Frère, J.-M., Verlaine, O., & Matagne, A. (12 September 2023). The measurement of true initial rates is not always absolutely necessary to estimate enzyme kinetic parameters. Scientific Reports, 13 (1), 15053. doi:10.1038/s41598-023-41805-y |
Pannus, P., Depickère, S., Kemlin, D., Georges, D., Houben, S., Olislagers, V., Waegemans, A., De Craeye, S., Francotte, A., Chaumont, F., Van Oostveldt, C., Heyndrickx, L., Michiels, J., Willems, E., Dhondt, E., Krauchuk, M., Schmickler, M.-N., Verbrugghe, M., Van Loon, N., ... Goossens, M. E. (24 April 2023). Third dose of COVID-19 mRNA vaccine closes the gap in immune response between naïve nursing home residents and healthy adults. Vaccine, 41 (17), 2829 - 2836. doi:10.1016/j.vaccine.2023.03.047 |
Kemlin, D., Gemander, N., Depickère, S., Olislagers, V., Georges, D., Waegemans, A., Pannus, P., Lemy, A., Goossens, M. E., Desombere, I., Michiels, J., Vandevenne, M., Heyndrickx, L., Ariën, K. K., Matagne, A., Ackerman, M. E., Le Moine, A., & Marchant, A. (10 February 2023). Humoral and cellular immune correlates of protection against COVID-19 in kidney transplant recipients. American Journal of Transplantation, 23 (5), 649 - 658. doi:10.1016/j.ajt.2023.02.015 |
Robert, C., Kerff, F., Bouillenne, F., Gavage, M., Vandevenne, M., Filée, P., & Matagne, A. (2023). Structural analysis of the interaction between human cytokine BMP-2 and the antagonist Noggin reveals molecular details of cell chondrogenesis inhibition. Journal of Biological Chemistry, 102892. doi:10.1016/j.jbc.2023.102892 |
Tomasi, L., Thiriard, A., Heyndrickx, L., Georges, D., Van den Wijngaert, S., Olislagers, V., Sharma, S., Matagne, A., Ackerman, M. E., Ariën, K. K., Goetghebuer, T., & Marchant, A. (November 2022). Younger Children Develop Higher Effector Antibody Responses to SARS-CoV-2 Infection. Open Forum Infectious Diseases, 9 (11), 554. doi:10.1093/ofid/ofac554 |
Grifnee, E., Kune, C., Delvaux, C., Quinton, L., Matagne, A., Mazzucchelli, G., Far, J., & De Pauw, E. (29 August 2022). Investigation of structure-stabilizing elements in proteins by ion mobility mass spectrometry and collision-induced unfolding [Poster presentation]. IMSC. |
Pannus, P., Neven, K. Y., De Craeye, S., Heyndrickx, L., Vande Kerckhove, S., Georges, D., Michiels, J., Francotte, A., Van Den Bulcke, M., Zrein, M., Van Gucht, S., Schmickler, M. N., Verbrugghe, M., Matagne, A., Thomas, I., Dierick, K., Weiner, J. A., Ackerman, M. E., Goriely, S., ... Marchant, A. (24 August 2022). Poor Antibody Response to BioNTech/Pfizer Coronavirus Disease 2019 Vaccination in Severe Acute Respiratory Syndrome Coronavirus 2-Naive Residents of Nursing Homes. Clinical Infectious Diseases, 75 (1), 695-e704. doi:10.1093/cid/ciab998 |
Neyman, V., Francis, F., Matagne, A., Dieu, M., Michaux, C., & Perpète, E. A. (2022). Purification and Characterization of Trehalase From Acyrthosiphon pisum, a Target for Pest Control. Protein Journal. doi:10.1007/s10930-021-10032-7 |
Poncin, M. A., Van Meerbeeck, P., Simpson, J. D., Clippe, A., Tyckaert, F., Bouillenne, F., Degand, H., Matagne, A., Morsomme, P., Knoops, B., & Alsteens, D. (27 November 2021). Role of the Redox State of Human Peroxiredoxin-5 on Its TLR4-Activating DAMP Function. Antioxidants (Basel, Switzerland), 10 (12), 1902. doi:10.3390/antiox10121902 |
Guillerm, J., Frère, J.-M., Meersman, F., & Matagne, A. (2021). The Right-Handed Parallel β-Helix Topology of Erwinia chrysanthemi Pectin Methylesterase Is Intimately Associated with Both Sequential Folding and Resistance to High Pressure. Biomolecules, 11 (8), 1083. doi:10.3390/biom11081083 |
