Thorn, D., Pain, C., Scarafone, N., Huynen, C., Preumont, S., Menzer, L., Duez, C., & Dumoulin, M. (20 November 2013). Switching to the Dark Side: Repositioning of Polyglutamine Repeat Promotes Amyloid Fibril Formation by the Model Protein, β-Lactamase BlaP [Paper presentation]. 4th Scandinavian Meeting on Amyloid Proteins and Disease, Lund, Sweden. |
de Genst, E., Chan, P., Pardon, E., Hsu, S., Kumita, J., Christodoulou, J., Menzer, L., Chirgadze, D., Robinson, C., Muyldermans, S., Matagne, A., Wyns, L., Dobson, C., & Dumoulin, M. (2013). A Nanobody Binding to Non-amyloidogenic Regions of the Protein Human Lysozyme Enhances Partial Unfolding but Inhibits Amyloid Fibril Formation. Journal of Physical Chemistry B. doi:10.1021/jp403425z Peer Reviewed verified by ORBi |
Dumont, J., pardon, E., Aumont-Nicaise, M., Menzer, L., Kumita, J., Willet, N., Jérôme, C., Mazzucchelli, G., Buell, A., Desmadril, M., De Pauw, E., Wyns, L., Dobson, C., & Dumoulin, M. (June 2012). Nanobodies as structural probes to investigate the mechanism of fibril formation by the amyloidogenic variants of human lysozyme [Poster presentation]. Gordon Research Conferences: Biopolymers. |
Kumita, J. R., Helmfors, L., Williams, J., Luheshi, L. M., Menzer, L., Dumoulin, M., Lomas, D. A., Crowther, D. C., Dobson, C. M., & Brorsson, A.-C. (2012). Disease-related amyloidogenic variants of human lysozyme trigger the unfolded protein response and disturb eye development in Drosophila melanogaster. FASEB Journal. doi:10.1096/fj.11-185983 Peer Reviewed verified by ORBi |
Dumont, J., Pardon, E., Aumont-Nicaise, M., Desmadril, M., Menzer, L., Wyns, L., steyaert, J., Dobson, C., & Dumoulin, M. (2011). Nanobodies as structural probes to investigate the mechanism of fibril formation by the amyloidogenic variants of human lysozyme [Poster presentation]. Amyloid Fibrils, Prions and Precursors: Molecules for Targeted Intervention, Halle (Saale), Germany. |
Dumont, J., Menzer, L., Pardon, E., Wyns, L., Steyaert, J., Dobson, C., & Dumoulin, M. (2010). Nanobodies as structural probes to investigate the mechanism of fibril formation by the amyloidogenic variants of human lysozyme [Poster presentation]. Single Domain Antibodies Come of Age, Ghent, Belgium. |
Dumont, J., Pardon, E., Menzer, L., Duez, C., Wyns, L., Steyaert, J., Dobson, C., & Dumoulin, M. (2010). Camelid single-domain antibody fragments as structural probes to study the mechanism of human lysozyme fibrils formation [Poster presentation]. Pôle d'attraction inter-universitaire PAI “P6/19, Liège, Belgium. |
Dumont, J., Pardon, E., Menzer, L., wyns, L., Dobson, C., & Dumoulin, M. (2010). Camelid single-domain antibody fragments as structural probes to study the mechanism of human lysozyme fibrils formation [Poster presentation]. Jacques Monod conference: Protein misfolding and assembly in ageing and disease, Roscoff, France. |
Frare, E., Mossuto, M. F., Polverino de Laureto, P., Tolin, S., Menzer, L., Dumoulin, M., Dobson, C. M., & Fontana, A. (30 January 2009). Characterization of Oligomeric Species on the Aggregation Pathway of Human Lysozyme. Journal of Molecular Biology, 387, 17-27. doi:10.1016/j.jmb.2009.01.049 Peer Reviewed verified by ORBi |
Dumont, J., Menzer, L., Scarafone, N., Duez, C., & Dumoulin, M. (2009). Production of four amyloidogenic variants of human lysozyme as inclusion bodies in Escherichia coli [Poster presentation]. Penicillin-recognizing enzymes: from enzyme kinetics to protein folding, Liège, Belgium. |
Menzer, L., Tocquin, P., Dony, N., Chevigné, A., Périlleux, C., Matagne, A., Dobson, C. M., & Dumoulin, M. (16 February 2008). Optimization of the Production of the Amyloidogenic Variants of Human Lysozyme [Poster presentation]. 3rd EURAMY meeting, Berlin, Germany. |
Chan, P. H., Pardon, E., Menzer, L., De Genst, E., Kumita, J., Christodoulou, J., Saerens, D., Brans, A., Bouillenne, F., Archer, D., Robinson, C., Muyldermans, S., Matagne, A., Redfield, C., Wyns, L., Dobson, C. M., & Dumoulin, M. (2008). Engineering a camelid antibody fragment that binds to the active site of human lysozyme and inhibits its conversion into amyloid fibrils. Biochemistry, 47, 11041-11054. doi:10.1021/bi8005797 Peer Reviewed verified by ORBi |
Durand-Dubief, M., Absalon, S., Menzer, L., Ngwabyt, S., Ersfeld, K., & Bastin, P. (2007). The Argonaute protein TbAGO1 contributes to large and mini-chromosome segregation and is required for control of RIME retroposons and RHS pseudogene-associated transcripts. Molecular and Biochemical Parasitology. doi:10.1016/j.molbiopara.2007.07.016 Peer Reviewed verified by ORBi |