Structural Classification of Toxic Amyloid Oligomers

The Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics

Hardy, J., & Selkoe, D. J. (2002) · Science · doi:10.1126/science.1072994 · Cited by 13,864 · see citing works

Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide

Haass, C., & Selkoe, D. J. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2101 · Cited by 4,744 · see citing works

Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo

Walsh, D. M., Klyubin, I., Fadeeva, J. V., Cullen, W. K., Anwyl, R., Wolfe, M. S., Rowan, M. J., & Selkoe, D. J. (2002) · Nature · doi:10.1038/416535a · Cited by 4,291 · see citing works

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 · see citing works

Diffusible, nonfibrillar ligands derived from Aβ _1–42 are potent central nervous system neurotoxins

Lambert, M. P., Barlow, A. K., Chromy, B. A., Edwards, C., Freed, R., Liosatos, M., Morgan, T. E., Rozovsky, I., Trommer, B., Viola, K. L., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6448 · Cited by 3,506 · see citing works

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 · see citing works

Atomic structures of amyloid cross-β spines reveal varied steric zippers

Sawaya, M. R., Sambashivan, S., Nelson, R. A., Ivanova, M. I., Sievers, S. A., Apostol, M. I., Thompson, M. J., Balbirnie, M., Wiltzius, J. J. W., McFarlane, H. T., et al. (2007) · Nature · doi:10.1038/nature05695 · Cited by 2,279 · see citing works

Structure of the cross-β spine of amyloid-like fibrils

Nelson, R. A., Sawaya, M. R., Balbirnie, M., Madsen, A. Ø., Riekel, C., Grothe, R., & Eisenberg, D. S. (2005) · Nature · doi:10.1038/nature03680 · Cited by 2,205 · see citing works

3D structure of Alzheimer's amyloid-β(1–42) fibrils

Lührs, T., Ritter, C., Adrian, M., Riek-Loher, D., Bohrmann, B., Döbeli, H., Schubert, D. A., & Riek, R. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506723102 · Cited by 2,001 · see citing works

A structural model for Alzheimer's β-amyloid fibrils based on experimental constraints from solid state NMR

Petkova, A. T., Ishii, Y., Balbach, J. J., Antzutkin, O. N., Leapman, R. D., Delaglio, F., & Tycko, R. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.262663499 · Cited by 1,847 · see citing works

Self-Propagating, Molecular-Level Polymorphism in Alzheimer's ß-Amyloid Fibrils

Petkova, A. T., Leapman, R. D., Guo, Z., Yau, W.-M., Mattson, M. P., & Tycko, R. (2005) · Science · doi:10.1126/science.1105850 · Cited by 1,687 · see citing works

Natural oligomers of the amyloid-β protein specifically disrupt cognitive function

Cleary, J. P., Walsh, D. M., Hofmeister, J. J., Shankar, G. M., Kuskowski, M. A., Selkoe, D. J., & Ashe, K. H. (2004) · Nature Neuroscience · doi:10.1038/nn1372 · Cited by 1,677 · see citing works

Soluble Amyloid β Peptide Concentration as a Predictor of Synaptic Change in Alzheimer's Disease

Lue, L.-F., Kuo, Y.-M., Roher, A. E., Brachova, L., Shen, Y., Sue, L., Beach, T., Kurth, J. H., Rydel, R. E., & Rogers, J. (1999) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)65184-x · Cited by 1,530 · see citing works

Intraneuronal Aβ Causes the Onset of Early Alzheimer’s Disease-Related Cognitive Deficits in Transgenic Mice

Billings, L. M., Oddo, S., Green, K. N., McGaugh, J. L., & LaFerla, F. M. (2005) · Neuron · doi:10.1016/j.neuron.2005.01.040 · Cited by 1,294 · see citing works

Amyloid pores from pathogenic mutations

Lashuel, H. A., Hartley, D. M., Petre, B. M., Walz, T., & Lansbury, P. T. (2002) · Nature · doi:10.1038/418291a · Cited by 1,291 · see citing works

