Half a century of amyloids: past, present and future

Alzheimer's disease: the amyloid cascade hypothesis

Hardy, J. A., & Higgins, G. A. (1992) · Science · doi:10.1126/science.1566067 · Cited by 7,484

Principles that Govern the Folding of Protein Chains

Anfinsen, C. B. (1973) · Science · doi:10.1126/science.181.4096.223 · Cited by 7,096

The amyloid hypothesis of Alzheimer's disease at 25 years

Selkoe, D. J., & Hardy, J. (2016) · EMBO Molecular Medicine · doi:10.15252/emmm.201606210 · Cited by 6,164

RELION: Implementation of a Bayesian approach to cryo-EM structure determination

Scheres, S. H. W. (2012) · Journal of Structural Biology · doi:10.1016/j.jsb.2012.09.006 · Cited by 5,446

Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis

Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., & Glabe, C. G. (2003) · Science · doi:10.1126/science.1079469 · Cited by 4,064

Amyloid-β protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory

Shankar, G. M., Li, S., Mehta, T. H., Garcia-Munoz, A., Shepardson, N. E., Smith, I., Brett, F. M., Farrell, M. A., Rowan, M. J., Lemere, C. A., et al. (2008) · Nature Medicine · doi:10.1038/nm1782 · Cited by 3,685

Funnels, pathways, and the energy landscape of protein folding: A synthesis

Bryngelson, J. D., Onuchic, J. N., Socci, N. D., & Wolynes, P. G. (1995) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.340210302 · Cited by 2,648

Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases

Bucciantini, M., Giannoni, E., Chiti, F., Baroni, F., Formigli, L., Zurdo, J., Taddei, N., Ramponi, G., Dobson, C. M., & Stefani, M. (2002) · Nature · doi:10.1038/416507a · Cited by 2,434

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

From Levinthal to pathways to funnels

Dill, K. A., & Chan, H. S. (1997) · Nature Structural & Molecular Biology · doi:10.1038/nsb0197-10 · Cited by 2,293

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

Cell-free Formation of RNA Granules: Low Complexity Sequence Domains Form Dynamic Fibers within Hydrogels

Kato, M., Han, T. W., Xie, S., Shi, K., Du, X., Wu, L. C., Mirzaei, H., Goldsmith, E. J., Longgood, J., Pei, J., et al. (2012) · Cell · doi:10.1016/j.cell.2012.04.017 · Cited by 2,012

Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death

Arrasate, M., Mitra, S., Schweitzer, E. S., Segal, M. R., & Finkbeiner, S. (2004) · Nature · doi:10.1038/nature02998 · Cited by 1,979

The neuroactive potential of the human gut microbiota in quality of life and depression

Valles-Colomer, M., Falony, G., Darzi, Y., Tigchelaar, E. F., Wang, J., Tito, R. Y., Schiweck, C., Kurilshikov, A., Joossens, M., Wijmenga, C., et al. (2019) · Nature Microbiology · doi:10.1038/s41564-018-0337-x · Cited by 1,963

Two Phase 3 Trials of Bapineuzumab in Mild-to-Moderate Alzheimer's Disease

Salloway, S., Sperling, R., Fox, N. C., Blennow, K., Klunk, W., Raskind, M., Sabbagh, M., Honig, L. S., Porsteinsson, A. P., Ferris, S., et al. (2014) · New England Journal of Medicine · doi:10.1056/nejmoa1304839 · Cited by 1,960

Molecular analysis of prion strain variation and the aetiology of 'new variant' CJD

Collinge, J., Sidle, K. C. L., Meads, J., Ironside, J., & Hill, A. F. (1996) · Nature · doi:10.1038/383685a0 · Cited by 1,735

Phase 3 Trials of Solanezumab for Mild-to-Moderate Alzheimer's Disease

Doody, R. S., Thomas, R. G., Farlow, M., Iwatsubo, T., Vellas, B., Joffe, S., Kieburtz, K., Raman, R., Sun, X., Aisen, P. S., et al. (2014) · New England Journal of Medicine · doi:10.1056/nejmoa1312889 · Cited by 1,668

Exogenous Induction of Cerebral ß-Amyloidogenesis Is Governed by Agent and Host

Meyer-Luehmann, M., Coomaraswamy, J., Bolmont, T., Kaeser, S., Schaefer, C., Kilger, E., Neuenschwander, A., Abramowski, D., Frey, P., Jaton, A. L., et al. (2006) · Science · doi:10.1126/science.1131864 · Cited by 971

