Fabrice Cornille
French Institute of Health and Medical Research
28 Papers
789 Citations
Fabrice Cornille is an academic researcher from French Institute of Health and Medical Research. The author has contributed to research in topics: Synaptobrevin & Peptide. The author has an hindex of 20, co-authored 28 publications. Previous affiliations of Fabrice Cornille include Washington University in St. Louis.
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Papers
Structure of the winged-helix protein hRFX1 reveals a new mode of DNA binding.
Gajiwala Ketan,Hua Chen,Fabrice Cornille,Bernard P. Roques,Walter Reith,Bernard Mach,Stephen K. Burley +6 more
TL;DR: A 1.5 Å-resolution structure of two copies of the DBD of human RFX1 (hRFX1) binding cooperatively to a symmetrical X-box is presented and a new model for interactions between linker histones and DNA is proposed.
342
Cleavage of members of the synaptobrevin/VAMP family by types D and F botulinal neurotoxins and tetanus toxin
S. Yamasaki,A. Baumeister,Thomas Binz,Juan Blasi,E. Link,Fabrice Cornille,Bernard P. Roques,E. M. Fykse,Thomas C. Südhof,Reinhard Jahn +9 more
TL;DR: It is shown that BoNT/D cleaves rat synaptobrevin 1 and 2 in toxified synaptosomes and in isolated vesicles and that the presence of Val76 instead of Gln76 dictates the reduced cleavability of synaptOBrevin isoforms by TeTx.
291
Nociceptin/Orphanin FQ Metabolism: Role of Aminopeptidase and Endopeptidase 24.15
TL;DR: The endogenous opioid receptor‐like1 (ORL1) ligand, nociceptin/orphanin FQ (FGGFTGARKSARKLANQ), a heptadecapeptide structurally resembling dynorphin A, has recently been identified and the major role played by metallopeptidases was confirmed by the complete protection of metabolism in the presence of EDTA.
115
NMR structure of the N-terminal SH3 domain of GRB2 and its complex with a proline-rich peptide from Sos
Nathalie Goudreau,Fabrice Cornille,Marc Duchesne,Fabienne Parker,Bruno Tocque,Christiane Garbay,Bernard-Pierre Roques +6 more
TL;DR: 1H NMR analysis of the complex between the Ser-32-GRB2-N-SH3 domain and the proline-rich peptide VPPPVPPRRR, derived from h-Sos, shows that relative to the SH3 peptide complexes described for PI3K, Fyn and Abl, the prolines in this complex binds in the opposite orientation.
106
A Sos-derived peptidimer blocks the Ras signaling pathway by binding both Grb2 SH3 domains and displays antiproliferative activity
Didier Cussac,Michel Vidal,Corinne Leprince,Wang-Qing Liu,Fabrice Cornille,Gilles Tiraboschi,Bernard P. Roques,Christiane Garbay +7 more
TL;DR: The designed peptidimers appear to be interesting leads to investigate signaling and intracellular processes and for designing selective inhibitors of tumorigenic Ras‐dependent processes.
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