Amyloid β-protein (Aβ) assembly: Aβ40 and Aβ42 oligomerize through distinct pathways

Bitan, G., Kirkitadze, M. D., Lomakin, A., Vollers, S. S., Benedek, G. B., & Teplow, D. B. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.222681699 · Cited by 1,280 · see citing works

Amyloid β-Protein Fibrillogenesis

Walsh, D. M., Lomakin, A., Benedek, G. B., Condron, M. M., & Teplow, D. B. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.35.22364 · Cited by 1,139 · see citing works

Rationalization of the effects of mutations on peptide andprotein aggregation rates

Chiti, F., Stefani, M., Taddei, N., Ramponi, G., & Dobson, C. M. (2003) · Nature · doi:10.1038/nature01891 · Cited by 1,072 · see citing works

Alzheimer's disease-affected brain: Presence of oligomeric Aβ ligands (ADDLs) suggests a molecular basis for reversible memory loss

Gong, Y., Chang, L., Viola, K. L., Lacor, P. N., Lambert, M. P., Finch, C. E., Krafft, G. A., & Klein, W. L. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1834302100 · Cited by 1,061 · see citing works

Assembly and aggregation properties of synthetic Alzheimer's A4/beta amyloid peptide analogs.

Burdick, D., Soreghan, B., Kwon, M., Kosmoski, J., Knauer, M., Henschen, A., Yates, J., Cotman, C., & Glabe, C. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)48529-8 · Cited by 1,014 · see citing works

Synaptic Targeting by Alzheimer's-Related Amyloid β Oligomers

Lacor, P. N., Buniel, M. C., Chang, L., Fernandez, S. J., Gong, Y., Viola, K. L., Lambert, M. P., Velasco, P. T., Bigio, E. H., Finch, C. E., et al. (2004) · The Journal of Neuroscience · doi:10.1523/jneurosci.3432-04.2004 · Cited by 954 · see citing works

Nanoparticle-based detection in cerebral spinal fluid of a soluble pathogenic biomarker for Alzheimer’s disease

Georganopoulou, D. G., Chang, L., Nam, J.-M., Thaxton, C. S., Mufson, E. J., Klein, W. L., & Mirkin, C. A. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0409336102 · Cited by 835 · see citing works

Fibrils Formed in Vitro from α-Synuclein and Two Mutant Forms Linked to Parkinson's Disease are Typical Amyloid

Conway, K. A., Harper, J. D., & Lansbury, P. T. (2000) · Biochemistry · doi:10.1021/bi991447r · Cited by 786 · see citing works

Fibril specific, conformation dependent antibodies recognize a generic epitope common to amyloid fibrils and fibrillar oligomers that is absent in prefibrillar oligomers

Kayed, R., Head, E., Sarsoza, F., Saing, T., Cotman, C. W., Necula, M., Margol, L., Wu, J., Breydo, L., Thompson, J. L., et al. (2007) · Molecular Neurodegeneration · doi:10.1186/1750-1326-2-18 · Cited by 773 · see citing works

The Relationship between Aβ and Memory in the Tg2576 Mouse Model of Alzheimer's Disease

Westerman, M. A., Cooper-Blacketer, D., Mariash, A., Kotilinek, L., Kawarabayashi, T., Younkin, L. H., Carlson, G. A., Younkin, S. G., & Ashe, K. H. (2002) · Journal of Neuroscience · doi:10.1523/jneurosci.22-05-01858.2002 · Cited by 714 · see citing works

Observation of metastable Aβ amyloid protofibrils by atomic force microscopy

Harper, J. D., Wong, S. S., Lieber, C. M., & Lansbury, P. T. (1997) · Chemistry & Biology · doi:10.1016/s1074-5521(97)90255-6 · Cited by 691 · see citing works

Small Molecule Inhibitors of Aggregation Indicate That Amyloid β Oligomerization and Fibrillization Pathways Are Independent and Distinct

Necula, M., Kayed, R., Milton, S., & Glabe, C. G. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m608207200 · Cited by 680 · see citing works

The mechanism of islet amyloid polypeptide toxicity is membrane disruption by intermediate-sized toxic amyloid particles.

