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Deleterious Effects of Amyloid β Oligomers Acting as an Extracellular Scaffold for mGluR5
Open accessAbstract
Soluble oligomers of amyloid beta (Abeta) play a role in the memory impairment characteristic of Alzheimer's disease. Acting as pathogenic ligands, Abeta oligomers bind to particular synapses and perturb their function, morphology, and maintenance. Events that occur shortly after oligomer binding have been investigated here in live hippocampal neurons by single particle tracking of quantum dot-labeled oligomers and synaptic proteins. Membrane-attached oligomers initially move freely, but their diffusion is hindered markedly upon accumulation at synapses. Concomitantly, individual metabotropic glutamate receptors (mGluR5) manifest strikingly reduced lateral diffusion as they become aberrantly clustered. This clustering of mGluR5 elevates intracellular calcium and causes synapse deterioration, responses prevented by an mGluR5 antagonist. As expected, clustering by artificial crosslinking also promotes synaptotoxicity. These results reveal a mechanism whereby Abeta oligomers induce the abnormal accumulation and overstabilization of a glutamate receptor, thus providing a mechanistic and molecular basis for Abeta oligomer-induced early synaptic failure.
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“Aβ oligomers can drive additional vicious cycles by stimulating metabotropic glutamate receptor 5 (mGluR5)146,147, which activates feedforward Ca2+–cAMP signaling and drive tau phosphorylation (Fig. 5, brown).”
From Stress weakens prefrontal networks: molecular insults to higher cognition (2015) · cites this paper as [146]
In the citing paper
“Aβ binds to α7 nicotinic acetylcholine receptors (α7 nAChRs) and to metabotropic glutamate receptors, in particular mGluR5 [31–33].”
From ApoE, ApoE Receptors, and the Synapse in Alzheimer's Disease (2017) · cites this paper as [32]
In the citing paper
“ADDL binding to synapses displays saturable kinetics (Renner et al., 2010)”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Renner et al., 2010
In the citing paper
“Double-labeling with synaptophysin or FM463 establishes this localization to be at functional synapses (Renner et al., 2010).”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Renner et al., 2010
In the citing paper
“single particle tracking of quantum dot-labeled Aβ oligomers has demonstrated the participation of metabotropic glutamate receptors (mGluR5) in oligomer binding and clustering at synapses (Renner et al., 2010).”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Renner et al., 2010
In the citing paper
“Initially, Aβ oligomers diffused as if bound to an untethered protein. Within minutes, however, movement slowed and oligomers became immobilized, typically at active synapses labeled with FM4-64. The synaptic trapping of oligomers was accompanied by co-clustering and immobilization of mGluR5 metabotropic glutamate receptors.”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Renner et al., 2010
In the citing paper
“protection also is afforded by antagonists of metabotropic mGluR5 receptors (Rammes et al., 2011; Renner et al., 2010; Wang et al., 2004).”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Renner et al., 2010
In the citing paper
“the recent finding that mGluR5 is implicated in the toxic clustering of Aβ oligomers at synapses and the ensuing aberrant calcium signaling (Renner et al., 2010) suggests that selective mGluR5 inhibitors may hold potential to block oligomer-induced synapse dysfunction.”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Renner et al., 2010
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Citations
Cites
Alzheimer's Disease Is a Synaptic Failure
Selkoe, D. J. (2002) · Science · doi:10.1126/science.1074069 · Cited by 4,420
Walsh, D. M., Klyubin, I., Fadeeva, J. V., Cullen, W. K., Anwyl, R., Wolfe, M. S., Rowan, M. J., & Selkoe, D. J. (2002) · Nature · doi:10.1038/416535a · Cited by 4,291
