Amyloid β oligomers in Alzheimer’s disease pathogenesis, treatment, and diagnosis
Open accessAbstract
Protein aggregation is common to dozens of diseases including prionoses, diabetes, Parkinson's and Alzheimer's. Over the past 15 years, there has been a paradigm shift in understanding the structural basis for these proteinopathies. Precedent for this shift has come from investigation of soluble Aβ oligomers (AβOs), toxins now widely regarded as instigating neuron damage leading to Alzheimer's dementia. Toxic AβOs accumulate in AD brain and constitute long-lived alternatives to the disease-defining Aβ fibrils deposited in amyloid plaques. Key experiments using fibril-free AβO solutions demonstrated that while Aβ is essential for memory loss, the fibrillar Aβ in amyloid deposits is not the agent. The AD-like cellular pathologies induced by AβOs suggest their impact provides a unifying mechanism for AD pathogenesis, explaining why early stage disease is specific for memory and accounting for major facets of AD neuropathology. Alternative ideas for triggering mechanisms are being actively investigated. Some research favors insertion of AβOs into membrane, while other evidence supports ligand-like accumulation at particular synapses. Over a dozen candidate toxin receptors have been proposed. AβO binding triggers a redistribution of critical synaptic proteins and induces hyperactivity in metabotropic and ionotropic glutamate receptors. This leads to Ca(2+) overload and instigates major facets of AD neuropathology, including tau hyperphosphorylation, insulin resistance, oxidative stress, and synapse loss. Because different species of AβOs have been identified, a remaining question is which oligomer is the major pathogenic culprit. The possibility has been raised that more than one species plays a role. Despite some key unknowns, the clinical relevance of AβOs has been established, and new studies are beginning to point to co-morbidities such as diabetes and hypercholesterolemia as etiological factors. Because pathogenic AβOs appear early in the disease, they offer appealing targets for therapeutics and diagnostics. Promising therapeutic strategies include use of CNS insulin signaling enhancers to protect against the presence of toxins and elimination of the toxins through use of highly specific AβO antibodies. An AD-dependent accumulation of AβOs in CSF suggests their potential use as biomarkers and new AβO probes are opening the door to brain imaging. Overall, current evidence indicates that Aβ oligomers provide a substantive molecular basis for the cause, treatment and diagnosis of Alzheimer's disease.
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Because pathogenic soluble aggregates of Aβ appear early in the sequence of Alzheimer's disease, they can represent interesting targets for therapeutics and diagnostics.
“Because pathogenic soluble aggregates of Aβ appear early in the sequence of AD, they can represent interesting targets for therapeutics and diagnostics [51].”
From Alzheimer's Disease: Treatment Strategies and Their Limitations. (2022) · cites this paper as [51]
Oligomers are suggested to be the most neurotoxic species in AD because their levels correlate better with cognitive symptoms than presence of plaques or NFTs.
“It is suggested that oligomers are the most neurotoxic species in AD as levels of these species correlate much better with cognitive symptoms than presence of plaques or NFTs [166].”
From Alzheimer's disease: experimental models and reality (2017) · cites this paper as [166]
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RETRACTED ARTICLE: A specific amyloid-β protein assembly in the brain impairs memory
Lesné, S., Koh, M. T., Kotilinek, L., Kayed, R., Glabe, C. G., Yang, A., Gallagher, M., & Ashe, K. H. (2006) · Nature · doi:10.1038/nature04533 · Cited by 2,769 · see citing works
RetractedAmyloid oligomers exacerbate tau pathology in a mouse model of tauopathy
Selenica, M.-L. B., Brownlow, M., Jimenez, J. P., Lee, D. C., Pena, G., Dickey, C. A., Gordon, M. N., & Morgan, D. (2013) · Neurodegenerative Diseases · doi:10.1159/000337230 · Cited by 10,359 · see citing works
Imaging brain amyloid in Alzheimer's disease with Pittsburgh Compound‐B
Klunk, W. E., Engler, H., Nordberg, A., Wang, Y., Blomqvist, G., Holt, D. P., Bergström, M., Savitcheva, I., Huang, G., Estrada, S., et al. (2004) · Annals of Neurology · doi:10.1002/ana.20009 · Cited by 4,496 · see citing works
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
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
Self-citationJournal of Biological Chemistry
Kurkinensp, M., CondongT, M. R., Blumberg, B., Barlow, D. P., Quiñones, S., Sausg, J., & Pihlajaniemisyy, T. (2021) · Journal of Biological Chemistry · doi:10.1074/jbc · Cited by 3,409 · see citing works
Yang, F., Lim, G. P., Begum, A. N., Ubeda, O. J., Simmons, M. R., Ambegaokar, S. S., Chen, P. P., Kayed, R., Glabe, C. G., Frautschy, S. A., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m404751200 · Cited by 2,336 · see citing works
The toxic Aβ oligomer and Alzheimer's disease: an emperor in need of clothes
Benilova, I., Karran, E., & De Strooper, B. (2012) · Nature Neuroscience · doi:10.1038/nn.3028 · Cited by 1,962 · see citing works
Mucke, L., Masliah, E., Yu, G.-Q., Mallory, M., Rockenstein, E. M., Tatsuno, G., Hu, K., Kholodenko, D., Johnson-Wood, K., & McConlogue, L. (2000) · The Journal of Neuroscience · doi:10.1523/jneurosci.20-11-04050.2000 · Cited by 1,856 · see citing works
A mutation in APP protects against Alzheimer’s disease and age-related cognitive decline
Jonsson, T., Atwal, J. K., Steinberg, S., Snaedal, J., Jonsson, P. V., Bjornsson, S., Stefansson, H., Sulem, P., Gudbjartsson, D., Maloney, J., et al. (2012) · Nature · doi:10.1038/nature11283 · Cited by 1,738 · 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
Cellular prion protein mediates impairment of synaptic plasticity by amyloid-β oligomers
Laurén, J., Gimbel, D. A., Nygaard, H. B., Gilbert, J. W., & Strittmatter, S. M. (2009) · Nature · doi:10.1038/nature07761 · Cited by 1,560 · see citing works
Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism
Cohen, S. I. A., Linse, S. S., Luheshi, L. M., Hellstrand, E., White, D. A., Rajah, L., Otzen, D. E., Vendruscolo, M., Dobson, C. M., & Knowles, T. P. J. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1218402110 · Cited by 1,410 · see citing works
Craft, S. (2012) · Archives of Neurology · doi:10.1001/archneurol.2011.233 · Cited by 1,253 · see citing works
Lacor, P. N., Buniel, M. C., Furlow, P. W., Sanz Clemente, A., Velasco, P. T., Wood, M., Viola, K. L., & Klein, W. L. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.3501-06.2007 · Cited by 1,188 · see citing works
Self-citationAlzheimer’s disease is type 3 diabetes—Evidence reviewed
de la Monte, S. M., & Wands, J. R. (2008) · Journal of Diabetes Science and Technology · doi:10.1177/193229680800200619 · Cited by 1,158 · see citing works
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
Self-citationNeurotoxicity of Amyloid -Protein: Synaptic and Network Dysfunction
Mucke, L., & Selkoe, D. J. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006338 · Cited by 1,000 · see citing works
Targeting small Aβ oligomers: the solution to an Alzheimer's disease conundrum?
