Cited by 522Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchParkinson's Disease Mechanisms and Treatments

The DOI matches its Crossref record, with a small difference in title or year; 26 of the 28 references it cites were found in a registry or an index.

Self-Assembly of Aβ 1 - 42 into Globular Neurotoxins

Chromy, Brett A., Nowak, Richard J., Lambert, Mary P., Viola, Kirsten L., Chang, Lei, Velasco, Pauline T., Jones, Bryan W., Fernandez, Sara J., Lacor, Pascale N., Horowitz, Peleg, Finch, Caleb E., Krafft, Grant A., Klein, William L.·2003·Biochemistry

DOI 10.1021/bi030029q

Open this paper in CoChat — free account

Abstract

Amyloid beta 1-42 (Abeta(1-42)) is a self-associating peptide that becomes neurotoxic upon aggregation. Toxicity originally was attributed to the presence of large, readily formed Abeta fibrils, but a variety of other toxic species are now known. The current study shows that Abeta(1-42) can self-assemble into small, stable globular assemblies free of fibrils and protofibrils. Absence of large molecules was verified by atomic force microscopy (AFM) and nondenaturing gel electrophoresis. Denaturing electrophoresis revealed that the globular assemblies comprised oligomers ranging from trimers to 24mers. Oligomers prepared at 4 degrees C stayed fibril-free for days and remained so when shifted to 37 degrees C, although the spectrum of sizes shifted toward larger oligomers at the higher temperature. The soluble, globular Abeta(1-42) oligomers were toxic to PC12 cells, impairing reduction of MTT and interfering with ERK and Rac signal transduction. Occasionally, oligomers were neither toxic nor recognized by toxicity-neutralizing antibodies, suggesting that oligomers could assume alternative conformations. Tests for oligomerization-blocking activity were carried out by dot-blot immunoassays and showed that neuroprotective extracts of Ginkgo biloba could inhibit oligomer formation at very low doses. The observed neurotoxicity, structure, and stability of synthetic Abeta(1-42) globular assemblies support the hypothesis that Abeta(1-42) oligomers play a role in triggering nerve cell dysfunction and death in Alzheimer's disease.

Integrity signals

Registry

Crossref · 10.1021/bi030029q

Cites

26 of 26 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

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
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
Self-citation
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 1,156
The neuronal MAP kinase cascade: a biochemical signal integration system subserving synaptic plasticity and memory
Sweatt, J. D. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00054.x · Cited by 1,131
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
Alzheimer's Disease: Molecular Understanding Predicts Amyloid-Based Therapeutics
Selkoe, D. J., & Schenk, D. (2003) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.43.100901.140248 · Cited by 829
α-Synuclein, Especially the Parkinson's Disease-associated Mutants, Forms Pore-like Annular and Tubular Protofibrils
Lashuel, H. A., Petre, B. M., Wall, J. S., Simon, M. N., Nowak, R. J., Walz, T., & Lansbury, P. T. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00735-0 · Cited by 819
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. P., Diehl, T., Vasquez, S., Vassilev, P. M., Teplow, D. B., & Selkoe, D. J. (1999) · The Journal of Neuroscience · doi:10.1523/jneurosci.19-20-08876.1999 · Cited by 817
The Relationship between Aβ and Memory in the Tg2576 Mouse Model of Alzheimer's Disease
Westerman, M. A., Cooper-Blacketer, D., Mariash, A., Kotilinek, L., Kawarabayashi, T., Younkin, L. H., Carlson, G. A., Younkin, S. G., & Ashe, K. H. (2002) · Journal of Neuroscience · doi:10.1523/jneurosci.22-05-01858.2002 · Cited by 731
Solution conformations and aggregational properties of synthetic amyloid β-peptides of Alzheimer's disease
Barrow, C. J., Yasuda, A., Kenny, P. T. M., & Zagorski, M. G. (1992) · Journal of Molecular Biology · doi:10.1016/0022-2836(92)90106-t · Cited by 644

Flagged first, then by citations

Show all 28 references

2 of the 28 references couldn’t be matched to a known paper.

