Jean-Marc LANCELIN

Professor

Contact

jean-marc.lancelin[@]isa-lyon.fr

Research

We develop the comprehensive analysis of the interaction properties of biological molecules using NMR and molecular modeling.  The nature the interaction properties are described through the mechanical statistics description of molecular dynamics by affordable massive calculations (GPU technology) correlated with NMR and in vitro activity assays. Undergoing research projects are associated in public-private partnerships supported by research agencies and foundations.

Biography

Prof. Lancelin received his background training in chemistry and biochemistry in Orléans, France from 1976 to 1980. He got his PhD in Physical Sciences in 1985 on the synthetic chemistry of complex natural products with antibiotic properties before being enrolled as CNRS research staff in 1985. He worked at Université d’Orléans, France, the RIKEN and Tokyo Metropolitan Medical Research Institute (RINSHOKEN) at post-doctoral member (Japan Society for Promotion of Sciences), at Institut de Biologie Structurale (IBS), Grenoble, France, then at Université Lyon 1 as Prof. since 1995. He was appointed as the director the Doctoral School of Chemistry of Lyon’s University between 2007 and 2015 and presently vice president of Université Lyon 1 delegated to the doctoral studies since 2016.

Keywords

NMR
molecular modeling
interaction properties
molecular dynamics
GPU technology

Publications

Publications HAL de jean-marc,lancelin

2016

Journal articles

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Mélissa Chow, Laura Troussicot, Marie Martin, Bastien Doumèche, Florence Guillière, et al.. Predicting and understanding the enzymatic inhibition of human peroxiredoxin 5 by 4-substituted pyrocatechols by combining funnel metadynamics, solution NMR, and steady-state kinetics. Biochemistry, American Chemical Society, 2016, 55 (24), pp.3469-3480 ⟨10.1021/acs.biochem.6b00367⟩. ⟨hal-01363618⟩
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2015

Journal articles

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Laura Troussicot, Florence Guillière, Vittorio Limongelli, Olivier Walker, Jean-Marc Lancelin. Funnel-metadynamics and solution NMR to estimate protein-ligand affinities. Journal of the American Chemical Society, American Chemical Society, 2015, 137 (3), pp.1273-1281. ⟨10.1021/ja511336z⟩. ⟨hal-01187402⟩
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2012

Journal articles

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Anja Lange, Mouhamad-Baligh Ismail, Gwladys Rivière, Maggy Hologne, Denis Lacabanne, et al.. Competitive binding of UBPY and ubiquitin to the STAM2 SH3 domain revealed by NMR. FEBS Letters, Wiley, 2012, 586 (19), pp.3379-3384. ⟨10.1016/j.febslet.2012.07.047⟩. ⟨hal-00819142⟩
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Gwladys Rivière, Maggy Hologne, Olivier Marcillat, Jean-Marc Lancelin. Dynamical properties of the loop 320s of substrate-free and substrate-bound muscle creatine kinase by NMR. FEBS Journal, Wiley, 2012, 279 (16), pp.2863-2875. ⟨10.1111/j.1742-4658.2012.08667.x⟩. ⟨hal-00873868⟩
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Anja Lange, Carlos Castaneda, Daniela Hoeller, Jean-Marc Lancelin, David Fushman, et al.. Evidence for cooperative and domain-specific binding of the signal transducing adaptor molecule 2 (STAM2) to lys(63)-linked diubiquitin. Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2012, 287 (22), pp.18687-18699. ⟨10.1074/jbc.M111.324954⟩. ⟨hal-00873866⟩
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Isabelle Krimm, Jean-Marc Lancelin, Jean-Pierre Praly. Binding evaluation of fragment-based scaffolds for probing allosteric enzymes.. Journal of Medicinal Chemistry, American Chemical Society, 2012, 55 (3), pp.1287-95. ⟨10.1021/jm201439b⟩. ⟨hal-00691495⟩
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Isabelle Krimm, Jean-Marc Lancelin, Jean-Pierre Praly. Binding evaluation of fragment-based scaffolds for probing allosteric enzymes. Journal of Medicinal Chemistry, American Chemical Society, 2012, 55 (3), pp.1287-1295. ⟨10.1021/jm201439b⟩. ⟨hal-01087963⟩
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2011

Journal articles

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Robert Blanvillain, Bennett Young, Yao-Min Cai, Valérie Hecht, Fabrice Varoquaux, et al.. The Arabidopsis peptide kiss of death is an inducer of programmed cell death. EMBO Journal, EMBO Press, 2011, 30 (6), pp.1173-1183. ⟨10.1038/emboj.2011.14⟩. ⟨hal-00873858⟩
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Anja Lange, Daniela Hoeller, Hans Wienk, Olivier Marcillat, Jean-Marc Lancelin, et al.. NMR Reveals a Different Mode of Binding of the Stam2 VHS Domain to Ubiquitin and Diubiquitin. Biochemistry, American Chemical Society, 2011, 50 (1), pp.48-62. ⟨10.1021/bi101594a⟩. ⟨hal-00873854⟩
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