The DOI matches its Crossref record; 68 of the 68 references it cites were found in a registry or an index.
Diffusible, nonfibrillar ligands derived from Aβ 1–42 are potent central nervous system neurotoxins
Open accessAbstract
Abeta1-42 is a self-associating peptide whose neurotoxic derivatives are thought to play a role in Alzheimer's pathogenesis. Neurotoxicity of amyloid beta protein (Abeta) has been attributed to its fibrillar forms, but experiments presented here characterize neurotoxins that assemble when fibril formation is inhibited. These neurotoxins comprise small diffusible Abeta oligomers (referred to as ADDLs, for Abeta-derived diffusible ligands), which were found to kill mature neurons in organotypic central nervous system cultures at nanomolar concentrations. At cell surfaces, ADDLs bound to trypsin-sensitive sites and surface-derived tryptic peptides blocked binding and afforded neuroprotection. Germ-line knockout of Fyn, a protein tyrosine kinase linked to apoptosis and elevated in Alzheimer's disease, also was neuroprotective. Remarkably, neurological dysfunction evoked by ADDLs occurred well in advance of cellular degeneration. Without lag, and despite retention of evoked action potentials, ADDLs inhibited hippocampal long-term potentiation, indicating an immediate impact on signal transduction. We hypothesize that impaired synaptic plasticity and associated memory dysfunction during early stage Alzheimer's disease and severe cellular degeneration and dementia during end stage could be caused by the biphasic impact of Abeta-derived diffusible ligands acting upon particular neural signal transduction pathways.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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?
In the citing paper
“However, recent in vivo studies have shown that soluble Aβ oligomers are more neurotoxic than amyloid plaques and most likely responsible for synaptic dysfunction and memory loss in AD.7–11”
From The effect of Cu2+ and Zn2+ on the Aβ42 peptide aggregation and cellular toxicity (2013) · cites this paper as [10]
In the citing paper
“However, recent in vivo studies have shown that the soluble Aβ oligomers are possibly more neurotoxic than amyloid plaques,14–17 and are likely responsible for synaptic dysfunction and memory loss in AD patients and AD animal models.18–21”
From Bifunctional Compounds for Controlling Metal-Mediated Aggregation of the Aβ42Peptide (2012) · cites this paper as [14]
In the citing paper
“recent studies have shown that the soluble Aβ oligomers are more neurotoxic both in vitro and in vivo.5−8”
From Small Bifunctional Chelators That Do Not Disaggregate Amyloid β Fibrils Exhibit Reduced Cellular Toxicity (2014) · cites this paper as [7]
In the citing paper
“For the preformed Aβ42 fibrils, no significant cell toxicity was observed in either the absence or presence of Cu2+ (Figure 9, lanes 1 and 2), supporting the previously reported diminished toxicity of Aβ42 fibrils.5,7,54−56”
From Small Bifunctional Chelators That Do Not Disaggregate Amyloid β Fibrils Exhibit Reduced Cellular Toxicity (2014) · cites this paper as [7]
In the citing paper
“This function may be critical in controlling Aβ deposition as well as levels of potentially neurotoxic Aβ oligomers (Lambert et al., 1998).”
From CX3CR1 in Microglia Regulates Brain Amyloid Deposition through Selective Protofibrillar Amyloid-β Phagocytosis (2010) · cites this paper as Lambert et al., 1998
In the citing paper
“While Aβ disrupts synaptic transmission 32,34,35 and induces synapse loss 17”
From NAD+ hydrolase Sarm1 is a key driver of synapse degeneration and memory loss in Alzheimer’s disease (2025) · cites this paper as [34]
In the citing paper
“In vitro, apoE and apoJ form stable complexes with A (11, 16 -20), alter the aggregation of various A peptides (21)(22)(23), and affect A neurotoxicity (24 -27).”
From Apolipoprotein E Receptors Mediate the Effects of β-Amyloid on Astrocyte Cultures (2000) · cites this paper as [27]
In the citing paper
“A 1-42 aged according to this protocol is a mixture of fibrils and soluble globular aggregates, and is active to astrocytes (37,38) and toxic to neurons (26,27).”
From Apolipoprotein E Receptors Mediate the Effects of β-Amyloid on Astrocyte Cultures (2000) · cites this paper as [27]
In the citing paper
“ApoJ has been shown to potentiate the formation of a neurotoxic species of A (26,27).”
