In Vitro Characterization of Conditions for Amyloid-β Peptide Oligomerization and Fibrillogenesis

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

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Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease

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

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Diffusible, nonfibrillar ligands derived from Aβ 1–42 are potent central nervous system neurotoxins

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Immunization with amyloid-β attenuates Alzheimer-disease-like pathology in the PDAPP mouse

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

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Mutation of the β-amyloid precursor protein in familial Alzheimer's disease increases β-protein production

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Acceleration of oligomerization, not fibrillization, is a shared property of both α-synuclein mutations linked to early-onset Parkinson's disease: Implications for pathogenesis and therapy

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

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Formation of Neurofibrillary Tangles in P301L Tau Transgenic Mice Induced by Aβ42 Fibrils

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Tuning Cellular Uptake of Molecular Probes by Rational Design of Their Assembly into Supramolecular Nanoprobes

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Fine structure study of Aβ 1–42 fibrillogenesis with atomic force microscopy

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Aβ Oligomers Induce Neuronal Cell Cycle Events in Alzheimer's Disease

Varvel, N. H., Bhaskar, K., Patil, A. R., Pimplikar, S. W., Herrup, K., & Lamb, B. T. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.2441-08.2008 · Cited by 141

Microglial derived tumor necrosis factor-α drives Alzheimer's disease-related neuronal cell cycle events

Bhaskar, K., Maphis, N. M., Xu, G., Varvel, N. H., Kokiko‐Cochran, O. N., Weick, J. P., Staugaitis, S. M., Cardona, A. E., Ransohoff, R. M., Herrup, K., et al. (2013) · Neurobiology of Disease · doi:10.1016/j.nbd.2013.10.007 · Cited by 141

The endocytic pathway in microglia during health, aging and Alzheimer’s disease

Solé-Domènech, S., Cruz, D. L., Capetillo-Zarate, E., & Maxfield, F. R. (2016) · Ageing Research Reviews · doi:10.1016/j.arr.2016.07.002 · Cited by 133

Inhibition of cyclin-dependent kinase 5 affects early neuroinflammatory signalling in murine model of amyloid beta toxicity

Wilkaniec, A., Gąssowska-Dobrowolska, M., Strawski, M., Adamczyk, A., & Czapski, G. A. (2018) · Journal of Neuroinflammation · doi:10.1186/s12974-017-1027-y · Cited by 133

β-Secretase-Cleaved Amyloid Precursor Protein Accumulates at Actin Inclusions Induced in Neurons by Stress or Amyloid β: A Feedforward Mechanism for Alzheimer's Disease

Maloney, M. T., Minamide, L. S., Kinley, A. W., Boyle, J. A., & Bamburg, J. R. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.3711-05.2005 · Cited by 140

Oligomeric and fibrillar species of β-amyloid (Aβ42) both impair mitochondrial function in P301L tau transgenic mice

Eckert, A., Hauptmann, S., Scherping, I., Meinhardt, J., Rhein, V. F., Dröse, S., Brandt, U., Fändrich, M., Müller, W. E., & Götz, J. (2008) · Journal of Molecular Medicine · doi:10.1007/s00109-008-0391-6 · Cited by 132

Simulations of nucleation and elongation of amyloid fibrils

Zhang, J., & Muthukumar, M. (2009) · The Journal of Chemical Physics · doi:10.1063/1.3050295 · Cited by 131

Calcium Ions Promote Formation of Amyloid β-Peptide (1–40) Oligomers Causally Implicated in Neuronal Toxicity of Alzheimer's Disease

Itkin, A., Duprès, V., Dufrêne, Y. F., Bechinger, B., Ruysschaert, J., & Raussens, V. (2011) · PLoS ONE · doi:10.1371/journal.pone.0018250 · Cited by 131

Small Molecule, Non-Peptide p75NTR Ligands Inhibit Aβ-Induced Neurodegeneration and Synaptic Impairment

