Mahri, S., Wilms, T., Hagedorm, P., Guichard, M.-J., Vanvarenberg, K., Dumoulin, M., Frijlink, H., & Vanbever, R. (01 October 2023). Nebulization of PEGylated recombinant human deoxyribonuclease I using vibrating membrane nebulizers: A technical feasibility study. European Journal of Pharmaceutical Sciences, 189, 106522. doi:10.1016/j.ejps.2023.106522 |
Liu, X., Kouassi, K. G. W., Vanbever, R., & Dumoulin, M. (September 2022). Impact of the PEG length and PEGylation site on the structural, thermodynamic, thermal, and proteolytic stability of mono-PEGylated alpha-1 antitrypsin. Protein Science: A Publication of the Protein Society, 31 (9), 4392. doi:10.1002/pro.4392 |
Caers, J., Duray, E., Vrancken, L., Marcion, G., Bocuzzi, V., De Veirman, K., Krasniqi, A., Lejeune, M., Withofs, N., Devoogdt, N., Dumoulin, M., Karlström, A. E., & D'Huyvetter, M. (2022). Radiotheranostic Agents in Hematological Malignancies. Frontiers in Immunology, 13, 911080. doi:10.3389/fimmu.2022.911080 |
Cantarutti, C., Vargas, C., Dongmo Foumthuim, C. J., Dumoulin, M., La Manna, S., Marasco, D., Santambrogio, C., Grandori, R., Scoles, G., Soler, M. A., Corazza, A., & Fortuna, S. (2021). Insights on peptide topology in the computational design of protein ligands: the example of lysozyme binding peptides. Chemical Physics. doi:10.1039/d1cp02536h |
Rondon, A., Mahri, S., Morales Yanes, F. J., Dumoulin, M., & Vanbever, R. (2021). Protein Engineering Strategies for Improved Pharmacokinetics. Advanced Functional Materials. doi:10.1002/adfm.202101633 |
Duray, E., Lejeune, M., Baron, F., Beguin, Y., Devoogdt, N., Krasniqi, A., Lauwers, Y., Zhao, Y. J., D'Huyvetter, M., Dumoulin, M., & Caers, J. (2021). A non-internalised CD38-binding radiolabelled single-domain antibody fragment to monitor and treat multiple myeloma. Journal of hematology & oncology, 14 (1), 183. doi:10.1186/s13045-021-01171-6 |
vettore, N., Moray, J., Brans, A., Herman, R., Charlier, P., kumita, J., Kerff, F., Dobson, C., & Dumoulin, M. (2021). Characterisation of the structural, dynamic and aggregation properties of the W64R amyloidogenic variant of human lysozyme. Biophysical Chemistry. doi:10.1016/j.bpc.2021.106563 |
Gómez-Benito, M., Granado, N., García-Sanz, P., Michel, A., Dumoulin, M., & Moratalla Rosario. (2020). Modeling Parkinson's Disease With the Alpha-Synuclein Protein. Frontier in Pharmocology. doi:10.3389/fphar.2020.00356 |
Dumoulin, M. (12 February 2020). Reflections on professor Sir Christopher M. Dobson (1949-2019). Biophysical Reviews, 12 (1), 13-18. doi:10.1007/s12551-020-00612-9 |
Cawez, F., Duray, E., Hu, Y., Vandenameele, J., Romao, E., Vinckle, C., Dumoulin, M., Galleni, M., Muyldermans, S., & Vandevenne, M. (25 May 2018). Combinatorial Design of a Nanobody that Specifically Targets Structured RNAs. Journal of Molecular Biology, 430 (11), 1652-1670. doi:10.1016/j.jmb.2018.03.032 |
Pansieri, J., Halim, M. A., Vendrely, C., Dumoulin, M., Legrand, F., Sallanon, Chierici, S., Denti, S., Dagany, X., Dugourd, P., Marquette, C., Antoine, R., & Forge, V. (2018). Mass and charge distributions of amyloid fibers involved in neurodegenerative diseases: Mapping heterogeneity and polymorphism. Chemical Science, 9 (10), 2791-2796. doi:10.1039/c7sc04542e |
Kay, J., Thorn, D., Rhazi, N., Dumoulin, M., Corazza, A., & Damblon, C. (2017). 1H, 13C and 15N backbone resonance assignments of the β-lactamase BlaP from Bacillus licheniformis 749/C and two mutational variants. Biomolecular NMR Assignments. doi:10.1007/s12104-017-9782-3 |