Klein, W. (2001) · Trends in Neurosciences · doi:10.1016/s0166-2236(00)01749-5 · Cited by 989 · see citing works
Self-citationSynaptic 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
Self-citationHaes, A. J., Chang, L., Klein, W. L., & Duyne, R. P. V. (2005) · Journal of the American Chemical Society · doi:10.1021/ja044087q · Cited by 866 · see citing works
Self-citationImmunization reverses memory deficits without reducing brain Aβ burden in Alzheimer's disease model
Dodart, J.-C., Bales, K. R., Gannon, K. S., Greene, S. J., DeMattos, R. B., Mathis, C., DeLong, C. A., Wu, S., Wu, X., Holtzman, D. M., et al. (2002) · Nature Neuroscience · doi:10.1038/nn842 · Cited by 858 · see citing works
Koffie, R. M., Meyer-Luehmann, M., Hashimoto, T., Adams, K. W., Mielke, M. L., Garcia-Alloza, M., Micheva, K. D., Smith, S. J., Kim, M. L., Lee, V. M., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0811698106 · Cited by 850 · see citing works
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
Self-citationBomfim, T. R., Forny‐Germano, L., Sathler, L. B., Brito‐Moreira, J., Houzel, J., Decker, H., Silverman, M. A., Kazi, H., Melo, H. M., McClean, P. L., et al. (2012) · Journal of Clinical Investigation · doi:10.1172/jci57256 · Cited by 830 · see citing works
Self-citationKayed, 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
Allanbutterfield, D., Castegna, A., Lauderback, C. M., & Drake, J. (2002) · Neurobiology of Aging · doi:10.1016/s0197-4580(01)00340-2 · Cited by 715 · see citing works
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
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 · see citing works
De Felice, F. G., Vieira, M. N. N., Bomfim, T. R., Decker, H., Velasco, P. T., Lambert, M. P., Viola, K. L., Zhao, W.-Q., Ferreira, S. T., & Klein, W. L. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0809158106 · Cited by 657 · see citing works
Self-citationSeeding of Normal Tau by Pathological Tau Conformers Drives Pathogenesis of Alzheimer-like Tangles
Guo, J. L., & Lee, V. M.-Y. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.209296 · Cited by 636 · see citing works
Siebner, H. R., Riemenschneider, M. J., Willoch, F., Minoshima, S., Schwaiger, M., Kurz, A., Drzezga, A. E., & Lautenschlager, N. T. (2003) · European Journal of Nuclear Medicine and Molecular Imaging · doi:10.1007/s00259-003-1194-1 · Cited by 603 · see citing works
Amyloid beta oligomers induce impairment of neuronal insulin receptors
Zhao, W., De Felice, F. G., Fernandez, S., Chen, H., Lambert, M. P., Quon, M. J., Krafft, G. A., & Klein, W. L. (2008) · The FASEB Journal · doi:10.1096/fj.06-7703com · Cited by 587 · see citing works
Self-citationUm, J. W., Kaufman, A. C., Kostylev, M., Heiss, J. K., Stagi, M., Takahashi, H., Kerrisk, M. E., Vortmeyer, A., Wisniewski, T., Koleske, A. J., et al. (2013) · Neuron · doi:10.1016/j.neuron.2013.06.036 · Cited by 572 · see citing works
Atomic View of a Toxic Amyloid Small Oligomer
Laganowsky, A. D., Liu, C., Sawaya, M. R., Whitelegge, J. P., Park, J., Zhao, M., Pensalfini, A., Soriaga, A. B., Landau, M., Teng, P. K., et al. (2012) · Science · doi:10.1126/science.1213151 · Cited by 564 · see citing works
Wang, H.-W., Pasternak, J. F., Kuo, H., Ristic, H., Lambert, M. P., Chromy, B., Viola, K. L., Klein, W. L., Stine, W. B., Krafft, G. A., et al. (2002) · Brain Research · doi:10.1016/s0006-8993(01)03058-x · Cited by 527 · see citing works
Self-citationSelf-Assembly of Aβ <sub>1</sub> <sub>-</sub> <sub>42</sub> into Globular Neurotoxins
Chromy, B. A., Nowak, R. J., Lambert, M. P., Viola, K. L., Chang, L., Velasco, P. T., Jones, B. W., Fernandez, S. J., Lacor, P. N., Horowitz, P., et al. (2003) · Biochemistry · doi:10.1021/bi030029q · Cited by 522 · see citing works
Self-citationAmyloid, hypometabolism, and cognition in Alzheimer disease: An [11C]PIB and [18F]FDG PET study
Edison, P., Archer, H. A., Hinz, R., Hammers, A., Pavese, N., Tai, Y. F., Hotton, G., Cutler, D., Fox, N., Kennedy, A., et al. (2007) · Neurology · doi:10.1212/01.wnl.0000244749.20056.d4 · Cited by 518 · see citing works
The Oligomerization of Amyloid β-Protein Begins Intracellularly in Cells Derived from Human Brain
Walsh, D. M., Tseng, B. P., Rydel, R. E., Podlisny, M. B., & Selkoe, D. J. (2000) · Biochemistry · doi:10.1021/bi001048s · Cited by 502 · see citing works
Resolving controversies on the path to Alzheimer's therapeutics
Selkoe, D. J. (2011) · Nature Medicine · doi:10.1038/nm.2460 · Cited by 494 · 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
Self-citationThe 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 · see citing works
Self-citationMainardi, M., Garbo, A. D., Caleo, M., Berardi, N., Sale, A., & Maffei, L. (2013) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00001 · Cited by 438 · see citing works
Alzheimer's disease-type neuronal tau hyperphosphorylation induced by Aβ oligomers
De Felice, F. G., Wu, D., Lambert, M. P., Fernandez, S. J., Velasco, P. T., Lacor, P. N., Bigio, E. H., Jerecic, J., Acton, P. J., Shughrue, P. J., et al. (2008) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2007.02.029 · Cited by 432 · see citing works
Self-citationPrion-like behaviour and tau-dependent cytotoxicity of pyroglutamylated amyloid-β
Nussbaum, J. M., Schilling, S., Cynis, H., Silva, A., Swanson, E., Wangsanut, T., Tayler, K., Wiltgen, B., Hatami, A., Rönicke, R., et al. (2012) · Nature · doi:10.1038/nature11060 · Cited by 427 · see citing works
Chadha, A. S., Sytnyk, V., Leshchyns’ka, I., & Schachner, M. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200409127 · Cited by 419 · see citing works
Molecular Mechanisms of Amyloid Oligomers Toxicity
Kayed, R., & Lasagna‐Reeves, C. A. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-129001 · Cited by 417 · see citing works
Lourenco, M. V., Clarke, J. R., Frozza, R. L., Bomfim, T. R., Forny‐Germano, L., Batista, A. F., Sathler, L. B., Brito‐Moreira, J., Amaral, O. B., Silva, C. A., et al. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.11.002 · Cited by 415 · see citing works
Self-citationCurcumin: an orally bioavailable blocker of TNF and other pro‐inflammatory biomarkers
Aggarwal, B. B., Gupta, S. C., & Sung, B. (2013) · British Journal of Pharmacology · doi:10.1111/bph.12131 · Cited by 401 · see citing works
Parkinson's Disease and Alpha Synuclein: Is Parkinson's Disease a Prion‐Like Disorder?
Olanow, C. W., & Brundin, P. (2013) · Movement Disorders · doi:10.1002/mds.25373 · Cited by 392 · see citing works
Temporal Profile of Amyloid-β (Aβ) Oligomerization in an in Vivo Model of Alzheimer Disease
Oddo, S., Caccamo, A., Tran, L., Lambert, M. P., Glabe, C. G., Klein, W. L., & LaFerla, F. M. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m507892200 · Cited by 379 · see citing works
Self-citationPolymorphism in the intermediates and products of amyloid assembly
Kodali, R. B., & Wetzel, R. B. (2007) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2007.01.007 · Cited by 376 · see citing works
Intraneuronal β-amyloid accumulation and synapse pathology in Alzheimer’s disease
Gouras, G. K., Tampellini, D., Takahashi, R. H., & Capetillo-Zarate, E. (2010) · Acta Neuropathologica · doi:10.1007/s00401-010-0679-9 · Cited by 372 · see citing works
McClean, P. L., & Hölscher, C. (2013) · Neuropharmacology · doi:10.1016/j.neuropharm.2013.08.005 · Cited by 359 · 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
Self-citationHow does brain insulin resistance develop in Alzheimer's disease?
De Felice, F. G., Lourenco, M. V., & Ferreira, S. T. (2014) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2013.12.004 · Cited by 337 · see citing works
Adolfsson, O., Pihlgren, M., Toni, N., Varisco, Y., Buccarello, A. L., Antoniello, K., Lohmann, S., Piorkowska, K., Gafner, V., Atwal, J. K., et al. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.4742-11.2012 · Cited by 317 · 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
Self-citationType 3 diabetes is sporadic Alzheimer׳s disease: Mini-review
de la Monte, S. M. (2014) · European Neuropsychopharmacology · doi:10.1016/j.euroneuro.2014.06.008 · Cited by 312 · see citing works
Synaptic changes in Alzheimer’s disease and its models
Pozueta, J., Lefort, R., & Shelanski, M. L. (2012) · Neuroscience · doi:10.1016/j.neuroscience.2012.05.050 · Cited by 305 · see citing works
Amyloid‐beta oligomerization in Alzheimer dementia versus high‐pathology controls
Esparza, T. J., Zhao, H., Cirrito, J. R., Cairns, N. J., Bateman, R. J., Holtzman, D. M., & Brody, D. L. (2012) · Annals of Neurology · doi:10.1002/ana.23748 · Cited by 304 · see citing works
Alzheimer's disease: synapses gone cold
Koffie, R. M., Hyman, B. T., & Spires‐Jones, T. L. (2011) · Molecular Neurodegeneration · doi:10.1186/1750-1326-6-63 · Cited by 302 · see citing works
Izzo, N. J., Xu, J., Zeng, C., Kirk, M. J., Mozzoni, K., Silky, C., Rehak, C., Yurko, R., Look, G. C., Rishton, G. M., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0111899 · Cited by 294 · see citing works
Exercise counteracts declining hippocampal function in aging and Alzheimer's disease
Intlekofer, K. A., & Cotman, C. W. (2012) · Neurobiology of Disease · doi:10.1016/j.nbd.2012.06.011 · Cited by 286 · 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
Tucker, S., Möller, C., Tegerstedt, K., Lord, A., Laudon, H., Sjödahl, J., Söderberg, L., Spens, E., Sahlin, C., Waara, E. R., et al. (2015) · Journal of Alzheimer’s Disease · doi:10.3233/jad-140741 · Cited by 272 · cited 1× · see citing works
“An antibody described as targeting protofibrillar AβOs, promoted by the Arctic mutation [74], reduced AβOs in the brains and CSF of the mouse model with no impact on Aβ monomers [169].”