Yang, T., Knowles, J. K., Lu, Q., Zhang, H., Arancio, O., Moore, L. A., Chang, T., Wang, Q., Andreasson, K. I., Rajadas, J., et al. (2008) · PLoS ONE · doi:10.1371/journal.pone.0003604 · Cited by 134

Apolipoprotein E and Low Density Lipoprotein Receptor-related Protein Facilitate Intraneuronal Aβ42 Accumulation in Amyloid Model Mice

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Tau phosphorylation and tau mislocalization mediate soluble Aβ oligomer‐induced AMPA glutamate receptor signaling deficits

Miller, E. C., Teravskis, P. J., Dummer, B. W., Zhao, X., Huganir, R. L., & Liao, D. (2014) · European Journal of Neuroscience · doi:10.1111/ejn.12507 · Cited by 131

miR-106b aberrantly expressed in a double transgenic mouse model for Alzheimer's disease targets TGF-β type II receptor

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Characterization of Chemical Exchange between Soluble and Aggregated States of β-Amyloid by Solution-State NMR upon Variation of Salt Conditions

Narayanan, S., & Reif, B. (2005) · Biochemistry · doi:10.1021/bi048264b · Cited by 128

GM1-Modified Lipoprotein-like Nanoparticle: Multifunctional Nanoplatform for the Combination Therapy of Alzheimer’s Disease

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Selection and characterization of Affibody ligands binding to Alzheimer amyloid β peptides

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Ammonium hydroxide treatment of Aβ produces an aggregate free solution suitable for biophysical and cell culture characterization

Ryan, T. M., Caine, J. M., Mertens, H. D. T., Kirby, N. M., Nigro, J., Breheney, K., Waddington, L. J., Streltsov, V. A., Curtain, C. C., Masters, C. L., et al. (2013) · PeerJ · doi:10.7717/peerj.73 · Cited by 133

Mechanism mediating oligomeric Aβ clearance by naïve primary microglia

Yang, C.-N., Shiao, Y.-J., Shie, F.-S., Guo, B.-S., Chen, P.-H., Cho, C.-Y., Chen, Y.-J., Huang, F.-L., & Tsay, H.-J. (2011) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.01.005 · Cited by 117

Protein Interactions and Misfolding Analyzed by AFM Force Spectroscopy

McAllister, C., Karymov, M. A., Kawano, Y., Lushnikov, A. Y., Mikheikin, A., Uversky, V. N., & Lyubchenko, Y. L. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.10.012 · Cited by 129

Inflammatory mechanisms in neurodegeneration

Nichols, M. R., St‐Pierre, M., Wendeln, A., Makoni, N. J., Gouwens, L. K., Garrad, E. C., Sohrabi, M., Neher, J. J., Tremblay, M., & Combs, C. K. (2019) · Journal of Neurochemistry · doi:10.1111/jnc.14674 · Cited by 129

Erythrocytic α-Synuclein as a potential biomarker for Parkinson’s disease

Tian, C., Liu, G., Gao, L., Soltys, D., Pan, C., Stewart, T., Shi, M. Y., Xie, Z., Liu, N., Feng, T., et al. (2019) · Translational Neurodegeneration · doi:10.1186/s40035-019-0155-y · Cited by 127

Protective mechanisms by cystatin C in neurodegenerative diseases

Levy, E. (2010) · Frontiers in Bioscience-Scholar · doi:10.2741/s170 · Cited by 122

The case for soluble Aβ oligomers as a drug target in Alzheimer's disease

Hefti, F. F., Goure, W. F., Jerecìć, J., Iverson, K. S., Walicke, P. A., & Krafft, G. A. (2013) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2013.03.002 · Cited by 122

Chitosan oligosaccharides alleviate cognitive deficits in an amyloid-β1–42-induced rat model of Alzheimer's disease

Jia, S., Zheng, L., Gao, Z., An, J., Wu, X., Li, X., Dai, X., Zheng, Q., & Sun, Y. (2015) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2015.11.011 · Cited by 121

