| Peptide-based covalent inhibitors bearing mild electrophiles to target a conserved his residue of the bacterial sliding clamp
Compain, G., Monsarrat, C., Blagojevic, J., Brillet, K., Dumas, P., Hammann, P., … Guichard, G. (2024). Peptide-based covalent inhibitors bearing mild electrophiles to target a conserved his residue of the bacterial sliding clamp. JACS Au, 4(2), 432-440. https://doi.org/10.1021/jacsau.3c00572 |
| Filling of a water-free void explains the allosteric regulation of the β<sub>1</sub>-adrenergic receptor by cholesterol
Abiko, L. A., Dias Teixeira, R., Engilberge, S., Grahl, A., Mühlethaler, T., Sharpe, T., & Grzesiek, S. (2022). Filling of a water-free void explains the allosteric regulation of the β1-adrenergic receptor by cholesterol. Nature Chemistry, 14, 1133-1141. https://doi.org/10.1038/s41557-022-01009-9 |
| Chimeric single α-helical domains as rigid fusion protein connections for protein nanotechnology and structural biology
Collu, G., Bierig, T., Krebs, A. S., Engilberge, S., Varma, N., Guixà-González, R., … Benoit, R. M. (2022). Chimeric single α-helical domains as rigid fusion protein connections for protein nanotechnology and structural biology. Structure, 30(1), 95-106. https://doi.org/10.1016/j.str.2021.09.002 |
| Probing ligand binding of endothiapepsin by 'temperature-resolved' macromolecular crystallography
Huang, C. Y., Aumonier, S., Engilberge, S., Eris, D., Smith, K. M. L., Leonarski, F., … Wang, M. (2022). Probing ligand binding of endothiapepsin by 'temperature-resolved' macromolecular crystallography. Acta Crystallographica Section D: Structural Biology, 78, 964-974. https://doi.org/10.1107/S205979832200612X |
| Crystal structure of a key enzyme for anaerobic ethane activation
Hahn, C. J., Lemaire, O. N., Kahnt, J., Engilberge, S., Wegener, G., & Wagner, T. (2021). Crystal structure of a key enzyme for anaerobic ethane activation. Science, 373(6550), 118-121. https://doi.org/10.1126/science.abg1765 |
| Biochemical, structural and dynamical studies reveal strong differences in the thermal-dependent allosteric behavior of two extremophilic lactate dehydrogenases
Iorio, A., Roche, J., Engilberge, S., Coquelle, N., Girard, E., Sterpone, F., & Madern, D. (2021). Biochemical, structural and dynamical studies reveal strong differences in the thermal-dependent allosteric behavior of two extremophilic lactate dehydrogenases. Journal of Structural Biology, 213(3), 107769 (11 pp.). https://doi.org/10.1016/j.jsb.2021.107769 |
| Iterative structure-based optimization of short peptides targeting the bacterial sliding clamp
Monsarrat, C., Compain, G., André, C., Engilberge, S., Martiel, I., Oliéric, V., … Burnouf, D. Y. (2021). Iterative structure-based optimization of short peptides targeting the bacterial sliding clamp. Journal of Medicinal Chemistry, 64(23), 17063-17078. https://doi.org/10.1021/acs.jmedchem.1c00918 |
| Facile fabrication of protein-macrocycle frameworks
Ramberg, K. O., Engilberge, S., Skorek, T., & Crowley, P. B. (2021). Facile fabrication of protein-macrocycle frameworks. Journal of the American Chemical Society, 143(4), 1896-1907. https://doi.org/10.1021/jacs.0c10697 |
| Krypton-derivatization highlights O<sub>2</sub>-channeling in a four-electron reducing oxidase
Engilberge, S., Wagner, T., Carpentier, P., Girard, E., & Shima, S. (2020). Krypton-derivatization highlights O2-channeling in a four-electron reducing oxidase. Chemical Communications, 56(74), 10863-10866. https://doi.org/10.1039/d0cc04557h |