From Apolipoprotein E Receptors Mediate the Effects of β-Amyloid on Astrocyte Cultures (2000) · cites this paper as [27]
In the citing paper
“ApoE, apoJ, and most recently ␣ 2 -macroglobulin have been shown to form a complex with A that may facilitate clearance of the peptide (25-27, 50, 51).”
From Apolipoprotein E Receptors Mediate the Effects of β-Amyloid on Astrocyte Cultures (2000) · cites this paper as [27]
In the citing paper
“Evidence suggests that increased uptake of these neurotoxic Aβ42 peptides results in accumulation and aggregation within neurons eventually leading the formation of plaques and neuronal death [40, 41].”
From The Sigma-2 Receptor/TMEM97, PGRMC1, and LDL Receptor Complex Are Responsible for the Cellular Uptake of Aβ42 and Its Protein Aggregates (2020) · cites this paper as [41]
In the citing paper
“Most importantly, these amyloid-free Aβ oligomers were potent CNS neurotoxins.”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Lambert et al., 1998
In the citing paper
“With chronic exposure, neurons ultimately were killed. Death was selective for subpopulations of vulnerable neurons and was prevented by knockout of Fyn, a protein tyrosine kinase linked to NMDA receptor signaling.”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Lambert et al., 1998
In the citing paper
“Investigation into the action of clusterin by Lambert, Klein and colleagues established that, concomitant with inhibition of amyloid formation, clusterin promotes accumulation of soluble Aβ oligomers (Lambert et al., 1998).”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Lambert et al., 1998
In the citing paper
“oligomers were found to inhibit functional synaptic plasticity (Lambert et al., 1998). Long-term potentiation (LTP) was inhibited within minutes. This rapid loss of LTP, measured in rat brain slices and in situ in mice, occurred without impact on baseline excitability, indicating impairment of signaling rather than degeneration.”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Lambert et al., 1998
In the citing paper
“In hippocampal slices, synthetic oligomers cause rapid LTP inhibition (Barghorn et al., 2005; Fa et al., 2010; Jurgensen et al., 2011; Lambert et al., 1998; Nimmrich et al., 2008; Rammes et al., 2011; Wang et al., 2002).”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Lambert et al., 1998
In the citing paper
“early studies showed that binding is lost upon controlled trypsin treatment of neurons (Lambert et al., 1998).”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Lambert et al., 1998
In the citing paper
“In vitro and in vivo studies have now indicated that soluble Aβ oligomers impair synaptic plasticity, inhibiting hippocampal long-term potentiation (LTP), the electrophysiological correlate of learning and memory (3 –6).”
From Synthetic amyloid-β oligomers impair long-term memory independently of cellular prion protein (2010) · cites this paper as [3]
Citations
Cites
Mass Spectrometric Sequencing of Proteins from Silver-Stained Polyacrylamide Gels
Shevchenko, A., Wilm, M. S., Vorm, O., & Mann, M. (1996) · Analytical Chemistry · doi:10.1021/ac950914h · Cited by 8,996
Terry, R. D., Masliah, E., Salmon, D. P., Butters, N., DeTeresa, R., Hill, R., Hansen, L. A., & Katzman, R. (1991) · Annals of Neurology · doi:10.1002/ana.410300410 · Cited by 4,397
Strittmatter, W. J., Saunders, A. M., Schmechel, D., Pericak-Vance, M., Enghild, J., Salvesen, G. S., & Roses, A. D. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.5.1977 · Cited by 4,268
Correlative Memory Deficits, Aβ Elevation, and Amyloid Plaques in Transgenic Mice
Hsiao, K., Chapman, P., Nilsen, S., Eckman, C., Harigaya, Y., Younkin, S., Yang, F., & Cole, G. (1996) · Science · doi:10.1126/science.274.5284.99 · Cited by 4,210
A simple method for organotypic cultures of nervous tissue
Stoppini, L., Buchs, P., & Muller, D. (1991) · Journal of Neuroscience Methods · doi:10.1016/0165-0270(91)90128-m · Cited by 3,096
Integrins and Signal Transduction Pathways: the Road Taken
Clark, E. A., & Brugge, J. S. (1995) · Science · doi:10.1126/science.7716514 · Cited by 2,911
Scheuner, D., Eckman, C., Jensen, M., Song, X., Citron, M., Suzuki, N., Bird, T. D., Hardy, J., Hutton, M., Kukull, W., et al. (1996) · Nature Medicine · doi:10.1038/nm0896-864 · Cited by 2,599
Jarrett, J. T., Berger, E. P., & Lansbury, P. T. (1993) · Biochemistry · doi:10.1021/bi00069a001 · Cited by 2,022
RAGE and amyloid-β peptide neurotoxicity in Alzheimer's disease
Yan, S. D., Chen, X., Fu, J., Chen, M., Zhu, H., Roher, A., Slattery, T., Zhao, L., Nagashima, M., Morser, J., et al. (1996) · Nature · doi:10.1038/382685a0 · Cited by 2,012
Neurotrophic and Neurotoxic Effects of Amyloid β Protein: Reversal by Tachykinin Neuropeptides
Yankner, B. A., Duffy, L. K., & Kirschner, D. A. (1990) · Science · doi:10.1126/science.2218531 · Cited by 1,975
Flagged first, then by citations
Research works printed but not linked: 2
- B Leveugle, A Scanameo, W Ding, H Fillit NeuroReport 5, 1389–1392 (1994).
