Profil

Matagne André

Département des sciences de la vie > Enzymologie et repliement des protéines

InBioS

See author's contact details
ORCID
0000-0001-6417-6791
Main Referenced Co-authors
Frère, Jean-Marie  (35)
Galleni, Moreno  (32)
Dumoulin, Mireille  (26)
Filée, Patrice (16)
Scarafone, Natacha  (13)
Main Referenced Keywords
circular dichroism (21); protein folding (12); enzyme kinetics (9); mass spectrometry (7); beta-lactamase (6);
Main Referenced Unit & Research Centers
CIP - Centre d'Ingénierie des Protéines - ULiège [BE] (6)
Giga-Systems Biology and Chemical Biology - ULiège (2)
Giga-Neurosciences - ULiège (1)
Molecular Biomimetics Lab (1)
Molecular Biomimetics and Protein Engineering (1)
Main Referenced Disciplines
Biochemistry, biophysics & molecular biology (117)
Chemistry (5)
Immunology & infectious disease (3)
Biotechnology (2)
Microbiology (2)

Publications (total 130)

The most downloaded
760 downloads
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 https://hdl.handle.net/2268/16641

The most cited

510 citations (Scopus®)

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 https://hdl.handle.net/2268/22269

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
Peer Reviewed verified by ORBi

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
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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
Peer Reviewed verified by ORBi

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
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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
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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.
Peer reviewed

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
Peer Reviewed verified by ORBi

Nyssen, P., Maho, A., Malempré, R., Matagne, A., Mouithys-Mickalad, A., & Hoebeke, M. (May 2022). Propofol inhibits the myeloperoxidase activity by acting as substrate through a redox process. Biochimica et Biophysica Acta - General Subjects, 1866 (5), 130100. doi:10.1016/j.bbagen.2022.130100
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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
Peer Reviewed verified by ORBi

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
Peer reviewed

Berrow, N., de Marco, A., Lebendiker, M., Garcia-Alai, M., Knauer, S. H., Lopez-Mendez, B., Matagne, A., Parret, A., Remans, K., Uebel, S., & Raynal, B. (2021). Quality control of purified proteins to improve data quality and reproducibility: results from a large-scale survey. European biophysics journal : EBJ. doi:10.1007/s00249-021-01528-2
Peer reviewed

de Marco, A., Berrow, N., Lebendiker, M., Garcia-Alai, M., Knauer, S. H., Lopez-Mendez, B., Matagne, A., Parret, A., Remans, K., Uebel, S., & Raynal, B. (2021). Quality control of protein reagents for the improvement of research data reproducibility. Nature Communications, 12 (1), 2795. doi:10.1038/s41467-021-23167-z
Peer Reviewed verified by ORBi

Kellner, R., Malempré, R., Vandenameele, J., Brans, A., Hennen, A.-F., Rochus, N., Di Paolo, A., Vandevenne, M., & Matagne, A. (2021). Protein formulation through automated screening of pH and buffer conditions, using the Robotein® high throughput facility. European biophysics journal : EBJ. doi:10.1007/s00249-021-01510-y
Peer reviewed

El Rayes, J., Szewczyk, J., Deghelt, M., Csoma, N., Matagne, A., Iorga, B. I., Cho, S.-H., & Collet, J.-F. (2021). Disorder is a critical component of lipoprotein sorting in Gram-negative bacteria. Nature Chemical Biology. doi:10.1038/s41589-021-00845-z
Peer Reviewed verified by ORBi

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
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Mignon, J., Mottet, D., Verrillo, G., Matagne, A., Perpète, E. A., & Michaux, C. (2021). Revealing Intrinsic Disorder and Aggregation Properties of the DPF3a Zinc Finger Protein. ACS Omega, 6 (29), 18793-18801. doi:10.1021/acsomega.1c01948
Peer Reviewed verified by ORBi

Malempré, R., Kellner, R., Vandenameele, J., & Matagne, A. (February 2020). High-throughput protein formulation screening [Poster presentation]. 4th plenary meeting of ARBRE-MOBIEU, Living Molecules: towards Integrative Biophysics of the Cell, Prague, Czechia.

