Amyloid β oligomers in Alzheimer’s disease pathogenesis, treatment, and diagnosis

Amyloid 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

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

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

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

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

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

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

Journal 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 3,427

Curcumin Inhibits Formation of Amyloid β Oligomers and Fibrils, Binds Plaques, and Reduces Amyloid in Vivo

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

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

High-Level Neuronal Expression of Aβ1–42in Wild-Type Human Amyloid Protein Precursor Transgenic Mice: Synaptotoxicity without Plaque Formation

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

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

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 1,722

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

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 1,450

Intranasal Insulin Therapy for Alzheimer Disease and Amnestic Mild Cognitive Impairment: A Pilot Clinical Trial

Craft, S. (2012) · Archives of Neurology · doi:10.1001/archneurol.2011.233 · Cited by 1,253

Aβ Oligomer-Induced Aberrations in Synapse Composition, Shape, and Density Provide a Molecular Basis for Loss of Connectivity in Alzheimer's Disease

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

Alzheimer’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

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

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

Neurotoxicity 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

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

Synaptic Targeting by Alzheimer's-Related Amyloid β Oligomers

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

Detection of a Biomarker for Alzheimer's Disease from Synthetic and Clinical Samples Using a Nanoscale Optical Biosensor

Haes, A. J., Chang, L., Klein, W. L., & Duyne, R. P. V. (2005) · Journal of the American Chemical Society · doi:10.1021/ja044087q · Cited by 881

Immunization 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

Oligomeric amyloid β associates with postsynaptic densities and correlates with excitatory synapse loss near senile plaques

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

An anti-diabetes agent protects the mouse brain from defective insulin signaling caused by Alzheimer’s disease–associated Aβ oligomers

Bomfim, 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 849

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

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

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

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

Evidence that amyloid beta-peptide-induced lipid peroxidation and its sequelae in Alzheimer’s disease brain contribute to neuronal death1

Allanbutterfield, D., Castegna, A., Lauderback, C. M., & Drake, J. (2002) · Neurobiology of Aging · doi:10.1016/s0197-4580(01)00340-2 · Cited by 715

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

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

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

Protection of synapses against Alzheimer's-linked toxins: Insulin signaling prevents the pathogenic binding of Aβ oligomers

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

Seeding 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

Cerebral metabolic changes accompanying conversion of mild cognitive impairment into Alzheimer's disease: a PET follow-up study

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

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

Metabotropic Glutamate Receptor 5 Is a Coreceptor for Alzheimer Aβ Oligomer Bound to Cellular Prion Protein

Um, 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

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 572

Environmental enrichment strengthens corticocortical interactions and reduces amyloid-β oligomers in aged mice

Mainardi, M., Garbo, A. D., Caleo, M., Berardi, N., Sale, A., & Maffei, L. (2014) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00001 · Cited by 550

Soluble oligomers of β amyloid (1-42) inhibit long-term potentiation but not long-term depression in rat dentate gyrus

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

Self-Assembly of Aβ 1 - 42 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

Amyloid, 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

Resolving controversies on the path to Alzheimer's therapeutics

Selkoe, D. J. (2011) · Nature Medicine · doi:10.1038/nm.2460 · Cited by 494

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

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

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

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 440

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

TNF-α Mediates PKR-Dependent Memory Impairment and Brain IRS-1 Inhibition Induced by Alzheimer’s β-Amyloid Oligomers in Mice and Monkeys

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 430

Prion-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

Prion protein recruits its neuronal receptor NCAM to lipid rafts to activate p59fyn and to enhance neurite outgrowth

Chadha, A. S., Sytnyk, V., Leshchyns’ka, I., & Schachner, M. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200409127 · Cited by 419

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 404

Curcumin: 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

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 401

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

Polymorphism 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

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

Liraglutide can reverse memory impairment, synaptic loss and reduce plaque load in aged APP/PS1 mice, a model of Alzheimer's disease

McClean, P. L., & Hölscher, C. (2013) · Neuropharmacology · doi:10.1016/j.neuropharm.2013.08.005 · Cited by 362