Shankar, G. M., Li, S., Mehta, T. H., Garcia-Munoz, A., Shepardson, N. E., Smith, I., Brett, F. M., Farrell, M. A., Rowan, M. J., Lemere, C. A., et al. (2008) · Nature Medicine · doi:10.1038/nm1782 · Cited by 3,685
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
Self-citationShankar, G. M., Bloodgood, B. L., Townsend, M., Walsh, D. M., Selkoe, D. J., & Sabatini, B. L. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.4970-06.2007 · Cited by 1,592
Regulation of NMDA receptor trafficking by amyloid-β
Snyder, E. M., Nong, Y., Almeida, C. G., Paul, S., Moran, T., Choi, E. Y., Nairn, A. C., Salter, M. W., Lombroso, P. J., Gouras, G. K., et al. (2005) · Nature Neuroscience · doi:10.1038/nn1503 · Cited by 1,561
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
Diffusion Dynamics of Glycine Receptors Revealed by Single-Quantum Dot Tracking
Dahan, M., Lévi, S., Luccardini, C., Rostaing, P., Riveau, B., & Triller, A. (2003) · Science · doi:10.1126/science.1088525 · Cited by 1,465
Self-citationAstrocyte Control of Synaptic Transmission and Neurovascular Coupling
Haydon, P. G., & Carmignoto, G. (2006) · Physiological Reviews · doi:10.1152/physrev.00049.2005 · Cited by 1,371
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
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Huang, Y., & Mucke, L. (2012) · Cell · doi:10.1016/j.cell.2012.02.040 · Cited by 1,758
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Spires-Jones, T. L., & Hyman, B. T. (2014) · Neuron · doi:10.1016/j.neuron.2014.05.004 · Cited by 1,201
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
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-citationApolipoprotein E and Apolipoprotein E Receptors: Normal Biology and Roles in Alzheimer Disease
Holtzman, D. M., Herz, J., & Bu, G. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006312 · Cited by 782
Stress weakens prefrontal networks: molecular insults to higher cognition
Arnsten, A. F. T. (2015) · Nature Neuroscience · doi:10.1038/nn.4087 · Cited by 752
Alzheimer amyloid-β oligomer bound to postsynaptic prion protein activates Fyn to impair neurons
Um, J. W., Nygaard, H. B., Heiss, J. K., Kostylev, M. A., Stagi, M., Vortmeyer, A. O., Wısnıewskı, T., Gunther, E. C., & Strittmatter, S. M. (2012) · Nature Neuroscience · doi:10.1038/nn.3178 · Cited by 682
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-citationAβ induces astrocytic glutamate release, extrasynaptic NMDA receptor activation, and synaptic loss
Talantova, M., Sanz-Blasco, S., Zhang, X., Xia, P., Akhtar, M. W., Okamoto, S.-I., Dziewczapolski, G., Nakamura, T., Cao, G., Pratt, A. E., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1306832110 · Cited by 600
Amyloid β Protein and Alzheimer’s Disease: When Computer Simulations Complement Experimental Studies
Nasica-Labouze, J., Nguyen, P. H., Sterpone, F., Berthoumieu, O., Buchete, N., Côté, S., Simone, A. D., Doig, A. J., Faller, P., García, A. E., et al. (2015) · Chemical Reviews · doi:10.1021/cr500638n · Cited by 591
Um, J. W., Kaufman, A. C., Kostylev, M., Heiss, J. K., Stagi, M., Takahashi, H., Kerrisk, M. E., Vortmeyer, A., Wisniewski, T., Koleske, A. J., et al. (2013) · Neuron · doi:10.1016/j.neuron.2013.06.036 · Cited by 572
Oligomeric Aβ-induced synaptic dysfunction in Alzheimer’s disease
Tu, S., Okamoto, S., Lipton, S. A., & Xu, H. (2014) · Molecular Neurodegeneration · doi:10.1186/1750-1326-9-48 · Cited by 613
Choquet, D., & Triller, A. (2013) · Neuron · doi:10.1016/j.neuron.2013.10.013 · Cited by 560
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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
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Tzioras, M., McGeachan, R. I., Durrant, C. S., & Spires-Jones, T. L. (2023) · Nature Reviews Neurology · doi:10.1038/s41582-022-00749-z · Cited by 504
Danysz, W., & Parsons, C. G. (2012) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2012.02057.x · Cited by 500
In situ visualization and dynamics of newly synthesized proteins in rat hippocampal neurons
Dieterich, D. C., Hodas, J. J. L., Gouzer, G., Shadrin, I. Y., Ngo, J. T., Triller, A., Tirrell, D. A., & Schuman, E. M. (2010) · Nature Neuroscience · doi:10.1038/nn.2580 · Cited by 470
