Zobrazeno 1 - 10
of 88
pro vyhledávání: '"André Aumelas"'
Autor:
Alexander S. Mankin, Jean-Marc Campagne, Tanja Florin, Camille Midrier, Emilie Racine, Marine Serri, Maxime Gualtieri, Steve Forst, Malgorzata Dobosz-Bartoszek, André Aumelas, Sophie Gaudriault, Diarmaid Hughes, Matthieu Sarciaux, Philippe Villain-Guillot, Jessica Houard, Yury S. Polikanov, Jean-Michel Bolla, Carina Vingsbo Lundberg, Douglas L. Huseby, Christelle Cotteaux-Lautard, Lucile Pantel, Renata Marcia de Figueiredo, Anne Lanois, Alain Givaudan
Publikováno v:
Molecular Cell
Molecular Cell, Elsevier, 2018, 70 (1), pp.83-94. ⟨10.1016/j.molcel.2018.03.001⟩
Molecular Cell, 2018, 70 (1), pp.83-94. ⟨10.1016/j.molcel.2018.03.001⟩
Molecular Cell, Elsevier, 2018, 70 (1), pp.83-94. ⟨10.1016/j.molcel.2018.03.001⟩
Molecular Cell, 2018, 70 (1), pp.83-94. ⟨10.1016/j.molcel.2018.03.001⟩
International audience; Growing resistance of pathogenic bacteria and shortage of antibiotic discovery platforms challenge the use of antibiotics in the clinic. This threat calls for exploration of unconventional sources of antibiotics and identifica
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8ad5c19bf12626207dae8889278ce5f4
https://hal.archives-ouvertes.fr/hal-01761351
https://hal.archives-ouvertes.fr/hal-01761351
Autor:
Jean Martinez, Jean-François Hernandez, Dorothée Berthomieu, Laurent Chiche, Youness Touati-Jallabe, Abdallah Hamze, André Aumelas, Vincent Lisowski
Publikováno v:
Chemistry - A European Journal. 17:2566-2570
Publikováno v:
Journal of Medicinal Chemistry. 54:1091-1095
Antimicrobial activity and solution structures of four 13-amino acid peptides derived from the fusion domain of viral hemagglutinin proteins are presented. The results show that carboxyl-terminal amidation is a key factor to switch a viral fusion dom
Autor:
Tanja Schneider, Evelyne Bachère, Hans-Georg Sahl, André Aumelas, Paulina Schmitt, Delphine Destoumieux-Garzón, Miriam Wilmes, Martine Pugnière
Publikováno v:
Journal of Biological Chemistry. 285:29208-29216
Three oyster defensin variants (Cg-Defh1, Cg-Defh2, and Cg-Defm) were produced as recombinant peptides and characterized in terms of activities and mechanism of action. In agreement with their spectrum of activity almost specifically directed against
Publikováno v:
International Journal of Peptide and Protein Research. 35:465-472
The coupling reagent (benzotriazol-1-yloxy)tris-(dimethylamino)phosphonium (BOP) hexafluorophosphate was tested in the synthesis of luliberin (LH-RH) with inexpensive classically protected Boc-amino acids, in slight excess, and benzhydryl amino resin
Autor:
Dung Le-Nguyen, Bruno Perly, Eve Mahe, Laurent Chiche, Patrick Berthault, Philippe Sizun, André Aumelas
Publikováno v:
International Journal of Peptide and Protein Research. 37:315-324
[Nle7]-endothelin was synthesized and studied by 1H NMR and distance geometry calculations. The NMR study was performed first in DMSO-d6 and then in 50% acetonitrile/water since this peptide aggregates in pure water. In both cases, all spin systems w
Autor:
Marc Rodriguez, Jean Martinez, Muriel Amblard, André Aumelas, M F Lignon, Marie-Christine Galas
Publikováno v:
Europe PubMed Central
Cyclic CCK analogues in which positions 28 and 31 have been replaced by lysine residues and whose side chains are bridged by a succinic moiety, were synthesized. They were tested for their ability to inhibit the binding of 125I-BH-CCK-8 to isolated r
Publikováno v:
International Journal of Peptide and Protein Research. 35:473-480
We report the results of a joint NMR and theoretical investigation devoted to the conformational properties of N-acetyl-N'-methylamides of aliphatic amino acids with side chains of increasing bulkiness: Gly, Ala, Leu, Ile, and tert.Leu. In this serie
Publikováno v:
International Journal of Peptide and Protein Research. 26:294-298
The synthesis of the hexapeptide Z-Tyr(SO-3)-Met-Gly-Trp-Met-Asp-NH2, representing the C-terminal sequence of cholecystokinin minus the C-terminal phenylalanyl residue is described. This peptide was shown to be the most potent cholecystokinin recepto
Publikováno v:
International Journal of Peptide and Protein Research. 34:268-276
The octapeptide Lys-Arg-Asn-Lys-Asn-Asn-Ile-Ala (Arg4 in the human sequence) is the C-terminal part of porcine oxyntomodulin, an endogeneous peptide which is a potent inhibitor of stimulated acid secretion. This octapeptide exhibits the whole range o