Vaccination with soluble Aβ oligomers generates toxicity‐neutralizing antibodies

Lambert, Mary P.; Viola, Kirsten L.; Chromy, Brett A.; Chang, Lei; Morgan, Todd E.; Yu, Jiaxin; Venton, Duane L.; Krafft, Grant A.; Finch, Caleb E.; Klein, William L.

doi:10.1046/j.1471-4159.2001.00592.x

Cited by 349Alzheimer's disease research and treatmentsNeuroinflammation and Neurodegeneration MechanismsDementia and Cognitive Impairment Research

Vaccination with soluble Aβ oligomers generates toxicity‐neutralizing antibodies

Lambert, Mary P., Viola, Kirsten L., Chromy, Brett A., Chang, Lei, Morgan, Todd E., Yu, Jiaxin, Venton, Duane L., Krafft, Grant A. +2 more·2001·Journal of Neurochemistry

DOI 10.1046/j.1471-4159.2001.00592.x

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Abstract

In recent studies of transgenic models of Alzheimer's disease (AD), it has been reported that antibodies to aged beta amyloid peptide 1-42 (Abeta(1-42)) solutions (mixtures of Abeta monomers, oligomers and amyloid fibrils) cause conspicuous reduction of amyloid plaques and neurological improvement. In some cases, however, neurological improvement has been independent of obvious plaque reduction, and it has been suggested that immunization might neutralize soluble, non-fibrillar forms of Abeta. It is now known that Abeta toxicity resides not only in fibrils, but also in soluble protofibrils and oligomers. The current study has investigated the immune response to low doses of Abeta(1-42) oligomers and the characteristics of the antibodies they induce. Rabbits that were injected with Abeta(1-42) solutions containing only monomers and oligomers produced antibodies that preferentially bound to assembled forms of Abeta in immunoblots and in physiological solutions. The antibodies have proven useful for assays that can detect inhibitors of oligomer formation, for immunofluorescence localization of cell-attached oligomers to receptor-like puncta, and for immunoblots that show the presence of SDS-stable oligomers in Alzheimer's brain tissue. The antibodies, moreover, were found to neutralize the toxicity of soluble oligomers in cell culture. Results support the hypothesis that immunizations of transgenic mice derive therapeutic benefit from the immuno-neutralization of soluble Abeta-derived toxins. Analogous immuno-neutralization of oligomers in humans may be a key in AD vaccines.

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Dot immunoblots of soluble extracts from human brain show major increases in Aβ oligomers in AD-affected tissue.
“Dot immunoblots of soluble extracts from human brain show major increases in oligomers in AD-affected tissue (Gong et al., 2003; Kayed et al., 2003; Lambert et al., 2001).”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Lambert et al., 2001

Diffusible, nonfibrillar ligands derived from Aβ 1–42 are potent central nervous system neurotoxins
Lambert, M. P., Barlow, A. K., Chromy, B. A., Edwards, C., Freed, R., Liosatos, M., Morgan, T. E., Rozovsky, I., Trommer, B., Viola, K. L., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6448 · Cited by 3,506 · see citing works
Self-citation
Immunization with amyloid-β attenuates Alzheimer-disease-like pathology in the PDAPP mouse
Schenk, D., Barbour, R., Dunn, W., Gordon, G., Grajeda, H., Guido, T., Hu, K., Huang, J., Johnson-Wood, K., Khan, K., et al. (1999) · Nature · doi:10.1038/22124 · Cited by 3,160 · see citing works
Peripherally administered antibodies against amyloid β-peptide enter the central nervous system and reduce pathology in a mouse model of Alzheimer disease
Bard, F., Cannon, C., Barbour, R., Burke, R.-L., Games, D., Grajeda, H., Guido, T., Hu, K., Huang, J., Johnson-Wood, K., et al. (2000) · Nature Medicine · doi:10.1038/78682 · Cited by 2,012 · see citing works
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 · see citing works
MODELS OF AMYLOID SEEDING IN ALZHEIMER'S DISEASE AND SCRAPIE: Mechanistic Truths and Physiological Consequences of the Time-Dependent Solubility of Amyloid Proteins
Harper, J. D., & Lansbury, P. T. (1997) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.66.1.385 · Cited by 1,652 · see citing works
Soluble Amyloid β Peptide Concentration as a Predictor of Synaptic Change in Alzheimer's Disease
Lue, L.-F., Kuo, Y.-M., Roher, A. E., Brachova, L., Shen, Y., Sue, L., Beach, T., Kurth, J. H., Rydel, R. E., & Rogers, J. (1999) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)65184-x · Cited by 1,530 · see citing works
Aβ peptide vaccination prevents memory loss in an animal model of Alzheimer's disease
Morgan, D., Diamond, D. M., Gottschall, P. E., Ugen, K. E., Dickey, C. A., Hardy, J., Duff, K., Jantzen, P. T., DiCarlo, G., Wilcock, D. M., et al. (2000) · Nature · doi:10.1038/35050116 · Cited by 1,488 · see citing works
Aβ peptide immunization reduces behavioural impairment and plaques in a model of Alzheimer's disease
Janus, C., Pearson, J., McLaurin, J., Mathews, P. M., Jiang, Y., Schmidt, S. D., Chishti, M. A., Horne, P., Heslin, D., French, J., et al. (2000) · Nature · doi:10.1038/35050110 · Cited by 1,431 · see citing works
Neurodegeneration induced by beta-amyloid peptides in vitro: the role of peptide assembly state
Pike, C., Burdick, D., Walencewicz, A., Glabe, C., & Cotman, C. (1993) · The Journal of Neuroscience · doi:10.1523/jneurosci.13-04-01676.1993 · Cited by 1,417 · see citing works
Beta-amyloid neurotoxicity requires fibril formation and is inhibited by congo red.