Lopes-Rodrigues, M., Matagne, A., Zanuy, D., Alemán, C., Perpète, E. A., & Michaux, C. (2020). Structural and functional characterization of Solanum tuberosum VDAC36. Proteins, 88 (6), 729-739. doi:10.1002/prot.25861
Peer Reviewed verified by ORBi

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
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Neirinckx, V., Hau, A.-C., Schuster, A., Fritah, S., Tiemann, K., Klein, E., Nazarov, P. V., Matagne, A., Szpakowska, M., Meyrath, M. M. R., Chevigné, A., Schmidt, M. H. H., & Niclou, S. P. (September 2019). The soluble form of pan-RTK inhibitor and tumor suppressor LRIG1 mediates downregulation of AXL through direct protein–protein interaction in glioblastoma. Neuro-Oncology Advances, 1 (1). doi:10.1093/noajnl/vdz024
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Vandenameele, J., De Meutter, J., Brans, A., Goormaghtigh, E., & Matagne, A. (02 April 2019). Robotein® : A robotic platform dedicated to high-throughput protein production and analysis [Paper presentation]. Les Journées Jeunes Chercheurs Transfrontalières - Reims, Reims, France.

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
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Turupcu, A., Bowen, A. M., Di Paolo, A., Matagne, A., Oostenbrink, C., Redfield, C., & Smith, L. J. (2019). An NMR and MD study of complexes of bacteriophage lambda lysozyme with tetra- and hexa-N-acetylchitohexaose. Proteins, 88 (1), 82-93. doi:10.1002/prot.25770
Peer Reviewed verified by ORBi

Hanozin, E., Grifnée, E., Gattuso, H., Matagne, A., Morsa, D., & De Pauw, E. (2019). Covalent Cross-Linking as an Enabler for Structural Mass Spectrometry. Analytical Chemistry. doi:10.1021/acs.analchem.9b02491
Peer Reviewed verified by ORBi

Hanozin, E., Grifnée, E., Gattuso, H., Matagne, A., Morsa, D., & De Pauw, E. (2019). Benchmarking IM-MS gas-phase data based on cross-linking strategies [Paper presentation]. 4th NVMS-BSMS Conference on Mass Spectrometry - Rolduc 2019.

Robert, C., Matagne, A., Filée, P., Bruck, F., & Alié, C. (27 October 2018). Production of pure and functional Bone Morphognetic Protein-2 [Poster presentation]. 12th International BMP Conference, Tokyo, Japan.

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
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Hanozin, E., Grifnée, E., Morsa, D., Matagne, A., & De Pauw, E. (June 2018). Can we correlate ion mobility mass spectrometry data with native solution structures? A crosslinking approach [Poster presentation]. 66th ASMS Conference on Mass Spectrometry and Allied Topics.

Matagne, A., & Dobson, C. M. (2018). Obituary: Nico van Nuland 1961-2017. European Biophysics Journal. doi:10.1007/s00249-018-1326-y

Dalla Serra, M., Gilbert, R. J. C., Matagne, A., & England, P. (2018). Biophysical Approaches to Protein Folding and Disease, a satellite meeting to the IUPAB-EBSA congress. European Biophysics Journal, 47 (2), 95-96. doi:10.1007/s00249-018-1288-0

