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Dumont Janice

Main Referenced Co-authors
Dumoulin, Mireille  (9)
Dobson, Christopher (6)
Menzer, Linda  (6)
Pardon, Els (5)
Wyns, Lode (5)
Main Referenced Keywords
Amyloid Fibril (5); Lysozyme (5); Nanobodies (5); Amyloid fibrils (1); fibres amyloïdes (1);
Main Referenced Unit & Research Centers
CIP - Centre d'Ingénierie des Protéines - ULiège [BE] (2)
Main Referenced Disciplines
Biochemistry, biophysics & molecular biology (9)
Biotechnology (1)

Publications (total 10)

The most downloaded
741 downloads
Pain, C., Dumont, J., & Dumoulin, M. (2015). Camelid single-domain antibody fragments: Uses and prospects to investigate protein misfolding and aggregation, and to treat diseases associated with these phenomena. Biochimie. doi:10.1016/j.biochi.2015.01.012 https://hdl.handle.net/2268/189396

The most cited

34 citations (Scopus®)

Pain, C., Dumont, J., & Dumoulin, M. (2015). Camelid single-domain antibody fragments: Uses and prospects to investigate protein misfolding and aggregation, and to treat diseases associated with these phenomena. Biochimie. doi:10.1016/j.biochi.2015.01.012 https://hdl.handle.net/2268/189396

Pain, C., Dumont, J., & Dumoulin, M. (2015). Camelid single-domain antibody fragments: Uses and prospects to investigate protein misfolding and aggregation, and to treat diseases associated with these phenomena. Biochimie. doi:10.1016/j.biochi.2015.01.012
Peer Reviewed verified by ORBi

Dumont, J. (2014). Etude des propriétés des variants amyloïdogéniques du lysozyme humain à l’aide de fragments d’anticorps à chaînes lourdes comme sondes structurales [Doctoral thesis, ULiège - Université de Liège]. ORBi-University of Liège. https://orbi.uliege.be/handle/2268/166571

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.

Dumont, J., Kumita, J., Menzer, L., Pardon, E., Aumont-Nicaise, M., Desmadril, M., Wyns, L., Steyaert, J., Dobson, C., & Dumoulin, M. (26 August 2011). VHHs as structural probes to investigate the mechanis of fibril formation by the amyloidogenic variants of human lysozyme [Paper presentation]. Amyloid Fibrils, Prions and Precursors: Molecules for Targeted Intervention, Halle, Germany.

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.

Hagan, C. L., Johnson, R. J. K., Dhulesia, A., Dumoulin, M., Dumont, J., De Genst, E., Christodoulou, J., Robinson, C. V., Dobson, C. M., & Kumita, J. R. (2010). A non-natural variant of human lysozyme (I59T) mimics the in vitro behaviour of the I56T variant that is responsible for a form of familial amyloidosis. Protein Engineering, Design and Selection, 23 (7), 499-506. doi:10.1093/protein/gzq023
Peer Reviewed verified by ORBi

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.

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.

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