Research works printed but not linked: 51

Lee V. M., 2001, Annu. Rev. Neurosci., 24
Pike C. J., 1991, Brain Res. 563, 311−314
Lorenzo A., 1994, Proc. Natl. Acad. Sci. U.S.A. 91, 12243−12247
Hardy J. A., 1992, Science 256, 184−185
Lambert M. P., 1998, Proc. Natl. Acad. Sci. U.S.A. 95, 6448−6453
Hardy J., 2002, Science 297, 353−356
Oda T., 1995, Exp. Neurol., 136, 31
Klein W. L., 2001, Trends Neurosci. 24, 219−224
Kim H. J., 2003, FASEB J., 17
Harper J. D., 1997, Chem. Biol. 4, 119−125
Kuo Y. M., 1996, J. Biol. Chem., 271
Lue L. F., 1999, Am. J. Pathol., 155
McLean C. A., 1999, Ann. Neurol. 46, 860−866
Westerman M. A., 2002, Soc. Neurosci. Abstr., 28, 690
Gong Y., 2003, Proc. Natl. Acad. Sci. U.S.A. 100, 10417−10422
Greene L. A., 1976, Proc. Natl. Acad. Sci. U.S.A. 73, 2424−2428
Klein W. L., 2002, Int. 41, 345−352.
Stine W. B., Jr., 1996, J. Protein Chem., 15
Betts S., 1999, Methods Enzymol. 309, 333−350
Laemmli U. K., 1970, Nature 227, 680−685
Berg M. M., 1997, J. Neurosci. Res., 50
Chromy B., 2001, Amyloid-Beta-Derived-Diffusible Ligands): A New Theory in Alzheimer's Disease Causation. 1−288
Stine W. B., Jr., 2003, J. Biol. Chem., 278
Lomakin A., 1996, Proc. Natl. Acad. Sci. U.S.A. 93, 1125−1129
Yu J., 2002, J. Mol. Neurosci., 19, 55
Liu Y., 1998, Proc. Natl. Acad. Sci. U.S.A. 95, 13266−13271
Xia Z., 1995, Science 270, 1326−1331
Yao Z., 2001, Brain Res. 889, 181−190
May P. C., 1992, Neurobiol. Aging 13, 605−607
El Agnaf O. M. A., 2001, J. Mol. Biol., 310
Bucciantini M., 2002, Nature 416, 507−511
Conway K. A., 2000, Proc. Natl. Acad. Sci. U.S.A. 97, 571−576
Koo E. H., 1999, Proc. Natl. Acad. Sci. U. S.A. 96, 9989−9990
Harper J. D., 1999, Biochemistry 38, 8972−8980
Schneider S. W., 1998, Pflugers Arch. 435, 362−367
Blackley H. K. L., 2000, J. Mol. Biol., 298
Volles M. J., 2001, Biochemistry 40, 7812−7819
Levine H., 1995, Neurobiol. Aging 16, 755−764
Bitan G., 2003, Proc. Natl. Acad. Sci. U.S.A. 100, 330−335
Tong L., 2001, J. Biol. Chem., 276
Wang H. W., 2002, Brain Res. 924, 133−140
Walsh D. M., 2002, Nature 416, 535−539
Nakayama A. Y., 2000, Hippocampus 10, 582−586
Lacor P. N., 2002, Soc. Neurosci. Abstr., 28, 751
Koistinaho M., 2001, Proc. Natl. Acad. Sci. U.S.A. 98, 14675−14680
Morgan D., 2000, Nature 408, 982−985
Dodart J. C., 2002, Nat. Neurosci. 5, 452−457
Birmingham K., 2002, 8, 199−200
Hock C., 2003, Neuron 38, 547−554
Lim G. P., 2001, Neurobiol. Aging 22, 983−991
Abbreviations Aβ, amyloid beta peptide