Lorenzo, A., & Yankner, B. A. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.25.12243 · Cited by 1,324 · see citing works
Amyloid β-Protein Fibrillogenesis
Walsh, D. M., Lomakin, A., Benedek, G. B., Condron, M. M., & Teplow, D. B. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.35.22364 · Cited by 1,139 · see citing works
Plaque-independent disruption of neural circuits in Alzheimer’s disease mouse models
Hsia, A. Y., Masliah, E., McConlogue, L., Yu, G.-Q., Tatsuno, G., Hu, K., Kholodenko, D., Malenka, R. C., Nicoll, R. A., & Mucke, L. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.6.3228 · Cited by 1,123 · see citing works
Age-Dependent Changes in Brain, CSF, and Plasma Amyloid β Protein in the Tg2576 Transgenic Mouse Model of Alzheimer's Disease
Kawarabayashi, T., Younkin, L. H., Saido, T. C., Shoji, M., Ashe, K. H., & Younkin, S. G. (2001) · The Journal of Neuroscience · doi:10.1523/jneurosci.21-02-00372.2001 · Cited by 1,053 · cited 1× · see citing works
“Samples of frontal cortex, temporal cortex and cerebellum from AD and age-matched control brains were obtained from the Northwestern University Alzheimer's Brain Bank, stored at 2808C and prepared for analysis by a modi®cation of the method of Kawarabayashi et al. (2001).”
Method
Amyloid β-Protein Fibrillogenesis
Walsh, D. M., Hartley, D. M., Kusumoto, Y., Fezoui, Y., Condron, M. M., Lomakin, A., Benedek, G. B., Selkoe, D. J., & Teplow, D. B. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.36.25945 · Cited by 1,046 · 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-citation
Protofibrillar Intermediates of Amyloid β-Protein Induce Acute Electrophysiological Changes and Progressive Neurotoxicity in Cortical Neurons
Hartley, D. M., Walsh, D. M., Ye, C., Diehl, T. S., Vasquez, S., Vassilev, P., Teplow, D. B., & Selkoe, D. J. (1999) · Journal of Neuroscience · doi:10.1523/jneurosci.19-20-08876.1999 · Cited by 965 · see citing works
Tau in Alzheimer's disease.
Mandelkow, E., & Mandelkow, E. (1998) · Trends in Cell Biology · doi:10.1016/s0962-8924(98)01368-3 · Cited by 951 · see citing works
Tau protein pathology in neurodegenerative diseases
Spillantini, M. G., & Goedert, M. (1998) · Trends in Neurosciences · doi:10.1016/s0166-2236(98)01337-x · Cited by 683 · see citing works
Water-soluble Aβ(N-40, N-42) oligomers in normal and Alzheimer disease brains
Kuo, Y.-M., Emmerling, M. R., Vigo-Pelfrey, C., Kasunic, T. C., Kirkpatrick, J. B., Murdoch, G. H., Ball, M. J., & Roher, A. E. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.8.4077 · Cited by 618 · see citing works
Morphology and Toxicity of Aβ-(1-42) Dimer Derived from Neuritic and Vascular Amyloid Deposits of Alzheimer's Disease
Roher, A. E., Chaney, M. O., Kuo, Y., Webster, S. D., Stine, W. B., Haverkamp, L. J., Woods, A. S., Cotter, R. J., Tuohy, J. M., Krafft, G. A., et al. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.34.20631 · Cited by 494 · see citing works
Self-citation
Radical AGEing in Alzheimer's disease
Smith, M. A., Sayre, L. M., Monnier, V. M., & Perry, G. L. (1995) · Trends in Neurosciences · doi:10.1016/0166-2236(95)93897-7 · Cited by 462 · see citing works
Isolation and culture of adult rat hippocampal neurons
Brewer, G. J. (1997) · Journal of Neuroscience Methods · doi:10.1016/s0165-0270(96)00136-7 · Cited by 438 · see citing works
Disaggregation of Alzheimer β-amyloid by site-directed mAb
Solomon, B., Koppel, R., Frankel, D., & Hanan, E. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.8.4109 · Cited by 420 · see citing works
Inhibition of PC12 cell redox activity is a specific,early indicator of the mechanism of beta-amyloid-mediated celldeath.