Janson, J., Ashley, R. H., Harrison, D. J., McIntyre, S., & Butler, P. C. (1999) · Diabetes · doi:10.2337/diabetes.48.3.491 · Cited by 614 · see citing works

Aggregation and secondary structure of synthetic amyloid βA4 peptides of Alzheimer's disease

Hilbich, C., Kisters–Woike, B., Reed, J., Masters, C. L., & Beyreuther, K. T. (1991) · Journal of Molecular Biology · doi:10.1016/0022-2836(91)90881-6 · Cited by 580 · see citing works

Globular amyloid β‐peptide ₁₋₄₂ oligomer − a homogenous and stable neuropathological protein in Alzheimer's disease

Barghorn, S., Nimmrich, V., Striebinger, A., Krantz, C., Keller, P., Janson, B., Bahr, M., Schmidt, M., Bitner, R. S., Harlan, J., et al. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03407.x · Cited by 559 · see citing works

Kinetic theory of fibrillogenesis of amyloid β-protein

Lomakin, A., Teplow, D. B., Kirschner, D. A., & Benedek, G. B. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.15.7942 · Cited by 529 · see citing works

X-ray diffraction from intraneuronal paired helical filaments and extraneuronal amyloid fibers in Alzheimer disease indicates cross-beta conformation.

Kirschner, D. A., Abraham, C., & Selkoe, D. J. (1986) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.83.2.503 · Cited by 517 · see citing works

Spherical aggregates of β-amyloid (amylospheroid) show high neurotoxicity and activate tau protein kinase I/glycogen synthase kinase-3β

Hoshi, M. M., Sato, M., Matsumoto, S., Noguchi, A., Yasutake, K., Yoshida, N., & Sato, K. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1237107100 · Cited by 494 · see citing works

Different Conformations of Amyloid β Induce Neurotoxicity by Distinct Mechanisms in Human Cortical Neurons

Deshpande, A. M., Mina, E. W., Glabe, C. G., & Busciglio, J. A. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.1189-06.2006 · Cited by 490 · see citing works

Amyloid β protein immunotherapy neutralizes Aβ oligomers that disrupt synaptic plasticity in vivo

Klyubin, I., Walsh, D. M., Lemere, C. A., Cullen, W. K., Shankar, G. M., Betts, V., Spooner, E. T., Jiang, L., Anwyl, R., Selkoe, D. J., et al. (2005) · Nature Medicine · doi:10.1038/nm1234 · Cited by 489 · see citing works

Vaccination with soluble Aβ oligomers generates toxicity‐neutralizing antibodies

Lambert, M. P., Viola, K. L., Chromy, B. A., Chang, L., Morgan, T. E., Yu, J., Venton, D. L., Krafft, G. A., Finch, C. E., & Klein, W. L. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00592.x · Cited by 349 · see citing works

The structural basis of yeast prion strain variants

Toyama, B. H., Kelly, M. J. S., Gross, J. D., & Weissman, J. S. (2007) · Nature · doi:10.1038/nature06108 · Cited by 339 · see citing works

Conformational Abs recognizing a generic amyloid fibril epitope

O’Nuallain, B., & Wetzel, R. B. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.022662599 · Cited by 331 · see citing works

Structural Organization of α-Synuclein Fibrils Studied by Site-directed Spin Labeling

Der-Sarkissian, A., Jao, C. C., Chen, J., & Langen, R. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305266200 · Cited by 328 · see citing works

Monoclonal antibodies that target pathological assemblies of Aβ

Lambert, M. P., Velasco, P. T., Chang, L., Viola, K. L., Fernandez, S., Lacor, P. N., Khuon, D., Gong, Y., Bigio, E. H., Shaw, P., et al. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04157.x · Cited by 314 · see citing works

