Publications and communications of Mireille Dumoulin

Redeghieri, P., Moray, J., Kerff, F., Gohy, S., Leal, T., Muyldermans, S., Vanbever, R., Morales Yánez, F. J.* , & Dumoulin, M.*. (27 November 2024). Enzymatic, structural, and biophysical characterization of a single-domain antibody (VHH) selectively and tightly inhibiting neutrophil elastase and exhibiting favorable developability properties. Protein Science: A Publication of the Protein Society, 33 (12), 5227. doi:10.1002/pro.5227

Redeghieri, P., Moray, J., Kerff, F., Mottais, A., Leal, T., Gohy, S., Muylderman, S., Vanbever, R., Morales Yánez, F. J., & Dumoulin, M. (15 November 2024). NbE201: a single-domain antibody fragment to inhibit neutrophil elastase and reduce inflammation [Paper presentation]. SFMBBM - PhD Day 2024 (UNamur), Namur, Belgium.

Godard, V., Rossini, M., Dumoulin, M., & Vanbever, R. (14 October 2024). DESIGN OF LONG-ACTING THERAPEUTIC PROTEINS FOR INHALATION [Paper presentation]. Journées de Recherche Respiratoire.

Morales-Yánez, F. J., Cawez, F., Redeghieri, P., Moray, J., Vincke, C., Struelens, G., Leal, T., Vanbever, R., Vanderplasschen, A., Muyldermans, S., Galleni, M., & Dumoulin, M. (16 September 2024). DIRECTIONAL SANDWICH PANNING IN SOLUTION TO SELECT INHIBITORY NANO-ANTIBODIES AGAINST FRAGILE ENZYMES INCLUDING PROTEASES [Paper presentation]. FASEB 2024 Advanced Course, Proteolysis: at the interface between health and disease, Bled, Slovenia.

Redeghieri, P., Moray, J., Kerff, F., Mottais, A., Vincke, C., Leal, T., Gohy, S., Morales Yánez, F. J.* , & Dumoulin, M.*. (16 September 2024). NbE201: a Single-Domain Antibody fragment to Inhibit Neutrophil Elastase and reduce inflammation [Paper presentation]. FEBS Wokshop 2024, Proteolysis: at the interface between health and disease, Bled, Slovenia.

Redeghieri, P., Moray, J., Kerff, F., Mottais, A., Vandersraeten, J., Vincke, C., Leal, T., Gohy, S., Muylderman, S., Vanbever, R., Morales-Yánez, F. J.* , & Dumoulin, M.*. (13 June 2024). A Single-Domain Antibody Fragment (VHH) Inhibiting Neutrophil Elastase for the Treatment of Inflammatory Lung Diseases​ [Paper presentation]. Proteolytic Enzymes and Their Inhibitors, Gordon Research Conference, Lucca, Italy.

Redeghieri, P., Moray, J., Kerff, F., Mottais, A., Vandersraeten, J., Vincke, C., Leal, T., Gohy, S., Muylderman, S., Vanbever, R., Morales Yánez, F. J.* , & Dumoulin, M.*. (09 June 2024). A Single-Domain Antibody Fragment (VHH) Inhibiting Neutrophil Elastase for the Treatment of Inflammatory Lung Diseases [Poster presentation]. Proteolytic Enzymes and Their Inhibitors (GRS) Gordon Research Seminar.

Redeghieri, P., Moray, J., Kerff, F., Leal, T., Muyldermans, S., Vanbever, R., Morales Yánez, F. J.* , & Dumoulin, M.*. (30 May 2024). ENZYMATIC, STRUCTURAL AND BIOPHYSICAL CHARACTERIZATION OF A SINGLE DOMAIN ANTIBODY (VHH) SELECTIVELY AND TIGHTLY INHIBITING NEUTROPHIL ELASTASE AND EXHIBITING FAVORABLE DEVELOPABILITY PROPERTIES [Paper presentation]. Interuniversity PhD Student Day, Louvain-la-Neuve, Belgium.

