Zobrazeno 1 - 10
of 36
pro vyhledávání: '"Jean-Paul Reboud"'
Autor:
Jean-Pierre Lavergne, Jean-Paul Reboud, Julie A. Pitcher, Robert J. Lefkowitz, Jennifer L. R. Freeman, Audrey Claing, Philippe Gonzalo
Publikováno v:
Biochemistry. 41:12850-12857
G protein-coupled receptor kinases are well characterized for their ability to phosphorylate and desensitize G protein-coupled receptors (GPCRs). In addition to phosphorylating the beta2-adrenergic receptor (beta2AR) and other receptors, G protein-co
Publikováno v:
Biochemistry. 39:13558-13564
The rat elongation factor eEF-2 catalyzes the translocation step of protein synthesis. Besides its well-characterized GTP/GDP binding properties, we have previously shown that ATP and ADP bind to eEF-2 [Sontag, B., Reboud, A. M., Divita, G., Di Pietr
Publikováno v:
Journal of Biological Chemistry. 272:20259-20262
The acidic ribosomal proteins P1-P2 from rat liver were overproduced for the first time by expression of their cDNA in Escherichia coli. They were tested for their ability to reactivate inactive P1-P2-deficient core particles derived from 60 S riboso
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 1048:238-244
Free- and EF-2-bound 80 S ribosomes, within the high-affinity complex with the non-hydrolysable GTP analog: guanylylmethylenediphosphonate (GuoPP(CH2)P), and the low-affinity complex with GDP, were treated with trypsin under conditions that modified
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 1048:231-237
The accessibility of three amino acids of EF-2, located within highly conserved regions near the N- and C-terminal extremities of the molecule (the E region and the ADPR region, respectively) to modifying enzymes has been compared within nucleotide-c
Publikováno v:
Journal of Biological Chemistry. 268:26082-26084
Elongation factor eEF-2 treated by N-bromosuccinimide under conditions which oxidize 2 Trp residues (Trp343 and Trp221) is inactivated in ribosome-dependent GTP hydrolysis and polyphenylalanine synthesis, and inactivation correlates with the specific
Autor:
Richard Haser, Jean-Paul Reboud, David Mandelman, Jean Pierre Lavergne, Philippe Gonzalo, Catherine Corbier
Publikováno v:
Acta crystallographica. Section D, Biological crystallography. 58(Pt 4)
Ribosomal P proteins have been shown to be involved in the binding of elongation factors and participate in factor-dependent GTP hydrolysis. The P proteins form the pentamer (P1/P2)(2)-P0 constituting the lateral flexible stalk of the 60S ribosomal s
Publikováno v:
The Journal of biological chemistry. 276(23)
In the 60 S ribosomal subunit, the lateral stalk made of the P-proteins plays a major role in translation. It contains P0, an insoluble protein anchoring P1 and P2 to the ribosome. Here, rat recombinant P0 was overproduced in inclusion bodies and sol
Autor:
Odile Filhol-Cochet, Jean-Paul Reboud, Patricia Bargis-Surgey, Cécile Vard, Philippe Gonzalo, Jean-Pierre Lavergne
Publikováno v:
European journal of biochemistry. 262(2)
The eukaryotic P1 and P2 ribosomal proteins which constitute, with P0, a pentamer forming the lateral stalk of the 60 S ribosomal subunit, exhibit several differences from their prokaryotic equivalents L7 and L12; in particular, P1 does not have the
Autor:
Cécile Alves de Olivera, Annick Moreira, Agnes Desbos, Jean-Claude Monier, Patricia Surgey, Jean-Paul Reboud, Jacques Bienvenu, Annick Venot, Hubert Perrier, Philippe Gonzalo, Jean-Pierre Lavergne, Nicole Fabien
The autoantibodies (aAbs) directed against the ribosomal P proteins (RPP aAbs) are known to react mainly against epitopes localized within the common C-terminal sequence of the three acidic ribosomal P proteins, P0, P1 and P2. In order to investigate
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1a4bed73e6978201917b190c4798784e
https://hal.archives-ouvertes.fr/hal-00314216
https://hal.archives-ouvertes.fr/hal-00314216