Protofibrillar Islet Amyloid Polypeptide Permeabilizes Synthetic Vesicles by a Pore-like Mechanism that May Be Relevant to Type II Diabetes

Anguiano, M., Nowak, R. J., & Lansbury, P. T. (2002) · Biochemistry · doi:10.1021/bi020314u · Cited by 293 · see citing works

The Pathogenesis of Alzheimer Disease: An Alternative to the Amyloid Hypothesis

Terry, R. D. (1996) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/00005072-199655100-00001 · Cited by 291 · see citing works

Template-assisted filament growth by parallel stacking of tau

Margittai, M., & Langen, R. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0401911101 · Cited by 276 · see citing works

Surfactant properties of Alzheimer's A beta peptides and the mechanism of amyloid aggregation.

Soreghan, B. A., Kosmoski, J. V., & Glabe, C. G. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)61939-3 · Cited by 267 · see citing works

Prefibrillar Amyloid Aggregates Could Be Generic Toxins in Higher Organisms

Baglioni, S., Casamenti, F., Bucciantini, M., Luheshi, L. M., Taddei, N., Chiti, F., Dobson, C. M., & Stefani, M. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.4809-05.2006 · Cited by 245 · see citing works

Amyloid β Oligomers (Aβ 1–42 Globulomer) Suppress Spontaneous Synaptic Activity by Inhibition of P/Q-Type Calcium Currents

Nimmrich, V., Grimm, C., Draguhn, A., Barghorn, S., Lehmann, A., Schoemaker, H., Hillen, H., Groß, G., Ebert, U., & Bruehl, C. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.4771-07.2008 · Cited by 233 · see citing works

Antibody-Mediated Resolution of Light Chain-Associated Amyloid Deposits

Hrncic, R., Wall, J. S., Wolfenbarger, D., Murphy, C. L., Schell, M., Weiss, D. T., & Solomon, A. (2000) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)64639-1 · Cited by 206 · see citing works

Soluble Amyloid Aβ-(1–40) Exists as a Stable Dimer at Low Concentrations

Garzon-Rodriguez, W., Sepulveda-Becerra, M., Milton, S. C. F., & Glabe, C. G. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.34.21037 · Cited by 204 · see citing works

Adult-derived neural precursors transplanted into multiple regions in the adult brain

Herrera, D. G., García‐Verdugo, J. M., & Álvarez-Buylla, A. (1999) · Annals of Neurology · doi:10.1002/1531-8249(199912)46:6 · Cited by 204 · see citing works

The prion strain phenomenon: Molecular basis and unprecedented features

Morales, R., Abid, K., & Soto, C. A. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2006.12.006 · Cited by 170 · see citing works

Identifying Structural Features of Fibrillar Islet Amyloid Polypeptide Using Site-directed Spin Labeling

Jayasinghe, S. A., & Langen, R. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406853200 · Cited by 153 · see citing works

Pauling and Corey's α-pleated sheet structure may define the prefibrillar amyloidogenic intermediate in amyloid disease

Armen, R. S., DeMarco, M. L., Alonso, D. O. V., & Daggett, V. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0401781101 · Cited by 138 · see citing works

Soluble Aβ oligomers ultrastructurally localize to cell processes and might be related to synaptic dysfunction in Alzheimer's disease brain

Kokubo, H., Kayed, R., Glabe, C. G., & Yamaguchi, H. (2004) · Brain Research · doi:10.1016/j.brainres.2004.10.041 · Cited by 110 · see citing works

A Ganglioside-induced Toxic Soluble Aβ Assembly

Yamamoto, N., Matsubara, E., Maeda, S., Minagawa, H., Takashima, A., Maruyama, W., Michikawa, M., & Yanagisawa, K. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m606202200 · Cited by 91 · see citing works

Conformation-sensitive Antibodies against Alzheimer Amyloid-β by Immunization with a Thioredoxin-constrained B-cell Epitope Peptide

