Ludovic Carlier
Affiliations: | 2007-2008 | Utrecht University, Utrecht, Netherlands |
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| Malard F, Sizun C, Thureau A, et al. (2023) Structural transitions in TCTP tumor protein upon binding to the anti-apoptotic protein family member Mcl-1. The Journal of Biological Chemistry. 104830 |
| Bourafai-Aziez A, Sebban M, Benabderrahmane M, et al. (2019) Binding mode of Pyridoclax to Myeloid cell leukemia-1 (Mcl-1) revealed by Nuclear Magnetic Resonance Spectroscopy, Docking and Molecular Dynamics Approaches. Journal of Biomolecular Structure & Dynamics. 1-26 |
| Hedir S, De Giorgi M, Fogha J, et al. (2018) Structure-guided design of pyridoclax derivatives based on Noxa / Mcl-1 interaction mode. European Journal of Medicinal Chemistry. 159: 357-380 |
| Charlier C, Bouvignies G, Pelupessy P, et al. (2017) Structure and dynamics of an intrinsically disordered protein region that partially folds upon binding by chemical-exchange NMR. Journal of the American Chemical Society |
| Carlier L, Haase AS, Burgos Zepeda MY, et al. (2012) The C-terminal domain of the Uup protein is a DNA-binding coiled coil motif. Journal of Structural Biology. 180: 577-84 |
| Carlier L, Haase AS, Burgos Zepeda MY, et al. (2012) The C-terminal domain of the Uup protein is a DNA-binding coiled coil motif. Journal of Structural Biology. 180: 577-84 |
| Carlier L, Byrne C, Miclet E, et al. (2012) Biophysical studies of the interaction between calmodulin and the R²â¸â·-T³¹¹ region of human estrogen receptor α reveals an atypical binding process. Biochemical and Biophysical Research Communications. 419: 356-61 |
| Carlier L, Haase AS, Burgos Zepeda MY, et al. (2012) Secondary structure and NMR resonance assignments of the C-terminal DNA-binding domain of Uup protein. Biomolecular Nmr Assignments. 6: 197-200 |
| Carlier L, Haase AS, Burgos Zepeda MY, et al. (2012) Secondary structure and NMR resonance assignments of the C-terminal DNA-binding domain of Uup protein. Biomolecular Nmr Assignments. 6: 197-200 |
| Favreau P, Benoit E, Hocking HG, et al. (2012) A novel µ-conopeptide, CnIIIC, exerts potent and preferential inhibition of NaV1.2/1.4 channels and blocks neuronal nicotinic acetylcholine receptors. British Journal of Pharmacology. 166: 1654-68 |