- 10.1146/annurev.bi.63.070194.003125 · DOI
Cited by
Sorted by citations
Items 501–600 of 1,060
Haes, A. J., & Duyne, R. P. V. (2004) · Expert Review of Molecular Diagnostics · doi:10.1586/14737159.4.4.527 · Cited by 181
Heredia, L., Helguera, P. R., de Olmos, S., Kedikian, G., Vigo, F. S., LaFerla, F. M., Staufenbiel, M., de Olmos, J. S., Busciglio, J. A., Cáceres, A., et al. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.5567-05.2006 · Cited by 184
Fluid Biomarkers for Synaptic Dysfunction and Loss
Camporesi, E., Nilsson, J., Brinkmalm, A., Becker, B., Ashton, N. J., Blennow, K., & Zetterberg, H. (2020) · Biomarker Insights · doi:10.1177/1177271920950319 · Cited by 165
Kumar, S., & Walter, J. (2011) · Aging · doi:10.18632/aging.100362 · Cited by 191
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 191
Yao, Z., Drieu, K., & Papadopoulos, V. (2001) · Brain Research · doi:10.1016/s0006-8993(00)03131-0 · Cited by 181
DeMattos, R. B., Brendza, R. P., Heuser, J. E., Kierson, M., Cirrito, J. R., Fryer, J., Sullivan, P. M., Fagan, A. M., Han, X., & Holtzman, D. M. (2001) · Neurochemistry International · doi:10.1016/s0197-0186(01)00049-3 · Cited by 180
Oliveira, T. G., Chan, R., Tian, H., Laredo, M., Shui, G., Staniszewski, A., Zhang, H., Wang, L., Kim, T., Duff, K., et al. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.3317-10.2010 · Cited by 179
Persistent remodeling and neurodegeneration in late-stage retinal degeneration
Pfeiffer, R. L., Marc, R. E., & Jones, B. W. (2019) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2019.07.004 · Cited by 184
Size-dependent neurotoxicity of β-amyloid oligomers
Čižas, P., Budvytytė, R., Morkūnienė, R., Moldovan, R., Broccio, M., Lösche, M., Niaura, G., Valinčius, G., & Borutaitė, V. (2010) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2010.02.001 · Cited by 186
Hoey, S. E., Williams, R. J., & Perkinton, M. S. (2009) · The Journal of Neuroscience · doi:10.1523/jneurosci.6017-08.2009 · Cited by 178
Mechanisms of Pathogenic Tau and Aβ Protein Spreading in Alzheimer’s Disease
d’Errico, P., & Meyer‐Luehmann, M. (2020) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.00265 · Cited by 191
In-situ atomic force microscopy study of β-amyloid fibrillization
Blackley, H. K. L., Sanders, G. H. W., Davies, M. C., Roberts, C. J., Tendler, S. J. B., & Wilkinson, M. J. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.3711 · Cited by 179
Low PiB PET retention in presence of pathologic CSF biomarkers in Arctic APP mutation carriers
Schöll, M., Wall, A., Thordardottir, S., Ferreira, D., Bogdanovic, N., Långström, B., Almkvist, O., Graff, C., & Nordberg, A. (2012) · Neurology · doi:10.1212/wnl.0b013e31825fdf18 · Cited by 169
Lewy Body Pathology in Alzheimer's Disease
Kotzbauer, P. T., Tojanowski, J. Q., & Lee, V. M. V. (2001) · Journal of Molecular Neuroscience · doi:10.1385/jmn:17:2:225 · Cited by 177
Ji, Z.-S., Miranda, R. D., Newhouse, Y. M., Weisgraber, K. H., Huang, Y., & Mahley, R. W. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m112109200 · Cited by 177