Shearman, M. S., RAGAN, C. I., & Iversen, L. L. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.4.1470 · Cited by 411 · see citing works
Huntingtin aggregates may not predict neuronal death in Huntington's disease
Kuemmerle, S., Gutekunst, C., Klein, A., Li, X., Li, S.-H., Beal, M. F., Hersch, S. M., & Ferrante, R. J. (1999) · Annals of Neurology · doi:10.1002/1531-8249(199912)46:6 · Cited by 387 · see citing works
Clusterin (apoJ) Alters the Aggregation of Amyloid β-Peptide (Aβ1-42) and Forms Slowly Sedimenting Aβ Complexes That Cause Oxidative Stress
Oda, T., Wals, P., Osterburg, H. H., Johnson, S. A., Pasinetti, G. M., Morgan, T. E., Rozovsky, I., Stine, W. B., Snyder, S. W., Holzman, T. F., et al. (1995) · Experimental Neurology · doi:10.1006/exnr.1995.1080 · Cited by 352 · see citing works
Self-citation
Biochemical detection of Aβ isoforms: implications for pathogenesis, diagnosis, and treatment of Alzheimer’s disease
Golde, T. E., Eckman, C. B., & Younkin, S. G. (2000) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/s0925-4439(00)00043-0 · Cited by 300 · see citing works
Amino Acid Derivatives of β-Cyclodextrin
Ashton, P. R., Königer, R., Stoddart, J. F., Alker, D., & Harding, V. D. (1996) · The Journal of Organic Chemistry · doi:10.1021/jo951396d · Cited by 273 · see citing works
Cytotoxic Amyloid Peptides Inhibit Cellular 3‐(4,5‐Dimethylthiazol‐2‐yl)‐2,5‐Diphenyltetrazolium Bromide (MTT) Reduction by Enhancing MTT Formazan Exocytosis
Liu, Y., & Schubert, D. A. (1997) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1997.69062285.x · Cited by 195 · see citing works
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 128 · see citing works
Amyloid β peptide alters intracellular vesicle trafficking and cholesterol homeostasis
Liu, Y., Peterson, D. A., & Schubert, D. A. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.22.13266 · Cited by 127 · see citing works
β‐Cyclodextrin interacts with the Alzheimer amyloid β‐A4 peptide
Camilleri, P., Haskins, N. J., & Hewlett, D. R. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)80467-2 · Cited by 117 · see citing works
Appearance of Sodium Dodecyl Sulfate-Stable Amyloid β-Protein (Aβ) Dimer in the Cortex During Aging
Enya, M., Morishima-Kawashima, M., Yoshimura, M., Shinkai, Y., Kusui, K., Khan, K., Games, D., Schenk, D., Sugihara, S., Yamaguchi, H., et al. (1999) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)65273-x · Cited by 111 · see citing works
Focal adhesion kinase expressed by nerve cell lines shows increased tyrosine phosphorylation in response to Alzheimer's A beta peptide.
Zhang, C., Lambert, M. P., Bunch, C., Barber, K., Wade, W. S., Krafft, G. A., & Klein, W. L. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47238-9 · Cited by 97 · see citing works
Self-citation
Soluble multimeric Alzheimer β(1–40) pre-amyloid complexes in dilute solution
LeVine, H. (1995) · Neurobiology of Aging · doi:10.1016/0197-4580(95)00052-g · Cited by 94 · see citing works
Modulation of Alzheimer’s β-amyloid neurotoxicity by site-directed single-chain antibody
Frenkel, D., Solomon, B., & Benhar, I. (2000) · Journal of Neuroimmunology · doi:10.1016/s0165-5728(99)00232-5 · Cited by 82 · see citing works
High affinity binding of monoclonal antibodies to the sequential epitope EFRH of β-amyloid peptide is essential for modulation of fibrillar aggregation
Frenkel, D., Balass, M., Katchalski‐Katzir, E., & Solomon, B. (1999) · Journal of Neuroimmunology · doi:10.1016/s0165-5728(99)00003-x · Cited by 64 · see citing works
Inflammation in Alzheimer’s Disease
Finch, C. E., Longo, V. D., Miyao, A., Morgan, T. E., Rozovsky, I., Soong, Y., Wei, M., Xie, Z., & Zanjani, H. (2001) · Humana Press eBooks · doi:10.1007/978-1-59259-006-3_4 · Cited by 50 · see citing works
Self-citation
Reversible Inactivation of Superoxide‐Sensitive Aconitase in Aβ1‐42‐Treated Neuronal Cell Lines
Longo, V. D., Viola, K. L., Klein, W. L., & Finch, C. E. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0751977.x · Cited by 46 · see citing works
Self-citation
Molecular Mechanisms of Neurodegenerative Diseases
Chesselet, M. (2000) · Humana Press eBooks · doi:10.1385/1592590063 · Cited by 38 · see citing works
SDS-Stable Complex Formation between Native Apolipoprotein E3 and β-Amyloid Peptides
Munson, G. W., Roher, A. E., Kuo, Y., Gilligan, S. M., Reardon, C. A., Getz, G. S., & LaDu, M. J. (2000) · Biochemistry · doi:10.1021/bi0017475 · Cited by 36 · see citing works
The Sixth International Conference on Alzheimer's Disease, Amsterdam, The Netherlands, July 1998. The amyloid cascade hypothesis debate: Emerging consensus on the role of Aβ and amyloid in Alzheimer's disease
Small, D. H. (1998) · Amyloid · doi:10.3109/13506129809007304 · Cited by 19 · see citing works
Sequence and nethylation in the βA4 region of the rabbit anyloid precursor protein gene
Davidson, J. S., West, R. L., Kotikalapudi, P., & Maroun, L. E. (1992) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(92)91141-c · Cited by 18 · see citing works
Further Progress on a β-Amyloid Vaccine
Helmuth, L. L. (2000) · Science · doi:10.1126/science.289.5478.375a · Cited by 15 · see citing works

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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 · see citing works
Localized Surface Plasmon Resonance Spectroscopy and Sensing
Willets, K. A., & Duyne, R. P. V. (2006) · Annual Review of Physical Chemistry · doi:10.1146/annurev.physchem.58.032806.104607 · Cited by 6,162 · see citing works
Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade
Chiti, F., & Dobson, C. M. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-045115 · Cited by 2,629 · 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
Aβ Oligomers – a decade of discovery
Walsh, D. M., & Selkoe, D. J. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04426.x · Cited by 1,938 · see citing works
P <scp>ROTOFIBRILS</scp> , P <scp>ORES</scp> , F <scp>IBRILS, AND</scp> N <scp>EURODEGENERATION</scp> : Separating the Responsible Protein Aggregates from The Innocent Bystanders
Caughey, B., & Lansbury, P. T. (2003) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.26.010302.081142 · Cited by 1,650 · see citing works
Oligomeric and fibrillar species of amyloid-β peptides differentially affect neuronal viability
Dahlgren, K. N., Manelli, A. M., Stine, W. B., Baker, L. K., Krafft, G. A., & LaDu, M. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201750200 · Cited by 1,452 · see citing works
Self-citation
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 · see citing works
Self-citation
Alzheimer's disease-affected brain: Presence of oligomeric Aβ ligands (ADDLs) suggests a molecular basis for reversible memory loss
Gong, Y., Chang, L., Viola, K. L., Lacor, P. N., Lambert, M. P., Finch, C. E., Krafft, G. A., & Klein, W. L. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1834302100 · Cited by 1,061 · see citing works
Self-citation
Synaptic Targeting by Alzheimer's-Related Amyloid β Oligomers
Lacor, P. N., Buniel, M. C., Chang, L., Fernandez, S. J., Gong, Y., Viola, K. L., Lambert, M. P., Velasco, P. T., Bigio, E. H., Finch, C. E., et al. (2004) · The Journal of Neuroscience · doi:10.1523/jneurosci.3432-04.2004 · Cited by 954 · see citing works
Self-citation
The Amyloid Beta Peptide: A Chemist’s Perspective. Role in Alzheimer’s and Fibrillization
Hamley, I. W. (2012) · Chemical Reviews · doi:10.1021/cr3000994 · Cited by 881 · see citing works
Aβ Oligomers Induce Neuronal Oxidative Stress through an N-Methyl-D-aspartate Receptor-dependent Mechanism That Is Blocked by the Alzheimer Drug Memantine
De Felice, F. G., Velasco, P. T., Lambert, M. P., Viola, K., Fernandez, S. J., Ferreira, S. T., & Klein, W. L. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m607483200 · Cited by 882 · see citing works
Self-citation
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 866 · see citing works
Self-citation
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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-citation
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Glabe, C. G. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.r800016200 · Cited by 783 · see citing works
A Localized Surface Plasmon Resonance Biosensor: First Steps toward an Assay for Alzheimer's Disease
Haes, A. J., Hall, W. P., Chang, L., Klein, W. L., & Duyne, R. P. V. (2004) · Nano Letters · doi:10.1021/nl049670j · Cited by 708 · see citing works
Self-citation
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Nortley, R., Korte, N., Izquierdo, P., Hirunpattarasilp, C., Mishra, A., Jaunmuktane, Z., Kyrargyri, V., Pfeiffer, T., Khennouf, L., Madry, C., et al. (2019) · Science · doi:10.1126/science.aav9518 · Cited by 682 · see citing works
Amyloid β oligomers in Alzheimer’s disease pathogenesis, treatment, and diagnosis
Viola, K. L., & Klein, W. L. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1386-3 · Cited by 628 · see citing works
Self-citation
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Hamley, I. W. (2007) · Angewandte Chemie International Edition · doi:10.1002/anie.200700861 · Cited by 619 · see citing works
Amyloid oligomers: formation and toxicity of Aβ oligomers
Sakono, M., & Zako, T. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07568.x · Cited by 602 · see citing works
Aβ toxicity in Alzheimer’s disease: globular oligomers (ADDLs) as new vaccine and drug targets
Klein, W. L. (2002) · Neurochemistry International · doi:10.1016/s0197-0186(02)00050-5 · Cited by 541 · see citing works
Self-citation
Evidence of fibril-like β-sheet structures in a neurotoxic amyloid intermediate of Alzheimer's β-amyloid
Chimon, S., Shaibat, M. A., Jones, C. R., Calero, D. C., Aizezi, B., & Ishii, Y. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1345 · Cited by 538 · see citing works
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 · see citing works
Self-citation
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Shankar, G. M., & Walsh, D. M. (2009) · Molecular Neurodegeneration · doi:10.1186/1750-1326-4-48 · Cited by 522 · see citing works
Small assemblies of unmodified amyloid $beta;-protein are the proximate neurotoxin in Alzheimer?s disease
Klein, W. L., Stine, W. B., & Teplow, D. B. (2004) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2004.02.010 · Cited by 487 · see citing works
Self-citation
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Suh, Y.-H., & Checler, F. (2002) · Pharmacological Reviews · doi:10.1124/pr.54.3.469 · Cited by 467 · see citing works
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 · see citing works
Self-citation
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-citation
Amyloid-β-Induced Pathological Behaviors Are Suppressed byGinkgo bilobaExtract EGb 761 and Ginkgolides in TransgenicCaenorhabditis elegans
Wu, Y., Wu, Z., Butko, P., Christen, Y., Lambert, M. P., Klein, W. L., Link, C. D., & Luo, Y. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.3448-06.2006 · Cited by 404 · see citing works
Self-citation
Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins?