Roussel, G., Caudano, Y., Matagne, A., Sansom, M. S., Perpète, E. A., & Michaux, C. (2018). Peptide-surfactant interactions: A combined spectroscopic and molecular dynamics simulation approach. Spectrochimica Acta. Part A, Molecular and Biomolecular Spectroscopy, 190, 464-470. doi:10.1016/j.saa.2017.09.056
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Piccirilli, A., Mercuri, P., Galleni, M., Aschi, M., Matagne, A., Amicosante, G., & Perilli, M. (2018). P174E Substitution in GES-1 and GES-5 beta-Lactamases Improves Catalytic Efficiency toward Carbapenems. Antimicrobial Agents and Chemotherapy, 62 (5). doi:10.1128/AAC.01851-17
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Dahmane, I., Montagner, C., Matagne, A., Dumbre, S., Herdewijn, P., & Terrak, M. (2018). Peptidoglycan glycosyltransferase-ligand binding assay based on tryptophan fluorescence quenching. Biochimie. doi:10.1016/j.biochi.2018.06.010
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Matagne, A., Bolle, L., El Mahyaoui, R., Baeyens-Volant, D., & Azarkan, M. (2017). The proteolytic system of pineapple stems revisited: Purification and characterization of multiple catalytically active forms. Phytochemistry, (138), 29-51. doi:10.1016/j.phytochem.2017.02.019
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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
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De Meutter, J., Vandenameele, J., Matagne, A., & Goormaghtigh, E. (2017). Infrared imaging of high density protein arrays. Analyst. doi:10.1039/c6an02048h
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Matagne, A., Vandenameele, J., De Meutter, J., Brans, A., & Goormaghtigh, E. (14 June 2016). Robotein : A robotic platform dedicated to high-throughput protein production and analysis [Poster presentation]. Core Technologies for Life Science (CTLS), Heidelberg, Germany.

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.

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
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Michaux, C., Roussel, G., Lopes-Rogrigues, M., Matagne, A., & Perpète, E. (2016). Unravelling the mechanisms of a protein refolding process based on the association of detergents and co-solvents. Journal of Peptide Science. doi:10.1002/psc.2893
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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
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Figueroa Yévenes, M., Vandenameele, J., Goormaghtigh, E., Valerio-Lepiniec, M., Minard, P., Matagne, A., & Van de Weerdt, C. (2016). Biophysical characterization data of the artificial protein Octarellin V.1 and binding test with its X-ray helpers. Data in Brief, 8, 1221-6. doi:10.1016/j.dib.2016.07.036
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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
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* These authors have contributed equally to this work.

Martina, C., Figueroa Yévenes, M., Moretti, R., Combs, S., Meiler, J., Van de Weerdt, C., & Matagne, A. (2016). A novel protocol for the design of artificial (β/α)8-barrel proteins [Poster presentation]. 13th Greta Pifat Mrzljak International School of Biophysics, Croatia.

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
Peer Reviewed verified by ORBi

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.