Self-citationAmyloid toxicity in Alzheimer’s disease
Reiss, A. B., Arain, H. A., Stecker, M. M., Siegart, N. M., & Kasselman, L. J. (2018) · Reviews in the Neurosciences · doi:10.1515/revneuro-2017-0063 · Cited by 447
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-citationSynapses and Alzheimer's Disease
Sheng, M., Sabatini, B. L., & Sudhof, T. C. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a005777 · Cited by 436
Nixon, R. A. (2017) · The FASEB Journal · doi:10.1096/fj.201700359 · Cited by 400
Synaptopathies: synaptic dysfunction in neurological disorders – A review from students to students
Lepeta, K., Lourenco, M. V., Schweitzer, B. C., Martino Adami, P. V., Banerjee, P., Catuara‐Solarz, S., de La Fuente Revenga, M., Guillem, A. M., Haidar, M., Ijomone, O. M., et al. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13713 · Cited by 386
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
Soluble Aβ oligomer production and toxicity
Larson, M. E., & Lesné, S. E. (2012) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07478.x · Cited by 356
Williams, T. L., & Serpell, L. C. (2011) · FEBS Journal · doi:10.1111/j.1742-4658.2011.08228.x · Cited by 335
Prions, prionoids and protein misfolding disorders
Scheckel, C., & Aguzzi, A. (2018) · Nature Reviews Genetics · doi:10.1038/s41576-018-0011-4 · Cited by 311
Alzheimer's disease: synapses gone cold
Koffie, R. M., Hyman, B. T., & Spires‐Jones, T. L. (2011) · Molecular Neurodegeneration · doi:10.1186/1750-1326-6-63 · Cited by 316
Izzo, N. J., Xu, J., Zeng, C., Kirk, M. J., Mozzoni, K., Silky, C., Rehak, C., Yurko, R., Look, G., Rishton, G., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0111899 · Cited by 157
Self-citationFreir, D. B., Nicoll, A. J., Klyubin, I. V., Panico, S., Donald, J. M. M., Risse, E., Asante, E. A., Farrow, M. A., Sessions, R. B., Saibil, H. R., et al. (2011) · Nature Communications · doi:10.1038/ncomms1341 · Cited by 300
de Wilde, M. C., Overk, C., Sijben, J., & Masliah, E. (2016) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2015.12.005 · Cited by 287
Larson, M. E., Sherman, M. A., Amar, F., Nuvolone, M., Schneider, J. A., Bennett, D. A., Aguzzi, A., & Lesné, S. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.1858-12.2012 · Cited by 290
RetractedMetabotropic glutamate receptors and neurodegenerative diseases
Ribeiro, F. M., Vieira, L. B., Pires, R. G. W., Olmo, R. P., & Ferguson, S. S. G. (2016) · Pharmacological Research · doi:10.1016/j.phrs.2016.11.013 · Cited by 288
Li, S., & Selkoe, D. J. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.15007 · Cited by 263
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Khalid, K., Tan, X., Zaid, H. F. M., Tao, Y., Chew, C. L., Chu, D., Lam, M. K., Ho, Y., Lim, J. W., & Lai, C. W. (2020) · Bioengineered · doi:10.1080/21655979.2020.1736240 · Cited by 276
Synaptic dysfunction in Alzheimer's disease: Mechanisms and therapeutic strategies
Chen, Y., Fu, A. K. Y., & Ip, N. Y. (2019) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2018.11.006 · Cited by 258
Amyloid-β Receptors: The Good, the Bad, and the Prion Protein
Jarosz-Griffiths, H. H., Noble, E., Rushworth, J. V., & Hooper, N. M. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.r115.702704 · Cited by 256
Endoplasmic Reticulum Ca2+ Handling in Excitable Cells in Health and Disease
Stutzmann, G. E., & Mattson, M. P. (2011) · Pharmacological Reviews · doi:10.1124/pr.110.003814 · Cited by 255
Pathogenesis of synaptic degeneration in Alzheimer's disease and Lewy body disease
Overk, C. R., & Masliah, E. (2014) · Biochemical Pharmacology · doi:10.1016/j.bcp.2014.01.015 · Cited by 242
Barry, A. E., Klyubin, I., Mc Donald, J. M., Mably, A. J., Farrell, M. A., Scott, M., Walsh, D. M., & Rowan, M. J. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.6500-10.2011 · Cited by 237
Analyzing dendritic spine pathology in Alzheimer’s disease: Problems and opportunities
Dorostkar, M. M., Zou, C., Blazquez-Llorca, L., & Herms, J. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1449-5 · Cited by 235