Stefani, M. (2012) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2012.03.002 · Cited by 175
Aβ42-Peptide Assembly on Lipid Bilayers
Yip, C. M., Darabie, A. A., & McLaurin, J. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00028-1 · Cited by 176
β-Amyloid Immunotherapy Prevents Synaptic Degeneration in a Mouse Model of Alzheimer's Disease
Buttini, M., Masliah, E., Barbour, R., Grajeda, H., Motter, R., Johnson-Wood, K., Khan, K., Seubert, P., Freedman, S., Schenk, D., et al. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.1697-05.2005 · Cited by 176
Transthyretin and familial amyloidotic polyneuropathy
Hou, X., Aguilar, M., & Small, D. H. (2007) · FEBS Journal · doi:10.1111/j.1742-4658.2007.05712.x · Cited by 178
Pereira Diniz, L., Tortelli, V., Matias, I., Morgado, J., Bérgamo Araujo, A. P., Melo, H. M., Seixas da Silva, G. S., Alves-Leon, S. V., de Souza, J. M., Ferreira, S. T., et al. (2017) · The Journal of Neuroscience · doi:10.1523/jneurosci.3351-16.2017 · Cited by 171
Bouter, Y., Dietrich, K., Wittnam, J. L., Rezaei-Ghaleh, N., Pillot, T., Papot-Couturier, S., Lefebvre, T., Sprenger, F., Wirths, O., Zweckstetter, M., et al. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1129-2 · Cited by 175
Perez-Cruz, C., Nolte, M. W., van Gaalen, M. M., Rustay, N. R., Termont, A., Tanghe, A., Kirchhoff, F., & Ebert, U. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.6142-10.2011 · Cited by 172
Lu, J., Ardah, M. T., Durairajan, S. S. K., Liu, L., Xie, L., Fong, W. F., Hasan, M. Y., Huang, J., El‐Agnaf, O. M. A., & Li, M. (2011) · ChemBioChem · doi:10.1002/cbic.201000604 · Cited by 180
Behavioral phenotypes of amyloid‐based genetically modified mouse models of Alzheimer's disease
Kobayashi, D. T., & Chen, K. S. (2005) · Genes Brain & Behavior · doi:10.1111/j.1601-183x.2005.00124.x · Cited by 182
Kapurniotu, A., Schmauder, A., & Tenidis, K. (2002) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.5244 · Cited by 173
Ambroggio, E. E., Kim, D. H., Separovic, F., Barrow, C. J., Barnham, K. J., Bagatolli, L. A., & Fidelio, G. D. (2005) · Biophysical Journal · doi:10.1529/biophysj.104.055582 · Cited by 174
The Role of Clusterin in Alzheimer’s Disease: Pathways, Pathogenesis, and Therapy
Yu, J.-T., & Tan, L. (2012) · Molecular Neurobiology · doi:10.1007/s12035-012-8237-1 · Cited by 174
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
Approaches to discovery and characterization of inhibitors of amyloid β-peptide polymerization
Findeis, M. A. (2000) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/s0925-4439(00)00034-x · Cited by 175
Jan, A., Adolfsson, O., Allaman, I., Buccarello, A. L., Magistretti, P. J., Pfeifer, A., Muhs, A., & Lashuel, H. A. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.172411 · Cited by 179
NELSON, R., GUO, Z., HALAGAPPA, V, PEARSON, M., GRAY, A., MATSUOKA, Y., BROWN, M., MARTIN, B., IYUN, T., & MAUDSLEY, S. (2007) · Experimental Neurology · doi:10.1016/j.expneurol.2007.01.037 · Cited by 173
Noguchi, A., Matsumura, S., Dezawa, M., Tada, M., Yanazawa, M., Ito, A., Akioka, M., Kikuchi, S., Sato, M., Ideno, S., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.000208 · Cited by 173