Van Assche, R., Borghgraef, C., Vaneyck, J., Dumoulin, M., Scoof, L., & Temmerman, L. (2017). In vitro aggregating β-lactamase-polyQ chimeras do not induce toxic effects in an in vivo Caenorhabditis elegans model. Journal of Negative Results in Biomedicine. doi:10.1186/s12952-017-0080-5 |
Pansieri, J., Plissonneau, M., Stransky-Heilkron, N., Dumoulin, M., Heinrich-Balard, L., Rivory, P., Morfin, J.-F., Toth, E., Saraiva, M. J., Allémann, E., Tillement, O., Forge, V., Lux, F., & Marquette, C. (2017). Multimodal imaging Gd-nanoparticles functionalized with Pittsburgh compound B or a nanobody for amyloid plaques targeting. Nanomedicine. doi:10.2217/nnm-2017-0079 |
Ahn, M., Hagan, Bernardo-Gancedo, De Genst, E., Newby, Christodoulou, J., Dhulesia, A., Dumoulin, M., Robinson, C., Dobson, C., & Kumita, J. (2016). The Significance of the Location of Mutations for the Native-State Dynamics of Human Lysozyme. Biophysical Journal. doi:10.1016/j.bpj.2016.10.028 |
Plissonneau, Pansieri, J., Heinrich-Balard, L., Morfin, N., Stransky-Heilkron, N., Rivory, P., Mowat, Dumoulin, M., Cohen, R., Allémann, E., Toth, E., Saraiva, M., Louis, C., Tillement, O., Forge, V., Lux, F., & Marquette, C. (25 July 2016). Gd-nanoparticles functionalization with specific peptides for ß-amyloid plaques targeting. Journal of Nanobiotechnology, 14 (1), 10.1186/s12951-016-0212. doi:10.1186/s12951-016-0212-y |
Montagner, C., Nigen, M., Jacquin, O., Willet, N., Dumoulin, M., Karsisiotis, A. I., Roberts, G. C. K., Damblon, C., Redfield, C., & Matagne, A. (2016). The role of active site flexible loops in catalysis and of zinc in conformational stability of Bacillus cereus 569/H/9 beta-lactamase. Journal of Biological Chemistry, 291 (31), 16124-16137. doi:10.1074/jbc.M116.719005 |
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 |
Huynen, C., Filée, P., Matagne, A., Galleni, M., & Dumoulin, M. (28 August 2013). Class A β -Lactamases as Versatile Scaffolds to Create Hybrid Enzymes: Applications from Basic Research to Medicine. BioMed Research International, 2013, 16. doi:10.1155/2013/827621 |
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 |
Gustot, A., Raussens, V., Dehousse, M., Dumoulin, M., Bryant, C. E., Ruysschaert, J.-M., & Lonez, C. (2013). Activation of innate immunity by lysozyme fibrils is critically dependent on cross-β sheet structure. Cellular and Molecular Life Sciences, DOI 10.1007/s00018-012-1245-5. doi:10.1007/s00018-012-1245-5 |
Scarafone, N., Pain, C., Fratamico, A., Gaspard, G., yilmaz, N., Filée, P., Galleni, M., Matagne, A., & Dumoulin, M. (March 2012). Amyloid-like fibril formation by polyQ proteins: a critical balance between the polyQ length and the constraints imposed by the host protein. PLoS ONE, 7 (3). doi:10.1371/journal.pone.0031253 |
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 |
Buell, A. K., Dhulesia, A., Mossuto, M. F., Cremades, N., Kumita, J. R., Dumoulin, M., Welland, M. E., Knowles, T. P. J., Salvatella, X., & Dobson, C. M. (2011). Population of nonnative States of lysozyme variants drives amyloid fibril formation. Journal of the American Chemical Society, 133 (20), 7737-43. doi:10.1021/ja109620d |
Mossuto, M. F., Bolognesi, B., Guixer, B., Dhulesia, A., Agostini, F., Kumita, J. R., Tartaglia, G. G., Dumoulin, M., Dobson, C. M., & Salvatella, X. (2011). Disulfide Bonds Reduce the Toxicity of the Amyloid Fibrils Formed by an Extracellular Protein. Angewandte Chemie International Edition. doi:10.1002/anie.201100986 |