α-Mangostin, a polyphenolic xanthone derivative from mangosteen, attenuates β-amyloid oligomers-induced neurotoxicity by inhibiting amyloid aggregation

Wang, Y., Xia, Z., Xu, J., Wang, Y., Hou, L., Qiu, Y. L., & Chen, H. (2011) · Neuropharmacology · doi:10.1016/j.neuropharm.2011.09.016 · Cited by 119

Photophysical study of Thioflavin T as fluorescence marker of amyloid fibrils

Freire, S., de Araujo, M. H., Al‐Soufi, W., & Novo, M. (2014) · Dyes and Pigments · doi:10.1016/j.dyepig.2014.05.004 · Cited by 119

Boom in the development of non‐peptidic β‐secretase (BACE1) inhibitors for the treatment of Alzheimer's disease

Silvestri, R. (2008) · Medicinal Research Reviews · doi:10.1002/med.20132 · Cited by 118

β-Azidoalanine as an IR Probe: Application to Amyloid Aβ(16-22) Aggregation

Oh, K., Lee, J., Joo, C., Han, H., & Cho, M. (2008) · The Journal of Physical Chemistry B · doi:10.1021/jp801558k · Cited by 119

Impact of amyloid imaging on drug development in Alzheimer's disease

Mathis, C. A., Lopresti, B. J., & Klunk, W. E. (2007) · Nuclear Medicine and Biology · doi:10.1016/j.nucmedbio.2007.06.015 · Cited by 121

Cu(II) Binding to Monomeric, Oligomeric, and Fibrillar Forms of the Alzheimer’s Disease Amyloid-β Peptide

Karr, J. W., & Szalai, V. A. (2008) · Biochemistry · doi:10.1021/bi702423h · Cited by 119

Self-Assembly of the Ionic Peptide EAK16: The Effect of Charge Distributions on Self-Assembly

Jun, S., Hong, Y., Imamura, H., Ha, B., Bechhoefer, J., & Chen, P. (2004) · Biophysical Journal · doi:10.1529/biophysj.103.038166 · Cited by 119

Cyclophilin D Deficiency Rescues Axonal Mitochondrial Transport in Alzheimer’s Neurons

Guo, L., Du, H., Yan, S., Wu, X., McKhann, G. M., Chen, J. X., & Yan, S. S. (2013) · PLoS ONE · doi:10.1371/journal.pone.0054914 · Cited by 118

Pulsed hydrogen–deuterium exchange mass spectrometry probes conformational changes in amyloid beta (Aβ) peptide aggregation

Zhang, Y., Rempel, D. L., Zhang, J., Sharma, A. K., Mirica, L. M., & Gross, M. L. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1309175110 · Cited by 118

Protofibril Formation of Amyloid β-Protein at Low pH via a Non-cooperative Elongation Mechanism

Carrotta, R., Manno, M., Bulone, D., Martorana, V., & Biagio, P. L. S. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500052200 · Cited by 117

Low-Density Lipoprotein Receptor-Related Protein 1 (LRP1) Mediates Neuronal Aβ42 Uptake and Lysosomal Trafficking

Fuentealba, R. A., Liu, Q., Zhang, J., Kanekiyo, T., Hu, X., Lee, J.-M., LaDu, M. J., & Bu, G. (2010) · PLoS ONE · doi:10.1371/journal.pone.0011884 · Cited by 116

Amyloid-β oligomers in cellular models of Alzheimer’s disease

Fontana, I. C., Zimmer, A. R., Rocha, A. S., Gosmann, G., Souza, D. O., Lourenco, M. V., Ferreira, S. T., & Zimmer, E. R. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.15030 · Cited by 115

Cystatin C Protects Neuronal Cells from Amyloid-β-induced Toxicity

Tizón, B., Ribé, E. M., Mi, W., Troy, C. M., & Levy, E. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-1291 · Cited by 115