Moretto, N., Bolchi, A., Rivetti, C., Imbimbo, B. P., Villetti, G., Pietrini, V., Polonelli, L., Signore, S. J. D., Smith, K. M., Ferrante, R. J., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m609690200 · Cited by 69 · see citing works

Probing the Conformation of the Prion Protein within a Single Amyloid Fibril Using a Novel Immunoconformational Assay

Novitskaya, V., Makarava, N., Bellon, A., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m601349200 · Cited by 63 · see citing works

Parallel β-domains: a new fold in protein structures

JURNAK, F. A., Yoder, M. D., Pickergill, R., et al. (1994) · Current Opinion in Structural Biology · doi:10.1016/0959-440x(94)90259-3 · Cited by 27 · see citing works

Oligomeric proteins ultrastructurally localize to cell processes, especially to axon terminals with higher density, but not to lipid rafts in Tg2576 mouse brain

Kokubo, H., Kayed, R., Glabe, C. G., Saido, T. C., Iwata, N., Helms, J. B., & Yamaguchi, H. (2005) · Brain Research · doi:10.1016/j.brainres.2005.03.017 · Cited by 18 · see citing works

Amyloid-β–induced neuronal dysfunction in Alzheimer's disease: from synapses toward neural networks

Palop, J. J., & Mucke, L. (2010) · Nature Neuroscience · doi:10.1038/nn.2583 · Cited by 1,651 · see citing works

Islet Amyloid Polypeptide, Islet Amyloid, and Diabetes Mellitus

Westermark, P., Andersson, A., & Westermark, G. T. (2011) · Physiological Reviews · doi:10.1152/physrev.00042.2009 · Cited by 1,044 · see citing works

Spatial Transcriptomics and In Situ Sequencing to Study Alzheimer’s Disease

Chen, W.-T., Lu, A., Craessaerts, K., Pavie, B., Sala Frigerio, C., Corthout, N., Qian, X., Laláková, J., Kühnemund, M., Voytyuk, I., et al. (2020) · Cell · doi:10.1016/j.cell.2020.06.038 · Cited by 949 · see citing works

Aβ Oligomers Cause Localized Ca ²⁺ Elevation, Missorting of Endogenous Tau into Dendrites, Tau Phosphorylation, and Destruction of Microtubules and Spines

Zempel, H., Thies, E., Mandelkow, E., & Mandelkow, E.-M. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.2357-10.2010 · Cited by 686 · see citing works

The Role of NMDA Receptors in Alzheimer’s Disease

Liu, J., Chang, L., Song, Y., Li, H., & Wu, Y. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00043 · Cited by 535 · see citing works

Deleterious Effects of Amyloid β Oligomers Acting as an Extracellular Scaffold for mGluR5

Renner, M., Lacor, P. N., Velasco, P. T., Xu, J., Contractor, A., Klein, W. L., & Triller, A. (2010) · Neuron · doi:10.1016/j.neuron.2010.04.029 · Cited by 468 · see citing works

Amyloid toxicity in Alzheimer’s disease

Reiss, A. B., Arain, H. A., Stecker, M. M., Siegart, N. M., & Kasselman, L. J. (2018) · Reviews in the Neurosciences · doi:10.1515/revneuro-2017-0063 · Cited by 447 · see citing works

Soluble Aβ oligomer production and toxicity

Larson, M. E., & Lesné, S. E. (2012) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07478.x · Cited by 356 · see citing works

Mechanism of amyloid plaque formation suggests an intracellular basis of Aβ pathogenicity

Friedrich, R. P., Tepper, K., Rönicke, R., Soom, M., Westermann, M., Reymann, K., Kaether, C., & Fändrich, M. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0904532106 · Cited by 303 · see citing works

Amyloid β-protein oligomers and Alzheimer’s disease

Hayden, E. Y., & Teplow, D. B. (2013) · Alzheimer's Research & Therapy · doi:10.1186/alzrt226 · Cited by 276 · see citing works

