L
Lauriane Lecoq
Researcher at University of Lyon
Publications - 37
Citations - 647
Lauriane Lecoq is an academic researcher from University of Lyon. The author has contributed to research in topics: Capsid & Medicine. The author has an hindex of 12, co-authored 28 publications receiving 389 citations. Previous affiliations of Lauriane Lecoq include Centre national de la recherche scientifique & Claude Bernard University Lyon 1.
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Journal ArticleDOI
Structural Studies of Self-Assembled Subviral Particles: Combining Cell-Free Expression with 110 kHz MAS NMR Spectroscopy.
Guillaume David,Marie-Laure Fogeron,Maarten Schledorn,Roland Montserret,Uta Haselmann,Uta Haselmann,Susanne Penzel,Aurélie Badillo,Lauriane Lecoq,Patrice Andre,Patrice Andre,Patrice Andre,Michael Nassal,Ralf Bartenschlager,Ralf Bartenschlager,Beat H. Meier,Anja Böckmann +16 more
TL;DR: It is shown that milligram amounts of the small envelope protein of the duck hepatitis B virus can be produced by cell-free expression, and that the protein self-assembles into subviral particles.
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Localizing Conformational Hinges by NMR: Where Do Hepatitis B Virus Core Proteins Adapt for Capsid Assembly?
Lauriane Lecoq,Shishan Wang,Thomas Wiegand,Stéphane Bressanelli,Michael Nassal,Beat H. Meier,Anja Böckmann +6 more
TL;DR: This study reveals the high sensitivity with which NMR can detect the residues allowing the subtle conformational adaptations needed in lattice formation and is important for understanding the formation and modulation of protein assemblies in general.
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Combining Cell-Free Protein Synthesis and NMR Into a Tool to Study Capsid Assembly Modulation.
Shishan Wang,Marie-Laure Fogeron,Maarten Schledorn,Marie Dujardin,Susanne Penzel,Dara Burdette,Jan Martin Berke,Michael Nassal,Lauriane Lecoq,Beat H. Meier,Anja Böckmann +10 more
TL;DR: The cell-free system is established as a tool for the study of capsid assembly modulation directly after synthesis by the ribosome, and the perspective of assessing the impact of natural or synthetic compounds, or even enzymes that perform post-translational modifications, on capsids structures is opened.
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A Substantial Structural Conversion of the Native Monomer Leads to in-Register Parallel Amyloid Fibril Formation in Light-Chain Amyloidosis.
Lauriane Lecoq,Thomas Wiegand,Francisco Javier Rodríguez-Alvarez,Riccardo Cadalbert,Guillermo A. Herrera,Luis del Pozo-Yauner,Beat H. Meier,Anja Böckmann +7 more
TL;DR: It is determined, by using differentially 15N:13C‐labeled samples, that the β‐strands are stacked in‐register parallel in the fibrils, and shows that the native globular folds rearrange substantially upon fibrillization, and rules out the previously hypothesized fibril formation from native monomers.
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Easy Synthesis of Complex Biomolecular Assemblies: Wheat Germ Cell-Free Protein Expression in Structural Biology
TL;DR: The tremendous potential of the rapidly evolving and highly versatile CFPS systems are highlighted, making them more widely used as common tools to recombinantly prepare particularly challenging recombinant eukaryotic proteins.