L
Ludovic Carlier
Researcher at École Normale Supérieure
Publications - 32
Citations - 1011
Ludovic Carlier is an academic researcher from École Normale Supérieure. The author has contributed to research in topics: Chemistry & Peptide. The author has an hindex of 12, co-authored 25 publications receiving 777 citations. Previous affiliations of Ludovic Carlier include Centre national de la recherche scientifique & University of Rouen.
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Journal ArticleDOI
Identification of an anti-inflammatory protein from Faecalibacterium prausnitzii, a commensal bacterium deficient in Crohn’s disease
Elodie Quévrain,Marie-Anne Maubert,Christophe Michon,Florian Chain,Florian Chain,Rodrigue Marquant,Rodrigue Marquant,Rodrigue Marquant,Julien Tailhades,Julien Tailhades,Julien Tailhades,Sylvie Miquel,Sylvie Miquel,Ludovic Carlier,Ludovic Carlier,Ludovic Carlier,Luis G. Bermúdez-Humarán,Luis G. Bermúdez-Humarán,Bénédicte Pigneur,Bénédicte Pigneur,Olivier Lequin,Olivier Lequin,Olivier Lequin,Pascale Kharrat,Pascale Kharrat,Ginette Thomas,Ginette Thomas,Dominique Rainteau,Camille Aubry,Camille Aubry,N. Breyner,N. Breyner,Carlos Afonso,Solange Lavielle,Solange Lavielle,Solange Lavielle,Jean-Pierre Grill,Jean-Pierre Grill,Gérard Chassaing,Gérard Chassaing,Gérard Chassaing,Jean-Marc Chatel,Jean-Marc Chatel,Germain Trugnan,Ramnik J. Xavier,P. Langella,P. Langella,Harry Sokol,Philippe Seksik +48 more
TL;DR: A 15 kDa protein with anti-inflammatory properties is produced by F. prausnitzii, a commensal bacterium involved in CD pathogenesis, and is able to inhibit the NF-κB pathway in intestinal epithelial cells and to prevent colitis in an animal model.
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Structure-activity relationships and structural conformation of a novel urotensin II-related peptide.
David Chatenet,Christophe Dubessy,Jérôme Leprince,Cédric Boularan,Ludovic Carlier,Isabelle Ségalas-Milazzo,Laure Guilhaudis,Hassan Oulyadi,Daniel Davoust,Elizabeth Scalbert,Bruno Pfeiffer,Pierre Renard,Marie-Christine Tonon,Isabelle Lihrmann,Pierre Pacaud,Hubert Vaudry +15 more
TL;DR: This work synthesized a series of URP analogs and measured their binding affinity on hGPR14-transfected cells and their contractile activity in a rat aortic ring bioassay to find the most potent antagonist in this series.
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A novel µ-conopeptide, CnIIIC, exerts potent and preferential inhibition of NaV1.2/1.4 channels and blocks neuronal nicotinic acetylcholine receptors
Philippe Favreau,Evelyne Benoit,Henry G. Hocking,Ludovic Carlier,Dieter D' hoedt,Enrico Leipold,René Markgraf,Sébastien Schlumberger,Marco Cordova,Hubert François Gaertner,Marianne Paolini-Bertrand,Oliver Hartley,Jan Tytgat,Stefan H. Heinemann,Daniel Bertrand,Rolf Boelens,Reto Stöcklin,Jordi Molgó +17 more
TL;DR: The pharmacology of a new µ‐conopeptide (µ‐CnIIIC) is characterized on a range of preparations and molecular targets to assess its potential as a myorelaxant.
Journal ArticleDOI
Time-Resolved Protein Side-Chain Motions Unraveled by High-Resolution Relaxometry and Molecular Dynamics Simulations
Samuel F. Cousin,Pavel Kadeřávek,Nicolas Bolik-Coulon,Yina Gu,Cyril Charlier,Ludovic Carlier,Lei Bruschweiler-Li,Thorsten Marquardsen,Jean-Max Tyburn,Rafael Brüschweiler,Fabien Ferrage +10 more
TL;DR: A new NMR method based on high-resolution relaxometry and high-field relaxation is presented to determine quantitatively both motional amplitudes and time scales of methyl-bearing side chains in the picosecond-to-nanosecond range and unambiguously identify slow motions in the low nanosecondrange.
Journal ArticleDOI
Structure and Dynamics of an Intrinsically Disordered Protein Region That Partially Folds upon Binding by Chemical-Exchange NMR.
Cyril Charlier,Guillaume Bouvignies,Philippe Pelupessy,Astrid Walrant,Rodrigue Marquant,Mikhail Kozlov,Pablo De Ioannes,Nicolas Bolik-Coulon,Sandrine Sagan,Patricia Cortes,Patricia Cortes,Aneel K. Aggarwal,Ludovic Carlier,Fabien Ferrage +13 more
TL;DR: An approach based on monitoring chemical exchange by NMR to investigate the state of an IDR that folds upon binding through the observation of the free state of the protein, and is widely applicable to the biophysical investigation of complexes of disordered proteins and folded proteins.