Rochel, Natacha

The crystal structure of the nuclear receptor for vitamin D bound to its natural ligand

Rochel, N., Wurtz, J. M., Mitschler, A., Klaholz, B., & Moras, D. (2000) · Molecular Cell

Vitamin D Research StudiesProtein Structure and Dynamics

Cited by 842

Retinoic Acid Receptors Recognize the Mouse Genome through Binding Elements with Diverse Spacing and Topology

Moutier, E., Ye, T., Choukrallah, M.-A., Urban, S., Osz, J., Chatagnon, A., Delacroix, L., Langer, D., Rochel, N., Moras, D., et al. (2012) · Journal of Biological Chemistry

Retinoids in leukemia and cellular processesGenomics and Chromatin Dynamics

Cited by 163

Structural basis for a molecular allosteric control mechanism of cofactor binding to nuclear receptors

Osz, J., Brélivet, Y., Peluso-Iltis, C., Cura, V., Eiler, S., Ruff, M., Bourguet, W., Rochel, N., & Moras, D. (2012) · Proceedings of the National Academy of Sciences

Estrogen and related hormone effectsNuclear Receptors and Signaling

Cited by 84

Structural analysis of nuclear receptors: From isolated domains to integral proteins

Brélivet, Y., Rochel, N., & Moras, D. (2012) · Molecular and Cellular Endocrinology

Protein Structure and DynamicsPeroxisome Proliferator-Activated Receptors

Cited by 64

Phosphorylation of the retinoic acid receptor alpha induces a mechanical allosteric regulation and changes in internal dynamics

Chebaro, Y., Amal, I., Rochel, N., Rochette-Egly, C., Stote, R. H., & Dejaegere, A. (2013) · PLoS Computational Biology

Protein Structure and DynamicsRetinoids in leukemia and cellular processes

Cited by 25

Allosteric Regulation in the Ligand Binding Domain of Retinoic Acid Receptorγ

Chebaro, Y., Sirigu, S., Amal, I., Lutzing, R., Stote, R. H., Rochette-Egly, C., Rochel, N., & Dejaegere, A. (2017) · PLOS ONE

Retinoids in leukemia and cellular processesProtein Structure and Dynamics

Cited by 8