Articles dans des revues avec comité de lecture (247)
  1. 71. Romero-Beviar, M., Martínez-Rodríguez, S., Prieto, J., Goormaghtigh, E., Ariz, U., Martínez-Chantar, M. D. L. L., Gómez, J., & Neira, J. L. (2010). The N-terminal domain of the enzyme I is a monomeric well-folded protein with a low conformational stability and residual structure in the unfolded state. Protein engineering, design & selection, 23(9), 729-742. doi:10.1093/protein/gzq045
  2. 72. 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
  3. 73. Aguado-Llera, D., Goormaghtigh, E., De Geest, N., Quan, X., Prieto, A., Hassan, B. A., Gómez, J., & Neira, J. L. (2010). The basic helix-loop-helix region of human neurogenin 1 is a monomeric natively unfolded protein which forms a. Biochemistry, 49(8), 1577-1589. doi:10.1021/bi901616z
  4. 74. Goldsztein, A., Babar, S., Voué, M., De Coninck, J., Conti, J., Marchand-Brynaert, J., Devouge, S., Homblé, F., & Goormaghtigh, E. (2010). Gastric ATPase phosphorylation/dephosphorylation monitored by new FTIR-based BIA-ATR biosensors. Spectroscopy, 24(3-4), 257-260. doi:10.3233/SPE-2010-0402
  5. 75. Gasper, R., Mijatovic, T., Kiss, R., & Goormaghtigh, E. (2010). FTIR spectroscopy reveals the concentration dependence of cellular modifications induced by anticancer drugs. Spectroscopy, 24, 45-49.
  6. 76. Benard, A., Desmedt, C., Durbecq, V., Rouas, G., Larsimont, D., Sotiriou, C., & Goormaghtigh, E. (2010). Discrimination between healthy and tumor tissues on formalin-fixed paraffin-embedded breast cancer samples using IR imaging. Spectroscopy, 24(1-2), 67-72. doi:10.3233/SPE-2010-0406
  7. 77. Gasper, R., Mijatovic, T., Kiss, R., & Goormaghtigh, E. (2010). FTIR spectroscopy reveals the concentration dependence of cellular modifications induced by anticancer drugs. Spectroscopy, 24(1-2), 45-49. doi:10.3233/SPE-2010-0401
  8. 78. Derenne, A., Gasper, R., & Goormaghtigh, E. (2010). Monitoring of metabolism perturbation in prostate PC-3 cancer cells by sub-lethal concentrations of methotrexate. Spectroscopy, 1(2), 55-60. doi:10.3233/SPE-2010-0404
  9. 79. Goormaghtigh, E., Derenne, A., Benard, A., Gasper, R., & Raussens, V. (2010). Data processing in FTIR imaging of cells: Towards protein secondary structure imaging. Spectroscopy, 24(1-2), 51-54. doi:10.3233/SPE-2010-0403
  10. 80. 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.
  11. 81. 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.
  12. 82. 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
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