Parties d'ouvrages collectifs (3)
  1. 1. 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_15
  2. 2. Raussens, V., & Waeytens, J. (2022). Characterization of Bacterial Amyloids by Nano-infrared Spectroscopy. In V. Arluison, F. Wien, & A. Marcoleta (Eds.), Characterization of Bacterial Amyloids by Nano-infrared Spectroscopy.(Methods in Molecular Biology, 2538).
  3. 3. Ruysschaert, J. M., & Raussens, V. (2018). ATR-FTIR Analysis of Amyloid Proteins. In B. L. Nilsson & T. M. Doran (Eds.), Peptide Self-Assembly: Methods and Protocols, Vol. 1777. Peptide Self-Assembly (1 ed., pp. 69-81). New York: Humana Press (Springer).(Methods in Molecular Biology).
    4.   Articles dans des revues avec comité de lecture (81)
  4. 1. 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/s00249-025-01811-6
  5. 2. 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.2025.149393
  6. 3. Mohammadi, A., Deroo, S., Leitner, A. A. L., Stengel, F., Krammer, E.-M., Aebersold, R., Prévost, M., & Raussens, V. (2025). Characterization of the N- and C-terminal domain interface of the three main apoE isoforms: A combined quantitative cross-linking mass spectrometry and molecular modeling study. Biochimica et biophysica acta (G). General subjects, 1869(4), 130768. doi:10.1016/j.bbagen.2025.130768
  7. 4. 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
  8. 5. Waeytens, J., De Meutter, J., Goormaghtigh, E., Dazzi, A., & Raussens, V. (2023). Determination of Secondary Structure of Proteins by Nanoinfrared Spectroscopy. Analytical chemistry. doi:10.1021/acs.analchem.2c01431
  9. 6. Turbant, F., Waeytens, J., Campidelli, C., Bombled, M., Martinez, D., Grélard, A., Habenstein, B., Raussens, V., Vélez, M., Wien, F., & Arluison, V. (2022). Unraveling Membrane Perturbations Caused by the Bacterial Riboregulator Hfq. International Journal of Molecular Sciences (CD-ROM), 23(15), 8739. doi:10.3390/ijms23158739
  10. 7. Waeytens, J., Mathurin, J., Deniset-Besseau, A., Arluison, V., Bousset, L., Rezaei, H., Raussens, V., & Dazzi, A. (2021). Probing amyloid fibril secondary structures by infrared nanospectroscopy: Experimental and theoretical considerations. Analyst, 146(1), 132-145. doi:10.1039/d0an01545h
  11. 8. Blond, P., Bevernaegie, R., Troian Gautier, L., Lagrost, C., Hubert, J., Reniers, F., Raussens, V., & Jabin, I. (2020). Ready-to-Use Germanium Surfaces for the Development of FTIR-Based Biosensors for Proteins. Langmuir. doi:10.1021/acs.langmuir.0c02681
  12. 9. Waeytens, J., Van Hemelryck, V., Deniset-Besseau, A., Ruysschaert, J. M., Dazzi, A., & Raussens, V. (2020). Characterization by Nano-Infrared Spectroscopy of Individual Aggregated Species of Amyloid Proteins. Molecules, 25(12). doi:10.3390/molecules25122899
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