A gut-brain neural circuit for nutrient sensory transduction

Kaelberer, M. M., Buchanan, K. L., Klein, M. E., Barth, B. B., Montoya, M. M., Shen, X., & Bohórquez, D. V. (2018) · Science · doi:10.1126/science.aat5236 · Cited by 932

The Amyloid-β Oligomer Hypothesis: Beginning of the Third Decade

Cline, E. N., Bicca, M. A., Viola, K. L., & Klein, W. L. (2018) · Journal of Alzheimer's Disease · doi:10.3233/jad-179941 · Cited by 870

Reconsideration of Amyloid Hypothesis and Tau Hypothesis in Alzheimer's Disease

Kametani, F., & Hasegawa, M. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00025 · Cited by 836

Structural Classification of Toxic Amyloid Oligomers

Glabe, C. G. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.r800016200 · Cited by 783

Amyloid β oligomers constrict human capillaries in Alzheimer's disease via signaling to pericytes

Nortley, R., Korte, N., Izquierdo, P., Hirunpattarasilp, C., Mishra, A., Jaunmuktane, Z., Kyrargyri, V., Pfeiffer, T., Khennouf, L., Madry, C., et al. (2019) · Science · doi:10.1126/science.aav9518 · Cited by 682

Distinct α-Synuclein Strains Differentially Promote Tau Inclusions in Neurons

Guo, J. L., Covell, D. J., Daniels, J. P., Iba, M., Stieber, A., Zhang, B., Riddle, D. M., Kwong, L. K., Xu, Y., Trojanowski, J. Q., et al. (2013) · Cell · doi:10.1016/j.cell.2013.05.057 · Cited by 680

The Human Gut Bacterial Genotoxin Colibactin Alkylates DNA

Wilson, M. R., Jiang, Y., Villalta, P. W., Stornetta, A., Boudreau, P. D., Carrá, A., Brennan, C. A., Chun, E., Ngo, L., Samson, L. D., et al. (2019) · Science · doi:10.1126/science.aar7785 · Cited by 635

Ubiquitin is detected in neurofibrillary tangles and senile plaque neurites of Alzheimer disease brains.

Perry, G., Friedman, R., Shaw, G., & Chau, V (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.9.3033 · Cited by 623

β-Amyloid peptides enhance α-synuclein accumulation and neuronal deficits in a transgenic mouse model linking Alzheimer's disease and Parkinson's disease

Masliah, E., Rockenstein, E., Veinbergs, I., Sagara, Y., Mallory, M., Hashimoto, M., & Mucke, L. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.211412398 · Cited by 607

Synergistic Interactions between Aβ, Tau, and α-Synuclein: Acceleration of Neuropathology and Cognitive Decline

Clinton, L. K., Blurton-Jones, M., Myczek, K., Trojanowski, J. Q., & LaFerla, F. M. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.0490-10.2010 · Cited by 576

Biological metals and metal-targeting compounds in major neurodegenerative diseases

Barnham, K. J., & Bush, A. I. (2014) · Chem. Soc. Rev. · doi:10.1039/c4cs00138a · Cited by 497

Alzheimer's disease: The amyloid cascade hypothesis: An update and reappraisal

Hardy, J. (2006) · Journal of Alzheimer s Disease · doi:10.3233/jad-2006-9s317 · Cited by 475

Graphene quantum dots prevent α-synucleinopathy in Parkinson’s disease

Kim, D., Yoo, J. M., Hwang, H., Lee, J., Lee, S. H., Yun, S. P., Park, M. J., Lee, M., Choi, S., Kwon, S. H., et al. (2018) · Nature Nanotechnology · doi:10.1038/s41565-018-0179-y · Cited by 455

The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease

Ferreira, S. T., & Klein, W. L. (2011) · Neurobiology of Learning and Memory · doi:10.1016/j.nlm.2011.08.003 · Cited by 442

Heparan sulfate proteoglycan as a cell-surface endocytosis receptor

Christianson, H. C., & Belting, M. (2014) · Matrix Biology · doi:10.1016/j.matbio.2013.10.004 · Cited by 429

The amyloid hypothesis on trial

Makin, S. (2018) · Nature · doi:10.1038/d41586-018-05719-4 · Cited by 360

Preparation and Characterization of Neurotoxic Tau Oligomers

Lasagna-Reeves, C. A., Castillo-Carranza, D. L., Guerrero-Muñoz, M. J., Jackson, G. R., & Kayed, R. (2010) · Biochemistry · doi:10.1021/bi1016233 · Cited by 359

