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725 results on '"Federici, Giorgio"'

3. Monitoring Sediment Transport During Floods in Tuscany

Author

Francalanci, Simona, Paris, Enio, Solari, Luca, Minatti, Lorenzo, Federici, Giorgio Valentino, Lollino, Giorgio, editor, Arattano, Massimo, editor, Rinaldi, Massimo, editor, Giustolisi, Orazio, editor, Marechal, Jean-Christophe, editor, and Grant, Gordon E., editor

Published
2015
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4. Bile Acids

Author

Federici, Giorgio, Blau, Nenad, editor, Duran, Marinius, editor, and Gibson, K. Michael, editor

Published
2008
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5. The Impact of Nitric Oxide Toxicity on the Evolution of the Glutathione Transferase Superfamily: A PROPOSAL FOR AN EVOLUTIONARY DRIVING FORCE*

Author

Bocedi, Alessio, Fabrini, Raffaele, Farrotti, Andrea, Stella, Lorenzo, Ketterman, Albert J., Pedersen, Jens Z., Allocati, Nerino, Lau, Peter C.K., Grosse, Stephan, Eltis, Lindsay D., Ruzzini, Antonio, Edwards, Thomas E., Morici, Laura, Del Grosso, Erica, Guidoni, Leonardo, Bovi, Daniele, Lo Bello, Mario, Federici, Giorgio, Parker, Michael W., Board, Philip G., and Ricci, Giorgio

Published
2013
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8. Novel pharmacokinetic behavior of intravenous busulfan in children with thalassemia undergoing hematopoietic stem cell transplantation: a prospective evaluation of pharmacokinetic and pharmacodynamic profile with therapeutic drug monitoring

Author

Gaziev, Javid, Nguyen, Laurent, Puozzo, Christian, Mozzi, Alessia Francesca, Casella, Marialuisa, Perrone Donnorso, Michela, Gravina, Paolo, Sodani, Pietro, Marziali, Marco, Isgrò, Antonella, Simone, Maria Domenica, Andreani, Marco, Formosa, Amanda, Testi, Manuela, Federici, Giorgio, Bernardini, Sergio, and Lucarelli, Guido

Published
2010
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23. Seven mutations in the human insulin gene linked to permanent neonatal/infancy-onset diabetes mellitus

Author

Colombo, Carlo, Porzio, Ottavia, Liu, Ming, Massa, Ornella, Vasta, Mario, Salardi, Silvana, Beccaria, Luciano, Monciotti, Carla, Toni, Sonia, Pedersen, Oluf, Hansen, Torben, Federici, Luca, Pesavento, Roberta, Cadario, Francesco, Federici, Giorgio, Ghirri, Paolo, Arvan, Peter, Iafusco, Dario, and Barbetti, Fabrizio.

Subjects
Diabetes -- Genetic aspects, Pancreatic beta cells -- Health aspects, Pancreatic beta cells -- Research, Gene mutations -- Complications and side effects, Gene mutations -- Research, Infants (Newborn) -- Diseases, Infants (Newborn) -- Genetic aspects, Infants (Newborn) -- Risk factors
Abstract

Permanent neonatal diabetes mellitus (PNDM) is a rare disorder usually presenting within 6 months of birth. Although several genes have been linked to this disorder, in almost half the cases documented in Italy, the genetic cause remains unknown. Because the Akita mouse bearing a mutation in the Ins2 gene exhibits PNDM associated with pancreatic [beta] cell apoptosis, we sequenced the human insulin gene in PNDM subjects with unidentified mutations. We discovered 7 heterozygous mutations in 10 unrelated probands. In 8 of these patients, insulin secretion was detectable at diabetes onset, but rapidly declined over time. When these mutant proinsulins were expressed in HEK293 cells, we observed defects in insulin protein folding and secretion. In these experiments, expression of the mutant proinsulins was also associated with increased Grp78 protein expression and XBP1 mRNA splicing, 2 markers of endoplasmic reticulum stress, and with increased apoptosis. Similarly transfected INS-1E insulinoma cells had diminished viability compared with those expressing WT proinsulin. In conclusion, we find that mutations in the insulin gene that promote proinsulin misfolding may cause PNDM., Introduction Neonatal diabetes is a rare monogenic disorder associated with defects of pancreatic [beta] cell mass and/or function. The disorder is distinguished by 2 clinical variants--transient and permanent--caused by specific [...]