Small-molecule sequestration of amyloid-β as a drug discovery strategy for Alzheimer’s disease
Heller, G. T., Aprile, F. A., Michaels, T. C. T., Limbocker, R., Perni, M., Ruggeri, F. S., Mannini, B., Löhr, T., Bonomi, M., Camilloni, C., et al. (2020) · Science Advances · doi:10.1126/sciadv.abb5924 · Cited by 166
Jin, T., Gu, Y., Zanusso, G., Sy, M., Kumar, A., Cohen, M. L., Gambetti, P. L., & Singh, N. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m005543200 · Cited by 173
Hu, N., Klyubin, I. V., Anwyl, R., & Rowan, M. J. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0908083106 · Cited by 176
Targeting amyloid clearance in Alzheimer's disease as a therapeutic strategy
Nalivaeva, N. N., & Turner, A. J. (2019) · British Journal of Pharmacology · doi:10.1111/bph.14593 · Cited by 177
Rapid Self-assembly of α-Synuclein Observed by In Situ Atomic Force Microscopy
Hoyer, W., Cherny, D., Subramaniam, V., & Jovin, T. M. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.04.051 · Cited by 172
NMDA- and β-Amyloid1–42-Induced Neurotoxicity Is Attenuated in Serine Racemase Knock-Out Mice
Inoue, R., Hashimoto, K., Harai, T., & Mori, H. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.5034-08.2008 · Cited by 171
Cytoskeletal pathologies of Alzheimer disease
Bamburg, J. R., & Bloom, G. S. (2009) · Cell Motility and the Cytoskeleton · doi:10.1002/cm.20388 · Cited by 175
Deregulation of excitatory neurotransmission underlying synapse failure in Alzheimer's disease
Paula‐Lima, A. C., Brito‐Moreira, J., & Ferreira, S. T. (2013) · Journal of Neurochemistry · doi:10.1111/jnc.12304 · Cited by 170
Neuroplasticity in Alzheimer's disease
Teter, B., & Ashford, J. W. (2002) · Journal of Neuroscience Research · doi:10.1002/jnr.10441 · Cited by 170
Rival, T., Page, R. M., Chandraratna, D. S., Sendall, T. J., Ryder, E. J., Liu, B., Lewis, H. D., Rosahl, T. W., Hider, R. C., Camargo, L. M., et al. (2009) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2009.06701.x · Cited by 171
A SAXS Study of Glucagon Fibrillation
Oliveira, C. L. P., Behrens, M. A., Pedersen, J. S., Erlacher, K., Otzen, D. E., & Pedersen, J. S. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.01.020 · Cited by 170
Amyloid-β signals through tau to drive ectopic neuronal cell cycle re-entry in Alzheimer's disease
Seward, M. E., Swanson, E., Norambuena, A., Reimann, A., Cochran, J. N., Li, R., Roberson, E. D., & Bloom, G. S. (2013) · Journal of Cell Science · doi:10.1242/jcs.1125880 · Cited by 178
Brouillette, J., Caillierez, R., Zommer, N., Pires, C. A., Benilova, I., Blum, D. L., Strooper, B. D., & Buée, L. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.5901-11.2012 · Cited by 186
Matsuzaki, K. (2014) · Accounts of Chemical Research · doi:10.1021/ar500127z · Cited by 173
Alzheimer's disease as a disorder of mechanisms underlying structural brain self-organization
Arendt, T. (2001) · Neuroscience · doi:10.1016/s0306-4522(00)00516-9 · Cited by 172
A High-Throughput Screen for Compounds That Inhibit Aggregation of the Alzheimer’s Peptide
