelli, Philip G. Board, G. Federici, A.M. Caccuri, Giorgio Ricci, Jamie Rossjohn, M. Lo Bello, A.P. Mazzetti, Michael W. Parker
Publikováno v:
Biochemical and Biophysical Research Communications. 252:184-189
Substrate selectivity, among glutathione transferase (GST) isoenzymes, appears to be determined by a few residues. As part of study to determine which residues are class-specific determinants, Tyr 108 (an important residue of the class Pi) has been c
Publikováno v:
Scopus-Elsevier
Purpose: To evaluate the capability of color Doppler ultrasonography to differentiate between benign and malignant soft-tissue tumors. Material and Methods: We reviewed the ultrasonographic (US) and color Doppler (CD) findings in 46 consecutive patie
Publikováno v:
Biochemistry. 37:9912-9917
Three-dimensional structures of the apo form of human pi class glutathione transferase have been determined by X-ray crystallography. The structures suggest the enzyme recognizes its substrate, glutathione, by an induced-fit mechanism. Compared to co
Autor:
M. Sette, M. Lo Bello, Aaron J. Oakley, Giorgio Ricci, A. M. Caccuri, Michael W. Parker, G. Federici, M. Paci, Maria Rita Nicotra
Publikováno v:
Biochemistry. 37:3020-3027
The conformation of the bound glutathione (GSH) in the active site of the human glutathione transferase P1-1 (EC 2.5.1.18) has been studied by transferred NOE measurements and compared with those obtained by X-ray diffraction data. Two-dimensional TR
Autor:
A.P. Mazzetti, Philip G. Board, Andrea Battistoni, Giorgio Federici, M. Lo Bello, Masami Muramatsu, Giorgio Ricci
Publikováno v:
Journal of Biological Chemistry. 270:1249-1253
In the human placental glutathione transferase, Cys-47 possesses, at physiological pH values, a pKavalue of 4.2 and may exist as an ion pair with the protonated ɛ-amino group of Lys-54. Using site-directed mutagenesis we investigate spectral, kineti
Autor:
A.M. Caccuri, Paolo Ascenzi, Andrea Battistoni, P Mazzetti, G. Federici, Giorgio Ricci, M. Lo Bello
Publikováno v:
Biochemical and Biophysical Research Communications. 200:1428-1434
Steady state kinetics measurements performed on human placenta glutathione transferase (GST P 1-1), utilizing 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole (NBD-Cl) as co-substrate, show that the kcat value (approximately equal to 1.2 s-1) is pH-independen