Published
2008

28. Interleukin 18 gene polymorphisms predict risk and outcome of Alzheimer's disease

Author

Bossu, Paola, Ciaramella, Antonio, Moro, Maria Luisa, Bellincampi, Lorenza, Bernardini, Sergio, Federici, Giorgio, Trequattrini, Alberto, Macciardi, Fabio, Spoletini, Ilaria, Di Iulio, Fulvia, Caltagirone, Carlo, and Spalletta, Gianfranco

Subjects
Alzheimer's disease -- Development and progression, Alzheimer's disease -- Genetic aspects, Alzheimer's disease -- Patient outcomes, Interleukin-18 -- Research, Genetic polymorphisms -- Research, Cytokines -- Research, Health, Psychology and mental health
Published
2007

31. Properties and utility of the peculiar mixed disulfide in the bacterial glutathione transferase B1-1

Author

Caccuri, Anna Maria, Antonini, Giovanni, Allocati, Nerino, Ilio, Carmine Di, Innocenti, Federica, Maria, Francesca De, Parker, Michael W., Masulli, Michele, Polizio, Francesca, Federici, Giorgio, and Ricci, Giorgio

Subjects
Microbial enzymes -- Physiological aspects, Glutathione metabolism -- Physiological aspects, Xenobiotics -- Physiological aspects, Enzymes -- Structure-activity relationship, Biological sciences, Chemistry
Abstract

The peculiar mixed disulfide between Cys10 and a glutathione molecule in the active site of the bacterial glutathione transferase is reduced by dithiothreitol but not by glutathione. Data indicate that the active site exhibits properties intermediate between those of glutathione transferases and thiol:disulfide oxidoreductase superfamily.

Published
2002

33. Valine 10 may act as a driver for product release from the active site of human glutathione transferase P1-1

Author

Micaloni, Chiara, Mazzetti, Anna P., Nuccetelli, Maria, Rossjohn, Jamie, McKinstry, William J., antonini, Giovanni, Caccuri, Anna M., Oakley, Aaron J., Federici, Giorgio, Ricci, Giorgio, Parker, Michael W., and Bello, Mario Lo

Subjects
Glutathione transferase -- Physiological aspects, Amino acids -- Structure-activity relationships, Binding sites (Biochemistry) -- Analysis, Enzyme kinetics -- Analysis, Biological sciences, Chemistry
Abstract

Crystallographic, kinetic, and spectroscopic studies of human glutathione transferase P1-1indicate that valine 10 residue, at the base of the H-site, mediates product orientation prior to their exit from enzyme's active site.

Published
2000

46. Solution structure of glutathione bound to human glutathione transferase P1-1: comparison of NMR measurements with the crystal structure

Author

Nicotra, Maria, Paci, Maurizio, Sette, Marco, Oakley, Aaron J., Parker, Michael W., Bello, Mario Lo, Caccuri, Anna Maria, Federici, Giorgio, and Ricci, Giorgio

Subjects
Glutathione -- Research, Glutathione transferase -- Research, Biological sciences, Chemistry
Abstract

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 TRNOESY and TRROESY experiments have been performed under fast-exchange conditions. The family of GSH conformers, compatible with TRNOE distance constraints, shows a backbone structure very similar to the crystal model. Interesting differences have been found in the side chain regions. After restrained energy minimization of a representative NMR conformer in the active site, the sulfur atom is not found in hydrogen-bonding distance of the hydroxyl group of Tyr 7. This situation is similar to the one observed in an 'atypical' crystal complex grown at low pH and low temperature. The NMR conformers display also a poorly defined structure of the glutamyl moiety, and the presence of an unexpected intermolecular NOE could indicate a different interaction of this substrate portion with the G-site. The NMR data seem to provide a snapshot of GSH in a precomplex where the GSH glutamyl end is bound in a different fashion. The existence of this precomplex is supported by pre-steady-state kinetic experiments [Caccuri, A. M., Lo Bello, M., Nuccetelli, M., Nicotra, M., Rossi, P., Antonini, G., Federici, G., and Ricci, G. (1998) Biochemistry 37, 3028-3034] and preliminary time-resolved fluorescence data.