BackgroundLost after translation: missorting of Tau protein and consequences for Alzheimer disease
Zempel, H., & Mandelkow�, E. (2014) · Trends in Neurosciences · doi:10.1016/j.tins.2014.08.004 · Cited by 272 · see citing works
McAlpine, F. E., Lee, J., Harms, A. S., Ruhn, K. A., Blurton-Jones, M. M., Hong, J. J., Das, P., Golde, T. E., LaFerla, F. M., Oddo, S., et al. (2009) · Neurobiology of Disease · doi:10.1016/j.nbd.2009.01.006 · Cited by 269 · see citing works
The Role of Stable α-Synuclein Oligomers in the Molecular Events Underlying Amyloid Formation
Lorenzen, N., Nielsen, S. B., Buell, A. K., Kaspersen, J. D., Arosio, P., Vad, B. S., Pasławski, W., Christiansen, G., Valnickova-Hansen, Z., Andreasen, M., et al. (2014) · Journal of the American Chemical Society · doi:10.1021/ja411577t · Cited by 255 · see citing works
Lee, E. B., Leng, L. Z., Zhang, B., Kwong, L. K., Trojanowski, J. Q., Abel, T. G., & Lee, V. M. ‐. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m511018200 · Cited by 252 · see citing works
Spreading of Neurodegenerative Pathology via Neuron-to-Neuron Transmission of -Amyloid
Nath, S., Agholme, L., Kurudenkandy, F. R., Granseth, B., Marcusson, J., & Hallbeck, M. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.0615-12.2012 · Cited by 244 · see citing works
Conformational Differences between Two Amyloid β Oligomers of Similar Size and Dissimilar Toxicity
Ladiwala, A. R. A., Litt, J., Kane, R. S., Aucoin, D., Smith, S. O., Ranjan, S., Davis, J., Nostrand, W. E. V., & Tessier, P. M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.329763 · Cited by 223 · see citing works
Janelsins, M. C., Mastrangelo, M. A., Park, K. M., Sudol, K. L., Narrow, W. C., Oddo, S., LaFerla, F. M., Callahan, L. M., Federoff, H. J., & Bowers, W. J. (2008) · The American Journal of Pathology · doi:10.2353/ajpath.2008.080528 · Cited by 220 · see citing works
Peng, S., Garzon, D. J., Marchese, M., Klein, W. L., Ginsberg, S. D., Francis, B. M., Mount, H. T. J., Mufson, E. J., Salehi, A., & Fahnestock, M. L. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.4736-08.2009 · Cited by 216 · see citing works
Self-citationCross‐seeding effects of amyloid β‐protein and α‐synuclein
Ono, K., Takahashi, R., Ikeda, T., & Yamada, M. (2012) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2012.07847.x · Cited by 213 · see citing works
Selective neuronal degeneration induced by soluble oligomeric amyloid beta‐protein
Kim, H., Chae, S., Lee, D., Chromy, B. A., Lee, S. C., Park, Y., Klein, W. L., Krafft, G. A., & Hong, S. (2002) · The FASEB Journal · doi:10.1096/fj.01-0987fje · Cited by 210 · see citing works
Self-citationThe secreted Wnt antagonist Dickkopf-1 is required for amyloid β-mediated synaptic loss
Purro, S. A., Dickins, E. M., & Salinas, P. C. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.4562-11.2012 · Cited by 195 · see citing works
Siemers, E., Friedrich, S. W., Dean, R. A., Gonzales, C., Farlow, M. R., Paul, S. M., & Demattos, R. B. (2010) · Clinical Neuropharmacology · doi:10.1097/wnf.0b013e3181cb577a · Cited by 192 · see citing works
Towards non-invasive diagnostic imaging of early-stage Alzheimer's disease
Viola, K. L., Sbarboro, J., Sureka, R., De, M., Bicca, M. A., Wang, J., Vasavada, S. R., Satpathy, S., Wu, S., Joshi, H. M., et al. (2014) · Nature Nanotechnology · doi:10.1038/nnano.2014.254 · Cited by 192 · see citing works
Self-citationGoure, W. F., Krafft, G. A., Jerecic, J., & Hefti, F. (2014) · Alzheimer's Research & Therapy · doi:10.1186/alzrt272 · Cited by 190 · see citing works
Out-of-register β-sheets suggest a pathway to toxic amyloid aggregates
Liu, C., Zhao, M., Jiang, L., Cheng, P.-N., Park, J.-Y., Sawaya, M. R., Pensalfini, A., Gou, D., Berk, A. J., Glabe, C. G., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1218792109 · Cited by 186 · see citing works
Figueiredo, C. P., Clarke, J. R., Ledo, J. H., Ribeiro, F. C., Costa, C., Melo, H. M., Mota-Sales, A. P., Saraiva, L. M., Klein, W. L., Sebollela, A. S., et al. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.0482-13.2013 · Cited by 181 · see citing works
Self-citationIzzo, N. J., Staniszewski, A., To, L., Fa, M., Teich, A. F., Saeed, F., Wostein, H., Walko, T., Vaswani, A., Wardius, M., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0111898 · Cited by 180 · see citing works
Li, S., Jin, M., Zhang, D., Yang, T., Koeglsperger, T., Fu, H., & Selkoe, D. J. (2013) · Neuron · doi:10.1016/j.neuron.2012.12.040 · Cited by 177 · see citing works
Chin, J., Palop, J. J., Yu, G.-Q., Kojima, N., Masliah, E., & Mucke, L. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.0277-04.2004 · Cited by 161 · see citing works
Lannfelt, L., Möller, C., Basun, H., Osswald, G., Sehlin, D., Satlin, A., Logovinsky, V., & Gellerfors, P. (2014) · Alzheimer s Research & Therapy · doi:10.1186/alzrt246 · Cited by 152 · see citing works
Jeong, J. S., Ansaloni, A., Mezzenga, R., Lashuel, H. A., & Dietler, G. (2013) · Journal of Molecular Biology · doi:10.1016/j.jmb.2013.02.005 · Cited by 152 · see citing works
Domert, J., Rao, S. B., Agholme, L., Brorsson, A., Marcusson, J. O., Hallbeck, M., & Nath, S. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2013.12.019 · Cited by 151 · see citing works
Moon, M., Kim, H. G., Choi, J. G., Oh, H., Lee, P. K. J., Ha, S. K., Kim, S. Y., Park, Y., Huh, Y., & Oh, M. S. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.04.121 · Cited by 150 · see citing works
Intracellular Aβ-oligomers and early inflammation in a model of Alzheimer's disease
Ferretti, M. T., Bruno, M. A., Ducatenzeiler, A., Klein, W. L., & Cuello, A. C. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.01.007 · Cited by 146 · see citing works
Self-citationEvaluating Amyloid-β Oligomers in Cerebrospinal Fluid as a Biomarker for Alzheimer’s Disease
Hölttä, M., Hansson, O., Andréasson, U., Hertze, J., Minthon, L., Nägga, K., Andreasen, N., Zetterberg, H., & Blennow, K. (2013) · PLoS ONE · doi:10.1371/journal.pone.0066381 · Cited by 142 · see citing works
Klein, W. L. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-129039 · Cited by 141 · see citing works
Self-citationGarai, K., & Frieden, C. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1222478110 · Cited by 138 · see citing works
Amyloid-β Annular Protofibrils Evade Fibrillar Fate in Alzheimer Disease Brain
Lasagna‐Reeves, C. A., Glabe, C. G., & Kayed, R. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.236257 · Cited by 136 · see citing works
Rosenblum, W. I. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2013.10.085 · Cited by 135 · see citing works
Pitt, J., Roth, W., Lacor, P., Smith, A. B., Blankenship, M., Velasco, P., De Felice, F., Breslin, P., & Klein, W. L. (2009) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2009.07.018 · Cited by 134 · see citing works
Self-citationMechanisms for the Insertion of Toxic, Fibril-like β-Amyloid Oligomers into the Membrane
Jang, H., Connelly, L. S., Arce, F. T., Ramachandran, S., Kagan, B. L., Lal, R., & Nussinov, R. (2012) · Journal of Chemical Theory and Computation · doi:10.1021/ct300916f · Cited by 133 · see citing works
Frackowiak, J., Żółtowska, A., & Wı́sniewski, H. M. (1994) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/00005072-199411000-00011 · Cited by 128 · see citing works
Kovács, G. G., Breydo, L., Green, R. J., Kis, V., Puska, G., Lőrincz, P., Perju‐Dumbrava, L., Giera, R., Pirker, W., Lutz, M. I., et al. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.05.020 · Cited by 128 · see citing works
Donepezil inhibits the amyloid-beta oligomer-induced microglial activation in vitro and in vivo
Kim, H. G., Moon, M., Choi, J. G., Park, G., Kim, A., Hur, J., Lee, K., & Oh, M. S. (2013) · NeuroToxicology · doi:10.1016/j.neuro.2013.10.004 · Cited by 127 · see citing works
Alzheimer’s β-peptide oligomer formation at physiologic concentrations
LeVine, H. (2004) · Analytical Biochemistry · doi:10.1016/j.ab.2004.08.014 · Cited by 123 · see citing works
Heraldo, F. H., Arantes, C., Santos, T. G., Machado, C. F., Roffé, M., Haji, G. N., Lee, K. S., Magalhães, A. C., Caetano, F. A., Mancini, G. L., et al. (2010) · The FASEB Journal · doi:10.1096/fj.10-161653 · Cited by 123 · see citing works
The case for soluble Aβ oligomers as a drug target in Alzheimer's disease
Hefti, F. F., Goure, W. F., Jerecı̀ć, 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 119 · see citing works
Purification and Characterization of Brain Clusterin
Oda, T., Pasinetti, G. M., Osterburg, H. H., Anderson, C., Johnson, S. A., & Finch, C. E. (1994) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1994.2580 · Cited by 118 · see citing works
Amyloid-β induced signaling by cellular prion protein and Fyn kinase in Alzheimer disease
Um, J. W., & Strittmatter, S. M. (2013) · Prion · doi:10.4161/pri.22212 · Cited by 113 · see citing works
Architecture of the Alzheimer?s A�P Ion Channel Pore
Arispe, N. J. (2004) · The Journal of Membrane Biology · doi:10.1007/s00232-003-0638-7 · Cited by 111 · see citing works
Drolle, E., Hane, F. T., Lee, B. Y., & Leonenko, Z. (2014) · Drug Metabolism Reviews · doi:10.3109/03602532.2014.882354 · Cited by 109 · see citing works
Tay, W. M., Huang, D., Rosenberry, T. L., & Paravastu, A. K. (2013) · Journal of Molecular Biology · doi:10.1016/j.jmb.2013.04.003 · Cited by 109 · see citing works
Richman, M., Wilk, S., Chemerovski‐Glikman, M., Wärmländer, S. K. T. S., Wahlström, A., Gräslund, A., & Rahimipour, S. (2013) · Journal of the American Chemical Society · doi:10.1021/ja310064v · Cited by 108 · see citing works
Specific Uptake of an Amyloid-β Protofibril-Binding Antibody-Tracer in AβPP Transgenic Mouse Brain
Magnusson, K., Sehlin, D., Syvänen, S., Svedberg, M. M., Philipson, O., Söderberg, L., Tegerstedt, K., Holmquist, M., Gellerfors, P., Максимилианович, Т. В., et al. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-130029 · Cited by 105 · see citing works
Tau-Based Therapeutic Approaches for Alzheimer's Disease - A Mini-Review
Boutajangout, A., & Wısnıewskı, T. (2014) · Gerontology · doi:10.1159/000358875 · Cited by 105 · see citing works
Rare Individual Amyloid-β Oligomers Act on Astrocytes to Initiate Neuronal Damage
Narayan, P. S., Holmström, K. M., Kim, D.-H., Whitcomb, D. J., Wilson, M. R., George‐Hyslop, P. S., Wood, N. W., Dobson, C. M., Cho, K., Abramov, A. Y., et al. (2014) · Biochemistry · doi:10.1021/bi401606f · Cited by 104 · see citing works
Impact of Apolipoprotein E on Alzheimer’s Disease
Hauser, P. S., & Ryan, R. O. (2013) · Current Alzheimer Research · doi:10.2174/15672050113109990156 · Cited by 101 · see citing works
Alzheimer’s disease Aβ assemblies mediating rapid disruption of synaptic plasticity and memory
Klyubin, I. V., Cullen, W. K., Hu, N., & Rowan, M. J. (2012) · Molecular Brain · doi:10.1186/1756-6606-5-25 · Cited by 101 · see citing works
Younan, N. D., Sarell, C. J., Davies, P., Brown, D. R., & Viles, J. H. (2013) · The FASEB Journal · doi:10.1096/fj.12-222588 · Cited by 100 · see citing works
Immunotherapy for Alzheimer's disease
Wısnıewskı, T., & Goñi, F. (2014) · Biochemical Pharmacology · doi:10.1016/j.bcp.2013.12.020 · Cited by 99 · see citing works
Guillot‐Sestier, M., Sunyach, C., Ferreira, S. T., Marzolo, M., Bauer, C., Thevenet, A., & Checler, F. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.323626 · Cited by 95 · see citing works
Sarkar, B., Mithu, V. S., Chandra, B., Mandal, A., Chandrakesan, M., Bhowmik, D., Madhu, P. K., & Maiti, S. (2014) · Angewandte Chemie International Edition · doi:10.1002/anie.201402636 · Cited by 93 · see citing works
Gabbita, S. P., Srivastava, M. K., Eslami, P., Johnson, M. F., Kobritz, N., Tweedie, D., Greig, N. H., Zemlan, F. P., Sharma, S. P., & Harris‐White, M. E. (2012) · Journal of Neuroinflammation · doi:10.1186/1742-2094-9-99 · Cited by 93 · see citing works
Pearson-Leary, J., & McNay, E. C. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-112192 · Cited by 91 · see citing works
Scala, C. D., Troadec, J., Lelièvre, C., Garmy, N., Fantini, J., & Chahinian, H. (2013) · Journal of Neurochemistry · doi:10.1111/jnc.12390 · Cited by 91 · see citing works
Kerchner, G. A., & Boxer, A. L. (2010) · Expert Opinion on Biological Therapy · doi:10.1517/14712598.2010.493872 · Cited by 90 · see citing works
Kuszczyk, M. A., Sanchez, S., Pankiewicz, J., Kim, J., Duszczyk, M., Guridi, M., Asuni, A. A., Sullivan, P. M., Holtzman, D. M., & Sadowski, M. J. (2013) · The American Journal of Pathology · doi:10.1016/j.ajpath.2013.01.034 · Cited by 89 · cited 1× · see citing works
“The peptide was also protective in vivo [90].”
