Moras, Dino
Centre National de la Recherche Scientifique · Inserm · Institut de génétique et de biologie moléculaire et cellulaire
10 papers on CoChatORCID 0000-0001-7028-2320
Most cited papers
- Verified
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
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Transmembrane Signaling across the Ligand-Gated FhuA Receptor
Locher, K. P., Rees, B., Koebnik, R., Mitschler, A., Moulinier, L., Rosenbusch, J. P., & Moras, D. (1998) · Cell
Bacterial Genetics and BiotechnologyDrug Transport and Resistance Mechanisms
Cited by 540
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Ultrahigh resolution drug design I: Details of interactions in human aldose reductase–inhibitor complex at 0.66 Å
Howard, E. I., Sanishvili, R., Cachau, R. E., Mitschler, A., Chevrier, B., Barth, P., Lamour, V., Van Zandt, M., Sibley, E., Bon, C., et al. (2004) · Proteins: Structure, Function, and Bioinformatics
Aldose Reductase and TaurineEnzyme Structure and Function
Cited by 319
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All-trans retinoic acid is a ligand for the orphan nuclear receptor RORβ
Stehlin-Gaon, C., Willmann, D., Zeyer, D., Sanglier, S., Van Dorsselaer, A., Renaud, J.-P., Moras, D., & Schüle, R. (2003) · Nature Structural & Molecular Biology
Retinoids in leukemia and cellular processesNuclear Receptors and Signaling
Cited by 231
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Molecular Structure of Human TFIIH
Schultz, P., Fribourg, S., Poterszman, A., Mallouh, V., Moras, D., & Egly, J. M. (2000) · Cell
Genomics and Chromatin DynamicsDNA Repair Mechanisms
Cited by 180
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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
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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
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Phosphorylation by PKA potentiates retinoic acid receptor α activity by means of increasing interaction with and phosphorylation by cyclin H/cdk7
Gaillard, E., Bruck, N., Brelivet, Y., Bour, G., Lalevée, S., Bauer, A., Poch, O., Moras, D., & Rochette-Egly, C. (2006) · Proceedings of the National Academy of Sciences
Retinoids in leukemia and cellular processesGenomics and Chromatin Dynamics
Cited by 76
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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
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In Vivo Topoisomerase I Inhibition Attenuates the Expression of Hypoxia-Inducible Factor 1α Target Genes and Decreases Tumor Angiogenesis
Guérin, E., Raffelsberger, W., Pencreach, E., Maier, A., Neuville, A., Schneider, A., Bachellier, P., Rohr, S., Petitprez, A., Poch, O., et al. (2012) · Molecular Medicine
Cancer therapeutics and mechanismsCancer, Hypoxia, and Metabolism
Cited by 44
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