Lashuel, H. A., & Lansbury, P. T. (2006) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583506004422 · Cited by 398 · see citing works
Inflammatory Response in the Hippocampus of PS1M146L/APP751SLMouse Model of Alzheimer's Disease: Age-Dependent Switch in the Microglial Phenotype from Alternative to Classic
Jimenez, S., Baglietto-Vargas, D., Caballero, C., Moreno-Gonzalez, I., Torres, M., Sanchez-Varo, R., Ruano, D., Vizuete, M., Gutierrez, A., & Vitorica, J. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.3024-08.2008 · Cited by 383 · see citing works
“form the ADDLs (Lambert et al., 2001), we diluted the 5 mM DMSO”
Method
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-citation
Soluble amyloid-Î² oligomers as synaptotoxins leading to cognitive impairment in Alzheimerâ€™s disease
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-β induces NLRP1-dependent neuronal pyroptosis in models of Alzheimer’s disease
Tan, M.-S., Tan, L., Jiang, T., Zhu, X.-C., Wang, H.-F., Jia, C.-D., & Yu, J. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.348 · Cited by 345 · see citing works
Self-citation
Oligomeric Intermediates in Amyloid Formation: Structure Determination and Mechanisms of Toxicity
Fändrich, M. (2012) · Journal of Molecular Biology · doi:10.1016/j.jmb.2012.01.006 · Cited by 339 · see citing works
Soluble fibrillar oligomer levels are elevated in Alzheimer's disease brain and correlate with cognitive dysfunction
Tomic, J. L., Pensalfini, A., Head, E., & Glabe, C. G. (2009) · Neurobiology of Disease · doi:10.1016/j.nbd.2009.05.024 · Cited by 336 · see citing works
18F-THK523: a novel in vivo tau imaging ligand for Alzheimer's disease
Fodero‐Tavoletti, M. T., Okamura, N., Furumoto, S., Mulligan, R. S., Connor, A. R., McLean, C., Cao, D., Rigopoulos, A., Cartwright, G. A., O'Keefe, G. J., et al. (2011) · Brain · doi:10.1093/brain/awr038 · Cited by 329 · 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-citation
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
Temporal memory deficits in Alzheimer’s mouse models: Rescue by genetic deletion of BACE1
Ohno, M., Chang, L., Tseng, W., Oakley, H., Citron, M., Klein, W. L., Vassar, R., & Disterhoft, J. F. (2006) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2005.04551.x · Cited by 298 · see citing works
Self-citation
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. C., Rishton, G. M., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0111899 · Cited by 294 · see citing works
Sensitive ELISA detection of amyloid‐β protofibrils in biological samples
Englund, H., Sehlin, D., Johansson, A., Nilsson, L. N. G., Gellerfors, P., Paulie, S., Lannfelt, L., & Pettersson, F. E. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04759.x · Cited by 292 · see citing works
Autophagic vacuoles are enriched in amyloid precursor protein-secretase activities: implications for β-amyloid peptide over-production and localization in Alzheimer’s disease
Yu, W. H., Kumar, A., Peterhoff, C., Shapiro Kulnane, L., Uchiyama, Y., Lamb, B. T., Cuervo, A. M., & Nixon, R. A. (2004) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2004.05.010 · Cited by 279 · see citing works
Protein Misfolded Oligomers: Experimental Approaches, Mechanism of Formation, and Structure-Toxicity Relationships
Bemporad, F., & Chiti, F. (2012) · Chemistry & Biology · doi:10.1016/j.chembiol.2012.02.003 · Cited by 270 · see citing works
Inhibition of Amyloid Formation
Härd, T., & Lendel, C. (2012) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.12.062 · Cited by 266 · see citing works
Preparation and characterization of toxic Aβ aggregates for structural and functional studies in Alzheimer's disease research
Jan, A., Hartley, D. M., & Lashuel, H. A. (2010) · Nature Protocols · doi:10.1038/nprot.2010.72 · Cited by 257 · see citing works
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 252 · see citing works
Mechanisms of Aβ mediated neurodegeneration in Alzheimer's disease
Crouch, P. J., Harding, S.-M. E., White, A. R., Camakaris, J., Bush, A. I., & Masters, C. L. (2007) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2007.07.013 · 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
The Interplay of Catalysis and Toxicity by Amyloid Intermediates on Lipid Bilayers: Insights from Type II Diabetes
Hebda, J. A., & Miranker, A. D. (2009) · Annual Review of Biophysics · doi:10.1146/annurev.biophys.050708.133622 · Cited by 223 · see citing works
Systemic Catabolism of Alzheimer's Aβ40 and Aβ42
Ghiso, J., Shayo, M., Calero, M., Ng, D., Tomidokoro, Y., Gandy, S., Rostagno, A., & Frangione, B. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407668200 · Cited by 209 · see citing works
Blockade of EphA4 signaling ameliorates hippocampal synaptic dysfunctions in mouse models of Alzheimer’s disease
Fu, A. K. Y., Hung, K.-W., Huang, H., Gu, S., Shen, Y., Cheng, E. Y. L., Ip, F. C. F., Huang, X., Fu, W.-Y., & Ip, N. Y. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1405803111 · Cited by 201 · see citing works
Targeting the neurotoxic species in Alzheimer's disease: inhibitors of Aβ oligomerization
Felice, F. G. D., Vieira, M. N. N., Saraiva, L. M., Figueroa‐Villar, J. D., Garcia-Abreu, J., Liu, R., Chang, L., Klein, W. L., & Ferreira, S. T. (2004) · The FASEB Journal · doi:10.1096/fj.04-1764com · Cited by 193 · see citing works
Self-citation
Ibuprofen reduces Aβ, hyperphosphorylated tau and memory deficits in Alzheimer mice
McKee, A. C., Carreras, I., Hossain, L., Ryu, H., Klein, W. L., Oddo, S., LaFerla, F. M., Jenkins, B. G., Kowall, N. W., & Dedeoglu, A. (2008) · Brain Research · doi:10.1016/j.brainres.2008.01.095 · Cited by 196 · see citing works
Self-citation
The Second-Generation Active A Immunotherapy CAD106 Reduces Amyloid Accumulation in APP Transgenic Mice While Minimizing Potential Side Effects
Wießner, C., Wiederhold, K., Tissot, A. C., Frey, P., Danner, S., Jacobson, L. H., Jennings, G. T., Lüönd, R. M., Ortmann, R., Reichwald, J., et al. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.0293-11.2011 · Cited by 190 · see citing works
Aromatic Small Molecules Remodel Toxic Soluble Oligomers of Amyloid β through Three Independent Pathways
Ladiwala, A. R. A., Dordick, J. S., & Tessier, P. M. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.173856 · Cited by 190 · see citing works
Preparation of Amyloid β‐Protein for Structural and Functional Studies
Teplow, D. B. (2006) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(06)13002-5 · Cited by 187 · see citing works
Solution State Characterization of Amyloid β-Derived Diffusible Ligands
Hepler, R. W., Grimm, K. M., Nahas, D. D., Breese, R., Chen-Dodson, E., Acton, P. J., Keller, P. M., Yeager, M. D., Wang, H., Shughrue, P. J., et al. (2006) · Biochemistry · doi:10.1021/bi061850f · Cited by 181 · see citing works
Toxic oligomers and islet beta cell death: guilty by association or convicted by circumstantial evidence?