BackgroundPrangkio, P., Yusko, E. C., Sept, D., Yang, J., & Mayer, M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0047261 · Cited by 86 · see citing works
Cognitive and Functional Decline and Their Relationship in Patients with Mild Alzheimer's Dementia
Liu‐Seifert, H., Siemers, E., Sundell, K. L., Price, K., Han, B., Selzler, K. J., Aisen, P. S. S., Cummings, J. L., Raskin, J., & Mohs, R. C. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-140792 · Cited by 82 · see citing works
Narayan, P. S., Ganzinger, K. A., McColl, J. T., Weimann, L., Meehan, S., Qamar, S., Carver, J. A., Wilson, M. R., George‐Hyslop, P. S., Dobson, C. M., et al. (2013) · Journal of the American Chemical Society · doi:10.1021/ja3103567 · Cited by 82 · see citing works
C-Terminal Turn Stability Determines Assembly Differences between Aβ40 and Aβ42
Roychaudhuri, R., Yang, M., Deshpande, A. M., Cole, G. M., Frautschy, S. A., Lomakin, A., Benedek, G. B., & Teplow, D. B. (2012) · Journal of Molecular Biology · doi:10.1016/j.jmb.2012.11.006 · Cited by 82 · see citing works
Chang, L., Bakhos, L., Wang, Z., Venton, D. L., & Klein, W. L. (2003) · Journal of Molecular Neuroscience · doi:10.1385/jmn:20:3:305 · Cited by 79 · see citing works
Self-citationUmeda, T., Tomiyama, T., Kitajima, E., Idomoto, T., Nomura, S., Lambert, M. P., Klein, W. L., & Mori, H. (2012) · Life Sciences · doi:10.1016/j.lfs.2011.12.022 · Cited by 78 · see citing works
Self-citationAmyloid-β and Tau Pathology of Alzheimer's Disease Induced by Diabetes in a Rabbit Animal Model
Bitel, C. L., Kasinathan, C., Kaswala, R. H., Klein, W. L., & Frederikse, P. H. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-120571 · Cited by 77 · see citing works
Self-citationSoejima, N., Ohyagi, Y., Nakamura, N., Himeno, E., Iinuma, K., Sakae, N., Yamasaki, R., Tabira, T., Murakami, K., Irie, K., et al. (2013) · Current Alzheimer Research · doi:10.2174/156720513804871372 · Cited by 76 · see citing works
Rasool, S., Martínez‐Coria, H., Wu, J., LaFerla, F. M., & Glabe, C. G. (2013) · Journal of Neurochemistry · doi:10.1111/jnc.12305 · Cited by 74 · see citing works
Cattepoel, S., Hanenberg, M., Kulic, L., & Nitsch, R. M. (2011) · PLoS ONE · doi:10.1371/journal.pone.0018296 · Cited by 73 · see citing works
Structural Insights into Aβ42 Oligomers Using Site-directed Spin Labeling
Gu, L., Liu, C., & Guo, Z. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.457739 · Cited by 73 · see citing works
Prà, I. D., Chiarini, A., Gui, L., Chakravarthy, B., Pacchiana, R., Gardenal, E., Whitfield, J. F., & Armato, U. (2014) · The Neuroscientist · doi:10.1177/1073858414529828 · Cited by 73 · see citing works
Takeda, S., Hashimoto, T., Roe, A. D., Hori, Y., Spires‐Jones, T. L., & Hyman, B. T. (2013) · The FASEB Journal · doi:10.1096/fj.13-229666 · Cited by 72 · see citing works
Perispinal etanercept: Potential as an Alzheimer therapeutic
Griffin, W. S. T. (2008) · Journal of Neuroinflammation · doi:10.1186/1742-2094-5-3 · Cited by 66 · see citing works
Immunotherapy for Alzheimer’s disease
Wilkinson, D. (2005) · CRC Press eBooks · doi:10.1201/b13935-7 · Cited by 65 · see citing works
Amyloid: Little proteins, big clues
Schnabel, J. (2011) · Nature · doi:10.1038/475s12a · Cited by 62 · see citing works
Wang, X.-P., Zhang, J.-H., Wang, Y.-J., Feng, Y. N., Zhang, X., Sun, X.-X., Li, J.-L., Du, X.-T., Lambert, M. P., Yang, S.-G., et al. (2009) · FEBS Letters · doi:10.1016/j.febslet.2008.12.064 · Cited by 61 · see citing works
Self-citationHandoko, M., Grant, M. K. O., Kuskowski, M. A., Zahs, K. R., Wallin, A., Blennow, K., & Ashe, K. H. (2013) · JAMA Neurology · doi:10.1001/jamaneurol.2013.48 · Cited by 61 · see citing works
Sörgjerd, K. M., Zako, T., Sakono, M., Stirling, P. C., Leroux, M. R., Saito, T., Nilsson, P., Sekimoto, M., Saido, T. C., & Maeda, M. (2013) · Biochemistry · doi:10.1021/bi301705c · Cited by 60 · see citing works
Different effects of Alzheimer's peptide Aβ(1–40) oligomers and fibrils on supported lipid membranes
Canale, C., Seghezza, S., Vilasi, S., Carrotta, R., Bulone, D., Diaspro, A., Biagio, P. L. S., & Dante, S. (2013) · Biophysical Chemistry · doi:10.1016/j.bpc.2013.07.010 · Cited by 60 · see citing works
Takahashi, R. H., Capetillo‐Zarate, E., Lin, M. T. S., Milner, T. A., & Gouras, G. K. (2013) · PLoS ONE · doi:10.1371/journal.pone.0051965 · Cited by 60 · see citing works
Membrane-Mediated Neuroprotection by Curcumin from Amyloid-β-Peptide-Induced Toxicity
Thapa, A., Vernon, B. C., la Peña, K. D., Soliz, G., Moreno, H. A., López, G. P., & Chi, E. Y. (2013) · Langmuir · doi:10.1021/la4020459 · Cited by 60 · see citing works
Evangelisti, E., Wright, D., Zampagni, M., Cascella, R., Fiorillo, C., Bagnoli, S., Relini, A., Nichino, D., Scartabelli, T., Nacmias, B., et al. (2013) · Current Alzheimer Research · doi:10.2174/1567205011310020004 · Cited by 59 · see citing works
Xiao, C., Davis, F., Chauhan, B. C., Viola, K. L., Lacor, P. N., Velasco, P. T., Klein, W. L., & Chauhan, N. B. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-122419 · Cited by 59 · see citing works
Self-citationGiménez‐Llort, L., Rivera-Hernández, G., Marin‐Argany, M., Sánchez‐Quesada, J. L., & Villegas, S. (2013) · mAbs · doi:10.4161/mabs.25424 · Cited by 57 · see citing works
Poor Physical Performance and Dementia in the Oldest Old
Bullain, S., Corrada, M. M., Shah, B. A., Mozaffar, F. H., Panzenboeck, M. M., & Kawas, C. H. (2012) · JAMA Neurology · doi:10.1001/jamaneurol.2013.583 · Cited by 56 · see citing works
Sarkar, B., Das, A. K., & Maiti, S. (2013) · Frontiers in Physiology · doi:10.3389/fphys.2013.00084 · Cited by 56 · see citing works
Velasco, P. T., Heffern, M. C., Sebollela, A. S., Popova, I. A., Lacor, P. N., Lee, K. B., Sun, X., Tiano, B. N., Viola, K. L., Eckermann, A. L., et al. (2012) · ACS Chemical Neuroscience · doi:10.1021/cn300122k · Cited by 55 · see citing works
Self-citationPrefibrillar Tau Oligomers in Mild Cognitive Impairment and Alzheimer's Disease
Mufson, E. J., Ward, S., & Binder, L. I. (2013) · Neurodegenerative Diseases · doi:10.1159/000353687 · Cited by 54 · see citing works
β-Amyloid oligomers in aging and Alzheimer’s disease
Zahs, K. R., & Ashe, K. H. (2013) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2013.00028 · Cited by 53 · see citing works
Murakami, K. (2014) · Bioscience Biotechnology and Biochemistry · doi:10.1080/09168451.2014.940275 · Cited by 52 · see citing works
Cellular Prion Protein as a Therapeutic Target in Alzheimer's Disease
Laurén, J. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-130950 · Cited by 51 · see citing works
Alzheimer's disease: which type of amyloid-preventing drug agents to employ?