Sorted by citations

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
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
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
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
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
Self-citation
Self-assembling peptide and protein amyloids: from structure to tailored function in nanotechnology
Wei, G., Su, Z., Reynolds, N. P., Arosio, P., Hamley, I. W., Gazit, E., & Mezzenga, R. (2017) · Chemical Society Reviews · doi:10.1039/c6cs00542j · Cited by 913
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
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 892
The Amyloid-β Oligomer Hypothesis: Beginning of the Third Decade
Cline, E. N., Bicca, M. A., Viola, K. L., & Klein, W. L. (2018) · Journal of Alzheimer's Disease · doi:10.3233/jad-179941 · Cited by 870
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 881
Self-citation
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
Self-citation
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 715
Self-citation
Small Molecule Inhibitors of Aggregation Indicate That Amyloid β Oligomerization and Fibrillization Pathways Are Independent and Distinct
Necula, M., Kayed, R., Milton, S., & Glabe, C. G. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m608207200 · Cited by 680
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
Self-citation
What is the role of protein aggregation in neurodegeneration?
Ross, C. A., & Poirier, M. A. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1742 · Cited by 623
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 633
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 551
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 543
The significance of the cholinergic system in the brain during aging and in Alzheimer’s disease
Schliebs, R., & Arendt, T. (2006) · Journal of Neural Transmission · doi:10.1007/s00702-006-0579-2 · Cited by 548
Physicochemical Properties of Cells and Their Effects on Intrinsically Disordered Proteins (IDPs)
Theillet, F., Binolfi, A., Frembgen-Kesner, T., Hingorani, K. S., Sarkar, M., Kyne, C., Li, C., Crowley, P. B., Gierasch, L. M., Pielak, G. J., et al. (2014) · Chemical Reviews · doi:10.1021/cr400695p · Cited by 521
Different Conformations of Amyloid β Induce Neurotoxicity by Distinct Mechanisms in Human Cortical Neurons
Deshpande, A. M., Mina, E. W., Glabe, C. G., & Busciglio, J. A. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.1189-06.2006 · Cited by 508
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 494
Self-citation
The Flavonoid Baicalein Inhibits Fibrillation of α-Synuclein and Disaggregates Existing Fibrils
Zhu, M., Rajamani, S., Kaylor, J. J., Han, S., Zhou, F., & Fink, A. L. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m403129200 · Cited by 480
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
Self-citation
Proteases and Proteolysis in Alzheimer Disease: A Multifactorial View on the Disease Process
De Strooper, B. (2010) · Physiological Reviews · doi:10.1152/physrev.00023.2009 · Cited by 455
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
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
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 418
Self-citation
Heat Shock Proteins 70 and 90 Inhibit Early Stages of Amyloid β-(1–42) Aggregation in Vitro
Evans, C. G., Wisén, S., & Gestwicki, J. E. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m606192200 · Cited by 396
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
Self-citation
Amyloid-β and tau complexity — towards improved biomarkers and targeted therapies
Polanco, J. C., Li, C., Bodea, L., Martínez‐Mármol, R., Meunier, F. A., & Götz, J. (2017) · Nature Reviews Neurology · doi:10.1038/nrneurol.2017.162 · Cited by 386
The CAMKK2-AMPK Kinase Pathway Mediates the Synaptotoxic Effects of Aβ Oligomers through Tau Phosphorylation
Mairet-Coello, G., Courchet, J., Pieraut, S., Courchet, V., Maximov, A., & Polleux, F. (2013) · Neuron · doi:10.1016/j.neuron.2013.02.003 · Cited by 351
Amyloid-β Aggregation
Finder, V. H., & Glockshuber, R. (2007) · Neurodegenerative Diseases · doi:10.1159/000100355 · Cited by 367
In silico study of amyloid β-protein folding and oligomerization
Urbanc, B., Cruz, L., Yun, S., Buldyrev, S. V., Bitan, G., Teplow, D. B., & Stanley, E. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0408153101 · Cited by 334
Inflammatory cytokine levels correlate with amyloid load in transgenic mouse models of Alzheimer's disease
Patel, N. S., Paris, D., Mathura, V. S., Quadros, A., Crawford, F., & MULLAN, M. J. (2005) · Journal of Neuroinflammation · doi:10.1186/1742-2094-2-9 · Cited by 335