Piccirilli, A., Brisdelli, F., Docquier, J.-D., Aschi, M., Cherubini, S., De Luca, F., Matagne, A., Amicosante, G., & Perilli, M. (2020). Amino acid replacement at position 228 induces fluctuation in the Ω-loop of KPC-3 and reduces the affinity against oxyimino cephalosporins: Kinetic and molecular dynamics studies. Catalysts, 10 (12), 1-14. doi:10.3390/catal10121474 |
De Franco, S., Vandenameele, J., Brans, A., Verlaine, O., Bendak, K., Damblon, C., Matagne, A., Segal, D., Galleni, M., Mackay, J., & Vandevenne, M. (21 February 2019). Exploring the suitability of RanBP2-type Zinc Fingers for RNA-binding protein design. Scientific Reports, 9 (1), 2484. doi:10.1038/s41598-019-38655-y |
Azarkan, M., Feller, G., Vandenameele, J., Herman, R., El Mahyaoui, R., Sauvage, E., Vanden Broeck, A., Matagne, A., Charlier, P., & Kerff, F. (2018). Biochemical and structural characterization of a mannose binding jacalin-related lectin with two-sugar binding sites from pineapple (Ananas comosus) stem. Scientific Reports. doi:10.1038/s41598-018-29439-x |
Chevigne, A., Campizi, V., Szpakowska, M., Bourry, D., Dumez, M.-E., Martins, J. C., Matagne, A., Galleni, M., & Jacquet, A. (2017). The Lys-Asp-Tyr Triad within the Mite Allergen Der p 1 Propeptide Is a Critical Structural Element for the pH-Dependent Initiation of the Protease Maturation. International Journal of Molecular Sciences, 18 (5). doi:10.3390/ijms18051087 |
Martina, C., Figueroa Yévenes, M., Combs, S., Moretti, R., Van de Weerdt, C., Matagne, A., & Meiler, J. (March 2016). A novel protocol for the design of artificial (β/α)8-barrel proteins [Poster presentation]. 67. Mosbacher Kolloquium, “Protein Design: From First Principles to Biomedical Applications”, Mosbach, Germany. |
Figueroa Yévenes, M., Sleutel, M., Vandevenne, M., Parvizi, G., Attout, S., Jacquin, O., Vandenameele, J., Fischer, A. W., Damblon, C., Goormaghtigh, E., Valerio-Lepiniec, M., Urvoas, A., Durand, D., Pardon, E., Steyaert, J., Minard, P., Maes, D., Meiler, J., Matagne, A., ... Van de Weerdt, C. (2016). The unexpected structure of the designed protein Octarellin V.1 forms a challenge for protein structure prediction tools. Journal of Structural Biology. doi:10.1016/j.jsb.2016.05.004 |
Jourdan, S.* , Francis, I.* , Kim, M., Salazar, J., Planckaert, S., Frère, J.-M., Matagne, A., Kerff, F., Devreese, B., Loria, R., & Rigali, S. (2016). The CebE/MsiK Transporter is a Doorway to the Cello-oligosaccharide-mediated Induction of Streptomyces scabies Pathogenicity. Scientific Reports. doi:10.1038/srep27144 * These authors have contributed equally to this work. |
Marcoccia, F., Bottoni, C., Sabatini, A., Colapietro, M., Mercuri, P., Galleni, M., Kerff, F., Matagne, A., Celenza, G., Amicosante, G., & Perilli, M. (2016). Kinetic Study of Laboratory Mutants of NDM-1 Metallo-beta-Lactamase and the Importance of an Isoleucine at Position 35. Antimicrobial Agents and Chemotherapy, 60 (4), 2366-72. doi:10.1128/AAC.00531-15 |
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 |
Vandenameele, J., De Meutter, J., Brans, A., Goormaghtigh, E., & Matagne, A. (14 October 2015). ROBOTEIN A robotic platform dedicated to high-throughput protein production and analysis [Poster presentation]. ELRIGfr conference, Bruxelles, Belgium. |
Bury, D., Dahmane, I., Derouaux, A., Dumbre, S., Herdewijn, P., Matagne, A., Breukink, E., Mueller-Seitz, E., Petz, M., & Terrak, M. (2015). Positive cooperativity between acceptor and donor sites of the peptidoglycan glycosyltransferase. Biochemical Pharmacology, 93 (2), 141-50. doi:10.1016/j.bcp.2014.11.003 |
