Zobrazeno 1 - 10
of 118
pro vyhledávání: '"Bernard-Pierre Roques"'
Autor:
J-B. Le Pecq, Bernard-Pierre Roques, A. Jacquemin-Sablon, Ch. Garbay-Jaureguiberry, P. Rigaudy
Publikováno v:
International Journal of Peptide and Protein Research. 30:347-355
In order to specifically direct cytotoxic agents against tumor cells bearing delta opioid receptors, the DNA intercalating agents ellipticine and 9-OH-ellipticine were coupled by quaternarization of the pyridine nitrogen to an enkephalin modified pen
Publikováno v:
International Journal of Peptide and Protein Research. 37:440-450
A conformational analysis has been performed on several peptide fragments (CCK4 to CCK7) of the cholecystokinin neuromodulator. The Monte-Carlo Metropolis method was used to explore the conformational space of all these flexible units and different e
Autor:
Huixiong Chen, Marie-Claude Fournie-Zaluski, Mohamed Selkti, Bernard-Pierre Roques, Alain Tomas, Thierry Prangé, Jean-François Gaucher
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 59:1200-1205
A new alpha-aminophosphinic compound able to inhibit both zinc-containing exopeptidases and endopeptidases has been crystallized with TLN as a model in order to investigate the mode of zinc recognition by the phosphinic moiety and to evaluate the pot
Autor:
Caroline Bennejean, Hervé Poras, Alain Tomas, Marie-Claude Fournie-Zaluski, Pierre Renard, Françoise Beslot, Nicolas Inguimbert, Mohamed Selkti, Elizabeth Scalbert, Bernard-Pierre Roques, Franck Teffo
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 12:2001-2005
We have previously reported the design of a lead compound 1a for the joint inhibition of neprilysin (NEP, EC 3.4.24.11), angiotensin converting enzyme (ACE, EC 3.4.15.1) and endothelin converting enzyme (ECE-1, EC 3.4.24.71), three metallopeptidases
Publikováno v:
Biochemistry. 41:4312-4320
The two highly conserved Zn(2+) finger motifs of the HIV-1 nucleocapsid protein, NCp7, strongly bind Zn(2+) through coordination of one His and three Cys residues. To further analyze the role of these residues, we investigated the Zn(2+) binding and
Publikováno v:
Journal of Computational Chemistry. 22:1038-1047
α- and β-mercaptocarboxamides constitute the Zn2+-ligating entity of several highly potent metalloenzyme inhibitors. We have studied their interaction energies with Zn2+ using the polarizable molecular mechanics procedure SIBFA, and compared them t
Publikováno v:
Biochemistry. 39:7722-7735
SH3 (src homology domain 3) domains are small protein modules that interact with proline-rich peptides. The structure of the N-terminal SH3 domain from growth factor receptor-binding protein 2 (Grb2), an adapter protein in the intracellular signaling
Publikováno v:
Biochemistry. 38:16816-16825
The critical functions of the HIV-1 nucleocapsid protein NCp7 in genomic RNA packaging and reverse transcription, essentially rely on interactions with nucleic acids. A significant progress in the knowledge of these interactions has been recently ach
Publikováno v:
Journal of Computational Chemistry. 20:1379-1390
In order to gain an understanding of the energetics of polycoordinated Zn2+ binding to the formate anion (the end side chain of the Asp and Glu residues of proteins), we compare three competing binding modes in the presence of five and six water mole
Publikováno v:
Biochemistry. 38:12984-12994
The structure of the 56 amino acid nucleocapsid protein NCp10 of retrovirus MoMuLV, which contains a single CX(2)CX(4)HX(4)C-type zinc finger, has been determined previously by NMR. The important role of NCp10 (or NCp7 for HIV-1) in the retroviral li