Jang, H., Connelly, L. S., Arce, F. T., Ramachandran, S., Lal, R., Kagan, B. L., & Nussinov, R. (2013) · Physical Chemistry Chemical Physics · doi:10.1039/c3cp00017f · Cited by 50 · see citing works
Structure–Activity Relationships of Organofluorine Inhibitors of β‐Amyloid Self‐Assembly
Török, B., Sood, A., Bag, S., Kulkarni, A., Borkin, D., Lawler, E., Dasgupta, S., Landge, S. M., Abid, M. A., Zhou, W., et al. (2012) · ChemMedChem · doi:10.1002/cmdc.201100569 · Cited by 48 · see citing works
Kalimo, H., Lalowski, M. M., Bogdanović, N., Philipson, O., Bird, T. D., Nochlin, D., Schellenberg, G. D., Brundin, R., Olofsson, T., Soliymani, R., et al. (2013) · Acta Neuropathologica Communications · doi:10.1186/2051-5960-1-60 · Cited by 48 · see citing works
Peters, C., Fernández-Pérez, E. J., Burgos, C. F., Flores-Espinoza, M. P., Castillo, C., Urrutia, J. C., Streltsov, V. A., Opazo, C., & Aguayo, L. G. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2013.06.001 · Cited by 46 · see citing works
Amyloid-β Protein Modulates Insulin Signaling in Presynaptic Terminals
Heras-Sandoval, D., Ferrera, P., & Arias, C. (2012) · Neurochemical Research · doi:10.1007/s11064-012-0800-7 · Cited by 45 · see citing works
Wasilewska‐Sampaio, A. P., Barbosa, A. C. A. P., Gomes, F. C. A., & Ferreira, S. T. (2007) · Current Alzheimer Research · doi:10.2174/156720507781077287 · Cited by 43 · see citing works
Specific Domains of Aβ Facilitate Aggregation on and Association with Lipid Bilayers
Yates, E. A., Owens, S. L., Lynch, M. F., Cucco, E. M., Umbaugh, C. S., & Legleiter, J. (2013) · Journal of Molecular Biology · doi:10.1016/j.jmb.2013.03.022 · Cited by 41 · see citing works
Kumar, A., Paslay, L. C., Lyons, D. F., Morgan, S. E., Correia, J. J., & Rangachari, V. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.355156 · Cited by 40 · see citing works
Maesako, M., Uemura, K., Iwata, A., Kubota, M., Watanabe, K., Uemura, M. T., Noda, Y., Asada‐Utsugi, M., Kihara, T., Takahashi, R., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0072796 · Cited by 39 · see citing works
Sitkiewicz, E., Kłoniecki, M., Poznański, J. T., Bal, W., & Dadlez, M. (2014) · Journal of Molecular Biology · doi:10.1016/j.jmb.2014.05.015 · Cited by 38 · see citing works
Immunotherapy alleviates amyloid-associated synaptic pathology in an Alzheimer’s disease mouse model
Dorostkar, M. M., Burgold, S., Filser, S., Barghorn, S., Schmidt, B., Anumala, U. R., Hillen, H., Klein, C., & Herms, J. W. (2014) · Brain · doi:10.1093/brain/awu280 · Cited by 38 · see citing works
Plasma Membrane Injury Depends on Bilayer Lipid Composition in Alzheimer's Disease
Evangelisti, E., Zampagni, M., Cascella, R., Becatti, M., Fiorillo, C., Caselli, A., Bagnoli, S., Nacmias, B., & Cecchi, C. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-131406 · Cited by 37 · see citing works
Xu, S., Guilan, L., Bao, X., Wu, J., Li, S., Zheng, B., Anwyl, R., & Wang, Q. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-130680 · Cited by 35 · see citing works
Wilcox, K. C., Marunde, M. R., Das, A., Velasco, P. T., Kuhns, B. D., Marty, M. T., Haoming, J., Luan, C.-H., Sligar, S. G., & Klein, W. L. (2015) · PLoS ONE · doi:10.1371/journal.pone.0125263 · Cited by 34 · see citing works
Self-citationZhang, L., Yagnik, G. B., Peng, Y., Wang, J., Xu, H. H., Hao, Y., Liu, Y., & Zhou, F. (2012) · Analytical Biochemistry · doi:10.1016/j.ab.2012.11.025 · Cited by 34 · see citing works
Izuo, N., Kume, T., Sato, M., Murakami, K., Irie, K., Izumi, Y., & Akaike, A. (2012) · ACS Chemical Neuroscience · doi:10.1021/cn300033k · Cited by 34 · see citing works
Tsigelny, I. F., Sharikov, Y., Kouznetsova, V. L., Greenberg, J. P., Wrasidlo, W., Gonzalez, T., Desplats, P., Michael, S. E., Trejo, M., Overk, C., et al. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-131589 · Cited by 33 · see citing works
Takamura, A., Sato, Y., Watabe, D., Okamoto, Y., Nakata, T., Kawarabayashi, T., Oddo, S., LaFerla, F. M., Shoji, M., & Matsubara, E. (2012) · Life Sciences · doi:10.1016/j.lfs.2012.04.038 · Cited by 33 · see citing works
Wilhelmus, M. M. M., de Jager, M., Bakker, E. N. T. P., & Drukarch, B. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-132492 · Cited by 32 · see citing works
Intracellular Localization of Amyloid-β Peptide in SH-SY5Y Neuroblastoma Cells
Zheng, L. P., Calvo‐Garrido, J., Hallbeck, M., Hultenby, K. R., Marcusson, J. O., Cedazo-Mı́nguez, Á., & Terman, A. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-122455 · Cited by 31 · see citing works
Metals, Membranes, and Amyloid-β Oligomers: Key Pieces in the Alzheimer's Disease Puzzle?
Watt, A. D., Villemagne, V. L., & Barnham, K. J. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-129017 · Cited by 31 · see citing works
The Off-rate of Monomers Dissociating from Amyloid-β Protofibrils
Grüning, C. S. R., Klinker, S., Wolff, M., Schneider, M., Toksöz, K., Klein, A. N., Nagel‐Steger, L., Willbold, D., & Hoyer, W. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.513432 · Cited by 31 · see citing works
Resende, R., Marques, S., Ferreiro, E. B., Simões, I., Oliveira, C. R., & Pereira, C. (2013) · Neurochemical Research · doi:10.1007/s11064-013-0982-7 · Cited by 31 · see citing works
Johnson, R. D., Steel, D. G., & Gafni, A. (2014) · Protein Science · doi:10.1002/pro.2479 · Cited by 29 · see citing works
Durán-González, J., Michi, E. D., Elorza, B., Perez-Cordova, M. G., Otalora, L. F. P., Touhami, A., Paulson, P. E., Perry, G. L., Murray, I. V. J., & Colom, L. V. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2013.02.005 · Cited by 28 · see citing works
Zhao, M., Wang, S., Wang, Y., Zhang, R., Li, Y., Su, Y.-J., Zhou, W.-W., Yu, X., & Liu, R. (2014) · Current Alzheimer Research · doi:10.2174/15672050113106660176 · Cited by 28 · see citing works
Roychaudhuri, R., Lomakin, A., Bernstein, S. L., Zheng, X.-Y., Condron, M., Benedek, G., Bowers, M., & Teplow, D. (2014) · Journal of Molecular Biology · doi:10.1016/j.jmb.2014.04.004 · Cited by 27 · see citing works
Plasma Amyloid-β Oligomers and Soluble Tumor Necrosis Factor Receptors as Potential Biomarkers of AD
Zhang, J., Mao, P., & Jia, J. (2014) · Current Alzheimer Research · doi:10.2174/1567205011666140317103222 · Cited by 27 · see citing works
Lee, M., Guo, J., Schwab, C., McGeer, E. G., & McGeer, P. L. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.12.005 · Cited by 27 · see citing works
Immunogenic properties of amyloid beta oligomers
Dalgediene, I., Lasickiene, R., Budvytyte, R., Valincius, G., Morkuniene, R., Borutaite, V., & Zvirbliene, A. (2013) · Journal of Biomedical Science · doi:10.1186/1423-0127-20-10 · Cited by 22 · see citing works
Antibodies bound to Aβ oligomers potentiate the neurotoxicity of Aβ by activating microglia
Morkūnienė, R., Žvirblienė, A., Dalgėdienė, I., Čižas, P., Jankevičiūtė, S., Baliūtytė, G., Jokubka, R., Jankunec, M., Valinčius, G., & Borutaitė, V. (2013) · Journal of Neurochemistry · doi:10.1111/jnc.12332 · Cited by 21 · see citing works
Han, X., Ma, Y., Liu, X., Wang, L., Qi, S., Zhang, Q., & Du, Y. (2012) · Journal of Neural Transmission · doi:10.1007/s00702-012-0803-1 · Cited by 20 · see citing works
Sebollela, A., Freitas-Corrêa, L., de Oliveira, F. F., Mendes, C. T., Wasilewska‐Sampaio, A. P., Camacho-Pereira, J., Galina, A., Brentani, H., Passetti, F., Felice, F. G. D., et al. (2009) · Neurotoxicity Research · doi:10.1007/s12640-009-9133-y · Cited by 20 · see citing works
Bartl, J., Meyer, A. H., Brendler, S., Riederer, P., & Grünblatt, E. (2012) · Journal of Neural Transmission · doi:10.1007/s00702-012-0852-5 · Cited by 19 · see citing works
Anti-Amyloid-β-Mediated Positron Emission Tomography Imaging in Alzheimer's Disease Mouse Brains
McLean, D., Cooke, M. J., Wang, Y., Green, D., Fraser, P. E., George‐Hyslop, P. S., & Shoichet, M. S. (2012) · PLoS ONE · doi:10.1371/journal.pone.0051958 · Cited by 14 · see citing works
Lee, S.-H., Kim, Y. S., Kim, H. Y., Kim, Y. H., Kim, M. S., Kong, J. Y., Lee, M.-H., Kim, D. J., & Ahn, Y. (2014) · PLoS ONE · doi:10.1371/journal.pone.0095733 · Cited by 13 · see citing works
