Buchli, B., Waldauer, S. A., Walser, R., Donten, M. L., Pfister, R., Blöchliger, N., … Hamm, P. (2013). Kinetic response of a photoperturbed allosteric protein. Proceedings of the National Academy of Sciences of the United States of America, 110(29), 11725-11730. https://doi.org/10.1073/pnas.1306323110 (Original work published)
Attanasio, F., Convertino, M., Magno, A., Caflisch, A., Corazza, A., Haridas, H., … Rizzarelli, E. (2013). Carnosine inhibits Aβ42 aggregation by perturbing the H-bond network in and around the central hydrophobic cluster. ChemBioChem, 14(5), 583-592. https://doi.org/10.1002/cbic.201200704 (Original work published)
Frydman-Marom, A., Convertino, M., Pellarin, R., Lampel, A., Shaltiel-Karyo, R., Segal, D., … Gazit, E. (2011). Structural basis for inhibiting β-amyloid oligomerization by a non-coded β-breaker-substituted endomorphin analogue. ACS Chemical Biology, 6(11), 1265-1276. https://doi.org/10.1021/cb200103h (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)
Scherzer-Attali, R., Pellarin, R., Convertino, M., Frydman-Marom, A., Egoz-Matia, N., Peled, S., … Segal, D. (2010). Complete phenotypic recovery of an Alzheimer’s disease model by a quinone-tryptophan hybrid aggregation inhibitor. PLoS One, 5(6), e11101. https://doi.org/10.1371/journal.pone.0011101 (Original work published 2010)
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)
Interlandi, G., Settanni, G., & Caflisch, A. (2006). Unfolding transition state and intermediates of the tumor suppressor p16INK4a investigated by molecular dynamics simulations. Proteins: Structure, Function, and Bioinformatics, 64(1), 178-192. https://doi.org/10.1002/prot.20953 (Original work published)
Böckmann, R. A., & Caflisch, A. (2005). Spontaneous formation of detergent micelles around the outer membrane protein OmpX. Biophysical Journal, 88(5), 3191-3204. https://doi.org/10.1529/biophysj.105.060426 (Original work published 2005)
Gsponer, J., Ferrara, P., & Caflisch, A. (2001). Flexibility of the murine prion protein and its Asp178Asn mutant investigated by molecular dynamics simulations. Journal of Molecular Graphics and Modelling, 20(2), 169-182. https://doi.org/doi:10.1016/S1093-3263(01)00117-6 (Original work published 2001)