
Centre de Neurophysique, Physiologie et Pathologie - CNRS UMR 8119
Université Paris Descartes
45 Rue des Saints Pères
75270 Paris Cedex 06
France
Fax : +33 (0) 1 42 86 20 80
Nathalie Evrard
Associate professor, MCU Université Paris Cité
Cell and Death in Hoste-Pathogene Interractions
Cell and Death in Hoste-Pathogene Interractions
Journal articles
2018
- ref_biblio
- Mickaël Fer, Laurent Le Corre, Nicolas Pietrancosta, Nathalie Evrard-Todeschi, Samir Olatunji, et al.. Bacterial Transferase MraY, a Source of Inspiration towards New Antibiotics. Current Medicinal Chemistry, 2018, 25 (42), pp.6013-6029. ⟨10.2174/0929867325666180330095154⟩. ⟨hal-02364241⟩
- Accès au bibtex
-
2017
- ref_biblio
- Maxime Melikian, Baptiste Eluard, Gildas Bertho, Véronique Baud, Nathalie Evrard-Todeschi. Model of the Interaction between the NF-κB Inhibitory Protein p100 and the E3 Ubiquitin Ligase β-TrCP based on NMR and Docking Experiments. Journal of Chemical Information and Modeling, 2017, 57 (2), pp.223-233. ⟨10.1021/acs.jcim.5b00409⟩. ⟨hal-03684765⟩
- Accès au bibtex
-
2012
- ref_biblio
- Gildas Bertho, Alexey Mantsyzov, Guillaume Bouvier, Nathalie Evrard-Todeschi. Contact-based ligand-clustering approach for the identification of active compounds in virtual screening. Advances and applications in bioinformatics and chemistry, 2012, pp.61. ⟨10.2147/AABC.S30881⟩. ⟨hal-03684866⟩
- Accès au bibtex
-
- ref_biblio
- Patricia Rada, Ana Rojo, Nathalie Evrard-Todeschi, Nadia Innamorato, Axelle Cotte, et al.. Structural and Functional Characterization of Nrf2 Degradation by the Glycogen Synthase Kinase 3/β-TrCP Axis. Molecular and Cellular Biology, 2012, 32 (17), pp.3486-3499. ⟨10.1128/MCB.00180-12⟩. ⟨hal-03684929⟩
- Accès au bibtex
-
2010
- ref_biblio
- Guillaume Bouvier, Nathalie Evrard-Todeschi, Jean-Pierre Girault, Gildas Bertho. Automatic clustering of docking poses in virtual screening process using self-organizing map. Bioinformatics, 2010, 26 (1), pp.53-60. ⟨10.1093/bioinformatics/btp623⟩. ⟨hal-03684971⟩
- Accès au bibtex
-
2008
- ref_biblio
- Nathalie Evrard-Todeschi, Julien Pons, Josyane Gharbi-Benarous, Gildas Bertho, Richard Benarous, et al.. Structure of the Complex between Phosphorylated Substrates and the SCF β-TrCP Ubiquitin Ligase Receptor: A Combined NMR, Molecular Modeling, and Docking Approach. Journal of Chemical Information and Modeling, 2008, 48 (12), pp.2350-2361. ⟨10.1021/ci800248u⟩. ⟨hal-03685021⟩
- Accès au bibtex
-
- ref_biblio
- Julien Pons, Nathalie Evrard-Todeschi, Gildas Bertho, Josyane Gharbi-Benarous, Valérie Tanchou, et al.. Transfer-NMR and Docking Studies Identify the Binding of the Peptide Derived from Activating Transcription Factor 4 to Protein Ubiquitin Ligase β-TrCP. Competition STD-NMR with β-Catenin. Biochemistry, 2008, 47 (1), pp.14-29. ⟨10.1021/bi7014212⟩. ⟨hal-03685028⟩
- Accès au bibtex
-
2002
- ref_biblio
- Gaël Coadou, Nathalie Evrard-Todeschi, Josyane Gharbi-Benarous, Richard Benarous, Jean-Pierre J.-P. Girault. HIV-1 encoded virus protein U (Vpu) solution structure of the 41–62 hydrophilic region containing the phosphorylated sites Ser52 and Ser56. International Journal of Biological Macromolecules, 2002, 30 (1), pp.23-40. ⟨10.1016/s0141-8130(01)00184-2⟩. ⟨hal-02356291⟩
- Accès au bibtex
-
1998
- ref_biblio
- Nathalie Evrard-Todeschi, Josyane Gharbi-Benarous, Valéry Larue, Jean-Pierre Girault. Predictive Study by Molecular Modeling To Promote Specific Probes of Glutamate Receptors, Using Methylated Cyclic Glutamic Acid Derivatives ( trans - and cis -ACPD). Comparison with Specific Agonists. Journal of Chemical Information and Computer Sciences, 1998, 38 (4), pp.742-760. ⟨10.1021/ci9802023⟩. ⟨hal-02371099⟩
- Accès au bibtex
-
1995
- ref_biblio
- Valéry Larue, Josyane Gharbi-Benarous, Nathalie Evrard-Todeschi, Francine C. Acher, Robert Azerad, et al.. ACPD Ligands for glutamic receptors: Conformational analysis by NMR spectroscopy and molecular dynamics. Simulation in water of glutamic acid analogues containing a cyclopentane ring.. Journal de Chimie Physique, 1995, 92, pp.1809-1812. ⟨hal-02865157⟩
- Accès au bibtex
-