Published
1998

47. Proton release upon glutathione binding to glutathione transferase P1-1: kinetic analysis of a multistep glutathione binding process

Author

Caccuri, Anna Maria, Bello, Mario Lo, Nuccetelli, Marzia, Nicotra, Maria, Rossi, Paolo, Antonini, Giovanni, Federici, Giorgio, and Ricci, Giorgio

Subjects
Protons -- Research, Glutathione transferase -- Research, Glutathione -- Research, Biological sciences, Chemistry
Abstract

The fate of the thiol proton coming from the ionization of the sulfhydryl group of GSH in the active site of glutathione transferase P1-1 has been studied. pH changes caused by the binding of GSH to the enzyme in the absence of any inorganic buffer indicate that the thiol proton leaves the active site when the binary complex is formed. The amount of protons released is stoichiometric to the amount of GSH thiolate formed in the G-site. The apparent [pK.sub.a] value for the bound GSH, calculated with this potentiometric approach, is 6.18 [+ or -] 0.09; very similar values are found by spectrophotometric (6.20 [+ or -] 0.12) and by kinetic (6.00 [+ or -] 0.08) experiments. Binding of S-hexylglutathione does not cause any proton release. Stopped-flow data obtained by means of an acid-base indicator show that the proton extrusion process (apparent [t.sub.1/2] = 1.1 [+ or -] 0.1 ms at 15 [degrees] C) is not rate limiting in turnover (apparent [t.sub.1/2] = 34 [+ or -] 4 ms at 15 [degrees] C). By comparing the kinetic behavior of three distinct events occurring during the binding of GSH to the enzyme, i.e., proton release, ionization of bound GSH and quenching of intrinsic fluorescence, it appears that the binding process follows a multistep mechanism possibly involving the conformational transition of a weak precomplex into the final Michaelis complex. This step is modulated by helix 2 motions and may be rate limiting at physiological GSH concentrations. These findings, coming from kinetic studies, are consistent with NMR data [Nicotra, M., Paci, M., Sette, M., Oakley, A. J., Parker, M. W., Lo Bello, M., Caccuri, A.M., Federici, G., and Ricci, G. (1998) Biochemistry 37, 3020-3027] and time-resolved fluorescence experiments [Stella, L., Caccuri, A.M., Rosato, N., Nicotra, M., Lo Bello, M., De Matteis, F., Mazzetti, A. P., Federici, G., and Ricci, G., manuscript in preparation].

Published
1998

48. The three-dimensional structure of the human pi class glutathione transferase P1-1 in complex with the inhibitor ethacrynic acid and its glutathione conjugate

Author

Oakley, Aaron J., Rossjohn, Jamie, Bello, Mario Lo, Caccuri, Anna Maria, Federici, Giorgio, and Parker, Michael W.

Subjects
Glutathione transferase -- Research, Molecular structure -- Analysis, Enzyme inhibitors -- Research, Ligand binding (Biochemistry) -- Observations, Diuretics -- Research, Biological sciences, Chemistry
Abstract

The diuretic drug ethacrynic acid (EA) and its glutathione conjugate bind to one ligand binding site (H site) of Pi class glutathione transferase P1-1, in a nonproductive mode. The Tyr108 residue is involved in the binding of EA to glutathione. EA requires bound glutathione to bind to the H site in a productive mode. The contacts made by the glutathione moiety with the protein, in the bound EA-glutathione conjugate, are similar to those observed in other enzymes with glutathione-based substrate and inhibitor. The glutathione binding site is occupied by solvent molecules.

Published
1997

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