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 |
Dumez, M.-E., Herman, J., Campisi, V., Bouaziz, A., Rosu, F., Luxen, A., Vandenberghe, I., De Pauw, E., Frère, J.-M., Matagne, A., Chevigne, A., & Galleni, M. (2013). The proline-rich motif of the proDer p 3 allergen propeptide is crucial for protease-protease interaction. PLoS ONE, 8 (9), 68014. doi:10.1371/journal.pone.0068014 |
Figueroa Yévenes, M., Oliveira, N., Lejeune, A., Kaufmann, K. W., Dorr, B. M., Matagne, A., Martial, J., Meiler, J., & Van de Weerdt, C. (2013). Octarellin VI: using rosetta to design a putative artificial (beta/alpha)8 protein. PLoS ONE, 8 (8), 71858. doi:10.1371/journal.pone.0071858 |
Smith, L. J., Bowen, A. M., Di Paolo, A., Matagne, A., & Redfield, C. (2013). The dynamics of lysozyme from bacteriophage lambda in solution probed by NMR and MD simulations. Chembiochem: A European Journal of Chemical Biology, 14 (14), 1780-8. doi:10.1002/cbic.201300193 |
Figueroa Yévenes, M., Taralla, S., Buscetta, M., Sanjuan Pacheco, W. A., Matagne, A., Lejeune, A., Martial, J., & Van de Weerdt, C. (16 November 2012). In silico and in vivo combinatorial design of Octarellin VI, an artificial protein modeled on the (B/A)8 fold [Poster presentation]. Protein Structures: From Computer to the Application, Louvain-la-Neuve, Belgium. |
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 |
Tiber, P. M., Orun, O., Nacar, C., Sezerman, U. O., Severcan, F., Severcan, M., Matagne, A., & Kan, B. (2011). Structural characterization of recombinant bovine Goalpha by spectroscopy and homology modeling. Spectroscopy, 26, 213-229. doi:10.3233/SPE-2011-0543 |
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 |
Chevigné, A., Barumandzadeh, R., Groslambert, S., Cloes, B., Dehareng, D., Filée, P., Marx, J.-C., Frère, J.-M., Matagne, A., Jacquet, A., & Galleni, M. (16 November 2007). Relationship between propeptide pH unfolding and inhibitory ability during ProDer p 1 activation mechanism. Journal of Molecular Biology, 374 (1), 170-185. doi:10.1016/j.jmb.2007.08.025 |
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 |
Douette, P., Navet, R., Bouillenne, F., Brans, A., Sluse-Goffart, C., Matagne, A., & Sluse, F. (May 2004). Secondary-structure characterization by far-UV CD of highly purified uncoupling protein 1 expressed in yeast. Biochemical Journal, 380 (Pt 1), 139-145. doi:10.1042/BJ20031957 |
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 |
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 |
Vilar, M., Galleni, M., Solmajer, T., Turk, B., Frère, J.-M., & Matagne, A. (August 2001). Kinetic Study of Two Novel Enantiomeric Tricyclic Beta-Lactams Which Efficiently Inactivate Class C Beta-Lactamases. Antimicrobial Agents and Chemotherapy, 45 (8), 2215-23. doi:10.1128/AAC.45.8.2215-2223.2001 |
Conrath, K. E., Lauwereys, M., Galleni, M., Matagne, A., Frère, J.-M., Kinne, J., Wyns, L., & Muyldermans, S. (2001). Beta-lactamase inhibitors derived from single-domain antibody fragments elicited in the camelidae. Antimicrobial Agents and Chemotherapy, 45 (10), 2807-12. doi:10.1128/AAC.45.10.2807-2812.2001 |
Matagne, A., Dubus, A., Galleni, M., & Frère, J.-M. (February 1999). The Beta-Lactamase Cycle: A Tale of Selective Pressure and Bacterial Ingenuity. Natural Product Reports, 16 (1), 1-19. doi:10.1039/a705983c |
Matagne, A., & Dobson, C. M. (April 1998). The Folding Process of Hen Lysozyme: A Perspective from the 'New View'. Cellular and Molecular Life Sciences, 54 (4), 363-71. doi:10.1007/s000180050165 |