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

How 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

Type 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 324

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 319

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 319

An Effector-Reduced Anti- -Amyloid (A ) Antibody with Unique A Binding Properties Promotes Neuroprotection and Glial Engulfment of A

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

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 316

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

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 300

Lost 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 284

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

Inhibition of soluble TNF signaling in a mouse model of Alzheimer's disease prevents pre-plaque amyloid-associated neuropathology

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 274

The Murine Version of BAN2401 (mAb158) Selectively Reduces Amyloid-β Protofibrils in Brain and Cerebrospinal Fluid of tg-ArcSwe Mice

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×

Targeting Amyloid-β Peptide (Aβ) Oligomers by Passive Immunization with a Conformation-selective Monoclonal Antibody Improves Learning and Memory in Aβ Precursor Protein (APP) Transgenic Mice

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 254

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 254

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

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 228

Decreased Brain-Derived Neurotrophic Factor Depends on Amyloid Aggregation State in Transgenic Mouse Models of Alzheimer's Disease

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 224

Cross‐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 222

Chronic Neuron-Specific Tumor Necrosis Factor-Alpha Expression Enhances the Local Inflammatory Environment Ultimately Leading to Neuronal Death in 3xTg-AD Mice

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

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 219

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 196

The 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

Safety and Changes in Plasma and Cerebrospinal Fluid Amyloid β After a Single Administration of an Amyloid β Monoclonal Antibody in Subjects With Alzheimer Disease

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

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

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

Environmental Novelty Activates β2-Adrenergic Signaling to Prevent the Impairment of Hippocampal LTP by Aβ Oligomers

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 189

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 187

Memantine Rescues Transient Cognitive Impairment Caused by High-Molecular-Weight A Oligomers But Not the Persistent Impairment Induced by Low-Molecular-Weight Oligomers

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 186

Alzheimer's Therapeutics Targeting Amyloid Beta 1–42 Oligomers I: Abeta 42 Oligomer Binding to Specific Neuronal Receptors Is Displaced by Drug Candidates That Improve Cognitive Deficits

Izzo, 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

Fyn Kinase Modulates Synaptotoxicity, But Not Aberrant Sprouting, in Human Amyloid Precursor Protein Transgenic Mice

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 162

Alzheimer's Therapeutics Targeting Amyloid Beta 1–42 Oligomers II: Sigma-2/PGRMC1 Receptors Mediate Abeta 42 Oligomer Binding and Synaptotoxicity

Izzo, N. J., Xu, J., Zeng, C., Kirk, M. J., Mozzoni, K., Silky, C., Rehak, C., Yurko, R., Look, G., Rishton, G., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0111899 · Cited by 157

Spreading of amyloid-β peptides via neuritic cell-to-cell transfer is dependent on insufficient cellular clearance

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 156

Perspectives on future Alzheimer therapies: amyloid-β protofibrils - a new target for immunotherapy with BAN2401 in Alzheimer’s disease

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 153

Novel Mechanistic Insight into the Molecular Basis of Amyloid Polymorphism and Secondary Nucleation during Amyloid Formation

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

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 151

6-Shogaol, an active constituent of ginger, attenuates neuroinflammation and cognitive deficits in animal models of dementia

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

Evaluating 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 147

Synaptotoxic Amyloid-β Oligomers: A Molecular Basis for the Cause, Diagnosis, and Treatment of Alzheimer's Disease?

Klein, W. L. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-129039 · Cited by 145

Why Alzheimer trials fail: removing soluble oligomeric beta amyloid is essential, inconsistent, and difficult

Rosenblum, W. I. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2013.10.085 · Cited by 142

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 139

Quantitative analysis of the time course of Aβ oligomerization and subsequent growth steps using tetramethylrhodamine-labeled Aβ

Garai, K., & Frieden, C. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1222478110 · Cited by 138

Alzheimer's-associated Aβ oligomers show altered structure, immunoreactivity and synaptotoxicity with low doses of oleocanthal

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

Mechanisms 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 134

Intracellular processing of disease-associated α-synuclein in the human brain suggests prion-like cell-to-cell spread

