Common core structure of amyloid fibrils by synchrotron X-ray diffraction 1 1Edited by F. E. Cohen

Structure of Rhombohedral 2 Zinc Insulin Crystals

ADAMS, M. J., BLUNDELL, T. L., DODSON, E. J., DODSON, G. G., VIJAYAN, M., BAKER, E. N., HARDING, M. M., HODGKIN, D. C., RIMMER, B., & SHEAT, S. (1969) · Nature · doi:10.1038/224491a0 · Cited by 503

The amyloid state and its association with protein misfolding diseases.

Knowles, T. P. J., Vendruscolo, M., & Dobson, C. M. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3810 · Cited by 2,382

Cryo-EM structures of tau filaments from Alzheimer’s disease

Fitzpatrick, A. W. P., Falcon, B., He, S., Murzin, A. G., Murshudov, G., Garringer, H. J., Crowther, R. A., Ghetti, B., Goedert, M., & Scheres, S. H. W. (2017) · Nature · doi:10.1038/nature23002 · Cited by 2,061

Unfolding the role of protein misfolding in neurodegenerative diseases

Soto, C. (2003) · Nature Reviews Neuroscience · doi:10.1038/nrn1007 · Cited by 1,506

The RIP1/RIP3 Necrosome Forms a Functional Amyloid Signaling Complex Required for Programmed Necrosis

Li, J., McQuade, T., Siemer, A. B., Napetschnig, J., Moriwaki, K., Hsiao, Y.-S., Damko, E., Moquin, D., Walz, T., McDermott, A., et al. (2012) · Cell · doi:10.1016/j.cell.2012.06.019 · Cited by 1,222

The expanding amyloid family: Structure, stability, function, and pathogenesis

Sawaya, M. R., Hughes, M. P., Rodriguez, J. A., Riek, R., & Eisenberg, D. S. (2021) · Cell · doi:10.1016/j.cell.2021.08.013 · Cited by 475

Matrix Metalloproteinase-9 Degrades Amyloid-β Fibrils in Vitro and Compact Plaques in Situ

Yan, P., Hu, X., Song, H., Yin, K., Bateman, R. J., Cirrito, J. R., Xiao, Q., Hsu, F. F., Turk, J. W., Xu, J., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602440200 · Cited by 380

Distinct β-sheet structure in protein aggregates determined by ATR-FTIR spectroscopy

Shivu, B., Seshadri, S., Li, J., Oberg, K. A., Uversky, V. N., & Fink, A. L. (2013) · Biochemistry · doi:10.1021/bi400625v · Cited by 289

Amyloid-β peptide (Aβ) neurotoxicity is modulated by the rate of peptide aggregation: Aβ dimers and trimers correlate with neurotoxicity

Hung, L. W., Ciccotosto, G. D., Giannakis, E., Tew, D. J., Perez, K., Masters, C. L., Cappai, R., Wade, J. D., & Barnham, K. J. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.3916-08.2008 · Cited by 210

Characterization of Alzheimer’s-like Paired Helical Filaments from the Core Domain of Tau Protein Using Solid-State NMR Spectroscopy

Andronesi, O. C., Bergen, M. V., Biernat, J., Seidel, K., Griesinger, C., Mandelkow, E., & Baldus, M. (2008) · Journal of the American Chemical Society · doi:10.1021/ja7100517 · Cited by 167

Biophysical Insights into How Surfaces, Including Lipid Membranes, Modulate Protein Aggregation Related to Neurodegeneration

Burke, K. A., Yates, E. A., & Legleiter, J. (2013) · Frontiers in Neurology · doi:10.3389/fneur.2013.00017 · Cited by 127

Fibril fragmentation in amyloid assembly and cytotoxicity: When size matters

Xue, W.-F., Hellewell, A. L., Hewitt, E. W., & Radford, S. E. (2010) · Prion · doi:10.4161/pri.4.1.11378 · Cited by 117

Amino-terminal domain stability mediates apolipoprotein E aggregation into neurotoxic fibrils

Hatters, D. M., Zhong, N., Rutenber, E., & Weisgraber, K. H. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.06.080 · Cited by 105

Microbial functional amyloids serve diverse purposes for structure, adhesion and defence

Shanmugam, N., Baker, M. O. D. G., Ball, S. R., Steain, M., Pham, C. L. L., & Sunde, M. (2019) · Biophysical Reviews · doi:10.1007/s12551-019-00526-1 · Cited by 75

Higher-order Molecular Packing in Amyloid-like Fibrils Constructed with Linear Arrangements of Hydrophobic and Hydrogen-bonding Side-chains

Saiki, M., Honda, S., Kawasaki, K., Zhou, D., Kaito, A., Konakahara, T., & Morii, H. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.03.022 · Cited by 57

Integrative Structural Biology in the Era of Accurate Structure Prediction

Masrati, G., Landau, M., Ben-Tal, N., Lupas, A., Kosloff, M., & Kosinski, J. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167127 · Cited by 53

Cysteine oxidation triggers amyloid fibril formation of the tumor suppressor p16INK4A

Göbl, C., Morris, V. K., van Dam, L., Visscher, M., Polderman, P. E., Hartlmüller, C., de Ruiter, H., Hora, M., Liesinger, L., Birner-Gruenberger, R., et al. (2020) · Redox Biology · doi:10.1016/j.redox.2019.101316 · Cited by 29

Structural Determinant of β-Amyloid Formation: From Transmembrane Protein Dimerization to β-Amyloid Aggregates

Papadopoulos, N., Suelves, N., Perrin, F., Vadukul, D. M., Vrancx, C., Constantinescu, S. N., & Kienlen-Campard, P. (2022) · Biomedicines · doi:10.3390/biomedicines10112753 · Cited by 20