Amyloid β-Protein Dimers Rapidly Form Stable Synaptotoxic Protofibrils

O'Nuallain, B., Freir, D. B., Nicoll, A. J., Risse, E., Ferguson, N., Herron, C. E., Collinge, J., & Walsh, D. M. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.3537-10.2010 · Cited by 259 · see citing works

Amyloid-β Receptors: The Good, the Bad, and the Prion Protein

Jarosz-Griffiths, H. H., Noble, E., Rushworth, J. V., & Hooper, N. M. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.r115.702704 · Cited by 256 · see citing works

Age-related macular degeneration (AMD): Alzheimer's disease in the eye?

Kaarniranta, K., Salminen, A., Haapasalo, A., Soininen, H., & Hiltunen, M. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-101908 · Cited by 248 · see citing works

Pathogenesis of synaptic degeneration in Alzheimer's disease and Lewy body disease

Overk, C. R., & Masliah, E. (2014) · Biochemical Pharmacology · doi:10.1016/j.bcp.2014.01.015 · Cited by 242 · see citing works

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 · see citing works

Analyzing dendritic spine pathology in Alzheimer’s disease: Problems and opportunities

Dorostkar, M. M., Zou, C., Blazquez-Llorca, L., & Herms, J. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1449-5 · Cited by 235 · see citing works

Increased Accumulation of Intraneuronal Amyloid β in HIV-Infected Patients

HNRC, Achim, C. L., Adame, A., Dumaop, W., Everall, I. P., & Masliah, E. (2009) · Journal of Neuroimmune Pharmacology · doi:10.1007/s11481-009-9152-8 · Cited by 205 · see citing works

Loss of α7 Nicotinic Receptors Enhances β-Amyloid Oligomer Accumulation, Exacerbating Early-Stage Cognitive Decline and Septohippocampal Pathology in a Mouse Model of Alzheimer's Disease

Hernandez, C. M., Kayed, R., Zheng, H., Sweatt, J. D., & Dineley, K. T. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.5038-09.2010 · Cited by 204 · see citing works

Substoichiometric Levels of Cu2+ Ions Accelerate the Kinetics of Fiber Formation and Promote Cell Toxicity of Amyloid-β from Alzheimer Disease

Sarell, C. J., Wilkinson, S. R., & Viles, J. H. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.171355 · Cited by 199 · see citing works

Targeting the proper amyloid-beta neuronal toxins: a path forward for Alzheimer’s disease immunotherapeutics

Goure, W. F., Krafft, G. A., Jerecic, J., & Hefti, F. (2014) · Alzheimer's Research & Therapy · doi:10.1186/alzrt272 · Cited by 190 · see citing works

Transgenic mouse models of alzheimer disease: Developing a better model as a tool for therapeutic interventions.

Kitazawa, M., Medeiros, R., & M. LaFerla, F. (2012) · Current Pharmaceutical Design · doi:10.2174/138161212799315786 · Cited by 178 · see citing works

Human IAPP–induced pancreatic β cell toxicity and its regulation by autophagy

Shigihara, N., Fukunaka, A., Hara, A., Komiya, K., Honda, A., Uchida, T., Abe, H., Toyofuku, Y., Tamaki, M., Ogihara, T., et al. (2014) · Journal of Clinical Investigation · doi:10.1172/jci69866 · Cited by 177 · see citing works

Cinnamon extract inhibits tau aggregation associated with Alzheimer’s disease in vitro

Peterson, D. W., George, R. C., Scaramozzino, F., LaPointe, N. E., Anderson, R. A., Graves, D. J., & Lew, J. (2009) · Journal of Alzheimer s Disease · doi:10.3233/jad-2009-1083 · Cited by 171 · see citing works

The culprit behind amyloid beta peptide related neurotoxicity in Alzheimer's disease: oligomer size or conformation?

