Výsledky vyhledávání - "Françoise, Vovelle"

Expression and characterization of the PEBP homolog genes fromDrosophila

Autor: Martine Decoville, Laurence Jouvensal, Gilles J. P. Rautureau, Daniel Locker, Françoise Vovelle, Françoise Schoentgen

Publikováno v: Archives of Insect Biochemistry and Physiology. 71:55-69

The phosphatidylethanolamine binding proteins (PEBPs) family is evolutionarily conserved and involved in different physiological phenomena. PEBPs were found in many species from bacteria to mammals. Despite numerous studies, PEBPs' biological functio

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0f35aab616519b1d7e08f1941049e14e
https://doi.org/10.1002/arch.20300

Zobrazit plný text záznamu

Peptides corresponding to the N- and C-terminal parts of PEBP are well-structured in solution: new insights into their possible interaction with partners in vivo

Autor: H. Labbé, Françoise Vovelle, Denise Sy, G Coadou, Françoise Schoentgen, Béatrice Vallée

Publikováno v: The Journal of Peptide Research. 61:47-57

Recently, it has been shown that mammalian PEBPs are implicated in several signalling pathways controlling the cellular cycle. In particular, during brain development, the N-terminal part of mammalian PEBP is specifically cleaved and the resulting 11

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::ba8e24f1b0e34a931e8ea53b0a0426ac
https://doi.org/10.1034/j.1399-3011.2003.21039.x

Zobrazit plný text záznamu

Rational design of peptides active against the gram positive bacteriaStaphylococcus aureus

Autor: Marc Guenneugues, Michèle Legrain, Céline Landon, Françoise Vovelle, Florent Barbault

Publikováno v: Proteins: Structure, Function, and Bioinformatics. 72:229-239

In an attempt to increase the antimicrobial activity of the insect defensin from Anopheles gambiae, which is active against Staphylococcus aureus at low concentration, hybrid defensins were designed by combining conserved sequence regions and variabl

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::77ee37e7b730a86b89dd34f80a99095f
https://doi.org/10.1002/prot.21912

Zobrazit plný text záznamu

Molecular Basis of the Tfs1/Ira2 Interaction: A Combined Protein Engineering and Molecular Modelling Study

Autor: Fabienne Godin, Denise Sy, Hélène Chautard, Béatrice Vallée, Françoise Vovelle, Hélène Bénédetti, Baptiste Legrand, Aurélie Gombault

Publikováno v: Journal of Molecular Biology
Journal of Molecular Biology, Elsevier, 2007, 374 (3), pp.604-617. ⟨10.1016/j.jmb.2007.09.057⟩

Tfs1p and Ylr179cp are yeast proteins belonging to the PEBP family. Tfs1p, but not Ylr179cp, has been shown to interact with and inhibit Ira2p, a GTPase-activating protein of Ras. Tfs1p has been shown to be a specific inhibitor of the CPY protease an

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::011ad8f80df5f41521634c76deab30c1
https://doi.org/10.1016/j.jmb.2007.09.057

Zobrazit plný text záznamu

Probing the Hydrophobic Cavity of Lipid Transfer Protein from Nicotiana tabacum through Xenon-Based NMR Spectroscopy

Autor: Patrick Berthault, Lionel Dubois, Céline Landon, Françoise Vovelle, J. Gaspard Huber, Hervé Desvaux, Pedro Da Silva, Michel Ponchet

Publikováno v: Journal of the American Chemical Society
Journal of the American Chemical Society, 2004, 126 (48), pp.15738-15746. ⟨10.1021/ja046195i⟩
Scopus-Elsevier
Journal of the American Chemical Society, American Chemical Society, 2004, 126 (48), pp.15738-15746. ⟨10.1021/ja046195i S0002-7863(04)06195-5⟩
Journal of the American Chemical Society, American Chemical Society, 2004, 126 (48), pp.15738-15746. ⟨10.1021/ja046195i⟩