Zraika, S., Hull, R. L., Verchere, C. B., Clark, A., Potter, K. J., Fraser, P. E., Raleigh, D. P., & Kahn, S. E. (2010) · Diabetologia · doi:10.1007/s00125-010-1671-6 · Cited by 181 · see citing works
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 · see citing works
Protein aggregation and neurodegenerative diseases: From theory to therapy
Kumar, V., Sami, N., Kashav, T., Islam, A., Ahmad, F., & Hassan, M. I. (2016) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2016.07.054 · Cited by 176 · see citing works
α-Synuclein Reactive Antibodies as Diagnostic Biomarkers in Blood Sera of Parkinson's Disease Patients
Yanamandra, K., Gruden, M. A., Casaite, V., Meskys, R., Forsgren, L., & Morozova-Roche, L. A. (2011) · PLoS ONE · doi:10.1371/journal.pone.0018513 · Cited by 171 · see citing works
The culprit behind amyloid beta peptide related neurotoxicity in Alzheimer's disease: oligomer size or conformation?
Broersen, K., Rousseau, F., & Schymkowitz, J. (2010) · Alzheimer's Research & Therapy · doi:10.1186/alzrt36 · Cited by 168 · see citing works
Human neural stem cells alleviate Alzheimer-like pathology in a mouse model
Lee, I.-S., Jung, K., Kim, I., Lee, H.-J., Kim, M., Yun, S., Hwang, K., Shin, J. E., & Park, K. I. (2015) · Molecular Neurodegeneration · doi:10.1186/s13024-015-0035-6 · Cited by 169 · see citing works
Residues 17–20 and 30–35 of beta‐amyloid play critical roles in aggregation
Liu, R., McAllister, C., Lyubchenko, Y. L., & Sierks, M. R. (2003) · Journal of Neuroscience Research · doi:10.1002/jnr.10859 · Cited by 165 · see citing works
Molecular mechanisms used by chaperones to reduce the toxicity of aberrant protein oligomers
Mannini, B., Cascella, R., Zampagni, M., van Waarde-Verhagen, M. A. W. H., Meehan, S., Roodveldt, C., Campioni, S., Boninsegna, M., Penco, A., Relini, A., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1117799109 · Cited by 162 · see citing works
Aluminum, copper, iron and zinc differentially alter amyloid-Aβ1–42 aggregation and toxicity
Bolognin, S., Luigi Messori, A., Drago, D., Gabbiani, C., Cendron, L., & Zatta, P. F. (2011) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2011.02.009 · Cited by 162 · see citing works
Immunotherapy for Alzheimer's disease
Gélinas, D. S., Silva, K. D., Fenili, D., George‐Hyslop, P. S., & McLaurin, J. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0404866101 · Cited by 156 · see citing works
Conformation-dependent antibodies target diseases of protein misfolding
Glabe, C. C. (2004) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2004.08.009 · Cited by 154 · see citing works
Trodusquemine enhances Aβ42 aggregation but suppresses its toxicity by displacing oligomers from cell membranes
Limbocker, R., Chia, S., Ruggeri, F. S., Perni, M., Cascella, R., Heller, G. T., Meisl, G., Mannini, B., Habchi, J., Michaels, T. C. T., et al. (2019) · Nature Communications · doi:10.1038/s41467-018-07699-5 · Cited by 149 · see citing works
α-Sheet secondary structure in amyloid β-peptide drives aggregation and toxicity in Alzheimer’s disease
Shea, D. W., Hsu, C.-C., Bi, T., Paranjapye, N., Childers, M. C., Cochran, J., Tomberlin, C., Wang, L., Paris, D., Zonderman, J. A., et al. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1820585116 · Cited by 148 · see citing works
Structure-based design of conformation- and sequence-specific antibodies against amyloid β
Perchiacca, J. M., Ladiwala, A. R. A., Bhattacharya, M., & Tessier, P. M. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1111232108 · Cited by 145 · see citing works
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 141 · see citing works
Self-citation
New class of inhibitors of amyloid-beta fibril formation. Implications for the mechanism of pathogenesis in Alzheimer's disease.
