M
Marie-Jeanne Clément
Researcher at Université Paris-Saclay
Publications - 25
Citations - 468
Marie-Jeanne Clément is an academic researcher from Université Paris-Saclay. The author has contributed to research in topics: Microtubule & Tubulin. The author has an hindex of 10, co-authored 24 publications receiving 376 citations. Previous affiliations of Marie-Jeanne Clément include French Institute of Health and Medical Research & Pierre-and-Marie-Curie University.
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Journal ArticleDOI
Phosphorylation controls the interaction of the connexin43 C-terminal domain with tubulin and microtubules.
Amal Saidi Brikci-Nigassa,Marie-Jeanne Clément,Tap Ha-Duong,Elisabeth Adjadj,Latifa Ziani,David Pastré,Patrick A. Curmi,Philippe Savarin +7 more
TL;DR: It is demonstrated here that the microtubule binding of Cx43 is mainly driven by a short region of 26 amino acid residues located within the intracellular tail of C X43, and a pathway for understanding the micro Tubule-dependent regulation of C x43 gap junctional communications and the involvement of CX43 in TGF-β signal transduction is proposed.
Journal ArticleDOI
NMR characterization and molecular modeling of fucoidan showing the importance of oligosaccharide branching in its anticomplementary activity
Marie-Jeanne Clément,Bérangère Tissot,Lionel Chevolot,Elisabeth Adjadj,Yuguo Du,Patrick A. Curmi,Régis Daniel +6 more
TL;DR: In this paper, nuclear magnetic resonance (NMR) characterization of the branched oligosaccharides and saturation transfer difference-NMR experiment of the interaction with the protein C4 allowed the identification of the glycan residues in close contact with the target protein.
Journal ArticleDOI
The PN2-3 Domain of Centrosomal P4.1-associated Protein Implements a Novel Mechanism for Tubulin Sequestration
Anthony Cormier,Marie-Jeanne Clément,Marcel Knossow,Sylvie Lachkar,Philippe Savarin,Flavio Toma,André Sobel,Benoît Gigant,Patrick A. Curmi +8 more
TL;DR: The PN2-3 fragment of CPAP is characterized as a protein with an unprecedented tubulin sequestering mechanism distinct from that of stathmin family proteins.
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Benomyl and colchicine synergistically inhibit cell proliferation and mitosis: evidence of distinct binding sites for these agents in tubulin.
Marie-Jeanne Clément,Krishnan Rathinasamy,Elisabeth Adjadj,Flavio Toma,Patrick A. Curmi,Dulal Panda +5 more
TL;DR: Benomyl and colchicine synergistically inhibited the proliferation of HeLa cells and blocked their cell cycle progression at mitosis and an analysis of the saturation transfer difference NMR data yielded an interesting insight into the col chicine-tubulin interaction.
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Both lipid environment and pH are critical for determining physiological solution structure of 3-D-conserved epitopes of the HIV-1 gp41-MPER peptide P1
Jérome Coutant,Huifeng Yu,Huifeng Yu,Marie-Jeanne Clément,Annette Alfsen,Annette Alfsen,Flavio Toma,Patrick A. Curmi,Morgane Bomsel,Morgane Bomsel +9 more
TL;DR: P1, in a lipid environment, is an optimized MPER‐derived peptide suitable for designing an immunogen inducing broadly neutralizing antibodies to HIV.