Kim, W., Kim, Y., Min, J., Kim, D. J., Chang, Y., & Hecht, M. H. (2006) · ACS Chemical Biology · doi:10.1021/cb600135w · Cited by 169
Verdile, G. (2004) · Pharmacological Research · doi:10.1016/j.phrs.2003.12.028 · Cited by 181
Broersen, K., Rousseau, F., & Schymkowitz, J. (2010) · Alzheimer's Research & Therapy · doi:10.1186/alzrt36 · Cited by 168
Askanas (2006) · doi:10.1212/01.wnl.0000192128.13875.1e · Cited by 168
Decker, H., Jürgensen, S., Adrover, M. F., Brito‐Moreira, J., Bomfim, T. R., Klein, W. L., Epstein, A. L., Felice, F. G. D., Jerusalinsky, D. A., & Ferreira, S. T. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.07058.x · Cited by 172
Self-citationSyme, C. D., & Viles, J. H. (2005) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2005.09.012 · Cited by 167
Integrins in synapse regulation
Park, Y. K., & Goda, Y. (2016) · Nature Reviews Neuroscience · doi:10.1038/nrn.2016.138 · Cited by 167
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 166
Lee, G. S., & Leugers, C. J. (2012) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-385883-2.00004-7 · Cited by 173
Klementiev, B., Novikova, T. A., Novitskaya, V., Walmod, P. S., Dmytriyeva, O., Pakkenberg, B., Berezin, V., & Bock, E. (2007) · Neuroscience · doi:10.1016/j.neuroscience.2006.11.060 · Cited by 166
The Proton-Pump Inhibitor Lansoprazole Enhances Amyloid Beta Production
Badiola, N., Alcalde, V., Pujol, A., Munter, L. M., Multhaup, G., Lleó, A., Coma, M., Soler‐López, M., & Aloy, P. (2013) · PLoS ONE · doi:10.1371/journal.pone.0058837 · Cited by 171
Designing Peptide Inhibitors for Oligomerization and Toxicity of Alzheimer's β-Amyloid Peptide
Austen, B., Paleologou, K. E., Ali, S. A. E., Qureshi, M. M., Allsop, D., & El‐Agnaf, O. M. A. (2008) · Biochemistry · doi:10.1021/bi701415b · Cited by 170
Conformation‐Dependent Anti‐Amyloid Oligomer Antibodies
Kayed, R., & Glabe, C. G. (2006) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(06)13017-7 · Cited by 167
Panicker, N., Saminathan, H., Jin, H., Neal, M., Harischandra, D. S., Gordon, R., Kanthasamy, K. A., Lawana, V., Sarkar, S., Luo, J. D., et al. (2015) · Journal of Neuroscience · doi:10.1523/jneurosci.0302-15.2015 · Cited by 166
Development of indole-3-propionic acid (OXIGON™) for alzheimer’s disease
Bendheim, P. E., Pöeggeler, B., Neria, E., Ziv, V., Pappolla, M. A., & Chain, D. G. (2002) · Journal of Molecular Neuroscience · doi:10.1007/s12031-002-0036-0 · Cited by 165
Secondary nucleation and elongation occur at different sites on Alzheimer’s amyloid-β aggregates
Scheidt, T., Łapińska, U., Kumita, J. R., Whiten, D. R., Klenerman, D., Wilson, M. R., Cohen, S. I. A., Linse, S. S., Vendruscolo, M., Dobson, C. M., et al. (2019) · Science Advances · doi:10.1126/sciadv.aau3112 · Cited by 156
Apolipoprotein E and cholesterol in aging and disease in the brain
de Chaves, E. P., Narayanaswami, V., Christoffersen, C., & Nielsen, L. B. (2008) · Future Lipidology · doi:10.2217/17460875.3.5.505 · Cited by 164
Alzheimer disease therapy: Can the amyloid cascade be halted?