Lashuel, H., Hartley, D., Balakhaneh, D., Aggarwal, A., Teichberg, S., & Callaway, D. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m206593200 · Cited by 141 · see citing works
Current progress in beta-amyloid immunotherapy
Schenk, D., Hagen, M., & Seubert, P. A. (2004) · Current Opinion in Immunology · doi:10.1016/j.coi.2004.07.012 · Cited by 134 · see citing works
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 · see citing works
Self-citation
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Miller, E. C., Teravskis, P. J., Dummer, B. W., Zhao, X., Huganir, R. L., & Liao, D. (2014) · European Journal of Neuroscience · doi:10.1111/ejn.12507 · Cited by 131 · see citing works
Alzheimer’s disease as oligomeropathy
Ono, K. (2018) · Neurochemistry International · doi:10.1016/j.neuint.2017.08.010 · Cited by 129 · see citing works
Reelin delays amyloid-beta fibril formation and rescues cognitive deficits in a model of Alzheimer’s disease
Pujadas, L., Rossi, D., Andrés, R., Teixeira, C. M., Serra-Vidal, B., Parcerisas, A., Maldonado, R., Giralt, E., Carulla, N., & Soriano, E. (2014) · Nature Communications · doi:10.1038/ncomms4443 · Cited by 129 · see citing works
FcγRIIb mediates amyloid-β neurotoxicity and memory impairment in Alzheimer’s disease
Kam, T.-I., Song, S., Gwon, Y., Park, H., Yan, J.-J., Im, I., Choi, J.-W., Choi, T.-Y., Kim, J., Song, D.-K., et al. (2013) · Journal of Clinical Investigation · doi:10.1172/jci66827 · Cited by 128 · see citing works
Self-citation
Plasmonic nanoparticles and their analytical applications: A review
Boken, J., Khurana, P., Thatai, S., Kumar, D., & Prasad, S. (2017) · Applied Spectroscopy Reviews · doi:10.1080/05704928.2017.1312427 · Cited by 127 · see citing works
Selection and characterization of Affibody ligands binding to Alzheimer amyloid β peptides
Grönwall, C., Jonsson, A., Lindström, S., Gunneriusson, E., Ståhl, S., & Herne, N. (2006) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2006.09.013 · Cited by 127 · see citing works
Antibodies against β‐amyloid reduce aβ oligomers, glycogen synthase kinase‐3β activation and τ phosphorylation in vivo and in vitro
Ma, Q., Lim, G. P., Harris‐White, M. E., Yang, F., Ambegaokar, S. S., Ubeda, O. J., Glabe, C. G., Teter, B., Frautschy, S. A., & Cole, G. M. (2006) · Journal of Neuroscience Research · doi:10.1002/jnr.20734 · Cited by 126 · see citing works
Ammonium hydroxide treatment of Aβ produces an aggregate free solution suitable for biophysical and cell culture characterization
Ryan, T. M., Caine, J. M., Mertens, H. D. T., Kirby, N. M., Nigro, J., Breheney, K., Waddington, L. J., Streltsov, V. A., Curtain, C. C., Masters, C. L., et al. (2013) · PeerJ · doi:10.7717/peerj.73 · Cited by 126 · see citing works
Monoclonal Antibodies against Aβ42 Fibrils Distinguish Multiple Aggregation State Polymorphisms in Vitro and in Alzheimer Disease Brain
Hatami, A., Albay, R., Monjazeb, S., Milton, S. C. F., & Glabe, C. G. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.594846 · Cited by 121 · see citing works
Alzheimer's Disease and the Amyloid β-Protein
Walsh, D. M., & Teplow, D. B. (2012) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-385883-2.00012-6 · Cited by 120 · see citing works
Kinetic characterization of amyloid-beta 1–42 aggregation with a multimethodological approach
Bartolini, M., Naldi, M., Fiori, J., Valle, F., Biscarini, F., Nicolau, D. V., & Andrisano, V. (2011) · Analytical Biochemistry · doi:10.1016/j.ab.2011.03.020 · Cited by 121 · see citing works
Amyloid β oligomerization is induced by brain lipid rafts
Kim, S., Yi, J.-S., & Ko, Y. (2006) · Journal of Cellular Biochemistry · doi:10.1002/jcb.20978 · Cited by 118 · see citing works
Retinal and Circulating miRNAs in Age-Related Macular Degeneration: An In vivo Animal and Human Study
Romano, G. L., Platania, C. B. M., Drago, F., Salomone, S., Ragusa, M., Barbagallo, C., Pietro, C. D., Purrello, M., Reibaldi, M., Avitabile, T., et al. (2017) · Frontiers in Pharmacology · doi:10.3389/fphar.2017.00168 · Cited by 117 · see citing works
The amyloid-cell membrane system. The interplay between the biophysical features of oligomers/fibrils and cell membrane defines amyloid toxicity
Cecchi, C., & Stefani, M. (2013) · Biophysical Chemistry · doi:10.1016/j.bpc.2013.06.003 · Cited by 115 · see citing works
Amyloid-β oligomers in cellular models of Alzheimer’s disease
Fontana, I. C., Zimmer, A. R., Rocha, A. S., Gosmann, G., Souza, D. O., Lourenco, M. V., Ferreira, S. T., & Zimmer, E. R. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.15030 · Cited by 115 · see citing works
Aggregation Pathways of the Amyloid β(1–42) Peptide Depend on Its Colloidal Stability and Ordered β-Sheet Stacking
Jiang, D., Rauda, I. E., Han, S., Chen, S., & Zhou, F. (2012) · Langmuir · doi:10.1021/la3021436 · Cited by 115 · see citing works
Amyloid-β oligomer detection by ELISA in cerebrospinal fluid and brain tissue