Vandevenne, M., GASPARD, G., Belgsir, E. M., Ramnath, M., Cenatiempo, Y., Delneuville, D., Dumoulin, M., Frère, J.-M., Matagne, A., Galleni, M., & Filee, P. (2011). Effects of monopropanediamino-beta-cyclodextrin on the denaturation process of the hybrid protein BlaPChBD. Biochimica et Biophysica Acta. doi:10.1016/j.bbapap.2011.05.007 |
De Genst, E. J., Guilliams, T., Wellens, J., O'Day, E. M., Waudby, C. A., Meehan, S., Dumoulin, M., Hsu, S.-T. D., Cremades, N., Verschueren, K. H. G., Pardon, E., Wyns, L., Steyaert, J., Christodoulou, J., & Dobson, C. M. (2010). Structure and properties of a complex of alpha-synuclein and a single-domain camelid antibody. Journal of Molecular Biology, 402 (2), 326-43. doi:10.1016/j.jmb.2010.07.001 |
Dhulesia, A., Cremades, N., Kumita, J. R., Hsu, S. T., Mossuto, M. F., Dumoulin, M., Nietlispach, D., Akke, M., Salvatella, X., & Dobson, C. M. (2010). Local Cooperativity in an Amyloidogenic State of Human Lysozyme Observed at Atomic Resolution. Journal of the American Chemical Society. doi:10.1021/ja103524m |
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 |
Mossuto, M. F., Dhulesia, A., Devlin, G., Frare, E., Kumita, J. R., Polverino de Laureto, P., Dumoulin, M., Fontana, A., Dobson, C. M., & Salvatella, X. (2010). The non-core regions of human lysozyme amyloid fibrils influence cytotoxicity. Journal of Molecular Biology, 402 (5), 783-96. doi:10.1016/j.jmb.2010.07.005 |
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 |
Vuchelen, A., O'Day, E., De Genst, E., Pardon, E., Wyns, L., Dumoulin, M., Dobson, C. M., Christodoulou, J., & Hsu, S.-T. D. (2009). (1)H, (13)C and (15)N assignments of a camelid nanobody directed against human alpha-synuclein. Biomolecular NMR Assignments, 3 (2), 231-3. doi:10.1007/s12104-009-9182-4 |
Kumita, J. R., Poon, S., Caddy, G. L., Hagan, C. L., Dumoulin, M., Yerbury, J. J., Stewart, E. M., Robinson, C. V., Wilson, M. R., & Dobson, C. M. (2007). The extracellular chaperone clusterin potently inhibits human lysozyme amyloid formation by interacting with prefibrillar species. Journal of Molecular Biology, 369, 157-161. doi:10.1016/j.jmb.2007.02.095 |
Vandevenne, M., Filée, P., Scarafone, N., Cloes, B., Gaspard, G., Yilmaz, N., Dumoulin, M., François, J.-M., Frère, J.-M., & Galleni, M. (2007). The Bacillus licheniformis BlaP beta-lactamase as a model protein scaffold to study the insertion of protein fragments. Protein Science: A Publication of the Protein Society, 16 (10), 2260-71. doi:10.1110/ps.072912407 |
Dumoulin, M., & Bader, R. (Crit. Eds.). (2006). Methods to study protein aggregation and amyloid formation. Protein and Peptide Letters, 13, 211-212. doi:10.2174/092986606775338399 |
Dumoulin, M., & Bader, R. (2006). A short historical survey of developments in amyloid research. Protein and Peptide Letters, 13 (3), 213-217. doi:10.2174/092986606775338434 |
Dumoulin, M., Kumita, J., & Dobson, C. M. (2006). Normal and aberrant biological self-assembly: Insights from studies of human lysozyme and its amyloidogenic variants. Accounts of Chemical Research, 39, 603-610. doi:10.1021/ar050070g |
Frare, E., Mossuto, M. F., Polverino de Laureto, P., Dumoulin, M., Dobson, C. M., & Fontana, A. (2006). Identification of the Core Structure of Lysozyme Amyloid Fibrils by Proteolysis. Journal of Molecular Biology, 361, 551-561. doi:10.1016/j.jmb.2006.06.055 |
Kumita, J., Johnson, R., Alcocer, M., Dumoulin, M., Holmqvist, F., McCammon, M., Robinson, C., Archer, D., & Dobson, C. M. (2006). Impact of the native-state stability of human lysozyme variants on protein secretion by Pichia pastoris. FEBS Journal, 273, 711-720. doi:10.1111/j.1742-4658.2005.05099.x |