Endocytic uptake of monomeric amyloid-β peptides is clathrin- and dynamin-independent and results in selective accumulation of Aβ(1–42) compared to Aβ(1–40)

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Recent therapeutic strategies targeting beta amyloid and tauopathies in Alzheimer's disease

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Methylation of the Imidazole Side Chains of the Alzheimer Disease Amyloid-β Peptide Results in Abolition of Superoxide Dismutase-like Structures and Inhibition of Neurotoxicity

Tickler, A. K., Smith, D. G., Ciccotosto, G. D., Tew, D. J., Curtain, C. C., Carrington, D., Masters, C. L., Bush, A. I., Cherny, R. A., Cappai, R., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414178200 · Cited by 115

Lipid membranes catalyse the fibril formation of the amyloid-β (1–42) peptide through lipid-fibril interactions that reinforce secondary pathways

Lindberg, D. J., Wesén, E. V., Björkeroth, J., Rocha, S., & Esbjörner, E. K. (2017) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2017.05.012 · Cited by 113

Unraveling the Early Events of Amyloid-β Protein (Aβ) Aggregation: Techniques for the Determination of Aβ Aggregate Size

Pryor, N. E., Moss, M. A., & Hestekin, C. N. (2012) · International Journal of Molecular Sciences · doi:10.3390/ijms13033038 · Cited by 113

Physiochemical characterization of the Alzheimer's disease‐related peptides Aβ1–42Arctic and Aβ1–42wt

Johansson, A., Berglind‐Dehlin, F., Karlsson, G., Edwards, K., Gellerfors, P., & Lannfelt, L. (2006) · FEBS Journal · doi:10.1111/j.1742-4658.2006.05263.x · Cited by 111

Atomic force microscopy to study molecular mechanisms of amyloid fibril formation and toxicity in Alzheimer’s disease

Drolle, E., Hane, F. T., Lee, B. Y., & Leonenko, Z. (2014) · Drug Metabolism Reviews · doi:10.3109/03602532.2014.882354 · Cited by 120

Direct Observation of Nucleation and Growth in Amyloid Self-Assembly

Liang, Y., Lynn, D. G., & Berland, K. M. (2010) · Journal of the American Chemical Society · doi:10.1021/ja910964c · Cited by 112

Deregulation of NMDA-receptor function and down-stream signaling in APP[V717I] transgenic mice

Dewachter, I., Filipkowski, R. K., Priller, C., Ris, L., Neyton, J., Croes, S., Terwel, D., Gysemans, M., Devijver, H., Borghgraef, P., et al. (2007) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2007.06.011 · Cited by 116

Synaptotoxicity in Alzheimer's Disease Involved a Dysregulation of Actin Cytoskeleton Dynamics through Cofilin 1 Phosphorylation

Rush, T., Hernández, J. M., Dollmeyer, M., Frandemiche, M., Borel, E., Boisseau, S., Jacquier‐Sarlin, M. R., & Buisson, A. (2018) · Journal of Neuroscience · doi:10.1523/jneurosci.1409-18.2018 · Cited by 118

Amyloid β-peptides interfere with mitochondrial preprotein import competence by a coaggregation process

Cenini, G., Rüb, C., Bruderek, M., & Voos, W. (2016) · Molecular Biology of the Cell · doi:10.1091/mbc.e16-05-0313 · Cited by 111

MicroRNA-153 negatively regulates the expression of amyloid precursor protein and amyloid precursor-like protein 2

Liang, C., Zhu, H., Xu, Y., Huang, L. J., Ma, C., Deng, W., Liu, Y. M., & Qin, C. (2011) · Brain Research · doi:10.1016/j.brainres.2011.10.051 · Cited by 111

Inhibiting ACAT1/SOAT1 in microglia stimulates autophagy-mediated lysosomal proteolysis and increases Aβ1-42 clearance

Shibuya, Y., Chang, C. C. Y., Huang, L.-H., Bryleva, E. Y., & Chang, T.-Y. (2014) · The Journal of Neuroscience · doi:10.1523/jneurosci.2567-14.2014 · Cited by 108