Broersen, K., Rousseau, F., & Schymkowitz, J. (2010) · Alzheimer's Research & Therapy · doi:10.1186/alzrt36 · Cited by 168 · see citing works

Microglial TYROBP/DAP12 in Alzheimer's Disease: Transduction of Physiological and Pathological Signals Across TREM2

Haure-Mirande, J.-V., Audrain, M., Ehrlich, M. E., & Gandy, S. (2022) · Molecular Neurodegeneration · doi:10.1186/s13024-022-00552-w · Cited by 159 · see citing works

Identification of an Aggregation-Prone Structure of Tau

Elbaum-Garfinkle, S., & Rhoades, E. (2012) · Journal of the American Chemical Society · doi:10.1021/ja305206m · Cited by 149 · see citing works

Osmotin attenuates amyloid beta-induced memory impairment, tau phosphorylation and neurodegeneration in the mouse hippocampus

Ali, T., Yoon, G. H., Shah, S. A., Lee, H. Y., & Kim, M. O. (2015) · Scientific Reports · doi:10.1038/srep11708 · Cited by 146 · see citing works

Prion-Protein-interacting Amyloid-β Oligomers of High Molecular Weight Are Tightly Correlated with Memory Impairment in Multiple Alzheimer Mouse Models

Kostylev, M. A., Kaufman, A. C., Nygaard, H. B., Patel, P., Haas, L. T., Gunther, E. C., Vortmeyer, A., & Strittmatter, S. M. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.643577 · Cited by 133 · see citing works

Intracellular amyloid and the neuronal origin of Alzheimer neuritic plaques

Pensalfini, A., Albay, R., Rasool, S., Wu, J. W., Hatami, A., Arai, H., Margol, L., Milton, S., Poon, W. W., Corrada, M. M., et al. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.07.011 · Cited by 120 · see citing works

CX3CR1 deficiency aggravates amyloid driven neuronal pathology and cognitive decline in Alzheimer’s disease

Puntambekar, S. S., Moutinho, M., Lin, P. B.-C., Jadhav, V., Tumbleson-Brink, D., Balaji, A., Benito, M. A., Xu, G., Oblak, A., Lasagna-Reeves, C. A., et al. (2022) · Molecular Neurodegeneration · doi:10.1186/s13024-022-00545-9 · Cited by 113 · see citing works

Senescence, brain inflammation, and oligomeric tau drive cognitive decline in Alzheimer's disease: Evidence from clinical and preclinical studies

Gaikwad, S., Senapati, S., Haque, M. A., & Kayed, R. (2024) · Alzheimer's & Dementia · doi:10.1002/alz.13490 · Cited by 117 · see citing works

Immunogenicity, Efficacy, Safety, and Mechanism of Action of Epitope Vaccine (Lu AF20513) for Alzheimer's Disease: Prelude to a Clinical Trial

Davtyan, H., Ghochikyan, A., Petrushina, I., Hovakimyan, A., Davtyan, A., Poghosyan, A., Marleau, A. M., Movsesyan, N., Kiyatkin, A., Rasool, S., et al. (2013) · The Journal of Neuroscience · doi:10.1523/jneurosci.4672-12.2013 · Cited by 112 · see citing works

Proteinopathy-induced neuronal senescence: a hypothesis for brain failure in Alzheimer’s and other neurodegenerative diseases

Golde, T. E., & Miller, V. M. (2009) · Alzheimer's Research & Therapy · doi:10.1186/alzrt5 · Cited by 98 · see citing works

Epitomic Characterization of the Specificity of the Anti-Amyloid Aβ Monoclonal Antibodies 6E10 and 4G8

Baghallab, I., Reyes-Ruiz, J. M., Abulnaja, K., Huwait, E., & Glabe, C. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-180582 · Cited by 95 · see citing works

New Insights in Amyloid Beta Interactions with Human Telomerase

Wang, J., Zhao, C., Zhao, A., Li, M., Ren, J., & Qu, X. (2015) · Journal of the American Chemical Society · doi:10.1021/ja511030s · Cited by 90 · see citing works

Cerebral Amyloid Angiopathy

(2012) · Progress in Molecular Biology and Translational Science · doi:10.1016/b978-0-12-385883-2.00006-0 · Cited by 84 · see citing works

An Unbalanced Synaptic Transmission: Cause or Consequence of the Amyloid Oligomers Neurotoxicity?

