M
Mireille Lambert
Researcher at University of Paris
Publications - 44
Citations - 3325
Mireille Lambert is an academic researcher from University of Paris. The author has contributed to research in topics: Cadherin & Myeloid leukemia. The author has an hindex of 27, co-authored 40 publications receiving 3035 citations. Previous affiliations of Mireille Lambert include French Institute of Health and Medical Research & Centre national de la recherche scientifique.
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Journal ArticleDOI
The LKB1/AMPK signaling pathway has tumor suppressor activity in acute myeloid leukemia through the repression of mTOR-dependent oncogenic mRNA translation.
Alexa S. Green,Alexa S. Green,Nicolas Chapuis,Nicolas Chapuis,Thiago Trovati Maciel,Lise Willems,Lise Willems,Mireille Lambert,Mireille Lambert,Christophe Arnoult,Olivier Boyer,Valérie Bardet,Valérie Bardet,Sophie Park,Marc Foretz,Marc Foretz,Benoit Viollet,Benoit Viollet,Norbert Ifrah,François Dreyfus,Olivier Hermine,Ivan C. Moura,Catherine Lacombe,Catherine Lacombe,Patrick Mayeux,Patrick Mayeux,Didier Bouscary,Jerome Tamburini +27 more
TL;DR: The induction of the LKB1/AMPK/TSC tumor suppressor axis is functional in AML and can be activated by the biguanide molecule metformin, resulting in a specific inhibition of mammalian target of rapamycin catalytic activity.
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A Molecular Clutch between the Actin Flow and N-Cadherin Adhesions Drives Growth Cone Migration
TL;DR: A strong correlation between growth cone velocity and the mechanical coupling between ligand-bound N-cadherin receptors and the retrograde actin flow is demonstrated, which supports a direct transmission of actin-based traction forces to N- cadher in adhesions, through catenin partners, driving growth cone advance and neurite extension.
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Immobilized dimers of N-cadherin-Fc chimera mimic cadherin-mediated cell contact formation: contribution of both outside-in and inside-out signals
TL;DR: Interestingly, bead-cell binding was altered by agents promoting microfilament and microtubule depolymerization or tyrosine phosphorylation, indicating a possible regulation of the adhesive properties of the extracellular domain of N-cadherin by intracellular factors (inside-out signaling).
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Lamellipodium extension and cadherin adhesion: two cell responses to cadherin activation relying on distinct signalling pathways.
Julie Gavard,Mireille Lambert,Inna Grosheva,Véronique Marthiens,Theano Irinopoulou,Jean-François Riou,Alexander D. Bershadsky,René-Marc Mège +7 more
TL;DR: The formation of de novo contacts was dissected by spreading cells on a highly active N-cadherin homophilic ligand to provide additional information on the mechanisms by which cadherin coordinates adhesion with dynamic changes in the cytoskeleton to control cell shape and intercellular junction organization.
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Dynamics of ligand-induced, Rac1-dependent anchoring of cadherins to the actin cytoskeleton
TL;DR: The results suggest that cadherin anchoring to the actin cytoskeleton is an adhesion-triggered, Rac1-regulated process enabling the transduction of mechanical forces across the cell membrane; they uncover novel aspects of the action of cadherins in cell sorting, cell migration, and growth cone navigation.