Toure, Y., Sindic, M., Dupont-Gillain, C. C., Matagne, A., & Rouxhet, G. P. (16 May 2015). Influence of substrate nature and β-lactoglobulin on cleanability after soiling by suspension spraying and drying. Chemical Engineering Science, 134, 823-833. doi:10.1016/j.ces.2015.05.039
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Baeyens-Volant, D., Matagne, A., El Mahyaoui, R., Wattiez, R., & Azarkan, M. (2015). A novel form of ficin from Ficus carica latex: Purification and characterization. Phytochemistry, 117, 154-167. doi:10.1016/j.phytochem.2015.05.019
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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
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de Ruyck, J., Janczak, M. W., Neti, S. S., Rothman, S. C., Schubert, H. L., Cornish, R. M., Matagne, A., Wouters, J., & Poulter, C. D. (2014). Determination of kinetics and the crystal structure of a novel type 2 isopentenyl diphosphate: dimethylallyl diphosphate isomerase from Streptococcus pneumoniae. Chembiochem: A European Journal of Chemical Biology, 15 (10), 1452-1458. doi:10.1002/cbic.201402046
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Houbart, V., Rozet, E., Matagne, A., Crommen, J., Servais, A.-C., & Fillet, M. (01 November 2013). Influence of sample and mobile phase composition on peptide retention behaviour and sensitivity in reversed-phase liquid chromatography/mass spectrometry. Journal of Chromatography. A, 1314, 199-207. doi:10.1016/j.chroma.2013.09.036
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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
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Ben Naya, R., Matti, K., Guellier, A., Matagne, A., Boquet, D., Thomas, D., Friboulet, A., Avalle, B., & Padiolleau-Lefevre, S. (2013). Efficient refolding of a recombinant abzyme : Structural and catalytic characterizations. Applied Microbiology and Biotechnology, 97 (17), 7721-31. doi:10.1007/s00253-012-4600-4
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Struvay, C., Negro, S., Matagne, A., & Feller, G. (2013). Energetics of protein stability at extreme environmental temperatures in bacterial trigger factors. Biochemistry, 52, 2982-2990. doi:10.1021/bi4002387
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Delvaux, D., Kerff, F., Murty, M. R. V. S., Lakaye, B., Czerniecki, J., Kohn, G., Wins, P., Herman, R., Gabelica, V., Heuze, F., Tordoir, X., Marée, R., Matagne, A., Charlier, P., De Pauw, E., & Bettendorff, L. (2013). Structural Determinants of Specificity and Catalytic Mechanism in mammalian 25-kDa Thiamine Triphosphatase. Biochimica et Biophysica Acta - General Subjects, 1830, 4513-4523. doi:10.1016/j.bbagen.2013.05.014
Peer Reviewed verified by ORBi

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
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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
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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
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Roussel, G., Perpete, E. A., Matagne, A., Tinti, E., & Michaux, C. (2013). Towards a universal method for protein refolding: The trimeric beta barrel membrane Omp2a as a test case. Biotechnology and Bioengineering, 110 (2), 417-23. doi:10.1002/bit.24722
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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
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Tenconi, E., Guichard, P., Motte, P., Matagne, A., & Rigali, S. (2013). Use of red autofluorescence for monitoring prodiginine biosynthesis. Journal of Microbiological Methods, 93, 138-143. doi:10.1016/j.mimet.2013.02.012
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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
Peer Reviewed verified by ORBi

Matagne, A., & Pain, R. (2012). Folding and Stability of Class A beta-Lactamases. In J.-M. Frère (Ed.), Beta-Lactamases (pp. 459-477). New York, United States: Nova.

Roussel, G., Matagne, A., De Bolle, X., Perpete, E., & Michaux, C. (2012). Purification, refolding and characterization of the trimeric Omp2a outer membrane porin from Brucella melitensis. Protein Expression and Purification, 83 (2), 198-204. doi:10.1016/j.pep.2012.04.003
Peer Reviewed verified by ORBi

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.

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.

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
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Cipolla, A., D'Amico, S., Barumandzadeh, R., Matagne, A., & Feller, G. (2011). Stepwise adaptations to low temperature as revealed by multiple mutants of a psychrophilic alpha-amylase from an Antarctic bacterium. Journal of Biological Chemistry, 286 (44), 38348–38355. doi:10.1074/jbc.M111.274423
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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
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Azarkan, M., Matagne, A., Wattiez, R., Bolle, L., Vandenameele, J., & Baeyens-Volant, D. (2011). Selective and reversible thiol-pegylation, an effective approach for purification and characterization of five fully active ficin (iso)forms from Ficus carica latex. Phytochemistry, 72 (14-15), 1718-31. doi:10.1016/j.phytochem.2011.05.009
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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.

Vercheval, L., Di Paolo, A., Borel, F., Ferrer, J.-L., Sauvage, E., Matagne, A., Frère, J.-M., Charlier, P., Galleni, M., & Kerff, F. (25 November 2010). Three factors that modulate the activity of class D β-lactamases and interfere with the post-translational carboxylation of Lys 70. Biochemical Journal, 432 (3), 495-504. doi:10.1042/BJ20101122
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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.