The hydrophobic cavity of Lipid Transfer Protein 1 from Nicotiana tabacum is investigated in detail by NMR using xenon as a spy. The analysis of the (129)Xe chemical shifts and self-relaxation times gives evidence of protein-xenon interaction. Thermo

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7ee497c6f09b350d14d18691d776d619
https://doi.org/10.1021/ja046195i

Zobrazit plný text záznamu

Characterization of the UDP-N-acetylgalactosamine binding domain of bovine polypeptide N-acetylgalactosaminyltransferase T1

Autor: Véronique Piller, Stéphanie Duclos, Pedro Da Silva, Friedrich Piller, Françoise Vovelle

Publikováno v: Protein Engineering, Design and Selection
Protein Engineering, Design and Selection, Oxford University Press (OUP), 2004, 17 (8), pp.635-646. ⟨10.1093/protein/gzh075⟩

UDP-GalNAc:polypeptide {alpha}N-acetylgalactosaminyltransferases (ppGaNTases) transfer GalNAc from UDP-GalNAc to Ser or Thr. Structural features underlying their enzymatic activity and their specificity are still unidentified. In order to get some in

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::045315cbcd346ed5ced32b3938ad04a5
https://doi.org/10.1093/protein/gzh075

Zobrazit plný text záznamu

Epithelial Innate Immunity

Autor: R. J. L. Munks, Joanne V. Hamilton, Philippe Bulet, Nathalie Boulanger, Michael J. Lehane, Françoise Vovelle, Reto Brun

Publikováno v: Journal of Biological Chemistry. 277:49921-49926

The gut epithelium is an essential interface in insects that transmit parasites. We investigated the role that local innate immunity might have on vector competence, taking Stomoxys calcitrans as a model. S. calcitrans is sympatric with tsetse flies,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::d42538f70ede26a6dd66a63baa24e3ea
https://doi.org/10.1074/jbc.m206296200

Zobrazit plný text záznamu

Interaction of Surfactants and Polymer-Grafted Lipids with a Plant Lipid Transfer Protein, LTP1

Autor: Denise Sy, Jean-Paul Douliez, Françoise Vovelle, Didier Marion

Publikováno v: Langmuir. 18:7309-7312

To probe the effect of charge and ligand polar head, we report on the interaction between a plant lipid transfer protein (LTP1) and cationic surfactants, anionic and nonionic polymer grafted lipids, cetyl trimethylammonium bromide (CTAB), dihexadecyl

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::c8a4b030a814398fccd30741867c8a31
https://doi.org/10.1021/la020163w

Zobrazit plný text záznamu

The solution structure of gomesin, an antimicrobial cysteine-rich peptide from the spider

Autor: Philippe Bulet, Anita Caille, Françoise Vovelle, Nicolas Mandard, Sirlei Daffre

Publikováno v: European Journal of Biochemistry. 269:1190-1198

Gomesin is the first peptide isolated from spider exhibiting antimicrobial activities. This highly cationic peptide is composed of 18 amino-acid residues including four cysteines forming two disulfide linkages. The solution structure of gomesin has b

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::5f029d0e7ddebf1baa93973e799541d2
https://doi.org/10.1046/j.0014-2956.2002.02760.x

Zobrazit plný text záznamu

Solution structure of a lipid transfer protein extracted from rice seeds

Autor: Marius Ptak, Françoise Vovelle, Se Won Suh, Jarek Poznanski, Jae Young Lee, Patrick Sodano

Publikováno v: European Journal of Biochemistry. 259:692-708

Nuclear magnetic resonance (NMR) spectroscopy was used to determine the three dimensional structure of rice nonspecific lipid transfer protein (ns-LTP), a 91 amino acid residue protein belonging to the broad family of plant ns-LTP. Sequence specific

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bcd35ae487cd8131ceb1fe87e1557bac
https://doi.org/10.1046/j.1432-1327.1999.00093.x

Zobrazit plný text záznamu

Vyhledávací nástroje:

Upřesnit hledání