Articles dans des revues avec comité de lecture (79)
  1. 10. 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
  2. 11. 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
  3. 12. Itkin, A., Salnikov, E. S., Aisenbrey, C., Raya, J., Glattard, E., Raussens, V., Ruysschaert, J. M., & Bechinger, B. (2017). Structural characterization of the amyloid precursor protein transmembrane domain and its γ-Cleavage Site. ACS Omega, 2(10), 6525-6534. doi:10.1021/acsomega.7b00619
  4. 13. Gallea, J. I., Sarroukh, R., Yunes-Quartino, P., Ruysschaert, J. M., Raussens, V., & Celej, M. S. (2016). Structural remodeling during amyloidogenesis of physiological Nα-acetylated α-synuclein. Biochimica et biophysica acta. Proteins and proteomics, 1864(5), 501-510. doi:10.1016/j.bbapap.2016.01.011
  5. 14. Ambroggio, E. E., Caruso, B., Villarreal, M. A., Raussens, V., & Fidelio, G. D. A. G. (2016). Reversing the peptide sequence impacts on molecular surface behaviour. Colloids and surfaces. B, Biointerfaces, 139, 25-32. doi:10.1016/j.colsurfb.2015.12.008
  6. 15. Hubin, E., Sarroukh, R., Deroo, S., Schierle, G. K., Kaminski, C., Serpell, L., Subramaniam, V., van Nuland, N. A. J., Broersen, K., & Raussens, V. (2015). Two distinct β-sheet structures in Italian-mutant amyloid-beta fibrils: A potential link to different clinical phenotypes. Cellular and molecular life sciences, 72(24), 4899-4913. doi:10.1007/s00018-015-1983-2
  7. 16. Gustot, A., Gallea, J. I., Sarroukh, R., Celej, M. S., Ruysschaert, J. M., & Raussens, V. (2015). Amyloid fibrils are the molecular trigger of inflammation in Parkinson's disease. Biochemical journal, 471(3), 323-333. doi:10.1042/BJ20150617
  8. 17. Hubin, E., Deroo, S., Schierle, G. K., Kaminski, C., Serpell, L., Subramaniam, V., van Nuland, N. A. J., Broersen, K., Raussens, V., & Sarroukh, R. (2015). Two distinct β-sheet structures in Italian-mutant amyloid-beta fibrils: a potential link to different clinical phenotypes. Cellular and molecular life sciences. doi:10.1007/s00018-015-1983-2
  9. 18. Hubin, E., Deroo, S., Schierle, G. K., Kaminski, C., Serpell, L., Subramaniam, V., van Nuland, N. A. J., Broersen, K., Raussens, V., & Sarroukh, R. (2015). Two distinct β-sheet structures in Italian-mutant amyloid-beta fibrils: a potential link to different clinical phenotypes. Cellular and molecular life sciences.
  10. 19. Deroo, S., Stengel, F., Mohammadi, A., Henry, N., Hubin, E., Krammer, E.-M., Aebersold, R., & Raussens, V. (2015). Chemical cross-linking/mass spectrometry maps the amyloid β peptide binding region on both apolipoprotein E domains. A C S Chemical Biology, 10(4), 1010-1016. doi:10.1021/cb500994j
  11. 20. Sarroukh, R., Goormaghtigh, E., Ruysschaert, J. M., & Raussens, V. (2013). ATR-FTIR: A "rejuvenated" tool to investigate amyloid proteins. Biochimica et biophysica acta. doi:10.1016/j.bbamem.2013.04.012
  12. 21. Gustot, A., Raussens, V., Dehousse, M., Dumoulin, M., Bryant, C. E., Ruysschaert, J. M., & Lonez, C. (2013). Activation of innate immunity by lysozyme fibrils is critically dependent on cross-β sheet structure. Cellular and molecular life sciences, 70(16), 2999-3012. doi:10.1007/s00018-012-1245-5
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