Meersman, F., Atilgan, C., Miles, A. J., Bader, R., Shang, W., Matagne, A., Wallace, B. A., & Koch, M. H. J. (October 2010). Consistent picture of the reversible thermal unfolding of hen egg-white lysozyme from experiment and molecular dynamics. Biophysical Journal, 99, 2255-2263. doi:10.1016/j.bpj.2010.07.060
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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.

Di Paolo, A., Balbeur, D., De Pauw, E., Redfield, C., & Matagne, A. (2010). Rapid Collapse into a Molten Globule Is Followed by Simple Two-State Kinetics in the Folding of Lysozyme from Bacteriophage lambda. Biochemistry, 49, 8646-8657. doi:10.1021/bi101126f
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Borgianni, L., Vandenameele, J., Matagne, A., Bini, L., Bonomo, R. A., Frère, J.-M., Rossolini, G. M., & Docquier, J.-D. (2010). Mutational analysis of VIM-2 reveals an essential determinant for metallo-beta-lactamase stability and folding. Antimicrobial Agents and Chemotherapy, 54 (8), 3197-204. doi:10.1128/AAC.01336-09
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Di Paolo, A., Duval, V., Matagne, A., & Redfield, C. (2010). Backbone 1H, 13C, and 15N resonance assignments for lysozyme from bacteriophage lambda. Biomolecular NMR Assignments, 4 (1), 111-4. doi:10.1007/s12104-010-9219-8
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Vandenameele, J., Lejeune, A., Di Paolo, A., Brans, A., Frère, J.-M., Schmid, F. X., & Matagne, A. (2010). Folding of class A beta-lactamases is rate-limited by peptide bond isomerization and occurs via parallel pathways. Biochemistry, 49 (19), 4264-75. doi:10.1021/bi100369d
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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
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Vandenameele, J., Matagne, A., & Damblon, C. (2010). 1H, 13C and 15N backbone resonance assignments for the BS3 class A beta-lactamase from Bacillus licheniformis. Biomolecular NMR Assignments, 4 (2), 195-7. doi:10.1007/s12104-010-9241-x
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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
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Jacquin, O., Balbeur, D., Damblon, C., Marchot, P., De Pauw, E., Roberts, G. C. K., Frère, J.-M., & Matagne, A. (2009). Positively Cooperative Binding of Zinc Ions to Bacillus cereus 569/H/9 beta-Lactamase II Suggests that the Binuclear Enzyme Is the Only Relevant Form for Catalysis. Journal of Molecular Biology, 392 (5), 1278-1291. doi:10.1016/j.jmb.2009.07.092
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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.

Lejeune, A., Pain, R. H., Charlier, P., Frère, J.-M., & Matagne, A. (29 January 2008). Tem-1 Beta-Lactamase Folds in a Nonhierarchical Manner with Transient Non-Native Interactions Involving the C-Terminal Region. Biochemistry, 47 (4), 1186-93. doi:10.1021/bi701927y
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Dumez, M.-E., Teller, N., Mercier, F., Tanaka, T., Vandenberghe, I., Vandenbranden, M., Devreese, B., Luxen, A., Frère, J.-M., Matagne, A., Jacquet, A., Galleni, M., & Chevigne, A. (2008). Activation mechanism of recombinant Der p 3 allergen zymogen - Contribution of cysteine protease Der p 1 and effect of propeptide glycosylation. Journal of Biological Chemistry, 283 (45), 30606-30617. doi:10.1074/jbc.M803041200
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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
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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
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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.

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.