Golde, T. E. (2003) · Journal of Clinical Investigation · doi:10.1172/jci17527 · Cited by 164
Rammes, G., Hasenjäger, A., Sroka-Saidi, K., Deussing, J. M., & Parsons, C. G. (2011) · Neuropharmacology · doi:10.1016/j.neuropharm.2011.01.051 · Cited by 163
Tchantchou, F., Lacor, P. N., Cao, Z., Lao, L., Hou, Y., Cui, C., Klein, W. L., & Luo, Y. (2009) · Journal of Alzheimer s Disease · doi:10.3233/jad-2009-1189 · Cited by 164
Self-citationKanmert, D., Cantlon, A., Muratore, C., Jin, M., O’Malley, T. T., Lee, G. S., Young‐Pearse, T. L., Selkoe, D. J., & Walsh, D. M. (2015) · Journal of Neuroscience · doi:10.1523/jneurosci.0387-15.2015 · Cited by 169
Crimins, J. L., Pooler, A. M., Polydoro, M., Luebke, J. I., & Spires‐Jones, T. L. (2013) · Ageing Research Reviews · doi:10.1016/j.arr.2013.03.002 · Cited by 173
Taylor, M., Moore, S., Mayes, J., Parkin, E. T., Beeg, M., Canovi, M., Gobbi, M., Mann, D. M. A., & Allsop, D. (2010) · Biochemistry · doi:10.1021/bi100144m · Cited by 166
Targeting Fyn Kinase in Alzheimer’s Disease
Nygaard, H. B. (2018) · Biological Psychiatry · doi:10.1016/j.biopsych.2017.06.004 · Cited by 162
Disrupting β-Amyloid Aggregation for Alzheimer Disease Treatment
Estrada, L. D., & Soto, C. A. (2006) · Current Topics in Medicinal Chemistry · doi:10.2174/156802607779318262 · Cited by 164
Structural Properties of EGCG-Induced, Nontoxic Alzheimer's Disease Aβ Oligomers
del Amo, J. M. L., Fink, U., Dasari, M., Grelle, G., Wanker, E. E., Bieschke, J., & Reif, B. (2012) · Journal of Molecular Biology · doi:10.1016/j.jmb.2012.01.013 · Cited by 160
Amin, F. U., Shah, S. A., Badshah, H., Khan, M., & Kim, M. O. (2017) · Journal of Nanobiotechnology · doi:10.1186/s12951-016-0227-4 · Cited by 161
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
Green, J. D., Kreplak, L., Goldsbury, C. S., Li‐Blatter, X., Stolz, M., Cooper, G. J. S., Seelig, A., Kistler, J., & Aebi, U. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.07.052 · Cited by 161
Fujita, K., Motoki, K., Tagawa, K., Chen, X., Hama, H., Nakajima, K., Homma, H., Tamura, T., Watanabe, H., Katsuno, M., et al. (2016) · Scientific Reports · doi:10.1038/srep31895 · Cited by 160
Intranasal insulin as a therapeutic option in the treatment of cognitive impairments
Benedict, C., Frey, W. H., Schiöth, H. B., Schultes, B., Jan Born, A., & Hallschmid, M. (2010) · Experimental Gerontology · doi:10.1016/j.exger.2010.08.026 · Cited by 165
Nanopore Analysis of β-Amyloid Peptide Aggregation Transition Induced by Small Molecules
Wang, H.-Y., Ying, Y., Yang, L., Kraatz, H., & Long, Y. (2011) · Analytical Chemistry · doi:10.1021/ac1029874 · Cited by 160
Alzheimer's disease and post-operative cognitive dysfunction
Xie, Z., & Tanzi, R. E. (2006) · Experimental Gerontology · doi:10.1016/j.exger.2006.01.014 · Cited by 159
Mahmoudi, M., Quinlan-Pluck, F., Monopoli, M. P., Sheibani, S., Vali, H., Dawson, K. A., & Lynch, I. (2012) · ACS Chemical Neuroscience · doi:10.1021/cn300196n · Cited by 162
Grimm, M. O. W., Mett, J., Stahlmann, C. P., Haupenthal, V. J., Zimmer, V. C., & Hartmann, T. (2013) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2013.00098 · Cited by 170
Astrocytes and the TGF-β1 Pathway in the Healthy and Diseased Brain: a Double-Edged Sword
Diniz, L. P., Matias, I. C. P., Siqueira, M., Stipursky, J., & Gomes, F. C. A. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-1396-y · Cited by 169
Association between conformational mutations in neuroserpin and onset and severity of dementia
Davis, R. L., Shrimpton, A. E., Carrell, R. W., Lomas, D. A., Gerhard, L., Baumann, B., Lawrence, D. A., Yepes, M., Kim, T. S., Ghetti, B. F., et al. (2002) · The Lancet · doi:10.1016/s0140-6736(02)09293-0 · Cited by 159
Effect of Surfaces on Amyloid Fibril Formation
Moores, B., Drolle, E., Attwood, S. J., Simons, J., & Leonenko, Z. (2011) · PLoS ONE · doi:10.1371/journal.pone.0025954 · Cited by 159
Wu, J., Breydo, L., Isas, J. M., Lee, J., Kuznetsov, Y. G., Langen, R., & Glabe, C. G. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.069542 · Cited by 163