Rushworth, J. V., & Hooper, N. M. (2010) · International Journal of Alzheimer s Disease · doi:10.4061/2011/603052 · Cited by 234
de Godoy, M. A., Saraiva, L. M., de Carvalho, L. R. P., Vasconcelos-dos-Santos, A., Beiral, H. J. V., Ramos, A. B., Silva, L. R. D. P., Leal, R. B., Monteiro, V. H. S., Braga, C. V., et al. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.807180 · Cited by 214
α‐synuclein assemblies sequester neuronal α3‐Na+/K+‐ATPase and impair Na+ gradient
Shrivastava, A. N., Redeker, V., Fritz, N., Pieri, L., Almeida, L. G., Spolidoro, M., Liebmann, T., Bousset, L., Renner, M. L., Léna, C., et al. (2015) · The EMBO Journal · doi:10.15252/embj.201591397 · Cited by 213
Self-citationUpdates in Alzheimer's disease: from basic research to diagnosis and therapies
Liu, E., Zhang, Y., & Wang, J. (2024) · Translational Neurodegeneration · doi:10.1186/s40035-024-00432-x · Cited by 241
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-citationSynapse pathology in Alzheimer’s disease
Griffiths, J., & Grant, S. G. N. (2022) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2022.05.028 · Cited by 212
Hu, N., Nicoll, A. J., Zhang, D., Mably, A. J., O’Malley, T. T., Purro, S. A., Terry, C., Collinge, J., Walsh, D. M., & Rowan, M. J. (2014) · Nature Communications · doi:10.1038/ncomms4374 · Cited by 192
A three-step model for the synaptic recruitment of AMPA receptors
Opazo, P., & Choquet, D. (2011) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2010.08.014 · Cited by 190
Goure, W. F., Krafft, G. A., Jerecic, J., & Hefti, F. (2014) · Alzheimer's Research & Therapy · doi:10.1186/alzrt272 · Cited by 190
Zhang, H., Wu, L., Pchitskaya, E. I., Zakharova, O. A., Saito, T., Saido, T. C., & Борисович, Б. И. (2015) · Journal of Neuroscience · doi:10.1523/jneurosci.1034-15.2015 · Cited by 185
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
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
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
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
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Bakota, L., & Brandt, R. (2016) · Drugs · doi:10.1007/s40265-015-0529-0 · Cited by 179
Tau reduction prevents Aβ-induced axonal transport deficits by blocking activation of GSK3β
Vossel, K. A., Xu, J. C., Fomenko, V., Miyamoto, T., Suberbielle, E., Knox, J. A., Ho, K., Kim, D. H., Yu, G.-Q., & Mucke, L. (2015) · Journal of Cell Biology · doi:10.1083/jcb.201407065 · Cited by 167
Self-citationDecker, 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-citationBukke, V. N., Archana, M., Villani, R., Romano, A. D., Wawrzyniak, A., Balawender, K., Orkisz, S., Beggiato, S., Serviddio, G., & Cassano, T. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21207452 · Cited by 161
Falker‐Gieske, C., Hartmann, A., Guett, I., Dohler, F., Altmeppen, H. C., Betzel, C., Schubert, R., Thurm, D., Wegwitz, F., Joshi, P., et al. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.13514 · Cited by 166
Why size matters – balancing mitochondrial dynamics in Alzheimer's disease
DuBoff, B., Feany, M. Β., & Götz, J. (2013) · Trends in Neurosciences · doi:10.1016/j.tins.2013.03.002 · Cited by 168
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
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Ashok, A., Singh, N., Chaudhary, S., Bellamkonda, V., Kritikos, A. E., Wise, A. S., Rana, N. A., McDonald, D., & Ayyagari, R. V. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21197290 · Cited by 164
More than cholesterol transporters: lipoprotein receptors in CNS function and neurodegeneration
Lane-Donovan, C., Philips, G. T., & Herz, J. (2014) · Neuron · doi:10.1016/j.neuron.2014.08.005 · Cited by 158
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Lane-Donovan, C., & Herz, J. (2017) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2016.12.001 · Cited by 157
He, Y., Wei, M., Wu, Y., Qin, H., Li, W., Ma, X., Cheng, J., Ren, J., Shen, Y., Chen, Z., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-09114-z · Cited by 159
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-citationFunctional organization of postsynaptic glutamate receptors
