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Lionel Mourey

Researcher at University of Toulouse

Publications -  103
Citations -  7957

Lionel Mourey is an academic researcher from University of Toulouse. The author has contributed to research in topics: Mycobacterium tuberculosis & Chemistry. The author has an hindex of 39, co-authored 91 publications receiving 7512 citations. Previous affiliations of Lionel Mourey include Wayne State University & Russian Academy of Sciences.

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Journal ArticleDOI

Microtubule nucleation by γ-tubulin complexes

Justin M. Kollman, +3 more
- 01 Nov 2011 - 
TL;DR: The first crystallographic analysis of a non-γ-tubulin γTuRC component has resulted in a new appreciation of the relationships among all γ TuRC proteins, leading to a refined model of their organization and function.
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Crystal structure of Escherichia coli TEM1 beta-lactamase at 1.8 A resolution.

Christian Jelsch, +3 more
- 01 Aug 1993 - 
TL;DR: It was found that the E. coli T EM1 and Staphylococcus aureus PC1 β‐lactamases crystal structures differ in the relative orientations of the two domains composing the enzymes, which result in a narrowed substrate binding cavity in the TEM1 enzyme.
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Assistance of Microbial Glycolipid Antigen Processing by CD1e

Sabrina Mariotti, +14 more
- 25 Nov 2005 - 
TL;DR: It is shown that the mycobacterial antigens hexamannosylated phosphatidyl-myo-inositols (PIM6) stimulate CD1b-restricted T cells only after partial digestion of the oligomannose moiety by lysosomal α-mannosidase and that soluble CD1e is required for this processing.
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Conformational changes induced by phosphorylation of the FixJ receiver domain.

Catherine Birck, +7 more
- 01 Jan 1999 - 
TL;DR: The cascade of phosphorylation-induced conformational changes in FixJN illustrates the role of conserved residues in stabilizing the phosphoryl group in the active site, triggering the structural transition and achieving the post-phosphorylation signaling events.
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The structure of a Staphylococcus aureus leucocidin component (LukF-PV) reveals the fold of the water-soluble species of a family of transmembrane pore-forming toxins

Jean-Denis Pedelacq, +9 more
- 15 Mar 1999 - 
TL;DR: The structure analysis and a multiple sequence alignment of all toxic components, suggest that LukF-PV represents the fold of any water-soluble secreted protein in this family of transmembrane pore-forming toxins.