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 131

Non-Fibrillar β-Amyloid Protein is Associated with Smooth Muscle Cells of Vessel Walls in Alzheimer Disease

Frackowiak, J., Żółtowska, A., & Wı́sniewski, H. M. (1994) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/00005072-199411000-00011 · Cited by 130

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

Alzheimer’s β-peptide oligomer formation at physiologic concentrations

LeVine, H. (2004) · Analytical Biochemistry · doi:10.1016/j.ab.2004.08.014 · Cited by 125

Metabotropic glutamate receptors transduce signals for neurite outgrowth after binding of the prion protein to laminili γ1 chain

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

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

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

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

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 117

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 115

The Alzheimer's Amyloid-β(1–42) Peptide Forms Off-Pathway Oligomers and Fibrils That Are Distinguished Structurally by Intermolecular Organization

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 111

Tau-Based Therapeutic Approaches for Alzheimer's Disease - A Mini-Review

Boutajangout, A., & Wısnıewskı, T. (2014) · Gerontology · doi:10.1159/000358875 · Cited by 110

In Vitro and Mechanistic Studies of an Antiamyloidogenic Self-Assembled Cyclic d , l -α-Peptide Architecture

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

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 107

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 105

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 105

The cellular prion protein traps Alzheimer's Aβ in an oligomeric form and disassembles amyloid fibers

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 104

α-Secretase-derived Fragment of Cellular Prion, N1, Protects against Monomeric and Oligomeric Amyloid β (Aβ)-associated Cell Death

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 103

Immunotherapy for Alzheimer's disease

Wısnıewskı, T., & Goñi, F. (2014) · Biochemical Pharmacology · doi:10.1016/j.bcp.2013.12.020 · Cited by 103

Impact of Apolipoprotein E on Alzheimer’s Disease

Hauser, P. S., & Ryan, R. O. (2013) · Current Alzheimer Research · doi:10.2174/15672050113109990156 · Cited by 103

Early intervention with a small molecule inhibitor for tumor nefosis factor-α prevents cognitive deficits in a triple transgenic mouse model of Alzheimer’s disease

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 96

Significant Structural Differences between Transient Amyloid‐β Oligomers and Less‐Toxic Fibrils in Regions Known To Harbor Familial Alzheimer′s Mutations

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

Mechanism of cholesterol‐assisted oligomeric channel formation by a short Alzheimer β‐amyloid peptide

Scala, C. D., Troadec, J., Lelièvre, C., Garmy, N., Fantini, J., & Chahinian, H. (2013) · Journal of Neurochemistry · doi:10.1111/jnc.12390 · Cited by 92

Bapineuzumab

Kerchner, G. A., & Boxer, A. L. (2010) · Expert Opinion on Biological Therapy · doi:10.1517/14712598.2010.493872 · Cited by 92

Intrahippocampal Administration of Amyloid-β1-42 Oligomers Acutely Impairs Spatial Working Memory, Insulin Signaling, and Hippocampal Metabolism

Pearson-Leary, J., & McNay, E. C. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-112192 · Cited by 91

Blocking the Interaction between Apolipoprotein E and Aβ Reduces Intraneuronal Accumulation of Aβ and Inhibits Synaptic Degeneration

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×

Multivariate Analyses of Amyloid-Beta Oligomer Populations Indicate a Connection between Pore Formation and Cytotoxicity

Prangkio, P., Yusko, E. C., Sept, D., Yang, J., & Mayer, M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0047261 · Cited by 88

Single Molecule Characterization of the Interactions between Amyloid-β Peptides and the Membranes of Hippocampal Cells

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 85

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 84

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

Femtomole Immunodetection of Synthetic and Endogenous Amyloid-β Oligomers and Its Application to Alzheimer's Disease Drug Candidate Screening

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 81

Do Astrocytes Collaborate with Neurons in Spreading the “Infectious” Aβ and Tau Drivers of Alzheimer’s Disease?