Scheefhals, N., & MacGillavry, H. D. (2018) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2018.05.002 · Cited by 166
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
Ryanodine receptors: physiological function and deregulation in Alzheimer disease
Prete, D. D., Checler, F., & Chami, M. (2014) · Molecular Neurodegeneration · doi:10.1186/1750-1326-9-21 · Cited by 153
Ardiles, Á. O., Tapia‐Rojas, C., Mandal, M., Alexandre, F., Kirkwood, A., Inestrosa, N. C., & Palacios, A. G. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1201209109 · Cited by 152
Haas, L. T., Salazar, S. V., Kostylev, M. A., Um, J. W., Kaufman, A. C., & Strittmatter, S. M. (2015) · Brain · doi:10.1093/brain/awv356 · Cited by 145
Klein, W. L. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-129039 · Cited by 145
Self-citationEvaluating Amyloid-β Oligomers in Cerebrospinal Fluid as a Biomarker for Alzheimer’s Disease
Hölttä, M., Hansson, O., Andréasson, U., Hertze, J., Minthon, L., Nägga, K., Andreasen, N., Zetterberg, H., & Blennow, K. (2013) · PLoS ONE · doi:10.1371/journal.pone.0066381 · Cited by 147
cAMP-PKA phosphorylation of tau confers risk for degeneration in aging association cortex
Carlyle, B. C., Nairn, A. C., Wang, M., Yang, Y., Jin, L. E., Simen, A. A., Ramos, B. P., Bordner, K. A., Craft, G. E., Davies, P., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1322360111 · Cited by 139
Ostapchenko, V. G., Chen, M., Guzmán, M. S., Xie, Y., Lavine, N. E., Fan, J., Beraldo, F. H., Martyn, A. C., Belrose, J. C., Mori, Y., et al. (2015) · Journal of Neuroscience · doi:10.1523/jneurosci.4081-14.2015 · Cited by 143
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Magi, S., Castaldo, P., Macrì, M. L., Maiolino, M., Matteucci, A., Bastioli, G., Gratteri, S., Amoroso, S., & Lariccia, V. (2016) · BioMed Research International · doi:10.1155/2016/6701324 · Cited by 151
Hamilton, A., Esseltine, J. L., DeVries, R. A., Cregan, S. P., & Ferguson, S. S. G. (2014) · Molecular Brain · doi:10.1186/1756-6606-7-40 · Cited by 138
Hamilton, A., Vasefi, M., Tuin, C. V., McQuaid, R. J., Anisman, H., & Ferguson, S. S. G. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.04.077 · Cited by 135
Toxic effects of amyloid fibrils on cell membranes: the importance of ganglioside GM1
Bucciantini, M., Nosi, D., Forzan, M., Russo, E., Calamai, M., Pieri, L., Formigli, L., Quercioli, F., Soria, S., Pavone, F. S., et al. (2011) · The FASEB Journal · doi:10.1096/fj.11-189381 · Cited by 126
Azam, S., Haque, M. E., Jakaria, M., Jo, S.-H., Kim, I., & Choi, D. (2020) · Cells · doi:10.3390/cells9020506 · Cited by 135
Heraldo, F. H., Arantes, C., Santos, T. G., Machado, C. F., Roffé, M., Haji, G. N., Lee, K. S., Magalhães, A. C., Caetano, F. A., Mancini, G. L., et al. (2010) · The FASEB Journal · doi:10.1096/fj.10-161653 · Cited by 123
Rueda‐Carrasco, J., Sokolova, D., Lee, S., Childs, T., Jurčáková, N., Crowley, G., Schepper, S. D., Ge, J. Z., Lachica, J., Toomey, C. E., et al. (2023) · The EMBO Journal · doi:10.15252/embj.2022113246 · Cited by 125
Cissé, M., Sanchez, P. E., Kim, D. H., Ho, K., Yu, G.-Q., & Mucke, L. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.1459-11.2011 · Cited by 124
Haas, L. T., Salazar, S. V., Smith, L. M., Zhao, H. R., Cox, T. O., Herber, C. S., Degnan, A. P., Balakrishnan, A. S., Macor, J. E., Albright, C. F., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.06.023 · Cited by 121
Amyloid-β nanotubes are associated with prion protein-dependent synaptotoxicity
Nicoll, A. J., Panico, S., Freir, D. B., Wright, D., Terry, C., Risse, E., Herron, C. E., O’Malley, T., Wadsworth, J. D. F., Farrow, M. A., et al. (2013) · Nature Communications · doi:10.1038/ncomms3416 · Cited by 119
Excitatory-inhibitory imbalance in Alzheimer's disease and therapeutic significance
Varela, E. V., Etter, G., & Williams, S. (2019) · Neurobiology of Disease · doi:10.1016/j.nbd.2019.04.010 · Cited by 122
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
Cellular prion protein is essential for oligomeric amyloid- -induced neuronal cell death
