Biomol NMR Assign

Autor: Gavin W. Collie, Gilles Guichard, Cameron D. Mackereth, Antoine Baudin, Antoine Loquet, Stéphane Chaignepain, Anne Guichard, Benoit Odaert, Mélanie Berbon, Agnès Hocquellet, Sabrina Rousseau

Publikováno v: Biomolecular NMR Assignments
Biomolecular NMR Assignments, Springer, 2018, 12 (2), pp.309-314. ⟨10.1007/s12104-018-9828-1⟩
Biomolecular NMR Assignments, 2018, 12 (2), pp.309-314

Death receptors (DR) selectively drive cancer cells to apoptosis upon binding to the Tumor necrosis factor-a-Related Apoptosis-Inducing Ligand (TRAIL). Complex formation induces the oligomerization of the death receptors DR4 (TRAIL-R1) and DR5 (TRAIL

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::51416df8e4c1ea70930ec001fa0c47d2
https://doi.org/10.1007/s12104-018-9828-1

Thioether Analogues of Disulfide-Bridged Cyclic Peptides Targeting Death Receptor 5: Conformational Analysis, Dimerisation and Consequences for Receptor Activation

Autor: Benoit Odaert, Sylvie Fournel, Roman Rohac, Neila Chekkat, Hinrich Gronemeyer, Karine Estieu-Gionnet, Gabrielle Zeder-Lutz, Valeria Pavet, Danièle Altschuh, Cristian R. Smulski, Marie-Charlotte Lechner, Karolina Pulka-Ziach, Gilles Guichard

Publikováno v: ChemBioChem. 16:293-301

Cyclic peptides containing redox-stable thioether bridges might provide a useful alternative to disulfide-bridged bioactive peptides. We report the effect of replacing the disulfide bridge with a lanthionine linkage in a 16-mer cyclic peptide that bi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a1e6fd8e96e301e3d7486e5d795787c4
https://doi.org/10.1002/cbic.201402485

Cell-Free Expression for the Study of Hydrophobic Proteins: The Example of Yeast ATP-Synthase Subunits

Autor: Isabelle Larrieu, Benoit Odaert, Claire Stines-Chaumeil, Corinne Sanchez, Marie-France Giraud, Edmond Yazo Kone, Alexandre Barras, James Tolchard

Publikováno v: Methods in Molecular Biology ISBN: 9781493971497

Small hydrophobic membrane proteins or proteins with hydrophobic domains are often difficult to produce in bacteria. The cell-free expression system was found to be a very good alternative for the expression of small hydrophobic subunits of the yeast

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::cb1656aedf0ba5b582a4bbb80d1baf10
https://doi.org/10.1007/978-1-4939-7151-0_4

Evidence for specific interaction between the RhoGAP domain from the yeast Rgd1 protein and phosphoinositides

Autor: Jean-William Dupuy, Marc Crouzet, Aurélie Vieillemard, Marc Bonneu, Benoit Odaert, Valérie Prouzet-Mauléon, Michel Hugues, Xavier Santarelli, François Doignon, Didier Thoraval

Publikováno v: Biochemical and Biophysical Research Communications. 405:74-78

The Rho GTPase activating protein Rgd1 increases the GTPase activity of Rho3p and Rho4p, which are involved in bud growth and cytokinesis, respectively, in the budding yeast Saccharomyces cerevisiae. Rgd1p is a member of the F-BAR family conserved in

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b7837bef9c0def6284a44ef526e89e5f
https://doi.org/10.1016/j.bbrc.2010.12.130

Aggregation of Cateslytin β-Sheets on Negatively Charged Lipids Promotes Rigid Membrane Domains. A New Mode of Action for Antimicrobial Peptides?

Autor: Bernard Desbat, Frantz Jean-Francois, Marie-Hélène Metz-Boutigue, Benoit Odaert, Michel Roux, Sabine Castano, Erick J. Dufourc

Publikováno v: Biochemistry
Biochemistry, 2008, 47 (24), pp.6394-6402. ⟨10.1021/bi800448h⟩
Biochemistry, American Chemical Society, 2008, 47 (24), pp.6394-6402. ⟨10.1021/bi800448h⟩

Cateslytin, a positively charged (5+) arginine-rich antimicrobial peptide (bCgA, RSMRLSFRARGYGFR), was chemically synthesized and studied against membranes that mimic bacterial or mammalian systems. Circular dichroism, polarized attenuated total refl

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fc41ba2e568852000c183be921cdb45d
https://doi.org/10.1021/bi800448h