Redeghieri, P., Moray, J., Kerff, F., Mottais, A., Vandersraeten, J., Vincke, C., Leal, T., Gohy, S., Muylderman, S., Vanbever, R., Morales Yánez, F. J.* , & Dumoulin, M.*. (23 May 2024). A single-domain antibody fragment (VHH) inhibiting neutrophil elastase for the treatment of inflammatory lung diseases [Paper presentation]. InBioS DAY, Liège, Belgium.

Dumoulin, M. (07 March 2024). ALPANANO : A PLATEFORM TO GENERATE VHHs [Paper presentation]. BioLiège.

Dumoulin, M. (15 November 2023). Nanobodies engineering, Techniques to measure the affinity and stability of Nanobodies, Applications of Nanobodies for research, therapy and diagnostic [Paper presentation]. Workshop entitled Revolutionizing precision therapies: Harnessing the power of Nanoantibodies, Quito, Ecuador.

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

Redeghieri, P., Moray, J., Kerff, F., Vincke, C., Leal, T., Muyldermans, S., Vanbever, R., Morales Yánez, F. J., & Dumoulin, M. (18 September 2023). In vitro characterisation of a Nanobody selectively inhibiting human Neutrophil elastase [Poster presentation]. Single domain antibodies conference 2023, Paris, France.

Cawez, F., Mercuri, P., Piccirilli, A., Perilli, M., Morales Yánez, F. J., Dumoulin, M., & Galleni, M. (02 June 2023). Selection and characterization of anti-NDM-1 nanobodies [Poster presentation]. 14 th Beta-Lactam and beta-lactamase meeting, L'Aquila, Italy.

CAERS, J., Duray, E., Dumoulin, M., & D’Huyvetter, M. (2023). ANTI-CD38 SINGLE-DOMAIN ANTIBODIES IN DISEASE MONITORING AND TREATMENT.

Cawez, F., Mercuri, P., Morales Yánez, F. J., Maalouf, R., Vandevenne, M., Kerff, F., Guérin, V., Mainil, J., Thiry, D., Saulmont, M., Vanderplasschen, A., Lafaye, P., Aymé, G., Bogaerts, P., Dumoulin, M., & Galleni, M. (2023). Development of Nanobodies as Theranostic Agents against CMY-2-Like Class C b-Lactamases. Antimicrobial Agents and Chemotherapy. doi:10.1128/aac.01499-22

Dumoulin, M., Morales Yánez, F. J., Redeghieri, P., Vanbever, R., Vanderstraeten, J., Leal, T., Mottais, A., Muyldermans, S., & Vincke, C. (2023). Single-domain antibody for the inhibition of neutrophil elastase activity.

Dumoulin, M. (29 November 2022). Nanobodies: Next antibody generation for research, diagnostic and therapeutic applications [Paper presentation]. Research seminar, U.

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

Redeghieri, P., Vanbever, R., & Dumoulin, M. (15 June 2022). Nanobodies as therapeutic nanomedicines for lungs inflammatory diseases [Paper presentation]. 5th InBios Day, Liège, Belgium.

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

Dumoulin, M. (15 October 2021). ALPANANO: A community platform to generate and select Nanobodies [Paper presentation]. GIGA Seminar, Liège, Belgium.

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

Dumoulin, M. (03 September 2021). Lysozyme misfolding and aggregation: from Oxbridge to Liège [Paper presentation]. The 18th one-day symposium of the Belgian Biophysical Society, Liège, Belgium.

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 and 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

Dumoulin, M. (25 November 2019). Use of single-domain camelid antibody fragments (VHHs or Nanobodies) to explore and modify the biological and pathological function(s) of proteins [Paper presentation]. Research seminars of Belgian Nuclear Research Centre, Mol, Belgium.

Dumoulin, M. (28 May 2019). DiaSyn: Development of a new in vivo radiotracer for alpha-synuclein [Paper presentation]. EuroNanomed Meeting -Review Seminar for funded projects, Bratislava, Slovakia.