Kudo, W., Hp, L., Zou, W.-Q., Wang, X., Perry, G., Zhu, X., Smith, M. A., Petersen, R. B., & Lee, H. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr542 · Cited by 116
Impaired regulation of synaptic actin cytoskeleton in Alzheimer's disease
Penzes, P., & VanLeeuwen, J. (2011) · Brain Research Reviews · doi:10.1016/j.brainresrev.2011.01.003 · Cited by 121
The dendritic hypothesis for Alzheimer's disease pathophysiology
Cochran, J. N., Hall, A. M., & Roberson, E. D. (2014) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2013.12.004 · Cited by 114
Penke, B., Szűcs, M., & Bogár, F. (2020) · Molecules · doi:10.3390/molecules25071659 · Cited by 119
Oligomeric Aβ in the monkey brain impacts synaptic integrity and induces accelerated cortical aging
Beckman, D., Ott, S., Donis-Cox, K., Janssen, W. G., Bliss-Moreau, E., Rudebeck, P. H., Baxter, M. G., & Morrison, J. H. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1902301116 · Cited by 111
APP Receptor? To Be or Not To Be
Deyts, C., Thinakaran, G., & Parent, A. (2016) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2016.01.005 · Cited by 121
Reversal of Fragile X Phenotypes by Manipulation of AβPP/Aβ Levels in Fmr1KO Mice
Westmark, C. J., Westmark, P. R., O'Riordan, K. J., Ray, B. C., Hervey, C. M., Salamat, M. S., Abozeid, S. H., Stein, K. M., Stodola, L. A., Tranfaglia, M., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0026549 · Cited by 110
Amyloid-β-Induced Dysregulation of AMPA Receptor Trafficking
Guntupalli, S., Widagdo, J., & Anggono, V. (2016) · Neural Plasticity · doi:10.1155/2016/3204519 · Cited by 110
Costa, R. O., Lacor, P. N., Ferreira, I. L., Resende, R., Auberson, Y. P., Klein, W. L., Oliveira, C. R., Rego, A. C., & Pereira, C. (2012) · Aging Cell · doi:10.1111/j.1474-9726.2012.00848.x · Cited by 116
Self-citationADDLs 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 113
Self-citationKazim, S. F., Chuang, S.-C., Zhao, W., Wong, R. K. S., Bianchi, R., & Iqbal, K. (2017) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2017.00071 · Cited by 109
Synaptic Dysfunction in Alzheimer’s Disease
Marcello, E. E., Epis, R., Saraceno, C., & Luca, M. D. (2012) · Advances in experimental medicine and biology · doi:10.1007/978-3-7091-0932-8_25 · Cited by 115
Calcium Dysregulation in Alzheimer's Disease: A Target for New Drug Development
Wang, Y., Shi, Y., & Wei, H. (2017) · Journal of Alzheimer’s Disease & Parkinsonism · doi:10.4172/2161-0460.1000374 · Cited by 106
Metadata
- Authors
- Renner, M., Lacor, P. N., Velasco, P. T., Xu, J., Contractor, A., Klein, W. L., & Triller, A.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- Northwestern University (US)
- Corresponding author
- Klein, William L.
- Triller, Antoine
- Venue
- Neuron
- Publisher
- Elsevier BV
- Published
- 2010-06
- Volume
- 66
- Issue
- 5
- Pages
- 739-754
- ISSN
- 0896-6273 (ISSN-L)
- PMC
- PMC3111138
- OpenAlex
- W2003655335
- Cited by
- 468
- References
- 62
- Citations by year
- 2026: 18 · 2025: 22 · 2024: 23 · 2023: 14 · 2022: 26 · 2021: 34 · 2020: 38 · 2019: 25 · 2018: 29 · 2017: 26 · 2016: 32 · 2015: 38 · 2014: 31 · 2013: 30 · 2012: 44
- FWCI
- 24.27
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Neuron (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- HAL (submittedVersion, cc-by-nc)
- Funders
- National Institute on Aging (R01AG029460)
- National Institute of Neurological Disorders and Stroke (R01NS058894)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- amyloid-beta oligomers, mGluR5, metabotropic glutamate receptors, receptor clustering, synaptic dysfunction, synaptotoxicity, Alzheimer's disease, hippocampal neurons, single-particle tracking, quantum dots, intracellular calcium, receptor diffusion, receptor cross-linking
- MeSH terms
- Animals, Cells, Cultured, Extracellular Matrix, Neurons, Protein Binding, Synapses, Amyloid beta-Peptides, Rats, Sprague-Dawley, Receptors, Metabotropic Glutamate, Mice, Knockout, Mice, Rats, Protein Stability, Receptor, Metabotropic Glutamate 5
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