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
Self-citation
Lipids revert inert Aβ amyloid fibrils to neurotoxic protofibrils that affect learning in mice
Martins, I. C., Kuperstein, I., Wilkinson, H. R., Maes, E., Vanbrabant, M., Jonckheere, W., Gelder, P. V., Hartmann, D., D’Hooge, R., Strooper, B. D., et al. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601953 · Cited by 318
Beta amyloid oligomers and fibrils stimulate differential activation of primary microglia
Sondag, C. M., Dhawan, G., & Combs, C. K. (2009) · Journal of Neuroinflammation · doi:10.1186/1742-2094-6-1 · Cited by 295
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
Copper and Oxidative Stress in the Pathogenesis of Alzheimer’s Disease
Eskici, G., & Axelsen, P. H. (2012) · Biochemistry · doi:10.1021/bi3006169 · Cited by 291
Extracellular Tau Oligomers Produce An Immediate Impairment of LTP and Memory
Fà, M., Puzzo, D., Piacentini, R., Staniszewski, A., Zhang, H., Baltrons, M. A., Puma, D. D. L., Chatterjee, I., Li, J., Saeed, F., et al. (2016) · Scientific Reports · doi:10.1038/srep19393 · Cited by 290
Aβ42 is More Rigid than Aβ40 at the C Terminus: Implications for Aβ Aggregation and Toxicity
Yan, Y., & Wang, C. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.09.046 · Cited by 277
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 263
Hydrogen Peroxide Is Generated during the Very Early Stages of Aggregation of the Amyloid Peptides Implicated in Alzheimer Disease and Familial British Dementia
Tabner, B. J., El‐Agnaf, O. M. A., Turnbull, S., German, M. J., Paleologou, K. E., Hayashi, Y., Cooper, L. J., Fullwood, N. J., & Allsop, D. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.c500238200 · Cited by 243
β-Amyloid-induced Dynamin 1 Degradation Is Mediated by N-Methyl-D-Aspartate Receptors in Hippocampal Neurons
Kelly, B. L., & Ferreira, A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605081200 · Cited by 244
Peptide and Protein Mimetics Inhibiting Amyloid β-Peptide Aggregation
Takahashi, T., & Mihara, H. (2008) · Accounts of Chemical Research · doi:10.1021/ar8000475 · Cited by 244
Nucleation-Dependent Polymerization Is an Essential Component of Amyloid-Mediated Neuronal Cell Death
Wogulis, M., Wright, S., Cunningham, D., Chilcote, T., Powell, K., & Rydel, R. E. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.2381-04.2005 · Cited by 233
Alzheimer's Disease-Like Pathology Induced by Amyloid-β Oligomers in Nonhuman Primates
Forny‐Germano, L., Silva, N. M. L. E., Batista, A. F., Brito‐Moreira, J., Gralle, M., Boehnke, S. E., Coe, B. C., Lablans, A., Marques, S. A., Martinez, A. M. B., et al. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.1353-14.2014 · Cited by 245
Self-citation
Brain and behavior changes in 12-month-old Tg2576 and nontransgenic mice exposed to anesthetics
Bianchi, S. L., Tran, T., Liu, C., Lin, S. S., Li, Y., Keller, J. M., Eckenhoff, R. G., & Eckenhoff, M. F. (2007) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2007.02.009 · Cited by 233
Congo red and thioflavin‐T analogs detect Aβ oligomers
Maezawa, I., Hong, H., Liu, R., Wu, C., Cheng, R. H., Kung, M., Kung, H. F., Lam, K. S., Oddo, S., LaFerla, F. M., et al. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04972.x · Cited by 230
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
Neurotoxic protein oligomers — what you see is not always what you get
Bitan, G., Fradinger, E. A., Spring, S. M., & Teplow, D. B. (2005) · Amyloid · doi:10.1080/13506120500106958 · Cited by 221
Amyloid peptides and proteins in review
Harrison, R. S., Sharpe, P. C., Singh, Y., & Fairlie, D. P. (2007) · Springer eBooks · doi:10.1007/112_2007_0701 · Cited by 222
Zinc-Amyloid β Interactions on a Millisecond Time-Scale Stabilize Non-fibrillar Alzheimer-Related Species
Noy, D., Solomonov, I., Sinkevich, O., Arad, T., Kjær, K., & Sagi, I. (2008) · Journal of the American Chemical Society · doi:10.1021/ja076282l · Cited by 216
Methylene Blue Inhibits Amyloid Aβ Oligomerization by Promoting Fibrillization
Necula, M., Breydo, L., Milton, S., Kayed, R., van der Veer, W. E., Tone, P., & Glabe, C. G. (2007) · Biochemistry · doi:10.1021/bi700411k · Cited by 213
Rapid glycation with D-ribose induces globular amyloid-like aggregations of BSA with high cytotoxicity to SH-SY5Y cells
Yan, W., Chen, L., Chen, J., Ge, L., & He, R. Q. (2009) · BMC Cell Biology · doi:10.1186/1471-2121-10-10 · Cited by 208
Neuronal amyloid-β accumulation within cholinergic basal forebrain in ageing and Alzheimer’s disease
