Articles dans des revues avec comité de lecture (463)
  1. 48. Sarroukh, R., Cerf, E., Derclaye, S., Dufrêne, Y. F., Goormaghtigh, E., Ruysschaert, J. M., & Raussens, V. (2010). Transformation of amyloid β(1-40) oligomers into fibrils is characterized by a major change in secondary structure. Cellular and molecular life sciences. doi:10.1007/s00018-010-0529-x
  2. 49. Campen, R. K., Ngo, T. T. M., Sovago, M., Ruysschaert, J. M., & Bonn, M. (2010). Molecular restructuring of water and lipids upon the interaction of DNA with lipid monolayers. Journal of the American Chemical Society, 132(23), 8037-8047. doi:10.1021/ja100838q
  3. 50. De Angelis, F., Lee, J., O'Connell, J. D., Miercke, L. J. W., Verschueren, K. H., Srinivasan, V., Bauvois, C., Govaerts, C., Robbins, R. A., Ruysschaert, J. M., Stroud, R. M., & Vandenbussche, G. (2010). Metal-induced conformational changes in ZneB suggest an active role of membrane fusion proteins in efflux resistance systems. Proceedings of the National Academy of Sciences of the United States of America, 107(24), 11038-11043. doi:10.1073/pnas.1003908107
  4. 51. Gustot, A., Smriti, I., Ruysschaert, J. M., McHaourab, H., & Govaerts, C. (2010). Lipid composition regulates the orientation of transmembrane helices in HorA, an ABC multidrug transporter. The Journal of biological chemistry, 285(19), 14144-14151. doi:10.1074/jbc.M109.079673
  5. 52. Lensink, M., Govaerts, C., & Ruysschaert, J. M. (2010). Identification of specific lipid-binding sites in integral membrane proteins. The Journal of biological chemistry, 285(14), 10519-10526. doi:10.1074/jbc.M109.068890
  6. 53. Lonez, C., Lensink, M., Kleiren, E., Vanderwinden, J.-M., Ruysschaert, J. M., & Vandenbranden, M. (2010). Fusogenic activity of cationic lipids and lipid shape distribution. Cellular and molecular life sciences, 67(3), 483-494. doi:10.1007/s00018-009-0197-x
  7. 54. Kleiren, E., Ruysschaert, J. M., Goormaghtigh, E., & Raussens, V. (2010). Development of a quantitative and conformation-sensitive ATR-FTIR biosensor for Alzheimer's disease: The effect of deuteration on the detection of the Aβ peptide. Spectroscopy, 24(1-2), 61-66.
  8. 55. Cerf, E., Ruysschaert, J. M., Goormaghtigh, E., & Raussens, V. (2010). ATR-FTIR, a new tool to analyze the oligomeric content of Aβ samples in the presence of apolipoprotein E isoforms. Spectroscopy, 3(4), 245-249.
  9. 56. Kleiren, E., Ruysschaert, J. M., Goormaghtigh, E., & Raussens, V. (2010). Development of a quantitative and conformation-sensitive ATR-FTIR biosensor for Alzheimer's disease: The effect of deuteration on the detection of the Aβ peptide. Spectroscopy, 24(1-2), 61-66. doi:10.3233/SPE-2010-0405
  10. 57. Cerf, E., Ruysschaert, J. M., Goormaghtigh, E., & Raussens, V. (2010). ATR-FTIR, a new tool to analyze the oligomeric content of Aβ samples in the presence of apolipoprotein e isoforms. Spectroscopy, 24(3-4), 245-249. doi:10.3233/SPE-2010-0439
  11. 58. Sarroukh, R., Cerf, E., Derclaye, S., Dufrêne, Y. F., Ruysschaert, J. M., Goormaghtigh, E., & Raussens, V. (2010). Aggregation of the A$beta$ (1-40) peptide: Secondary structure change from oligomers to fibrils. Alzheimer's & Dementia, 6(4), S242.
  12. 59. Cerf, E., Sarroukh, R., Tamamizu-Kato, S., Breydo, L., Derclaye, S., Dufrêne, Y. F., Narayanaswami, V., Goormaghtigh, E., Ruysschaert, J. M., & Raussens, V. (2009). Antiparallel beta-sheet: a signature structure of the oligomeric amyloid beta-peptide. Biochemical journal, 421(3), 415-423. doi:10.1042/BJ20090379
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