Dumoulin, M. (31 August 2018). Use of Nanobodies as structural probes to study protein misfolding and aggregation [Paper presentation]. The 16th one-day symposium on Protein Folding and Stability, Liège, Belgium.

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

Kay, J., Corazza, A., Dumoulin, M., & Damblon, C. (Other coll.). (01 February 2018). BLUU-Tramp: a new H/D exchange method to identify the protein unfolding landscape [Poster presentation]. Jennifer Kay, Liège, Belgium.

Napp, A., Houbart, V., Demelenne, A., Merville, M.-P., Crommen, J., Dumoulin, M., Garraux, G., Servais, A.-C., & Fillet, M. (2018). Separation and determination of alpha-synuclein monomeric and oligomeric species using two electrophoretic approaches. Electrophoresis, 39 (23), 3022-3031. doi:10.1002/elps.201800224

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

Vettore, N., Kumita, J., Moray, J., Brans, A., Kerff, F., Dobson, C., & Dumoulin, M. (15 September 2016). CHARACTERISATION OF THE STRUCTURAL, DYNAMIC AND AGGREGATION PROPERTIES OF THE W64R AMYLOIDOGENIC MUTANT OF LYSOZYME [Poster presentation]. CNRS - Jacques Monod Conference “Protein misfolding in disease - Toxic aggregation-prone proteins in aging and age-related diseases: from structure to pathology and spreading" - Roscoff.

Dumoulin, M. (29 July 2016). Model polyQ proteins based on the B-lactamase BlaP : How non-polyQ regions influence the polyQ length-dependent aggregation process [Paper presentation]. Departemental seminars, Department of Chemistry, Graduate School of Science, Kobe University, Hyogo 657-8501, KOBE, Japan.

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

Dumoulin, M. (29 July 2015). Model polyQ proteins based on the B-lactamase BlaP : How non-polyQ regions influence the polyQ length-dependent aggregation process [Paper presentation]. Kobe University Research Seminars.

Willet, N., Bastin, F., Dorval, F., Huynen, C., Dumoulin, M., & Duwez, A.-S. (02 July 2015). AFM for monitoring the elongation of amyloid fibrils made of polyQ proteins [Paper presentation]. Journée du Département de Chimie, Liège, Belgium.

Huynen, C., Willet, N., Buell, A. K., Duwez, A.-S., Jérôme, C., & Dumoulin, M. (2015). Influence of the protein context on the polyglutamine length-dependent elongation of amyloid fibrils. Biochimica et Biophysica Acta - Proteins and Proteomics, 1854, 239-248. doi:10.1016/j.bbapap.2014.12.002

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., Willet, N., Buell, A. K., Maritan, M., Duwez, A.-S., Jérôme, C., & Dumoulin, M. (26 November 2014). Role of the polyQ length and non-polyQ regions during the aggregation process into amyloid fibrils of model polyQ proteins [Poster presentation]. Science for Business - BioWin Day 2014, Louvain-La-Neuve, Belgium.

Dumoulin, M. (30 October 2014). Mechanism of aggregation of polyglutamine (polyQ) proteins which are associated with neurodegenerative amyloidoses: Creation and characterization of polyQ hybrid proteins made from the beta-lacatamse BlaP [Paper presentation]. Chemistry mini symposium: Protein Amyloid Degeneration Still an Open Challenge.

Huynen, C., Willet, N., Buell, A. K., Maritan, M., Duwez, A.-S., Jérôme, C., & Dumoulin, M. (18 October 2014). Role of non-polyQ regions on the aggregation process by polyQ proteins into amyloid fibrils [Poster presentation]. 25th Regensburger Faltertage, Regensburg, Germany.