Sciaccaluga, M., Megaro, A., Bellomo, G., Ruffolo, G., Romoli, M., Palma, E., & Costa, C. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22115991 · Cited by 70 · see citing works

Olfactory dysfunction: its early temporal relationship and neural correlates in the pathogenesis of Alzheimer’s disease

Daulatzai, M. A. (2015) · Journal of Neural Transmission · doi:10.1007/s00702-015-1404-6 · Cited by 63 · see citing works

Neuron Specific Toxicity of Oligomeric Amyloid-β: Role for JUN-Kinase and Oxidative Stress

Ebenezer, P. J., Weidner, A. M., LeVine, H., Markesbery, W. R., Murphy, M. P., Zhang, L., Dasuri, K., Fernandez-Kim, S. O., Bruce-Keller, A. J., Gavilán, E., et al. (2010) · Journal of Alzheimer's Disease · doi:10.3233/jad-2010-101161 · Cited by 58 · see citing works

Modulation of the Aβ peptide aggregation pathway by KP1019 limits Aβ-associated neurotoxicity

Jones, M. R., Mu, C., Wang, M. C. P., Webb, M. I., Walsby, C. J., & Storr, T. (2015) · Metallomics · doi:10.1039/c4mt00252k · Cited by 50 · see citing works

Targeting Generation of Antibodies Specific to Conformational Epitopes of Amyloid β-Derived Neurotoxins

Lambert, M., Velasco, P., Viola, K., & Klein, W. (2009) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/187152709787601876 · Cited by 29 · see citing works

Deletion of Specific Sphingolipids in Distinct Neurons Improves Spatial Memory in a Mouse Model of Alzheimer’s Disease

Herzer, S., Hagan, C., von Gerichten, J., Dieterle, V., Munteanu, B., Sandhoff, R., Hopf, C., & Nordström, V. (2018) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2018.00206 · Cited by 27 · see citing works

Serum amyloid P secreted by bone marrow adipocytes drives skeletal amyloidosis

Kumar, S., Song, K., Wang, J., Baghel, M. S., Zeng, Y., Shen, K., Zheng, J., Crane, J., Demehri, S., Gao, P., et al. (2025) · Nature Aging · doi:10.1038/s43587-025-00924-z · Cited by 16 · see citing works

AD Vaccines: Conclusions and Future Directions

Wisniewski, T. (2009) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/187152709787847289 · Cited by 14 · see citing works

Beta-amyloid oligomers: recent developments

Borutaite, V., Morkuniene, R., & Valincius, G. (2011) · bmc · doi:10.1515/bmc.2011.019 · Cited by 9 · see citing works

Protein Aggregation and Its Consequences for Human Disease

Dobson, C. M. (2006) · Protein and Peptide Letters · doi:10.2174/092986606775338362 · Cited by 176 · see citing works

Advances in the Simulation of Protein Aggregation at the Atomistic Scale

Carballo‐Pacheco, M., & Strodel, B. (2016) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.6b00059 · Cited by 125 · see citing works

Oligomer Formation of Amyloid-β(29–42) from Its Monomers Using the Hamiltonian Replica-Permutation Molecular Dynamics Simulation

Itoh, S., & Okumura, H. (2016) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.6b03828 · Cited by 50 · see citing works

基礎の部 ● 演題 2デスミン心筋症マウスに対するニコランジルの心筋保護効果

三部篤 (2011) · Therapeutic research

Temperature-Dependent Structural Variability of Prion Protein Amyloid Fibrils

Žiaunys, M., Sakalauskas, A., Mikalauskaitė, K., Sniečkutė, R., & Smirnovas, V. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22105075 · Cited by 36 · see citing works