Parties d'ouvrages collectifs (3)

  1. 1. 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).
  2. 2. 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).
  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 (77)

  5. 1. 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
  6. 2. 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
  7. 3. 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
  8. 4. 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
  9. 5. Ruysschaert, J. M., & Raussens, V. (2018). ATR-FTIR Analysis of Amyloid Proteins. Methods in molecular biology, 1777, 69-81. doi:10.1007/978-1-4939-7811-3_3
  10. 6. Henry, N., Krammer, E.-M., Stengel, F., Adams, Q., Van Liefferinge, F., Hubin, E., Chaves, R., Efremov, R., Aebersold, R., Vandenbussche, G., Prévost, M., Raussens, V., & Deroo, S. (2018). Lipidated apolipoprotein E4 structure and its receptor binding mechanism determined by a combined cross-linking coupled to mass spectrometry and molecular dynamics approach. PLoS computational biology, 14(6), e1006165. doi:10.1371/journal.pcbi.1006165
  11. 7. Blond, P., Mattiuzzi, A., Valkenier, H., Troian Gautier, L., Bergamini, J., Doneux, T., Goormaghtigh, E., Raussens, V., & Jabin, I. (2018). Grafting of Oligo(ethylene glycol)-Functionalized Calix[4]arene-Tetradiazonium Salts for Antifouling Germanium and Gold Surfaces. Langmuir, 34(21), 6021-6027. doi:10.1021/acs.langmuir.8b00464
  12. 8. Sidhu, A., Segers-Nolten, I., Raussens, V., Claessens, M. M. A. E. M., & Subramaniam, V. (2017). Distinct Mechanisms Determine α-Synuclein Fibril Morphology during Growth and Maturation. ACS Chemical Neuroscience, 8(3), 538-547. doi:10.1021/acschemneuro.6b00287
  13. 9. Valkenier, H., Malytskyi, V., Blond, P., Retout, M., Mattiuzzi, A., Goole, J., Raussens, V., Jabin, I., & Bruylants, G. (2017). Controlled Functionalization of Gold Nanoparticles with Mixtures of Calix[4]arenes Revealed by Infrared Spectroscopy. Langmuir, 33(33), 8253-8259. doi:10.1021/acs.langmuir.7b02140

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