Matsubara, E., Takamura, A., Okamoto, Y., Oono, H., Nakata, T., Wakasaya, Y., Kawarabayashi, T., & Shoji, M. (2013) · BioMed Research International · doi:10.1155/2013/984041 · Cited by 12 · see citing works
In Vivo and Ex Vivo Imaging of Amyloid-β Cascade Aggregates with a Pronucleon™ Peptide
Nyborg, A. C., Moll, J. R., Wegrzyn, R. D., Havas, D., Hutter‐Paier, B., Feurstein, G., & Rudolph, A. S. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-122107 · Cited by 11 · see citing works
Apolipoprotein E receptor pathways in Alzheimer disease
Schmidt, V., Carlo, A.-S., & Willnow, T. E. (2014) · WIREs Systems Biology and Medicine · doi:10.1002/wsbm.1262 · Cited by 10 · see citing works
Ringman, J. M., Tomic, J. L., Coppola, G., Elashoff, D. A., Gylys, K. H., & Glabe, C. G. (2012) · Dementia and Geriatric Cognitive Disorders Extra · doi:10.1159/000345771 · Cited by 9 · see citing works
Yuan, Z., Du, M., Chen, Y., & Dou, F. (2013) · PubMed Central · doi:10.3969/j.issn.1673-5374.2013.33.004 · Cited by 6 · see citing works
NEWS FROM THE SOCIETY FOR NEUROSCIENCE ANNUAL MEETING
Robinson, R. J. (2012) · Neurology Today · doi:10.1097/01.nt.0000425719.88852.88 · Cited by 2 · see citing works
Barbero (2014) · doi:10.1016/j · Cited by 1 · see citing works
(2018) · Digital Commons@Becker (Washington University School of Medicine) · doi:10.1371/journal
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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 · see citing works
Self-citationAlzheimer's disease: experimental models and reality
Drummond, E., & Wisniewski, T. (2017) · Acta Neuropathologica · doi:10.1007/s00401-016-1662-x · Cited by 810 · see citing works
A vicious cycle of β amyloid−dependent neuronal hyperactivation
Zott, B., Simon, M. M., Hong, W., Unger, F., Chen-Engerer, H.-J., Frosch, M. P., Sakmann, B., Walsh, D. M., & Konnerth, A. (2019) · Science · doi:10.1126/science.aay0198 · Cited by 640 · see citing works
Alzheimer's Disease: Treatment Strategies and Their Limitations.
Passeri, E., Elkhoury, K., Morsink, M., Broersen, K., Linder, M., Tamayol, A., Malaplate, C., Yen, F. T., & Arab-Tehrany, E. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232213954 · Cited by 592 · see citing works
“Because pathogenic soluble aggregates of Aβ appear early in the sequence of AD, they can represent interesting targets for therapeutics and diagnostics [51].”
BackgroundSöderberg, L., Johannesson, M., Nygren, P., Laudon, H., Eriksson, F., Osswald, G., Möller, C., & Lannfelt, L. (2022) · Neurotherapeutics · doi:10.1007/s13311-022-01308-6 · Cited by 444 · see citing works
The amyloid cascade hypothesis: are we poised for success or failure?
Karran, E., & De Strooper, B. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13632 · Cited by 402 · see citing works
Ferreira, S. T., Lourenco, M. V., Oliveira, M. M., & De Felice, F. G. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00191 · Cited by 373 · see citing works
Amyloid Beta in Aging and Alzheimer’s Disease
Sehar, U., Rawat, P., Reddy, A. P., Kopel, J. J., & Reddy, P. H. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232112924 · Cited by 385 · see citing works
Tolar, M., Abushakra, S., Hey, J. A., Porsteinsson, A., & Sabbagh, M. (2020) · Alzheimer's Research & Therapy · doi:10.1186/s13195-020-00663-w · Cited by 354 · see citing works
Alzheimer's disease: From immunotherapy to immunoprevention
Jucker, M., & Walker, L. C. (2023) · Cell · doi:10.1016/j.cell.2023.08.021 · Cited by 353 · see citing works
de la Monte, S. M. (2017) · Drugs · doi:10.1007/s40265-016-0674-0 · Cited by 331 · see citing works
The clinical promise of biomarkers of synapse damage or loss in Alzheimer’s disease
the Synaptic Health Endpoints Working Group, Colom-Cadena, M., Spires-Jones, T., Zetterberg, H., Blennow, K., Caggiano, A., DeKosky, S. T., Fillit, H., Harrison, J. E., Schneider, L. S., et al. (2020) · Alzheimer's Research & Therapy · doi:10.1186/s13195-020-00588-4 · Cited by 328 · see citing works
Jeremic, D., Jiménez-Díaz, L., & Navarro-López, J. D. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2021.101496 · Cited by 306 · see citing works
Role of tau protein in Alzheimer’s disease: The prime pathological player
Muralidar, S., Ambi, S. V., Sekaran, S., Thirumalai, D., & Palaniappan, B. (2020) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.07.327 · Cited by 278 · see citing works
Clearance of cerebral Aβ in Alzheimer’s disease: reassessing the role of microglia and monocytes
Zuroff, L. R., Daley, D. A., Black, K. L., & Koronyo‐Hamaoui, M. (2017) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-017-2463-7 · Cited by 275 · 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
Memantine for the Treatment of Dementia: A Review on its Current and Future Applications
Folch, J., Busquets, O., Ettcheto, M., Sánchez-López, E., Castro-Torres, R. D., Verdaguer, E., Garcia, M. L., Olloquequi, J., Casadesús, G., Beas-Zarate, C., et al. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-170672 · Cited by 245 · see citing works
Tolar, M., Hey, J., Power, A., & Abushakra, S. R. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22126355 · Cited by 246 · see citing works
Saleem, S., & Kannan, R. R. (2018) · Cell Death Discovery · doi:10.1038/s41420-018-0109-7 · Cited by 241 · see citing works
Antibody-based PET imaging of amyloid beta in mouse models of Alzheimer’s disease
Sehlin, D., Fang, X. T., Cato, L., Antoni, G., Lannfelt, L., & Syvänen, S. (2016) · Nature Communications · doi:10.1038/ncomms10759 · Cited by 223 · see citing works
Ahmad, A., Ali, T., Park, H. Y., Badshah, H., Rehman, S. U., & Kim, M. O. (2016) · Molecular Neurobiology · doi:10.1007/s12035-016-9795-4 · Cited by 216 · see citing works
RetractedLiu, Z., Li, T., Li, P., Wei, N., Zhao, Z., Liang, H., Ji, X., Chen, W., Xue, M., & Wei, J. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2015/352723 · Cited by 208 · see citing works
Challenges for Alzheimer's Disease Therapy: Insights from Novel Mechanisms Beyond Memory Defects
Frozza, R. L., Lourenco, M. V., & Felice, F. G. D. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00037 · Cited by 202 · see citing works
Hong, W., Wang, Z., Liu, W., O’Malley, T. T., Jin, M., Willem, M., Haass, C., Frosch, M. P., & Walsh, D. M. (2018) · Acta Neuropathologica · doi:10.1007/s00401-018-1846-7 · Cited by 166 · see citing works
The Role of ADAM10 in Alzheimer’s Disease
Yuan, X., Sun, S., Tan, C., Yu, J., & Tan, L. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170061 · Cited by 160 · see citing works
Imbalanced cholesterol metabolism in Alzheimer's disease
Xue-shan, Z., Peng, J., Wu, Q., Zhong, R., Li-hong, P., Tang, Z., Jiang, Z., Wang, G., & Liu, L. (2016) · Clinica Chimica Acta · doi:10.1016/j.cca.2016.02.024 · Cited by 155 · see citing works
Amyloid β oligomers (AβOs) in Alzheimer’s disease
Mroczko, B., Groblewska, M., Litman‐Zawadzka, A., Kornhuber, J., & Lewczuk, P. (2017) · Journal of Neural Transmission · doi:10.1007/s00702-017-1820-x · Cited by 146 · see citing works
Rusek, M., Smith, J., El-Khatib, K., Aikins, K., Czuczwar, S. J., & Pluta, R. M. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24010864 · Cited by 145 · see citing works
Cummings, J. (2019) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2018.05.006 · Cited by 140 · see citing works
Arad, E., Green, H., Jelinek, R., & Rapaport, H. (2020) · Journal of Colloid and Interface Science · doi:10.1016/j.jcis.2020.03.075 · Cited by 140 · see citing works
Galectin-3 promotes Aβ oligomerization and Aβ toxicity in a mouse model of Alzheimer’s disease
Tao, C.-C., Cheng, K.-M., Ma, Y.-L., Hsu, W.-L., Chen, Y.-C., Fuh, J.-L., Lee, W.-J., Chao, C.-C., & Lee, E. H. Y. (2020) · Cell Death & Differentiation · doi:10.1038/s41418-019-0348-z · Cited by 138 · see citing works
Liu, P., Zhang, T., Chen, Q., Li, C., Chu, Y., Guo, Q., Zhang, Y., Zhou, W., Chen, H., Zhou, Z., et al. (2021) · Advanced Materials · doi:10.1002/adma.202100746 · Cited by 137 · see citing works
Aβ and tau prion-like activities decline with longevity in the Alzheimer’s disease human brain
