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Friedman, R., & Caflisch, A. (2011). Surfactant effects on amyloid aggregation kinetics. Journal of Molecular Biology, 414(2), 303-312. https://doi.org/10.1016/j.jmb.2011.10.011 (Original work published)

Huang, D., & Caflisch, A. (2011). Small molecule binding to proteins: Affinity and binding/unbinding dynamics from atomistic simulations. ChemMedChem, 6(9), 1578-80. https://doi.org/10.1002/cmdc.201100237 (Original work published)

Seeber, M., Felline, A., Raimondi, F., Muff, S., Friedman, R., Rao, F., … Fanelli, F. (2011). Wordom: A user-friendly program for the analysis of molecular structures, trajectories, and free energy surfaces. Journal of Computational Chemistry, 32(6), 1183-1194. https://doi.org/10.1002/jcc.21688 (Original work published)

Schuetz, P., Wuttke, R., Schuler, B., & Caflisch, A. (2010). Free energy surfaces from single-distance information. The Journal of Physical Chemistry B, 114(46), 15227-15235. https://doi.org/10.1021/jp1053698 (Original work published)

Pellarin, R., Schuetz, P., Guarnera, E., & Caflisch, A. (2010). Amyloid fibril polymorphism is under kinetic control. Journal of the American Chemical Society, 132(42), 14960-14970. https://doi.org/10.1021/ja106044u (Original work published)

Paoli, B., Pellarin, R., & Caflisch, A. (2010). Slow folding of cross-linked alpha-helical peptides due to steric hindrance. The Journal of Physical Chemistry B, 114(5), 2023-2027. https://doi.org/10.1021/jp910216j (Original work published)

Guarnera, E., Pellarin, R., & Caflisch, A. (2009). How does a simplified-sequence protein fold? Biophys J, 97(6), 1737-1746. https://doi.org/10.1016/j.bpj.2009.06.047 (Original work published)

Su, X.-C., Ozawa, K., Yagi, H., Lim, S. P., Wen, D., Ekonomiuk, D., … Otting, G. (2009). NMR study of complexes between low molecular mass inhibitors and the West Nile virus NS2B-NS3 protease. FEBS Journal, 276(15), 4244-4255. https://doi.org/10.1111/j.1742-4658.2009.07132.x (Original work published 2009)