Huynen, C., Willet, N., Buell, A. K., Maritan, M., Duwez, A.-S., Jérôme, C., & Dumoulin, M. (28 July 2014). Role of non-polyQ regions on the aggregation process by polyQ proteins into amyloid fibrils [Poster presentation]. Neurobiology of Brain Disorders, Neurodegeneration and Aging-Related Disorders of the Nervous System, Girona, Spain.

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.

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

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.

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

Pain, C., Scarafone, N., Maruccia, C., Jaspar, A., Buys, N., Willibal, K., Filée, P., Galleni, M., Matagne, A., Steyaert, J., Pardon, E., & Dumoulin, M. (27 August 2011). Generation of single-domain antidoby fragments raised against proteins containing polyglutamine expansions [Paper presentation]. Amyloid Fibrils, Prions and Precursors: Molecules for Targeted Intervention, Halle, Germany.

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.

Dumoulin, M. (26 August 2011). Engineering specific nanobodies to probe the molecular mechanism of lysozyme amyloid fibril formation [Paper presentation]. Amyloid Fibrils, Prions and Precursors: Molecules for Targeted Intervention, Halle, Germany.

Chavignon, C., Pardon, E. (Other coll.), Wyns, L. (Other coll.), Muyldermans, S. (Other coll.), & Dumoulin, M. (Other coll.). (August 2011). VHHs as model proteins to investigate amyloid fibril formation: effect of seeding and cross-seeding on the stability of fibrils [Poster presentation]. Amyloid 2011 - Amyloid fibrils, prions and precursors: Molecules for targeted intervention, Halle, Germany.

Pain, C., Scarafone, N., Jaspar, A., Buys, N., Willibal, K., Filée, P., Galleni, M., Matagne, A., Steyaert, J., Pardon, E., & Dumoulin, M. (25 January 2011). Generation of camelid single-domain antibody fragments raised against proteins containing polyglutamine expansions [Poster presentation]. Interuniversity Attraction Poles, Liège, Belgium.

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

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.

Dumoulin, M., & Chavignon, C. (January 2011). Mechanism of amyloid fibril formation by human lysozyme and VHHs [Paper presentation]. PAI - Proteins : interactions involved in folding, function and supramolecular assemblages, Liège, Belgium.

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

Pain, C., Scarafone, N., Jaspar, A., Buys, N., Willibal, K., Filée, P., Galleni, M., Matagne, A., Steyaert, J., Pardon, E., & Dumoulin, M. (10 December 2010). Generation of camelid single-domain antibody fragments raised against proteins containing polyglutamine expansions [Poster presentation]. Journée des doctorants, Liège, Belgium.

Dumoulin, M. (15 October 2010). Engineering Nanobodies that Binds to Human Lysozyme and Inhibit its Conversion to Amyloid Fibrils: Prospects in Systemic and Neurodegenerative Diseases" [Paper presentation]. Single Domain Antibodies Come of Age, Ghent, Belgium.

Pain, C., Scarafone, N., Jaspar, A., Buys, N., Willibal, K., Filée, P., Galleni, M., Matagne, A., Steyaert, J., Pardon, E., & Dumoulin, M. (14 October 2010). Generation of camelid single-domain antibody fragments raised against proteins containing polyglutamine expansions [Poster presentation]. Single Domain Antibodies Come of Age, Ghent, Belgium.

Chavignon, C., Dumoulin, M., Pardon, E. (Other coll.), Wyns, L. (Other coll.), & Muyldermans, S. (Other coll.). (October 2010). VHHs as model proteins to investigate amyloid fibril formation: effect of seeding and cross-seeding on aggregation kinetics and stability of fibrils [Poster presentation]. Single domain antibodies, come of age, Gand, Belgium.

Scarafone, N., Pain, C., Filée, P., Galleni, M., Matagne, A., & Dumoulin, M. (07 June 2010). Interplay between the effects of the length of the polyglutamine tract and its structural context on the aggregation of polyglutamine (polyQ) proteins [Poster presentation]. Conférence Jacques Monod : Protein misfolding and aggregation in ageing and disease, Roscoff, France.

