Robert, C., Kerff, F., Bouillenne, F., Gavage, M., Vandevenne, M., Filée, P., & Matagne, A. (2023). Structural analysis of the interaction between human cytokine BMP-2 and the antagonist Noggin reveals molecular details of cell chondrogenesis inhibition. Journal of Biological Chemistry, 102892. doi:10.1016/j.jbc.2023.102892 |
Poncin, M. A., Van Meerbeeck, P., Simpson, J. D., Clippe, A., Tyckaert, F., Bouillenne, F., Degand, H., Matagne, A., Morsomme, P., Knoops, B., & Alsteens, D. (27 November 2021). Role of the Redox State of Human Peroxiredoxin-5 on Its TLR4-Activating DAMP Function. Antioxidants (Basel, Switzerland), 10 (12), 1902. doi:10.3390/antiox10121902 |
Frère, J.-M., Bogaerts, P., Huang, T.-D., Stefanic, P., Moray, J., Bouillenne, F., & Brans, A. (2020). Interactions between Avibactam and Ceftazidime-Hydrolyzing Class D β-Lactamases. Biomolecules, 10 (3). doi:10.3390/biom10030483 |
Demelenne, A., NAPP, A., Bouillenne, F., Crommen, J., Servais, A.-C., & Fillet, M. (2019). Insulin aggregation assessment by capillary gel electrophoresis without sodium dodecyl sulfate: Comparison with size-exclusion chromatography. Talanta, 199, 457-463. doi:10.1016/j.talanta.2019.02.074 |
Miranda Astudillo, H. V., Yadav, S., Colina-Tenorio, L., Bouillenne, F., Degand, H., Morsomme, P., Boekema, E., & Cardol, P. (2018). The atypical subunit composition of respiratory complexes I and IV is associated with original extra structural domains in Euglena gracilis. Scientific Reports, 8 (1), 9698. doi:10.1038/s41598-018-28039-z |
Rodríguez, M. M., Herman, R., Ghiglione, B., Kerff, F., D'Amico González, G., Bouillenne, F., Galleni, M., Handelsman, J., Charlier, P., Gutkind, G., Sauvage, E., & Power, P. (July 2017). Crystal Structure and Kinetic Analysis of the Class B3 Di-Zinc Metallo-β-Lactamase LRA-12 from an Alaskan Soil Metagenome. PLoS ONE, 12 (7), 0182043. doi:10.1371/journal.pone.0182043 |
Sauvage, E., Herman, R., Petrella, S., Duez, C., Bouillenne, F., Frère, J.-M., & Charlier, P. (2005). Crystal structure of the Actinomadura R39 DD-peptidase reveals new domains in penicillin-binding proteins. Journal of Biological Chemistry, 280 (35), 31249-56. doi:10.1074/jbc.M503271200 |
Duez, C., Hallut, S., Rhazi, N., Amoroso, A. M., Bouillenne, F., & Coyette, J. (July 2004). The ponA gene of Enterococcus faecalis JH2-2 codes for a low-affinity class a penicillin-binding protein. Journal of Bacteriology, 186 (13), 4412-4416. doi:10.1128/JB.186.13.4412-4416.2004 |
Douette, P., Navet, R., Bouillenne, F., Brans, A., Sluse-Goffart, C., Matagne, A., & Sluse, F. (May 2004). Secondary-structure characterization by far-UV CD of highly purified uncoupling protein 1 expressed in yeast. Biochemical Journal, 380 (Pt 1), 139-145. doi:10.1042/BJ20031957 |
Georlette, D., Blaise, V., Bouillenne, F., Damien, B., Thorbjarnardottir, S. H., Depiereux, E., Gerday, C., Uversky, V. N., & Feller, G. (February 2004). Adenylation-dependent conformation and unfolding pathways of the NAD(+)-dependent DNA ligase from the thermophile Thermus scotoductus. Biophysical Journal, 86 (2), 1089-1104. doi:10.1016/S0006-3495(04)74184-3 |
Georlette, D., Blaise, V., Dohmen, C., Bouillenne, F., Damien, B., Depiereux, E., Gerday, C., Uversky, V. N., & Feller, G. (12 December 2003). Cofactor binding modulates the conformational stabilities and unfolding patterns of NAD(+)-dependent DNA ligases from Escherichia coli and Thermus scotoductus. Journal of Biological Chemistry, 278 (50), 49945-49953. doi:10.1074/jbc.M307761200 |
Cheggour, A., Fanuel, L., Duez, C., Joris, B., Bouillenne, F., Devreese, B., Van Driessche, G., Van Beeumen, J., Frère, J.-M., & Goffin, C. (November 2000). The Dppa Gene of Bacillus Subtilis Encodes a New D-Aminopeptidase. Molecular Microbiology, 38 (3), 504-13. doi:10.1046/j.1365-2958.2000.02117.x |