Bruggink, K. A., Jongbloed, W., Biemans, E. A. L. M., Veerhuis, R., Claassen, J. A. H. R., Kuiperij, H. B., & Verbeek, M. M. (2012) · Analytical Biochemistry · doi:10.1016/j.ab.2012.09.014 · Cited by 114 · see citing works
Single Chain Variable Fragments against β-Amyloid (Aβ) Can Inhibit Aβ Aggregation and Prevent Aβ-Induced Neurotoxicity
Liu, R., Yuan, B., Emadi, S., Zameer, A., Schulz, P., McAllister, C., Lyubchenko, Y. L., Goud, G. N., & Sierks, M. R. (2004) · Biochemistry · doi:10.1021/bi049933o · Cited by 113 · see citing works
MAPK recruitment by β‐amyloid in organotypic hippocampal slice cultures depends on physical state and exposure time
Bell, K. A., O’Riordan, K. J., Sweatt, J. D., & Dineley, K. T. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02722.x · Cited by 114 · see citing works
ADDLs and the signaling web that leads to Alzheimer’s disease
Krafft, G. A., & Klein, W. L. (2010) · Neuropharmacology · doi:10.1016/j.neuropharm.2010.07.012 · Cited by 111 · see citing works
Self-citation
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Klein, W. L. (2006) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2005.11.003 · Cited by 107 · see citing works
Self-citation
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Legleiter, J. A., Lotz, G. P., Miller, J. M. L., Ko, J., Ng, C.-P., Williams, G. L., Finkbeiner, S. M., Patterson, P. H., & Muchowski, P. J. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.016923 · Cited by 108 · see citing works
Different β-amyloid oligomer assemblies in Alzheimer brains correlate with age of disease onset and impaired cholinergic activity
Bao, F., Wicklund, L., Lacor, P. N., Klein, W. L., Nordberg, A. K., & Marutle, A. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.05.003 · Cited by 106 · see citing works
Self-citation
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Stains, C. I., Mondal, K., & Ghosh, I. (2007) · ChemMedChem · doi:10.1002/cmdc.200700140 · Cited by 108 · 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-citation
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Klein, W. (2001) · Trends in Neurosciences · doi:10.1016/s0166-2236(00)01749-5 · Cited by 989 · see citing works
Self-citation
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Montañés, M., Marcos, I., Canudas, J., Lacosta, A. M., Pesini, P., & Sarasa, M. (2017) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2017.06.2255 · Cited by 1 · see citing works
Anti-Aβ1–11 Antibody Binds to Different β-Amyloid Species, Inhibits Fibril Formation, and Disaggregates Preformed Fibrils but Not the Most Toxic Oligomers
Mamikonyan, G., Necula, M., Mkrtichyan, M., Ghochikyan, A., Petrushina, I., Movsesyan, N., Mina, E. W., Kiyatkin, A. B., Glabe, C. G., Cribbs, D. H., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m700088200 · Cited by 93 · see citing works
Immunization with Small Amyloid-β-derived Cyclopeptide Conjugates Diminishes Amyloid-β-Induced Neurodegeneration in Mice
Mulder, C. K., Dong, Y., Brugghe, H. F., Timmermans, H., Tilstra, W., Westdijk, J., van Riet, E., STEEG, H. V., Hoogerhout, P., & Eisel, U. L. M. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-151136 · Cited by 7 · see citing works

Authors: 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.
Affiliations: Northwestern University (US)
University of Southern California (US)
University of Illinois Chicago (US)
Corresponding author: Klein, William L.
ORCID: Viola, Kirsten L.
Chang, Lei
Morgan, Todd E.
Yu, Jiaxin
Finch, Caleb E.
Klein, William L.
Venue: Journal of Neurochemistry
Publisher: Wiley
Published: 2001-11
Volume: 79
Issue: 3
Pages: 595-605
ISSN: 0022-3042 (ISSN-L)
1471-4159
DOI: 10.1046/j.1471-4159.2001.00592.x
OpenAlex: W1857351893
Cited by: 349
References: 45
Citations by year: 2026: 12 · 2025: 8 · 2024: 4 · 2023: 11 · 2022: 6 · 2021: 8 · 2020: 15 · 2019: 10 · 2018: 5 · 2017: 11 · 2016: 6 · 2015: 10 · 2014: 18 · 2013: 20 · 2012: 20
FWCI: 8.37
Type: journal article
Language: en
Open access: closed
Licence: onlinelibrary.wiley.com/termsAndConditions#vor (vor, 2440 d)
Locations: Journal of Neurochemistry (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health
National Institute on Aging (AG-13499, P01 AG13138, R01AG013499)
Topics: Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Keywords: Alzheimer's disease, amyloid-beta oligomers, amyloid-beta 42, immunization, neutralizing antibodies, amyloid plaques, amyloid protofibrils, oligomer toxicity, Alzheimer's disease vaccine, transgenic mice
MeSH terms: Alzheimer Disease, Animals, Antibody Specificity, Epitopes, Fluorescent Antibody Technique, Hippocampus, Humans, Neurons, Peptide Fragments, Solubility, Vaccination, Amyloid beta-Peptides, PC12 Cells, Neuroprotective Agents, Rats

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Vaccination with soluble Aβ oligomers generates toxicity‐neutralizing antibodies

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