Diversity, biogenesis and function of microbial amyloids

Blanco, L. P., Evans, M. L., Smith, D. R., Badtke, M. P., & Chapman, M. R. (2012) · Trends in Microbiology · doi:10.1016/j.tim.2011.11.005 · Cited by 320

Tau-Targeted Multifunctional Nanocomposite for Combinational Therapy of Alzheimer’s Disease

Chen, Q., Du, Y., Zhang, K., Liang, Z., Li, J., Yu, H., Ren, R., Feng, J., Jin, Z., Li, F., et al. (2018) · ACS Nano · doi:10.1021/acsnano.7b07625 · Cited by 280

Passive Immunization with Tau Oligomer Monoclonal Antibody Reverses Tauopathy Phenotypes without Affecting Hyperphosphorylated Neurofibrillary Tangles

Castillo-Carranza, D. L., Sengupta, U., Guerrero-Muñoz, M. J., Lasagna-Reeves, C. A., Gerson, J. E., Singh, G., Estes, D. M., Barrett, A. D. T., Dineley, K. T., Jackson, G. R., et al. (2014) · The Journal of Neuroscience · doi:10.1523/jneurosci.3192-13.2014 · Cited by 278

Soluble Aβ Seeds Are Potent Inducers of Cerebral β-Amyloid Deposition

Langer, F., Eisele, Y. S., Fritschi, S. K., Staufenbiel, M., Walker, L. C., & Jucker, M. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.3088-11.2011 · Cited by 237

A Self-Destructive Nanosweeper That Captures and Clears Amyloid β-Peptides

Luo, Q., Lin, Y.-X., Yang, P.-P., Wang, Y., Qi, G.-B., Qiao, Z.-Y., Li, B.-N., Zhang, K., Zhang, J.-P., Wang, L., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-04255-z · Cited by 191

Peripheral clearance of amyloid β peptide by complement C3-dependent adherence to erythrocytes

Rogers, J., Li, R., Mastroeni, D., Grover, A., Leonard, B., Ahern, G., Cao, P., Kolody, H., Vedders, L., Kolb, W. P., et al. (2006) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.09.043 · Cited by 175

Advances in the treatment of hereditary transthyretin amyloidosis: a review

Gertz, M. A., Mauermann, M. L., Grogan, M., & Coelho, T. (2019) · Brain and Behavior · doi:10.1002/brb3.1371 · Cited by 102

Target engagement in an Alzheimer trial: crenezumab lowers amyloid β oligomers in cerebrospinal fluid

Yang, T., Dang, Y., Ostaszewski, B., Mengel, D., Steffen, V., Rabe, C., Bittner, T., Walsh, D. M., & Selkoe, D. J. (2019) · Annals of Neurology · doi:10.1002/ana.25513 · Cited by 91

Structure-based inhibitors halt prion-like seeding by Alzheimer's disease-and tauopathy-derived brain tissue samples

Seidler, P. M., Boyer, D. R., Murray, K. A., Yang, T. P., Bentzel, M., Sawaya, M. R., Rosenberg, G., Cascio, D., Williams, C. K., Newell, K. L., et al. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.009688 · Cited by 70

AlphaFold and the amyloid landscape

Pinheiro, F., Santos, J., & Ventura, S. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167059 · Cited by 88

Fluorescent peptide nanoparticles to detect amyloid-beta aggregation in cerebrospinal fluid and serum for Alzheimer’s disease diagnosis and progression monitoring

Sun, L., Liu, D., Fu, D., Yue, T., Scharre, D., & Zhang, L. (2021) · Chemical Engineering Journal · doi:10.1016/j.cej.2020.126733 · Cited by 32

Trace_y: Software algorithms for structural analysis of individual helical filaments by three-dimensional contact point reconstruction atomic force microscopy

Xue, W.-F. (2025) · Structure · doi:10.1016/j.str.2024.11.007 · Cited by 14

Hfq C-terminal region forms a β-rich amyloid-like motif without perturbing the N-terminal Sm-like structure

Berbon, M., Martinez, D., Morvan, E., Grélard, A., Kauffmann, B., Waeytens, J., Wien, F., Arluison, V., & Habenstein, B. (2023) · Communications Biology · doi:10.1038/s42003-023-05462-1 · Cited by 14

A genetically encoded selection for amyloid-β oligomer binders

Lee, B., Mannone, J. A., & Wang, T. (2025) · Nature Chemical Biology · doi:10.1038/s41589-025-01975-4 · Cited by 3