Zobrazeno 1 - 10
of 95
pro vyhledávání: '"Raymond Julien"'
Publikováno v:
Canadian Journal of Education / Revue canadienne de l'éducation, 2017 Jan 01. 40(3), 26-59.
Externí odkaz:
https://www.jstor.org/stable/90014771
Autor:
Pol-André Apoil, Antoine Blancher, Arnaud Gleizes, Lionel Forestier, Jacques Izopet, Christophe Pasquier, Peter Winterton, Raymond Julien, Bénédicte Puissant-Lubrano
Publikováno v:
VirusDisease
VirusDisease, Springer, 2015, 26 (1-2), pp.62-69. ⟨10.1007/s13337-015-0252-1⟩
VirusDisease, Springer, 2015, 26 (1-2), pp.62-69. ⟨10.1007/s13337-015-0252-1⟩
International audience; Chimpanzees are susceptible to experimental infection by human deficiency virus (HIV)-1, but unlike humans, they exceptionally develop an immunodeficiency syndrome after HIV-1 inoculation. To explore the difference between hum
Publikováno v:
Journal of Molecular Evolution
Journal of Molecular Evolution, Springer Verlag, 2006, 63, pp.353-364
Journal of Molecular Evolution, Springer Verlag, 2006, 63, pp.353-364
Numerous vertebrates have four alpha-1,3/4-fucosyltransferase genes (FUT9, FUT7, FUT4, and FUT Lewis) belonging to the same family. Until now, studies on the evolution of this family have mainly focused on Lewis genes but how the other alpha-1,3/4-fu
Publikováno v:
Glycobiology. 14:347-356
All vertebrate alpha3- and alpha3/4-FUTs possess the characteristic acceptor-binding motif VxxHH(W/R)(D/E). FUT6 and FUTb enzymes, harboring R in the acceptor-binding motif, transfer fucose in alpha1,3 linkage, whereas FUT3 and FUT5 enzymes with W at
Publikováno v:
Genetica. 118:157-170
The fucosyltransferase gene family encodes enzymes that transfer fucose in α1,2, α1,3/4 and α1,6 linkages on a large variety of glycans. The most ancient genes harbour a split coding sequence, and encode enzyme that transfer fucose at or near O- a
Autor:
Rafael Oriol, Raymond Julien, Fabrice Dupuy, Christophe Javaud, Jean-Michel Petit, Abderrahman Maftah, Jean-Claude Michalski
Publikováno v:
Molecular Biology and Evolution. 17:1661-1672
Based on PCR strategies and expression studies, we define the genomic organization of the FUT8b gene. This gene encodes the only known mammalian enzyme transferring fucose in an alpha1-->6 linkage on the asparagine-branched GlcNAc residue of the chit
Autor:
Abderrahman Maftah, Raymond Julien, Scott Thomas, Ten-Yang Yen, Bruce A. Macher, Eric H. Holmes, François Gallet, Rajesh K. Joshi, Anton T. Nguyen, Tracy Long
Publikováno v:
Journal of Biological Chemistry
Journal of Biological Chemistry, 2000, 275 (32), pp.24237-24245. ⟨10.1074/jbc.m000888200⟩
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2000, 275 (32), pp.24237-24245. ⟨10.1074/jbc.m000888200⟩
Journal of Biological Chemistry, 2000, 275 (32), pp.24237-24245. ⟨10.1074/jbc.m000888200⟩
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2000, 275 (32), pp.24237-24245. ⟨10.1074/jbc.m000888200⟩
Human α1,3 fucosyltransferases (FucTs) contain four highly conserved cysteine (Cys) residues, in addition to a free Cys residue that lies near the binding site for GDP-fucose (Holmes, E. H., Xu, Z., Sherwood, A. L., and Macher, B. A. (1995)J. Biol.
Autor:
Katiana Saunier, Hubert Levéziel, Rafael Oriol, Ahmad Oulmouden, Jean-Pierre Barreaud, Didier Delourme, Jacques Souchaire, Jean-Michel Petit, Raymond Julien
Publikováno v:
Glycobiology. 10:611-621
To investigate the synthesis of alpha2-fucosylated epitopes in the bovine species, we have characterized cDNAs from various tissues. We found three distinct alpha2-fucosyltransferase genes, named bovine fut1, fut2, and sec1 which are homologous to hu
Autor:
Fabrice Dupuy, Abderrahman Maftah, Raymond Julien, Rosella Mollicone, Jean-Michel Petit, Rafael Oriol
Publikováno v:
Journal of Biological Chemistry. 274:12257-12262
Alignment of 15 vertebrate α1,3-fucosyltransferases revealed one arginine conserved in all the enzymes employing exclusively type 2 acceptor substrates. At the equivalent position, a tryptophan was found in FUT3-encoded Lewis α1,3/1,4-fucosyltransf
Publikováno v:
Biochimie. 80:289-293
The vasoactive intestinal peptide (VIP) is an ubiquitous peptide of great potential for applications. Development of new bioactive VIP analogs using production in recombinant E coli has been carried out in our laboratory. This work presents a new mul