Publications and communications of Mireille Dumoulin

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.