Baker‐Nigh, A., Vahedi, S., Davis, E., Weıntraub, S., Bigio, E. H., Klein, W. L., & Geula, C. (2015) · Brain · doi:10.1093/brain/awv024 · Cited by 211
Self-citation
Lysozyme Amyloid Oligomers and Fibrils Induce Cellular Death via Different Apoptotic/Necrotic Pathways
Gharibyan, A. L., Zamotin, V., Yanamandra, K., Moskaleva, O. S., Margulis, B. A., Kostanyan, I. A., & Morozova‐Roche, L. A. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.10.101 · Cited by 209
Drusen deposits associated with aging and age-related macular degeneration contain nonfibrillar amyloid oligomers
Luibl, V. (2006) · Journal of Clinical Investigation · doi:10.1172/jci25843 · Cited by 203
EGb 761 enhances adult hippocampal neurogenesis and phosphorylation of CREB in transgenic mouse model of Alzheimer's disease
Tchantchou, F., Xu, Y., Wu, Y., Christen, Y., & Luo, Y. (2007) · The FASEB Journal · doi:10.1096/fj.06-7649com · Cited by 203
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 201
Self-citation
A label-free electrical impedimetric biosensor for the specific detection of Alzheimer's amyloid-beta oligomers
Rushworth, J. V., Ahmed, A., Jarosz-Griffiths, H., Pollock, N. M., Hooper, N. M., & Millner, P. A. (2013) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2013.12.036 · Cited by 200
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 196
Self-citation
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
Self-citation
The role of insulin and neurotrophic factor signaling in brain aging and Alzheimer’s Disease
Cole, G. M., & Frautschy, S. A. (2006) · Experimental Gerontology · doi:10.1016/j.exger.2006.08.009 · Cited by 193
Exosomes neutralize synaptic-plasticity-disrupting activity of Aβ assemblies in vivo
An, K., Klyubin, I. V., Kim, Y., Jung, J. H., Mably, A. J., O’Dowd, S., Lynch, T., Kanmert, D., Lemere, C. A., Finan, G. M., et al. (2013) · Molecular Brain · doi:10.1186/1756-6606-6-47 · Cited by 196
Curcumin Attenuates Amyloid-β Aggregate Toxicity and Modulates Amyloid-β Aggregation Pathway
Thapa, A., Jett, S. D., & Chi, E. Y. (2015) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.5b00214 · Cited by 188
A Sensitive Aβ Oligomer Assay Discriminates Alzheimer's and Aged Control Cerebrospinal Fluid
Savage, M. J., Kalinina, J., Wolfe, A. L., Tugusheva, K., Korn, R., Cash-Mason, T., Maxwell, J. W., Hatcher, N. G., Haugabook, S. J., Wu, G., et al. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.1675-13.2014 · Cited by 187
SUMO on the road to neurodegeneration
Dorval, V., & Fraser, P. E. (2007) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2007.03.017 · Cited by 188
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
Self-citation
Actin dynamics and cofilin‐actin rods in alzheimer disease
Bamburg, J. R., & Bernstein, B. W. (2016) · Cytoskeleton · doi:10.1002/cm.21282 · Cited by 181
Structural features and cytotoxicity of amyloid oligomers: Implications in Alzheimer's disease and other diseases with amyloid deposits
Stefani, M. (2012) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2012.03.002 · Cited by 175
Structural, morphological, and functional diversity of amyloid oligomers
Breydo, L., & Uversky, V. N. (2015) · FEBS Letters · doi:10.1016/j.febslet.2015.07.013 · Cited by 177
Metformin activates chaperone-mediated autophagy and improves disease pathologies in an Alzheimer disease mouse model
Xu, X., Sun, Y., Cen, X., Shan, B., Zhao, Q., Xie, T., Wang, Z., Hou, T., Xue, Y., Zhang, M., et al. (2021) · Protein & Cell · doi:10.1007/s13238-021-00858-3 · Cited by 171
How Do Membranes Initiate Alzheimer’s Disease? Formation of Toxic Amyloid Fibrils by the Amyloid β-Protein on Ganglioside Clusters
Matsuzaki, K. (2014) · Accounts of Chemical Research · doi:10.1021/ar500127z · Cited by 173
Methionine oxidation, α-synuclein and Parkinson's disease
Glaser, C. B., Yamin, G., Uversky, V. N., & Fink, A. L. (2004) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2004.10.008 · Cited by 180
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
Identical oligomeric and fibrillar structures captured from the brains of R6/2 and knock-in mouse models of Huntington's disease
Sathasivam, K., Lane, A., Legleiter, J. A., Warley, A., Woodman, B., Finkbeiner, S. M., Paganetti, P., Muchowski, P. J., Wilson, S., & Bates, G. P. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp467 · Cited by 166
Artificial Peptide-Nanospheres Self-Assembled from Three-Way Junctions of β-Sheet-Forming Peptides
Matsuura, K., Murasato, K., & Kimizuka, N. (2005) · Journal of the American Chemical Society · doi:10.1021/ja052644i · Cited by 157
Noradrenaline activation of neurotrophic pathways protects against neuronal amyloid toxicity
