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Reference62 articles.
1. Ando, T., & Uchihashi, T. (2013). High-speed AFM and imaging of biomoleculr processes. In T. Ondarçuhu & J.-P. Aime (Eds.), Nanoscale liquid interfaces: Wetting, patterning and force microscopy at the molecular scale (pp. 713–742). Pan Stanford Publishing.
2. Ando, T., Uchihashi, T., & Scheuring, S. (2014). Filming biomolecular processes by high-speed atomic force microscopy. Chemical Reviews, 114, 3120–3188.
3. Banerjee, S., Sun, Z., Hayden, E. Y., Teplow, D. B., & Lyubchenko, Y. L. (2017). Nanoscale dynamics of amyloid β-42 oligomers as revealed by high-speed atomic force microscopy. ACS Nano, 11, 12202–12209.
4. Blake, C., & Serpell, L. (1996). Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous β-helix. Structure, 4, 989–998.
5. Bousset, L., Pieri, L., Ruiz-Arlandis, G., Gath, J., Jensen, P. H., Habenstein, B., Madiona, K., Olieric, V., Böckmann, A., Meier, B. H., & Melki, R. (2013). Structural and functional characterization of two alpha-synuclein strains. Nature Communications, 4, 2575.