Dehabadi, M. H., Caflisch, A., Ilie, I. M., & Firouzi, R. (2022). Interactions of curcumin’s degradation products with the Aβ dimer: a computational study. The Journal of Physical Chemistry B, 126(39), 7627-7637. https://doi.org/10.1021/acs.jpcb.2c05846 (Original work published)

Ilie, I. M., & Caflisch, A. (2018). Disorder at the tips of a disease-relevant Aβ42 amyloid fibril: A molecular dynamics study. The Journal of Physical Chemistry B, 122(49), 11072–11082. https://doi.org/10.1021/acs.jpcb.8b05236 (Original work published)

Bacci, M., Vymětal, J., Mihajlovic, M., Caflisch, A., & Vitalis, A. (2017). Amyloid β fibril elongation by monomers involves disorder at the tip. Journal of Chemical Theory and Computation, 13(10), 5117-5130. https://doi.org/10.1021/acs.jctc.7b00662 (Original work published)

Ben Halima, S., Mishra, S., Raja, K. M. P., Willem, M., Baici, A., Simons, K., … Rajendran, L. (2016). Specific inhibition of β-secretase processing of the Alzheimer disease amyloid precursor protein. Cell Reports, 14(9), 2127-2141. https://doi.org/10.1016/j.celrep.2016.01.076 (Original work published)

Scherzer-Attali, R., Convertino, M., Pellarin, R., Gazit, E., Segal, D., & Caflisch, A. (2013). Methylations of tryptophan-modified naphthoquinone affect its inhibitory potential toward Aβ aggregation. The Journal of Physical Chemistry B, 117(6), 1780-1789. https://doi.org/10.1021/jp309066p (Original work published)

Mishra, S., & Caflisch, A. (2011). Dynamics in the active site of β-secretase: A network analysis of atomistic simulations. Biochemistry, 50(43), 9328-9339. https://doi.org/10.1021/bi2011948 (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)

Gorfe, A. A., & Caflisch, A. (2005). Functional plasticity in the substrate binding site of beta-secretase. Structure, 13(10), 1487-1498. https://doi.org/10.1016/j.str.2005.06.015 (Original work published 2005)

Tartaglia, G. G., Cavalli, A., Pellarin, R., & Caflisch, A. (2005). Prediction of aggregation rate and aggregation-prone segments in polypeptide sequences. Protein Science, 14(10), 2723-2734. https://doi.org/10.1110/ps.051471205 (Original work published 2005)

Tartaglia, G. G., Cavalli, A., Pellarin, R., & Caflisch, A. (2004). The role of aromaticity, exposed surface, and dipole moment in determining protein aggregation rates. Protein Science, 13(7), 1939-1941. https://doi.org/10.1110/ps.04663504 (Original work published 2004)