Lesné, S., Kotilinek, L., & Ashe, K. H. (2007) · Neuroscience · doi:10.1016/j.neuroscience.2007.10.054 · Cited by 159
The synapse as a treatment avenue for Alzheimer’s Disease
Peng, L., Bestard‐Lorigados, I., & Song, W. (2022) · Molecular Psychiatry · doi:10.1038/s41380-022-01565-z · Cited by 162
The Molecular Chaperone αB-crystallin Enhances Amyloid β Neurotoxicity
Stege, G. J. J., Renkawek, K., Overkamp, P., Verschuure, P., van Rijk, A. F., Reijnen-Aalbers, A., Boelens, W. C., Bosman, G. J. C. G. M., & JONG, W. W. D. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.1167 · Cited by 157
Wang, Z., Jackson, R. J., Hong, W., Taylor, W. M., Corbett, G. T., Moreno, A. J., Liu, W., Li, S., Frosch, M. P., Slutsky, I., et al. (2017) · Journal of Neuroscience · doi:10.1523/jneurosci.2009-17.2017 · Cited by 157
Aβ Oligomer-Induced Synapse Degeneration in Alzheimer’s Disease
Wilcox, K. C., Lacor, P. N., Pitt, J. E., & Klein, W. L. (2011) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-011-9691-4 · Cited by 159
Self-citationImmunohistological detection of Chlamydia pneumoniae in the Alzheimer's disease brain
Hammond, C. J., Hallock, L. R., Howanski, R. J., Appelt, D. M., Little, C. S., & Balin, B. J. (2010) · BMC Neuroscience · doi:10.1186/1471-2202-11-121 · Cited by 156
BRICHOS Domains Efficiently Delay Fibrillation of Amyloid β-Peptide
Willander, H., Presto, J., Askarieh, G., Biverstål, H., Frohm, B., Knight, S. D., Johansson, J., & Linse, S. S. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.393157 · Cited by 155
Reddy, G., Straub, J. E., & Thirumalai, D. (2009) · The Journal of Physical Chemistry B · doi:10.1021/jp808914c · Cited by 157
Corbett, G. T., Wang, Z., Hong, W., Colom‐Cadena, M., Rose, J. L., Liao, M., Asfaw, A., Hall, T. C., Ding, L., DeSousa, A., et al. (2019) · Acta Neuropathologica · doi:10.1007/s00401-019-02114-9 · Cited by 161
Stereoselective Interactions of Peptide Inhibitors with the β-Amyloid Peptide
Chalifour, R. J., McLaughlin, R. W., Lavoie, L., Morissette, C., Tremblay, N., Boulé, M., Sarazin, P., Stéa, D., Lacombe, D., Tremblay, P., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212694200 · Cited by 156
Insulin Receptor Dysfunction Impairs Cellular Clearance of Neurotoxic Oligomeric Aβ
Zhao, W.-Q., Lacor, P. N., Chen, H., Lambert, M. P., Quon, M. J., Krafft, G. A., & Klein, W. L. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.011015 · Cited by 154
Self-citationNoradrenaline 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
Retinal pathological features and proteome signatures of Alzheimer’s disease
Koronyo, Y., Rentsendorj, A., Mirzaei, N., Regis, G. C., Sheyn, J., Shi, H., Barrón, E., Cook‐Wiens, G., Rodriguez, A., Medeiros, R., et al. (2023) · Acta Neuropathologica · doi:10.1007/s00401-023-02548-2 · Cited by 162
Metadata
- Authors
- 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., Wals, P., Zhang, C., Finch, C. E., Krafft, G. A., & Klein, W. L.
- Affiliations
- Northwestern University (US)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 1998-05-26
- Volume
- 95
- Issue
- 11
- Pages
- 6448-6453
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC27787
- OpenAlex
- W2165021720
- Cited by
- 3,506
- References
- 68
- Citations by year
- 2026: 61 · 2025: 69 · 2024: 82 · 2023: 81 · 2022: 101 · 2021: 115 · 2020: 137 · 2019: 105 · 2018: 127 · 2017: 138 · 2016: 139 · 2015: 152 · 2014: 171 · 2013: 188 · 2012: 196
- FWCI
- 29.85
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › 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
- amyloid-beta 42, neurotoxicity, Alzheimer's disease, Fyn tyrosine kinase, neuroprotection, hippocampal long-term potentiation, synaptic plasticity, signal transduction, organotypic brain cultures
- MeSH terms
- Alzheimer Disease, Animals, Brain, Cell Membrane, Cells, Cultured, Ligands, Neurotoxins, Amyloid beta-Peptides, Cell Death, Mice
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