Matagne, A., Lamotte-Brasseur, J., & Frère, J.-M. (01 March 1998). Catalytic Properties of Class a Beta-Lactamases: Efficiency and Diversity. Biochemical Journal, 330 ((Pt 2)), 581-98. doi:10.1042/bj3300581 |
Matagne, A., & Frère, J.-M. (19 January 1995). Contribution of Mutant Analysis to the Understanding of Enzyme Catalysis: The Case of Class a Beta-Lactamases. Biochimica et Biophysica Acta, 1246 (2), 109-27. doi:10.1016/0167-4838(94)00177-I |
Matagne, A., Ledent, P., Monnaie, D., Felici, A., Jamin, M., Raquet, X., Galleni, M., Klein, D., Francois, I., & Frère, J.-M. (January 1995). Kinetic Study of Interaction between Brl 42715, Beta-Lactamases, and D-Alanyl-D-Alanine Peptidases. Antimicrobial Agents and Chemotherapy, 39 (1), 227-31. doi:10.1128/aac.39.1.227 |
Matagne, A., Ghuysen, M. F., & Frère, J.-M. (01 November 1993). Interactions between Active-Site-Serine Beta-Lactamases and Mechanism-Based Inactivators: A Kinetic Study and an Overview. Biochemical Journal, 295 ((Pt 3)), 705-711. doi:10.1042/bj2950705 |
Matagne, A., Lamotte-Brasseur, J., & Frère, J.-M. (01 October 1993). Interactions between Active-Site Serine Beta-Lactamases and So-Called Beta-Lactamase-Stable Antibiotics. Kinetic and Molecular Modelling Studies. European Journal of Biochemistry, 217 (1), 61-67. doi:10.1111/j.1432-1033.1993.tb18218.x |
Matagne, A., Lamotte-Brasseur, J., Dive, G., Knox, J. R., & Frère, J.-M. (01 August 1993). Interactions between Active-Site-Serine Beta-Lactamases and Compounds Bearing a Methoxy Side Chain on the Alpha-Face of the Beta-Lactam Ring: Kinetic and Molecular Modelling Studies. Biochemical Journal, 293 ((Pt 3)), 607-611. doi:10.1042/bj2930607 |
Lenzini, V. M., Magdalena, J., Fraipont, C., Joris, B., Matagne, A., & Dusart, J. (October 1992). Induction of a Streptomyces Cacaoi Beta-Lactamase Gene Cloned in S. Lividans. Molecular and General Genetics, 235 (1), 41-8. doi:10.1007/BF00286179 |
Matagne, A., Joris, B., & Frère, J.-M. (01 December 1991). Anomalous Behaviour of a Protein During Sds/Page Corrected by Chemical Modification of Carboxylic Groups. Biochemical Journal, 280 ((Pt 2)), 553-6. doi:10.1042/bj2800553 |
Matagne, A., Joris, B., Van Beeumen, J., & Frère, J.-M. (01 February 1991). Ragged N-Termini and Other Variants of Class a Beta-Lactamases Analysed by Chromatofocusing. Biochemical Journal, 273 (273), 503-10. doi:10.1042/bj2730503 |
BRANNIGAN, J., Matagne, A., Jacob, F., Damblon, C., Joris, B., KLEIN, D., SPRATT, B. G., & Frère, J.-M. (1991). THE MUTATION LYS234HIS YIELDS A CLASS-A BETA-LACTAMASE WITH A NOVEL PH-DEPENDENCE. Biochemical Journal, 278 (Part 3), 673-678. doi:10.1042/bj2780673 |
Matagne, A., Misselyn-Bauduin, A. M., Joris, B., Erpicum, T., Granier, B., & Frère, J.-M. (01 January 1990). The Diversity of the Catalytic Properties of Class a Beta-Lactamases. Biochemical Journal, 265 (1), 131-46. doi:10.1042/bj2650131 |
De Meester, F., Matagne, A., Dive, G., & Frère, J.-M. (01 January 1989). Unexpected Influence of Ionic Strength on Branched-Pathway Interactions between Beta-Lactamases and Beta-Halogenopenicillanates. Biochemical Journal, 257 (1), 245-9. doi:10.1042/bj2570245 |
Fraipont, C., Duez, C., Matagne, A., Molitor, C., Dusart, J., Frère, J.-M., & Ghuysen, J.-M. (1989). Cloning and amplified expression in Streptomyces lividans of the gene encoding the extracellular β-lactamase of Actinomadura R39. Biochemical Journal, 262 (3), 849-854. doi:10.1042/bj2620849 |