Dumoulin, M., Canet, D., Last, A. M., Pardon, E., Archer, D. B., Muyldermans, S., Wyns, L., Matagne, A., Robinson, C. V., Redfield, C., & Dobson, C. M. (25 February 2005). Reduced global copperativity is a common feature underlying the amyloidogenicity of pathogenic lysozyme mutations. Journal of Molecular Biology, 346 (3), 773-788. doi:10.1016/j.jmb.2004.11.020 |
Johnson, R. J. K., Christodoulou, J., Dumoulin, M., Caddy, G. L., Alcocer, M. J. C., Murtagh, G. J., Kumita, J., Larsson, G., Robinson, C. V., Archer, D. B., Luisi, B., & Dobson, C. M. (2005). Rationalising Lysozyme Amyloidosis: Insights from the Structure and Solution Dynamics of T70N Lysozyme. Journal of Molecular Biology, 352, 823-836. doi:10.1016/j.jmb.2005.07.040 |
Dumoulin, M., & Dobson, C. (2004). Probing the origins, diagnosis and treatment of amyloid diseases using antibodies. Biochimie, 86, 589-600. doi:10.1016/j.biochi.2004.09.012 |
Dumoulin, M., Last, A. M., Desmyter, A., Decanniere, K., Canet, D., Larsson, G., Spencer, A., Archer, D. B., Sasse, J., Muyldermans, S., Wyns, L., Redfield, C., Matagne, A., Robinson, C. V., & Dobson, C. M. (14 August 2003). A camelid antibody fragment inhibits the formation of amyloid fibrils by human lysozyme. Nature, 424 (6950), 783-788. doi:10.1038/nature01870 |
Murtagh, M., Archer, D., Dumoulin, M., Ridout, S., Matthews, M., Arshad, S. H., & Alcocer, M. (2003). In vitro stability and immunoreactivity of the native and recombinant plant food 2S albumins Ber e 1 and SFA-8. Clinical and Experimental Allergy, 8, 1147-1152. doi:10.1046/j.1365-2222.2003.01736.x |
Alcocer, M., Murtagh, G. J., Bailey, K., Dumoulin, M., Meseguer, A. S., Parker, M., & Archer, D. (2002). The Disulphide Mapping, Folding and Characterisation of Recombinant Ber e 1, an Allergenic Protein, and SFA8, Two Sulphur-rich 2 S Plant Albumins. Journal of Molecular Biology, 324, 165-175. doi:10.1016/S0022-2836(02)01061-6 |
Dumoulin, M., Conrath, K., Van Meirhaeghe, A., Meersman, F., Heremans, K., Frenken, L. G. J., Muyldermans, S., Wyns, L., & Matagne, A. (2002). Single-domain antibody fragments with high conformational stability. Protein Science: A Publication of the Protein Society, 11 (3), 500-15. doi:10.1110/ps.34602 |
Murtagh, G., Dumoulin, M., Alcocer, M., & Archer, D. (2002). Stability of recombinant 2 S albumin allergens in vitro. Biochemical Society Transactions, 30, 913-915. doi:10.1042/BST0300913 |
Dumoulin, M., Ueno, H., Hayashi, R., & Balny, C. (1999). Contribution of the carbohydrate moiety to conformational stability of the carboxypeptidase Y high pressure study. European Journal of Biochemistry, 262 (2), 475-83. doi:10.1046/j.1432-1327.1999.00397.x |
Dumoulin, M., & Hayashi, R. (1998). High presure: a unique tool for pressurisation. Food Science and Technology International, 4, 99-113. |
Dumoulin, M., Osawa, S., & Hayashi, R. (1998). Textural properties of pressure-induced gels of food proteins obtained under different temperatures including zero. Journal of Food Science, 63, 92-96. doi:10.1111/j.1365-2621.1998.tb15683.x |
Dumoulin, M., Ozawa, S., & Hayashi, R. (1997). Textural properties of pressure-induced gels of food proteins obtained under different temperatures. In K. Heremans (Ed.), High Pressure Research in Biosciences and Biotechnology (pp. 383-388). Leuven, Belgium: Leuven University Press. |
Dumoulin, M., Ozawa, S., & Hayashi, R. (1997). Textural properties of pressure-induced gels of food proteins obtained under different temperatures. In A. Suzuki & R. Hayashi (Eds.), High Pressure Bioscience and Technology (pp. 101-108). Kyoto, Japan: San-ei Shuppan. |