Aoyagi, A., Condello, C., Stöhr, J., Yue, W., Rivera, B. M., Lee, J. C., Woerman, A. L., Halliday, G. M., van Duinen, S. G., Ingelsson, M., et al. (2019) · Science Translational Medicine · doi:10.1126/scitranslmed.aat8462 · Cited by 130 · see citing works
APOE-amyloid interaction: Therapeutic targets
Wısnıewskı, T., & Drummond, E. (2020) · Neurobiology of Disease · doi:10.1016/j.nbd.2020.104784 · Cited by 125 · see citing works
Alzheimer's disease failed clinical trials
Asher, S., & Priefer, R. (2022) · Life Sciences · doi:10.1016/j.lfs.2022.120861 · Cited by 124 · see citing works
Felice, F. G. D., & Lourenco, M. V. (2015) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2015.00094 · Cited by 120 · see citing works
Counteracting the effects of TNF receptor‐1 has therapeutic potential in Alzheimer's disease
Steeland, S., Gorlé, N., Vandendriessche, C., Balusu, S., Brkić, M., Cauwenberghe, C. V., Imschoot, G. V., Wonterghem, E. V., Rycke, R. M. D., Kremer, A., et al. (2018) · EMBO Molecular Medicine · doi:10.15252/emmm.201708300 · Cited by 119 · see citing works
Chiral modulation of amyloid beta fibrillation and cytotoxicity by enantiomeric carbon dots
Malishev, R., Arad, E., Bhunia, S. K., Shaham‐Niv, S., Kolusheva, S., Gazit, E., & Jelinek, R. (2018) · Chemical Communications · doi:10.1039/c8cc03235a · Cited by 122 · see citing works
Exploring ER stress response in cellular aging and neuroinflammation in Alzheimer's disease
Uddin, M. S., Yu, W. S., & Lim, L. W. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2021.101417 · Cited by 118 · see citing works
Oligomeropathies and pathogenesis of Alzheimer and Parkinson's diseases
Forloni, G., Artuso, V., Vitola, P. L., & Balducci, C. (2016) · Movement Disorders · doi:10.1002/mds.26624 · Cited by 115 · see citing works
Song, Q., Song, H., Xu, J., Huang, J., Meng, H., Gu, X. Q., Chen, J., Zheng, G., Chen, H., & Gao, X. (2016) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.6b00781 · Cited by 113 · see citing works
Grundman, M., Morgan, R. E., Lickliter, J. D., Schneider, L. S., DeKosky, S. T., Izzo, N. J., Guttendorf, R. J., Higgin, M., Pribyl, J., Mozzoni, K., et al. (2018) · Alzheimer s & Dementia Translational Research & Clinical Interventions · doi:10.1016/j.trci.2018.11.001 · Cited by 110 · see citing works
Kočiš, P., Tolar, M., Yu, Y., Sinko, W., Ray, S. S., Blennow, K., Fillit, H. M., & Hey, J. A. (2017) · CNS Drugs · doi:10.1007/s40263-017-0434-z · Cited by 110 · see citing works
Österlund, N., Moons, R., Ilag, L. L., Sobott, F., & Gräslund, A. (2019) · Journal of the American Chemical Society · doi:10.1021/jacs.9b04596 · Cited by 110 · see citing works
Detectable Neuropsychological Differences in Early Preclinical Alzheimer’s Disease: A Meta-Analysis
Han, D.-K. S., Nguyen, C. P., Stricker, N., & Nation, D. (2017) · Neuropsychology Review · doi:10.1007/s11065-017-9345-5 · Cited by 103 · see citing works
Alzheimer’s Disease: Etiology, Neuropathology and Pathogenesis
Sheppard, O., & Coleman, M. P. (2020) · Exon Publications eBooks · doi:10.36255/exonpublications.alzheimersdisease.2020.ch1 · Cited by 112 · see citing works
Fišar, Z. (2022) · Biomolecules · doi:10.3390/biom12111676 · Cited by 110 · see citing works
Kumar, S., Wirths, O., Stüber, K., Wunderlich, P., Koch, P., Theil, S., Rezaei‐Ghaleh, N., Zweckstetter, M., Bayer, T. A., Brüstle, O., et al. (2016) · Acta Neuropathologica · doi:10.1007/s00401-016-1546-0 · Cited by 106 · see citing works
Izzo, N. J., Yuede, C. M., Mozzoni, K., Limegrover, C. S., Rehak, C., Yurko, R., Waybright, L., Look, G. C., Rishton, G. M., Safferstein, H., et al. (2021) · Alzheimer s & Dementia · doi:10.1002/alz.12302 · Cited by 101 · see citing works
Faucher, P., Mons, N., Micheau, J., Louis, C., & Beracochea, D. J. (2016) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2015.00245 · Cited by 100 · see citing works
Oh, S. J., Lee, H., Jeong, Y. J., Nam, K. R., Kang, K. J., Han, S. J., Lee, K. C., Lee, Y. J., & Choi, J. Y. (2020) · Scientific Reports · doi:10.1038/s41598-020-72755-4 · Cited by 100 · see citing works
The role of ubiquitin proteasomal system and autophagy-lysosome pathway in Alzheimer’s disease
Zhang, Y., Chen, X., Zhao, Y., Ponnusamy, M., & Liu, Y. (2017) · Reviews in the Neurosciences · doi:10.1515/revneuro-2017-0013 · Cited by 99 · see citing works
Toader, C., Tătaru, C. P., Munteanu, O., Șerban, M., Covache-Busuioc, R.-A., Ciurea, A. V., & Enyedi, M. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252312613 · Cited by 106 · see citing works
Multi-target-directed phenol–triazole ligands as therapeutic agents for Alzheimer's disease
Jones, M. R., Mathieu, É., Dyrager, C., Faissner, S., Vaillancourt, Z., Korshavn, K. J., Lim, M. H., Ramamoorthy, A., Yong, V. W., Tsutsui, S., et al. (2017) · Chemical Science · doi:10.1039/c7sc01269a · Cited by 96 · see citing works
P‐glycoprotein: a role in the export of amyloid‐β in Alzheimer's disease?
Chai, A. B., Leung, G. K. F., Callaghan, R., & Gelissen, I. C. (2019) · FEBS Journal · doi:10.1111/febs.15148 · Cited by 98 · see citing works
Qi, C., Bao, J., Wang, J., Zhu, H., Xue, Y., Wang, X., Li, H., Sun, W., Gao, W., Lai, Y., et al. (2016) · Chemical Science · doi:10.1039/c6sc02464e · Cited by 95 · see citing works
TREM2 in Alzheimer’s Disease: Microglial Survival and Energy Metabolism
Zheng, H., Cheng, B., Li, Y., Li, X., Chen, X., & Zhang, Y.-W. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00395 · Cited by 94 · see citing works
Xu, J., Gao, H. Y., Zhang, L., Rong, S., Yang, W. Q., Ma, C., Chen, M., Huang, Q., Deng, Q., & Huang, F. (2019) · Journal of Pineal Research · doi:10.1111/jpi.12584 · Cited by 93 · see citing works
Amyloid, tau and metabolic PET correlates of cognition in early and late-onset Alzheimer’s disease
Tanner, J. A., Iaccarino, L., Edwards, L., Asken, B. M., Gorno‐Tempini, M. L., Kramer, J. H., Pham, J. Q., Perry, D. C., Possin, K. L., Malpetti, M., et al. (2022) · Brain · doi:10.1093/brain/awac229 · Cited by 88 · see citing works
The relationship between amyloid-beta and brain capillary endothelial cells in Alzheimer’s disease
Su, Q., Guo, J.-H., Zhang, Y.-L., Wang, J., & Zhang, Z.-N. (2022) · Neural Regeneration Research · doi:10.4103/1673-5374.335829 · Cited by 91 · see citing works
Raefsky, S. M., Furman, R., Milne, G., Pollock, E., Axelsen, P., Mattson, M. P., & Shchepinov, M. S. (2018) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2018.02.024 · Cited by 90 · see citing works
Amyloid-β and Tau in Alzheimer’s disease: pathogenesis, mechanisms, and interplay
Abdulkhaliq, A. A., Kim, B., Almoghrabi, Y. M., Khan, J., Ajoolabady, A., Ren, J., Bahijri, S., Tuomilehto, J., Borai, A., & Pratico, D. (2026) · Cell Death & Disease · doi:10.1038/s41419-025-08186-8 · Cited by 87 · see citing works
Rai, H., Gupta, S., Kumar, S., Yang, J., Singh, S. K., Ran, C., & Modi, G. P. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c01619 · Cited by 86 · see citing works
Naturally Occurring Antioxidant Therapy in Alzheimer’s Disease
Collins, A. E., Saleh, T. M., & Kalisch, B. E. (2022) · Antioxidants · doi:10.3390/antiox11020213 · Cited by 87 · see citing works
Amyloid β‐induced astrogliosis is mediated by β1‐integrin via NADPH oxidase 2 in Alzheimer's disease
Wyssenbach, A., Quintela‐López, T., Llavero, F., Zugaza, J. L., Matute, C., & Alberdi, E. M. (2016) · Aging Cell · doi:10.1111/acel.12521 · Cited by 81 · see citing works
Hou, T., Yang, H., Wang, W., Wu, Q., Tian, Y., & Jia, J. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-171110 · Cited by 84 · see citing works
Alzheimer's Disease Puzzle: Delving into Pathogenesis Hypotheses
(2024) · aging and disease · doi:10.14336/ad.2023.0608 · Cited by 183 · see citing works
Protein Phosphorylation is a Key Mechanism in Alzheimer’s Disease
Oliveira, J., Costa, M., de Almeida, M. S. C., Silva, O. A. B. D. C. E., & Henriques, A. G. (2017) · Journal of Alzheimer's Disease · doi:10.3233/jad-170176 · Cited by 68 · see citing works
Salvadores, N., Moreno‐González, I., Gamez, N., Quiroz, G., Vegas‐Gomez, L., Escandón, M., Jiménez, S., Vitórica, J., Gutiérrez, A., Soto, C. A., et al. (2022) · Acta Neuropathologica Communications · doi:10.1186/s40478-022-01332-9 · Cited by 81 · see citing works
