Research Topics
Species | Giorgio PochettiSummaryAffiliation: Institute of Crystallography Country: Italy Publications
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Detail Information
Publications
Insights into the mechanism of partial agonism: crystal structures of the peroxisome proliferator-activated receptor gamma ligand-binding domain in the complex with two enantiomeric ligandsGiorgio Pochetti
Istituto di Cristallografia, Consiglio Nazionale delle Ricerche, Montelibretti, 00016 Monterotondo Stazione, Roma, Italia
J Biol Chem 282:17314-24. 2007..Mutation analysis confirms the importance of Leu(465), Leu(469), and Ile(472) in the activation by (R)-1 and underscores the key role of Gln(286) in the PPARgamma activity...
Extra binding region induced by non-zinc chelating inhibitors into the S1' subsite of matrix metalloproteinase 8 (MMP-8)Giorgio Pochetti
Istituto di Cristallografia CNR, Area della Ricerca Roma 1, Via Salaria Km 29, 300, I 00016 Monterotondo Stazione, Roma, Italy
J Med Chem 52:1040-9. 2009....
Structural insight into peroxisome proliferator-activated receptor gamma binding of two ureidofibrate-like enantiomers by molecular dynamics, cofactor interaction analysis, and site-directed mutagenesisGiorgio Pochetti
Istituto di Cristallografia, Consiglio Nazionale delle Ricerche, Montelibretti, 00015 Monterotondo Stazione, Roma, Italia
J Med Chem 53:4354-66. 2010..Molecular modeling studies were performed to provide a molecular explanation for the different behavior of the mutants...
Crystal structure of the peroxisome proliferator-activated receptor gamma (PPARgamma) ligand binding domain complexed with a novel partial agonist: a new region of the hydrophobic pocket could be exploited for drug designRoberta Montanari
Consiglio Nazionale delle Ricerche, Roma 00016, Italy
J Med Chem 51:7768-76. 2008..Moreover, the structure of the complex with the S-enantiomer reveals a new region of the PPARgamma-LBD never sampled before by other ligands...
Structural insight into the stereoselective inhibition of MMP-8 by enantiomeric sulfonamide phosphonatesGiorgio Pochetti
Istituto di Cristallografia, C.N.R, Monterotondo Stazione, Rome, Italy
J Med Chem 49:923-31. 2006..The reasons for the preferential MMP-8 inhibition by the R-phosphonate are underlined and the differences in the mode of binding of analogous alpha-arylsulfonylamino hydroxamates and carboxylates are discussed...
Computational study of the catalytic domain of human neutrophil collagenase. specific role of the S3 and S'3 subsites in the interaction with a phosphonate inhibitorMassimiliano Aschi
Dipartimento di Chimica, Ingegneria Chimica e Materiali, , L'Aquila, Italy
J Comput Aided Mol Des 16:213-25. 2002..The role of the S3, S'3 and S'1 subsites in determining the inhibitor binding is discussed...
N-Hydroxyurea as zinc binding group in matrix metalloproteinase inhibition: mode of binding in a complex with MMP-8Cristina Campestre
Dipartimento di Scienze del Farmaco, Universita degli Studi G D Annunzio, Chieti, Italy
Bioorg Med Chem Lett 16:20-4. 2006....
Stereoselectivity by enantiomeric inhibitors of matrix metalloproteinase-8: new insights from molecular dynamics simulationsMassimiliano Aschi
Dipartimento di Chimica, Ingegneria Chimica e Materiali, Universita di L Aquila, Italia
J Med Chem 50:211-8. 2007....