Neuroprotective and Ameliorative Actions of Polyunsaturated Fatty Acids Against Neuronal Diseases: Beneficial Effect of Docosahexaenoic Acid on Cognitive Decline in Alzheimer’s Disease

Hashimoto, M., & Hossain, S. (2011) · Journal of Pharmacological Sciences · doi:10.1254/jphs.10r33fm · Cited by 113

“Click Peptide” Based on the “O-Acyl Isopeptide Method”: Control of Aβ1−42 Production from a Photo-Triggered Aβ1−42 Analogue

Taniguchi, A., Sohma, Y., Kimura, M., Okada, T., Ikeda, K., Hayashi, Y., Kimura, T., Hirota, S., Matsuzaki, K., & Kiso, Y. (2005) · Journal of the American Chemical Society · doi:10.1021/ja057100v · Cited by 108

β‐Amyloid protein oligomers induced by metal ions and acid pH are distinct from those generated by slow spontaneous ageing at neutral pH

Klug, G. M., Lošić, D., Supundi, Subasinghe, S., Aguilar, M., Martin, L. L., & Small, D. H. (2003) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2003.03815.x · Cited by 109

Synaptic transmission block by presynaptic injection of oligomeric amyloid beta

Moreno, H., Yu, E., Pigino, G. F., Hernandez, A. I., Kim, N., Moreira, J. E., Sugimori, M., & Llinás, R. R. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0900944106 · Cited by 113

Adsorption of Amyloid β (1–40) Peptide at Phospholipid Monolayers

Maltseva, E., Kerth, A., Blume, A., Möhwald, H., & Brezesinski, G. (2005) · ChemBioChem · doi:10.1002/cbic.200500116 · Cited by 106

Preferential accumulation of Aβ(1−42) on gel phase domains of lipid bilayers: An AFM and fluorescence study

Choucair, A., Chakrapani, M., Chakravarthy, B., Katsaras, J., & Johnston, L. J. (2006) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2006.09.005 · Cited by 105

Amyloid-β induces lipid droplet-mediated microglial dysfunction via the enzyme DGAT2 in Alzheimer’s disease

Prakash, P., Manchanda, P., Paouri, E., Bisht, K., Sharma, K., Rajpoot, J., Wendt, V., Hossain, A., Wijewardhane, P. R., Randolph, C. E., et al. (2025) · Immunity · doi:10.1016/j.immuni.2025.04.029 · Cited by 104

TRPA1 channels promote astrocytic Ca2+ hyperactivity and synaptic dysfunction mediated by oligomeric forms of amyloid-β peptide

Bosson, A., Paumier, A., Boisseau, S., Jacquier‐Sarlin, M. R., Buisson, A., & Albrieux, M. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0194-8 · Cited by 111

Role of aggregation conditions in structure, stability, and toxicity of intermediates in the Aβ fibril formation pathway

Lee, S., Fernández, E., & Good, T. A. (2007) · Protein Science · doi:10.1110/ps.062514807 · Cited by 104

Experimental traumatic brain injury induces rapid aggregation and oligomerization of amyloid-beta in an Alzheimer’s disease mouse model

Washington, P. M., Morffy, N., Parsadanian, M., Zapple, D. N., & Burns, M. P. (2014) · Journal of Neurotrauma · doi:10.1089/neu.2013.3017 · Cited by 103

Neuromodulatory Action of Picomolar Extracellular Aβ42 Oligomers on Presynaptic and Postsynaptic Mechanisms Underlying Synaptic Function and Memory

Gulisano, W., Melone, M., Ripoli, C., Tropea, M. R., Li Puma, D. D., Giunta, S., Cocco, S., Marcotulli, D., Origlia, N., Palmeri, A., et al. (2019) · The Journal of Neuroscience · doi:10.1523/jneurosci.0163-19.2019 · Cited by 100

