Contributions to collective works (3)
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Waeytens, J., Turbant, F., Arluison, V., Raussens, V., & Wien, F. (2022). Analysis of Bacterial Amyloid Interaction with Lipidic Membrane by Orientated Circular Dichroism and Infrared Spectroscopies. In Analysis of Bacterial Amyloid Interaction with Lipidic Membrane by Orientated Circular Dichroism and Infrared Spectroscopies.(Methods in Molecular Biology, 2538). doi:10.1007/978-1-0716-2529-3_153.
Busi, F., Turbant, F., Waeytens, J., El Hamoui, O., Wien, F., & Arluison, V. (2022). Evaluation of Amyloid Inhibitor Efficiency to Block Bacterial Survival. In Evaluation of Amyloid Inhibitor Efficiency to Block Bacterial Survival.(Methods in Molecular Biology, 2538). Peer-reviewed journal articles (25)
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Leyder, T., Mignon, J., Bongiovanni, E., Machiels, Q., Waeytens, J., Raussens, V., Monari, A., Mottet, D., & Michaux, C. (2026). Unveiling the effect of phosphorylation and phosphomimetics on the structural and aggregation properties of the amyloidogenic intrinsically disordered protein DPF3a. International journal of biological macromolecules, 335, 149393. doi:10.1016/j.ijbiomac.2025.1493932.
Nyström, S., Odino, D., Relini, A., Canale, C., Parlato, R., Knelissen, Y., Lasorsa, A., Roos, W., van der Wel, P., Hoffmann, S. V., Jones, N. C., Van Hemelryck, V., Waeytens, J., Raussens, V., & Hammarström, P. (2026). Standardization of cross-site biophysical studies of bovine insulin amyloids is challenged by structural polymorphism. European biophysics journal. doi:10.1007/s00249-025-01811-63.
Villanueva, M. E., Ruysschaert, J. M., Waeytens, J., Bouchet, A. M., & Losada Perez, P. (2025). Tuning the Spontaneous Formation of Helical Lipid Nanotubes by Bilayer Compositional Control. Langmuir, 41(50), 34119-34129. doi:10.1021/acs.langmuir.5c053544.
Salini, A., Gonnelli, P. M., Padoan, C., Helali, Y., Waeytens, J., Fusco, S., & Cannella, D. (2025). Repurposing Commercial Hydrolytic and Oxidative Enzymes toward Synergistic PLA Depolymerization. ACS Sustainable Chemistry and Engineering, 13(48), 20705-20716. doi:10.1021/acssuschemeng.5c069017.
Turbant, F., Machiels, Q., Waeytens, J., Wien, F., & Arluison, V. (2024). The Amyloid Assembly of the Bacterial Hfq Is Lipid-Driven and Lipid-Specific. International journal of molecular sciences, 25(3), 1434. doi:10.3390/ijms250314348.
Berbon, M., Martinez, D., Morvan, E., Grélard, A., Kauffmann, B., Waeytens, J., Wien, F., Arluison, V., & Habenstein, B. (2023). Hfq C-terminal region forms a β-rich amyloid-like motif without perturbing the N-terminal Sm-like structure. Communications Biology, 6(1), 1075. doi:10.1038/s42003-023-05462-19.
Turbant, F., Waeytens, J., Blache, A., Esnouf, E., Raussens, V., Węgrzyn, G., Achouak, W., Wien, F., & Arluison, V. (2023). Interactions and Insertion of Escherichia coli Hfq into Outer Membrane Vesicles as Revealed by Infrared and Orientated Circular Dichroism Spectroscopies. International Journal of Molecular Sciences (CD-ROM), 24(14), 11424. doi:10.3390/ijms241411424