Counts, S., & Mufson, E. J. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.06622.x · Cited by 160
Modification of nanostructured materials for biomedical applications
Xu, T., Zhang, N., Nichols, H. L., Shi, D., & Wen, X. (2006) · Materials Science and Engineering C · doi:10.1016/j.msec.2006.05.029 · Cited by 155
Kinetics of amyloid formation and membrane interaction with amyloidogenic proteins
Murphy, R. M. (2007) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2006.12.014 · Cited by 157
Prion Protein-mediated Toxicity of Amyloid-β Oligomers Requires Lipid Rafts and the Transmembrane LRP1
Rushworth, J. V., Jarosz-Griffiths, H., Watt, N. T., & Hooper, N. M. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.400358 · Cited by 157
Large Aggregates Are the Major Soluble Aβ Species in AD Brain Fractionated with Density Gradient Ultracentrifugation
Sehlin, D., Englund, H., Simu, B., Karlsson, M., Ingelsson, M., Nikolajeff, F. K., Lannfelt, L., & Pettersson, F. E. (2012) · PLoS ONE · doi:10.1371/journal.pone.0032014 · Cited by 150
Amyloid β oligomers (AβOs) in Alzheimer’s disease
Mroczko, B., Groblewska, M., Litman‐Zawadzka, A., Kornhuber, J., & Lewczuk, P. (2017) · Journal of Neural Transmission · doi:10.1007/s00702-017-1820-x · Cited by 150
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 147
Endo-lysosomal Aβ concentration and pH trigger formation of Aβ oligomers that potently induce Tau missorting
Schützmann, M. P., Hasecke, F., Bachmann, S., Zielinski, M., Hänsch, S., Schroeder, G. F., Zempel, H., & Hoyer, W. (2021) · Nature Communications · doi:10.1038/s41467-021-24900-4 · Cited by 152
Capturing Intermediate Structures of Alzheimer's β-Amyloid, Aβ(1−40), by Solid-State NMR Spectroscopy
Chimon, S., & Ishii, Y. (2005) · Journal of the American Chemical Society · doi:10.1021/ja054039l · Cited by 143
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
Self-citation
Fine structure study of Aβ 1–42 fibrillogenesis with atomic force microscopy
Arimon, M., Díez‐Pérez, I., Kogan, M. J., Durany, N., Giralt, E., Sanz, F., & Fernàndez‐Busquets, X. (2005) · The FASEB Journal · doi:10.1096/fj.04-3137fje · Cited by 141
Can herbs provide a new generation of drugs for treating Alzheimer’s disease?
Anekonda, T. S., & Reddy, P. H. (2005) · Brain Research Reviews · doi:10.1016/j.brainresrev.2005.09.001 · Cited by 140
Zinc ion rapidly induces toxic, off-pathway amyloid-β oligomers distinct from amyloid-β derived diffusible ligands in Alzheimer’s disease
Lee, M., Yu, W., Shih, Y., Chen, C., Guo, Z., Huang, S., Chan, J. C. C., & Chen, Y. (2018) · Scientific Reports · doi:10.1038/s41598-018-23122-x · Cited by 141
Cholesterol in Alzheimers Disease: Unresolved Questions
Stefani, M., & Liguri, G. (2009) · Current Alzheimer Research · doi:10.2174/156720509787313899 · Cited by 136
Structural properties of Aβ protofibrils stabilized by a small molecule
Williams, A. D., Sega, M., Chen, M., Kheterpal, I., Geva, M., Berthelier, V., Kaleta, D. T., Cook, K. D., & Wetzel, R. B. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0408582102 · Cited by 133
β-Secretase-Cleaved Amyloid Precursor Protein Accumulates at Actin Inclusions Induced in Neurons by Stress or Amyloid β: A Feedforward Mechanism for Alzheimer's Disease
Maloney, M. T., Minamide, L. S., Kinley, A. W., Boyle, J. A., & Bamburg, J. R. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.3711-05.2005 · Cited by 140
p21-activated Kinase-aberrant Activation and Translocation in Alzheimer Disease Pathogenesis
Ma, Q., Yang, F., Calon, F., Ubeda, O. J., Hansen, J. E., Weisbart, R. H., Beech, W. K., Frautschy, S. A., & Cole, G. M. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m708034200 · Cited by 131
In vitro neuroprotective effects of naringenin nanoemulsion against β-amyloid toxicity through the regulation of amyloidogenesis and tau phosphorylation
Md, S., Gan, S. Y., Haw, Y. H., Ho, C. L., Wong, S., & Choudhury, H. (2018) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2018.06.190 · Cited by 134
Physicochemical characteristics of soluble oligomeric Aβand their pathologic role in Alzheimer's disease
Watson, D., Castaño, E., Kokjohn, T. A., Kuo, Y., Lyubchenko, Y. L., Pinsky, D. J., Connolly, E. S., Esh, C. L., Luehrs, D. C., Stine, W. B., et al. (2005) · Neurological Research · doi:10.1179/016164105x49436 · Cited by 129
Reactivity of Apolipoprotein E4 and Amyloid β Peptide
Ji, Z.-S., Müllendorff, K., Cheng, I. H., Miranda, R. D., Huang, Y., & Mahley, R. W. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m506646200 · Cited by 127
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