Dumoulin, M. (08 April 2010). Fibril formation by human lysozyme [Paper presentation]. Christopher Dobson 60th Birthday Symposium; From Neuroscience to Nanoscience, Cambridge, United Kingdom.

Chavignon, C., Dumoulin, M., Pardon, E. (Other coll.), Wyns, L. (Other coll.), & Muyldermans, S. (Other coll.). (March 2010). VHHs as model proteins to investigate amyloid fibril formation: aggregation kinetics and fibril stability [Poster presentation]. PAI - Proteins : interactions involved in folding, function and supramolecular assemblages, Liège, Belgium.

Chevigne, A., Dumez, M.-E., Dumoulin, M., Matagne, A., Jacquet, A., & Galleni, M. (2010). Comparative study of mature and zymogen mite cysteine protease stability and pH unfolding. Biochimica et Biophysica Acta, 1800 (9), 937-945. doi:10.1016/j.bbagen.2010.05.011

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

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.

Dumoulin, M. (2010). Familial amyloidosis caused by lysozyme mutations. In M. Ramirez-Alvarado, J. W. Kelly, ... C. Dobson (Eds.), Protein Misfolding Diseases: Basis of Protein Misfolding, Pathophysiology, Current, and Emerging Therapies (pp. 867-884). Hoboken (New Jersey), United States: John Wileys & Sons.

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

Dumoulin, M. (01 October 2009). Les amyloses : Du mécanisme de formation des fibres amyloïdes aux perspectives thérapeutiques [Paper presentation]. BioLiège, Liège, Belgium.

Dumoulin, M. (04 July 2009). Understanding the Mechanism of Amyloid Fibrils Formation by Human Lysozyme [Paper presentation]. Penicillin-recognizing enzymes: from enzymes kinetics to protein folding, University of Liège, Belgium.

Dumoulin, M. (02 July 2009). Understanding the mechanism of amyloid fibril formation by human lysozyme [Paper presentation]. Penicillin-recognizing enzymes: from enzyme kinetics to protein folding (Symposium in honour of Professor Jean-Marie Frère), Liège, Belgium.

Chavignon, C., Pardon, E. (Other coll.), Wyns, L. (Other coll.), Muyldermans, S. (Other coll.), & Dumoulin, M. (Other coll.). (July 2009). VHHs as model proteins to investigate amyloid fibril formation [Poster presentation]. Symposium international en l'honneur du Professeur Jean-Marie Frère: "Penicilin-recognizing enzymes: from enzyme kinetics to protein folding", Liège, Belgium.

Scarafone, N., Filée, P., Galleni, M., Matagne, A., & Dumoulin, M. (28 April 2009). Effect of polyQ insertions on the structural, thermodynamic and aggregating properties of the beta-lactamase from B. Licheniformis 749/C (BlaP) [Poster presentation]. Conférence Jacques Monod : Protein folds in infectious and neurodegenerative diseases, Aussois, France.

El Hajjaji, H., Dumoulin, M., Matagne, A., Colau, D., Messens, J., & Collet, J.-F. (13 February 2009). The Zinc Center Influences the Redox and Thermodynamic Properties of Escherichia coli Thioredoxin 2. Journal of Molecular Biology, 386 (1), 60-71. doi:10.1016/j.jmb.2008.11.046

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

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.

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

Scarafone, N., Filée, P., Galleni, M., Matagne, A., & Dumoulin, M. (September 2008). Chimeric proteins as models to study the mechanism of aggregation associated with polyglutamine expansions [Poster presentation]. 20th Faltertage: Folding in vitro, folding in vivo and folding h.c, Wittenberg, Germany.

Scarafone, N., Filée, P., Galleni, M., Matagne, A., & Dumoulin, M. (September 2008). Chimeric proteins as models to study the mechanism of aggregation associated with polyglutamine expansions [Paper presentation]. 20th Faltertage: Folding in vitro, folding in vivo and folding h.c, Wittenberg, Germany.

Scarafone, N., Filée, Galleni, M., Matagne, A., & Dumoulin, M. (22 July 2008). Creation of chimeric proteins as models to study the mechanism of aggregation associated with polyglutamine expansions [Paper presentation]. 22nd Annual Symposium of The Protein Society, San Diego, United States.

Scarafone, N., Filée, P., Galleni, M., Matagne, A., & Dumoulin, M. (20 July 2008). Creation of chimeric proteins as models to study the mechanism of aggregation associated with polyglutamine expansions [Poster presentation]. 22nd Annual Symposium of The Protein Society, San Diego, United States.

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

Scarafone, N., Filée, P., Galleni, M., Matagne, A., & Dumoulin, M. (May 2007). Creation of chimeric proteins as models to study the mechanism of aggregation of proteins with expanded polyglutamine repeats [Poster presentation]. VII European Symposium of The Protein Society, Stockholm-Uppsala, Sweden.

Dumoulin, M., Johnson, R. J. K., Bellotti, V., & Dobson, C. (2007). Human lysozyme amyloidosis. In V. Uversky & A. L. Fink (Eds.), Protein Misfolding, Aggregation and Conformational Diseases. II. Molecular Basis of Conformational Diseases (pp. 285-308). Dordrecht, Netherlands: Kluwer Academic.

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

Scarafone, N., Filée, P., Galleni, M., Matagne, A., & Dumoulin, M. (2007). Creation of chimeric proteins as models to study the mechanism of aggregation of proteins with expanded polyglutamine repeats [Poster presentation]. Joint Meeting of the Belgian Physical Society and the Belgian Biophysical Society, Antwerpen, Belgium.

Tocquin, P., Dumoulin, M., Dony, N., Detry, N., & Périlleux, C. (2007). Plant-based production of human lysozyme mutants [Poster presentation]. Bioforum, Liège, Belgium.

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

Scarafone, N., Filée, P., Galleni, M., Dumoulin, M., & Matagne, A. (December 2006). Creation of chimeric proteins as models to study the mechanism of aggregation of polyglutamine proteins [Poster presentation]. Young scientists day, 194th Meeting of the Belgian Society of Biochemistry and Molecular Biology, and International Franqui Chair 2005/2006, Gembloux, Belgium.

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

Dumoulin, M., Bellotti, V., & Dobson, C. (2005). Hereditary systemic amyloidosis associated with mutational variants of human lysozyme. In J. Sipe (Ed.), In Amyloid Proteins: The Beta Pleated Sheet Conformation and Disease (pp. 635-656). Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KgaA.

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

Saerens, D., Pellis, M., Loris, R., Pardon, E., Dumoulin, M., Matagne, A., Wyns, L., & Muyldermans, S. (2005). Identification of a universal VHH framework to graft non-canonical antigen-binding loops of camel single-domain antibodies. Journal of Molecular Biology, 352, 597-607. doi:10.1016/j.jmb.2005.07.038

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., Matsukawa, H., Ueno, H., Clery, C., Masson, P., & Hayashi, R. (2000). Effect of glycosylation on the mechanism of renaturation of carboxypeptidase Y. In Trends in High Pressure Bioscience and Biotechnology. Amsterdam, Netherlands: Elsevier Science B.V.

Dumoulin, M. (1999). High pressure-induced cold denaturation of proteins: Structural and functional study on wild type and unglycosylated carboxypeptidase Y [Doctoral thesis, Université de Kyoto]. ORBi-University of Liège. https://orbi.uliege.be/handle/2268/77627

Dumoulin, M., Ueno, H., Hayashi, R., & Balny, C. (1999). Use of high pressure to investigate the role of carbohydrate moiety in the conformational stability of carboxypeptidase Y. In Advances in High Pressure Bioscience and Biotechnology. Germany: H. Ludwig.

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. (1998). Evolution des produits hautes pression au Japon. Industries Agroalimentaires.

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.