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 79

Amyloid-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 78

Hypercholesterolemia accelerates intraneuronal accumulation of Aβ oligomers resulting in memory impairment in Alzheimer's disease model mice

Umeda, 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

Intracellular Accumulation of Toxic Turn Amyloid-β is Associated with Endoplasmic Reticulum Stress in Alzheimer's Disease

Soejima, 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

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 75

Chronic Intranasal Treatment with an Anti-Aβ30-42 scFv Antibody Ameliorates Amyloid Pathology in a Transgenic Mouse Model of Alzheimer's Disease

Cattepoel, S., Hanenberg, M., Kulic, L., & Nitsch, R. M. (2011) · PLoS ONE · doi:10.1371/journal.pone.0018296 · Cited by 74

Systemic vaccination with anti‐oligomeric monoclonal antibodies improves cognitive function by reducing Aβ deposition and tau pathology in 3xTg‐AD mice

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

Brain interstitial oligomeric amyloid β increases with age and is resistant to clearance from brain in a mouse model of Alzheimer's disease

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 74

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

Amyloid: Little proteins, big clues

Schnabel, J. (2011) · Nature · doi:10.1038/475s12a · Cited by 65

Immunotherapy for Alzheimer’s disease

Wilkinson, D. (2005) · CRC Press eBooks · doi:10.1201/b13935-7 · Cited by 65

Accumulation of Intraneuronal β-Amyloid 42 Peptides Is Associated with Early Changes in Microtubule-Associated Protein 2 in Neurites and Synapses

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 62

Conformation‐dependent single‐chain variable fragment antibodies specifically recognize beta‐amyloid oligomers

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 62

Correlation of Specific Amyloid-β Oligomers With Tau in Cerebrospinal Fluid From Cognitively Normal Older Adults

Handoko, 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 62

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 62

Human Prefoldin Inhibits Amyloid-β (Aβ) Fibrillation and Contributes to Formation of Nontoxic Aβ Aggregates

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 61

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

Early intervention in the 3xTg-AD mice with an amyloid β-antibody fragment ameliorates first hallmarks of Alzheimer disease

Giménez‐Llort, L., Rivera-Hernández, G., Marin‐Argany, M., Sánchez‐Quesada, J. L., & Villegas, S. (2013) · mAbs · doi:10.4161/mabs.25424 · Cited by 60

Lipid Rafts Mediate Amyloid-Induced Calcium Dyshomeostasis and Oxidative Stress in Alzheimer’s Disease

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

Brain Transit and Ameliorative Effects of Intranasally Delivered Anti-Amyloid-β Oligomer Antibody in 5XFAD Mice

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

Synapse-Binding Subpopulations of Aβ Oligomers Sensitive to Peptide Assembly Blockers and scFv Antibodies

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 57

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

Thermodynamically stable amyloid-β monomers have much lower membrane affinity than the small oligomers

Sarkar, B., Das, A. K., & Maiti, S. (2013) · Frontiers in Physiology · doi:10.3389/fphys.2013.00084 · Cited by 56

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 55

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 55

Prefibrillar 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

Conformation-specific antibodies to target amyloid β oligomers and their application to immunotherapy for Alzheimer’s disease

Murakami, K. (2014) · Bioscience Biotechnology and Biochemistry · doi:10.1080/09168451.2014.940275 · Cited by 53

The Arctic AβPP mutation leads to Alzheimer’s disease pathology with highly variable topographic deposition of differentially truncated Aβ

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 52

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

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 49

Inhibition of amyloid beta-induced synaptotoxicity by a pentapeptide derived from the glycine zipper region of the neurotoxic peptide

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

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

Specific Soluble Oligomers of Amyloid-β Peptide Undergo Replication and Form Non-fibrillar Aggregates in Interfacial Environments

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 43

Cyclic AMP Enhancers and Aβ Oligomerization Blockers as Potential Therapeutic Agents in Alzheimers Disease

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

Continuation of Exercise Is Necessary to Inhibit High Fat Diet-Induced β-Amyloid Deposition and Memory Deficit in Amyloid Precursor Protein Transgenic Mice

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 41

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

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NEWS FROM THE SOCIETY FOR NEUROSCIENCE ANNUAL MEETING

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Untitled work

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(2018) · Digital Commons@Becker (Washington University School of Medicine) · doi:10.1371/journal

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