Authors: 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., Finch, C. E., Krafft, G. A., & Klein, W. L.
Affiliations: Northwestern University (US)
Corresponding author: Klein, William L.
ORCID: Nowak, Richard J.
Viola, Kirsten L.
Chang, Lei
Horowitz, Peleg
Finch, Caleb E.
Klein, William L.
Venue: Biochemistry
Publisher: American Chemical Society (ACS)
Published: 2003-10-17
Volume: 42
Issue: 44
Pages: 12749-12760
ISSN: 0006-2960 (ISSN-L)
1520-4995
DOI: 10.1021/bi030029q
OpenAlex: W1964741226
Cited by: 522
References: 28
Citations by year: 2026: 10 · 2025: 11 · 2024: 10 · 2023: 11 · 2022: 18 · 2021: 11 · 2020: 12 · 2019: 8 · 2018: 17 · 2017: 19 · 2016: 10 · 2015: 26 · 2014: 26 · 2013: 33 · 2012: 37
FWCI: 15.33
Type: journal article
Language: en
Open access: closed
Locations: Biochemistry (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health (1p01ag015501-01)
National Institute on Aging (P01-AG15501, R01-AG18877, R01AG018877)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
Keywords: amyloid-beta 42, peptide self-assembly, oligomerization, Alzheimer's disease, ERK signaling, Rac signaling, oligomer conformation
MeSH terms: Animals, Epitopes, Body Temperature, Cell Survival, Diffusion, Humans, Ligands, Neurotoxins, Nitroblue Tetrazolium, Peptide Fragments, Plant Extracts, Protein Conformation, Amyloid beta-Peptides, PC12 Cells, Neuroprotective Agents, Ginkgo biloba, Rats

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Self-Assembly of Aβ 1 - 42 into Globular Neurotoxins

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks