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Robert Chênevert grad student 1986 Universite Laval (Canada)
 (Récepteurs moléculaires: influences des éthers en couronne et des cyclodextrines sur quelques réactions organiques.)
Donald J. Cram post-doc 1985-1986 UCLA
William F. DeGrado post-doc 1986-1988 DuPont Central Research and Development
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Martial B, Raîche-Marcoux G, Lefèvre T, et al. (2020) The Structure of a Parkinson's Disease-Involved α-Synuclein Peptide is Modulated by Membrane Composition and Physical State. The Journal of Physical Chemistry. B
Paquet-Côté PA, Paradis JP, Auger M, et al. (2020) Crown ether modified peptides: Length and crown ring size impact on membrane interactions. Biochimica Et Biophysica Acta. Biomembranes. 183261
Dionne U, Chartier FJM, López de Los Santos Y, et al. (2018) Direct Phosphorylation of SRC Homology 3 Domains by Tyrosine Kinase Receptors Disassembles Ligand-Induced Signaling Networks. Molecular Cell
Fillion M, Goudreault M, Voyer N, et al. (2016) Amphiphilicity Is a Key Determinant in the Membrane Interactions of Synthetic 14-mer Cationic Peptide Analogues. Biochemistry. 55: 6919-6930
Godbout R, Légaré S, Auger M, et al. (2016) Membrane Assembly and Ion Transport Ability of a Fluorinated Nanopore. Plos One. 11: e0166587
Pham VH, Maaroufi H, Christian B, et al. (2016) Inhibition of Helicobacter pylori Glu-tRNA(G) (ln) amidotransferase by novel analogues of the putative transamidation intermediates. Febs Letters
Savoie JD, Otis F, Bürck J, et al. (2015) Crown ether helical peptides are preferentially inserted in lipid bilayers as a transmembrane ion channels. Biopolymers. 104: 427-33
Fillion M, Valois-Paillard G, Lorin A, et al. (2015) Membrane interactions of synthetic peptides with antimicrobial potential: effect of electrostatic interactions and amphiphilicity. Probiotics and Antimicrobial Proteins. 7: 66-74
Carpentier C, Godbout R, Otis F, et al. (2015) Synthesis and use of N-Fmoc-l-fluoroalanine Tetrahedron Letters. 56: 1244-1246
Fillion M, Noël M, Lorin A, et al. (2014) Investigation of the mechanism of action of novel amphipathic peptides: insights from solid-state NMR studies of oriented lipid bilayers. Biochimica Et Biophysica Acta. 1838: 2173-9
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