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., 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
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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
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Vreuls, C., Filée, P., Van Melckebeke, H., Aerts, T., De Deyn, P., Llabres, G., Matagne, A., Simorre, J. P., Frère, J.-M., & Joris, B. (15 November 2004). Guanidinium chloride denaturation of the dimeric Bacillus licheniformis Blal repressor highlights an independent domain unfolding pathway. Biochemical Journal, 384 (Pt 1), 179-190. doi:10.1042/BJ20040658
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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
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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
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Matagne, A., Galleni, M., Laraki, N., Amicosante, G., Rossolini, G., & Frère, J.-M. (2002). Beta-lactamases, an old but ever renascent problem. In A. van Broekhoven (Ed.), Novel Frontiers in the Production of Compounds for Biomedical Use. Dordrecht, Netherlands: Kluwer Academic Publishers.
Peer reviewed

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
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Lejeune, A., Vanhove, M., Lamotte-Brasseur, J., Pain, R. H., Frère, J.-M., & Matagne, A. (August 2001). Quantitative Analysis of the Stabilization by Substrate of Staphylococcus Aureus Pc1 Beta-Lactamase. Chemistry and Biology, 8 (8), 831-42. doi:10.1016/S1074-5521(01)00053-9
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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
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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
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Bouillenne, F., Matagne, A., Joris, B., & Frère, J.-M. (2000). Technique for a rapid and efficient purification of the SHV-1 and PSE-2 beta-lactamases. Journal of Chromatography. B, Biomedical Sciences and Applications, 737 (1-2), 261-5. doi:10.1016/S0378-4347(99)00436-3
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Matagne, A., Jamin, M., Chung, E. W., Robinson, C. V., Radford, S. E., & Dobson, C. M. (2000). Thermal unfolding of an intermediate is associated with non-arrhenius kinetics in the folding of hen lysozyme. Journal of Molecular Biology, 297 (1), 193-210. doi:10.1006/jmbi.2000.3540
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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
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Frère, J.-M., Dubus, A., Galleni, M., Matagne, A., & Amicosante, G. (February 1999). Mechanistic Diversity of Beta-Lactamases. Biochemical Society Transactions, 27 (2), 58-63. doi:10.1042/bst0270058
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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
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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
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Matagne, A., Chung, E. W., Ball, L. J., Radford, S. E., Robinson, C. V., & Dobson, C. M. (1998). The origin of the alpha-domain intermediate in the folding of hen lysozyme. Journal of Molecular Biology, 277 (5), 997-1005. doi:10.1006/jmbi.1998.1657
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Matagne, A., Radford, S. E., & Dobson, C. M. (1997). Fast and slow tracks in lysozyme folding: Insight into the role of domains in the folding process. Journal of Molecular Biology, 267 (5), 1068-1074. doi:10.1006/jmbi.1997.0963
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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
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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
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STRYNADKA, N. C. J., JENSEN, S. E., JOHNS, K., BLANCHARD, H., PAGE, M., Matagne, A., Frère, J.-M., & JAMES, M. N. G. (1994). STRUCTURAL AND KINETIC CHARACTERIZATION OF A BETA-LACTAMASE-INHIBITOR PROTEIN. Nature, 368 (6472), 657-660. doi:10.1038/368657a0
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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
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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
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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
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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
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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
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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
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Frère, J.-M., Joris, B., Granier, B., Matagne, A., Ackerman, F., & Bourguignon-Bellefroid, C. (1991). Diversity of the Mechanisms of Resistance to Beta-Lactam Antibiotics. Research in Microbiology, 142 (6, Jul-Aug), 705-10. doi:10.1016/0923-2508(91)90084-N
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Frère, J.-M., Joris, B., Jacob, F., Matagne, A., Monnaie, D., Jamin, M., Hadonou, M., Bourguignon-Bellefroid, C., Varetto, L., Wilkin, J.-M., Dubus, A., Damblon, C., Adam, M., Ledent, P., De Meester, F., & Galleni, M. (1991). Mechanism of action of β-lactamases and DD-peptidases. In U. K. Pandit & F. C. Alderweireldt (Eds.), Bioorganic Chemistry in Healthcare and Technology (pp. 161-170). New York, United States - New York: Plenum Press.
Peer reviewed

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
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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
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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
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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
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