Rahbaran, M., Zekiy, A. O., Bahramali, M., Jahangir, M., Mardasi, M., Sakhaei, D., Thangavelu, L. P., Shomali, N., Zamani, M., Mohammadi, A., et al. (2022) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-022-00359-z · Cited by 80 · see citing works
Nanoscale structure of amyloid-β plaques in Alzheimer’s disease
Querol‐Vilaseca, M., Colom‐Cadena, M., Pegueroles, J., Núñez‐Llaves, R., Luque-Cabecerans, J., Muñoz, L., Andilla, J., Belbin, O., Spires‐Jones, T. L., Gelpí, E., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-41443-3 · Cited by 77 · see citing works
Xie, Z., Zhao, J., Wang, H., Jiang, Y., Yang, Q., Fu, Y., Zeng, H., Hölscher, C., Xu, J., & Zhang, Z. (2020) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2020.109886 · Cited by 77 · see citing works
Kim, J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22062929 · Cited by 77 · see citing works
Li, Y., Xu, D., Sun, A., Ho, S., Poon, C., Chan, H., Ng, O. T.-W., Yung, K. K. L., Yan, H., Li, H., et al. (2017) · Chemical Science · doi:10.1039/c7sc03974c · Cited by 77 · see citing works
Chen, S., Zhang, B., Wang, Y., Li, H., Xiong, R., Zhao, Z., Chu, X., Li, Q., & Sun, S. (2016) · Drug Design Development and Therapy · doi:10.2147/dddt.s99958 · Cited by 75 · see citing works
Zhang, S., Wang, P., Ren, L., Hu, C., & Bi, J. (2016) · Alzheimer s Research & Therapy · doi:10.1186/s13195-016-0206-x · Cited by 74 · see citing works
Johnson, E. C. B., Ho, K., Yu, G.-Q., Das, M., Sanchez, P. E., Djukic, B., Lopez, I., Yu, X., Gill, M., Zhang, W., et al. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-00393-5 · Cited by 73 · see citing works
Grochowska, K. M., Yuanxiang, P., Bär, J., Raman, R., Brugal, G. N., Sahu, G., Schweizer, M., Bikbaev, A. F., Schilling, S., Demuth, H., et al. (2017) · EMBO Reports · doi:10.15252/embr.201643519 · Cited by 73 · see citing works
Hey, J. A., Kočiš, P., Hort, J., Abushakra, S. R., Power, A., Vyhnálek, M., Yu, Y., & Tolar, M. (2018) · CNS Drugs · doi:10.1007/s40263-018-0554-0 · Cited by 73 · see citing works
Du, Y., Qu, J., Zhang, W., Bai, M., Zhou, Q., Zhang, Z., Li, Z., & Miao, J. (2016) · Neuropharmacology · doi:10.1016/j.neuropharm.2016.04.008 · Cited by 72 · see citing works
Li, H., Jia, J., Wang, W., Hou, T., Tian, Y., Wu, Q., Xu, L., Wei, Y., & Wang, X. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-180126 · Cited by 71 · see citing works
Koronyo‐Hamaoui, M., Sheyn, J., Hayden, E. Y., Li, S., Fuchs, D.-T. S., Regis, G. C., Lopes, D. H. J., Black, K. L., Bernstein, K. E., Teplow, D. B., et al. (2019) · Brain · doi:10.1093/brain/awz364 · Cited by 70 · see citing works
Targeting Tau Hyperphosphorylation via Kinase Inhibition: Strategy to Address Alzheimer's Disease
Naqvi, A. A. T., Hasan, G. M., & Hassan, M. I. (2020) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026620666200106125910 · Cited by 70 · see citing works
Rodríguez‐Ortiz, C. J., Prieto, G. A., Martini, A. C., Forner, S., Trujillo‐Estrada, L., LaFerla, F. M., Baglietto‐Vargas, D., Cotman, C. W., & Kitazawa, M. (2020) · Aging Cell · doi:10.1111/acel.13118 · Cited by 67 · see citing works
Tryptophan metabolites modify brain Aβ peptide degradation: A role in Alzheimer's disease?
Maitre, M., Klein, C., Patte-Mensah, C., & Mensah-Nyagan, A. (2020) · Progress in neurobiology · doi:10.1016/j.pneurobio.2020.101800 · Cited by 63 · see citing works
Noguchi‐Shinohara, M., Ono, K., Hamaguchi, T., Nagai, T., Kobayashi, S., Komatsu, J., Samuraki-Yokohama, M., Iwasa, K., Yokoyama, K., Nakamura, H., et al. (2020) · Scientific Reports · doi:10.1038/s41598-020-73729-2 · Cited by 67 · see citing works
Koppensteiner, P., Trinchese, F., Fà, M., Puzzo, D., Gulisano, W., Yan, S., Poussin, A., Liu, S., Orozco, I. J., Dale, E., et al. (2016) · Scientific Reports · doi:10.1038/srep32553 · Cited by 64 · see citing works
Chen, T., Yang, Y., Zhu, S., Lu, Y., Zhu, L., Wang, Y., & Wang, X. (2020) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2020.104382 · Cited by 64 · see citing works
Chen, Y., Wang, S., Ren, J., Zhao, H., Cui, M., Li, N., Li, M. C., & Zhang, C. (2022) · Analytical Chemistry · doi:10.1021/acs.analchem.2c01602 · Cited by 65 · see citing works
Ding, Y. J., Zhao, J., Zhang, X., Wang, S., Viola, K. L., Chow, F. E., Zhang, Y., Lippa, C. F., Klein, W. L., & Gong, Y. (2019) · Frontiers in Neurology · doi:10.3389/fneur.2019.01140 · Cited by 65 · see citing works
Self-citationLi, S., Jin, M., Liu, L., Dang, Y., Ostaszewski, B. L., & Selkoe, D. J. (2018) · Acta Neuropathologica Communications · doi:10.1186/s40478-018-0626-x · Cited by 64 · see citing works
Neurochemical correlation between major depressive disorder and neurodegenerative diseases
Réus, G. Z., Titus, S. E., Abelaira, H. M., Freitas, S. M., Tuon, T., Quevedo, J., & Budni, J. (2016) · Life Sciences · doi:10.1016/j.lfs.2016.06.027 · Cited by 63 · see citing works
The Implication of the Brain Insulin Receptor in Late Onset Alzheimer’s Disease Dementia
Folch, J., Ettcheto, M., Busquets, O., Sánchez‐López, E., Castro-Torres, R. D., Verdaguer, E., Manzine, P. R., Poor, S. R., García, M. L., Olloquequi, J., et al. (2018) · Pharmaceuticals · doi:10.3390/ph11010011 · Cited by 63 · see citing works
Johannesson, M., Söderberg, L., Zachrisson, O., Fritz, N., Kylefjord, H., Gkanatsiou, E., Button, E. B., Svensson, A.-S., Rachalski, A., Nygren, P., et al. (2024) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2024.103949 · Cited by 66 · see citing works
Lues, I., Weber, F., Meyer, A., Uli, B., Hoffmann, T., Kühn‐Wache, K., Manhart, S., Heiser, U. F., Pokorny, R., Chiesa, J., et al. (2015) · Alzheimer s & Dementia Translational Research & Clinical Interventions · doi:10.1016/j.trci.2015.08.002 · Cited by 62 · see citing works
Fan, Q., Liu, Y., Wang, X., Zhang, Z., Fu, Y., Liu, L., Wang, P., Ma, H., Ma, H., Seeram, N. P., et al. (2020) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.9b00673 · Cited by 62 · see citing works
Supramolecular Copolymers of Peptides and Lipidated Peptides and Their Therapeutic Potential
Qiu, R., Sasselli, I. R., Álvarez, Z., Sai, H., Ji, W., Palmer, L. C., & Stupp, S. I. (2022) · Journal of the American Chemical Society · doi:10.1021/jacs.2c00433 · Cited by 61 · see citing works
Meng, X. W., Li, T., Wang, X., Lv, X., Sun, Z., Zhang, J., Feng, S., Kang, S., Kim, S., An, S. S. A., et al. (2019) · Alzheimer s Research & Therapy · doi:10.1186/s13195-019-0535-7 · Cited by 63 · see citing works
Xi, Y., Zhang, Y., Zhou, Y., Liu, Q., Chen, X., Liu, X., Grune, T., Shi, L. S., Hou, M., & Liu, Z. (2022) · Redox Biology · doi:10.1016/j.redox.2022.102595 · Cited by 62 · see citing works
Seong, S. H., Ali, M. Y., Kim, H., Jung, H. A., & Choi, J. S. (2017) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2017.05.033 · Cited by 61 · see citing works
- Authors
- Viola, K. L., & Klein, W. L.
- Affiliations
- Northwestern University (US)
- Corresponding author
- Klein, William L.
- Venue
- Acta Neuropathologica
- Published
- 2015-01-22
- Volume
- 129
- Issue
- 2
- Pages
- 183-206
- ISSN
- 0001-6322 (ISSN-L)
- 1432-0533
- PMC
- PMC4390393
- OpenAlex
- W2055775253
- Cited by
- 628
- References
- 198
- Citations by year
- 2026: 42 · 2025: 45 · 2024: 55 · 2023: 51 · 2022: 75 · 2021: 69 · 2020: 66 · 2019: 58 · 2018: 60 · 2017: 53 · 2016: 42 · 2015: 10
- FWCI
- 6.76
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Acta Neuropathologica (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health
- National Institute on Aging (AG045637, AG029460, R01AG022547, AG022547, R01AG029460, R21AG045637)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- amyloid-beta oligomers, Alzheimer's disease pathogenesis, protein aggregation, neurotoxicity, synaptic dysfunction, glutamate receptors, calcium overload, tau hyperphosphorylation, insulin resistance, oxidative stress, synaptic loss, cerebrospinal fluid biomarkers, diabetes comorbidity, hypercholesterolemia, Alzheimer's disease therapeutics
- MeSH terms
- Alzheimer Disease, Animals, Humans, Neurons, Amyloid beta-Peptides
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