Origin of metastable oligomers and their effects on amyloid fibril self-assembly

Hasecke, F., Miti, T., Perez, C., Barton, J., Schölzel, D., Gremer, L., Grüning, C. S. R., Matthews, G., Meisl, G., Knowles, T. P. J., et al. (2018) · Chemical Science · doi:10.1039/c8sc01479e · Cited by 103

p75NTR Regulates Aβ Deposition by Increasing Aβ Production But Inhibiting Aβ Aggregation with Its Extracellular Domain

Wang, Y., Wang, X., Lu, J.-J., Li, Q., Gao, C., Liu, X.-H., Sun, Y., Yang, M., Lim, Y. P., Evin, G. M., et al. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.2733-10.2011 · Cited by 99

An improved method for generating consistent soluble amyloid-beta oligomer preparations for in vitro neurotoxicity studies

Ryan, D. A., Narrow, W. C., Federoff, H. J., & Bowers, W. J. (2010) · Journal of Neuroscience Methods · doi:10.1016/j.jneumeth.2010.05.001 · Cited by 102

Amyloid beta dimers/trimers potently induce cofilin-actin rods that are inhibited by maintaining cofilin-phosphorylation

Davis, R. C., Marsden, I. T., Maloney, M. T., Minamide, L. S., Podlisny, M. B., Selkoe, D. J., & Bamburg, J. R. (2011) · Molecular Neurodegeneration · doi:10.1186/1750-1326-6-10 · Cited by 102

Thermodynamic Analysis of the Molecular Interactions between Amyloid β-Peptide 42 and (−)-Epigallocatechin-3-gallate

Wang, S., Liu, F., Dong, X., & Sun, Y. P. (2010) · The Journal of Physical Chemistry B · doi:10.1021/jp1001435 · Cited by 99

Amyloid‐β interrupts the PI3K‐Akt‐mTOR signaling pathway that could be involved in brain‐derived neurotrophic factor‐induced Arc expression in rat cortical neurons

Chen, T., Wang, D., & Chen, S. (2009) · Journal of Neuroscience Research · doi:10.1002/jnr.22057 · Cited by 99

A hydrogel biosensor for high selective and sensitive detection of amyloid-beta oligomers

Sun, L., Zhong, Y., Gui, J., Wang, X., Zhuang, X., & Weng, J. (2018) · International Journal of Nanomedicine · doi:10.2147/ijn.s152163 · Cited by 100

High ability of apolipoprotein E4 to stabilize amyloid‐β peptide oligomers, the pathological entities responsible for Alzheimer's disease

Cerf, E., Gustot, A., Goormaghtigh, E., Ruysschaert, J.-M., & Raussens, V. (2011) · The FASEB Journal · doi:10.1096/fj.10-175976 · Cited by 92

Sequestration of Toxic Oligomers by HspB1 as a Cytoprotective Mechanism

Ojha, J., Masilamoni, G. J., Dunlap, D. D., Udoff, R. A., & Cashikar, A. G. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.01187-10 · Cited by 99

ApoE and Aβ1–42 Interactions: Effects of Isoform and Conformation on Structure and Function

Manelli, A. M., Stine, W. B., Van Eldik, L. J., & LaDu, M. J. (2004) · Journal of Molecular Neuroscience · doi:10.1385/jmn:23:3:235 · Cited by 95

Epilepsy, amyloid-β, and D1 dopamine receptors: a possible pathogenetic link?

Costa, C., Parnetti, L., D'Amelio, M., Tozzi, A., Tantucci, M., Romigi, A., Siliquini, S., Cavallucci, V., Di Filippo, M., Mazzocchetti, P., et al. (2016) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2016.08.025 · Cited by 94

Stable, Metastable, and Kinetically Trapped Amyloid Aggregate Phases

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Amyloid β (Aβ) Peptide Directly Activates Amylin-3 Receptor Subtype by Triggering Multiple Intracellular Signaling Pathways

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