The DOI matches its Crossref record; 62 of the 62 references it cites were found in a registry or an index.
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.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
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?
The cited source says what the claim attributes to it.
In the citing paper
“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
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
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
Self-citation
Cited by
Sorted by citations
Items 301–400 of 468
Fragile X mental retardation protein expression in Alzheimer’s disease
Renoux, A. J., Carducci, N. M., Ahmady, A. A., & Todd, P. K. (2014) · Frontiers in Genetics · doi:10.3389/fgene.2014.00360 · Cited by 23
Mayordomo‐Cava, J., Iborra‐Lázaro, G., Djebari, S., Temprano‐Carazo, S., Sánchez‐Rodríguez, I., Jeremic, D., Gruart, A., Delgado-Garcia, J. M., Jiménez‐Díaz, L., & Navarro‐López, J. D. (2020) · Biology · doi:10.3390/biology9070175 · Cited by 21
A Noncanonical Postsynaptic Transport Route for a GPCR Belonging to the Serotonin Receptor Family
Liebmann, T., Kruusmägi, M., Sourial-Bassillious, N., Bondar, A. A., Svenningsson, P., Flajolet, M., Greengard, P., Scott, L., Brismar, H., & Aperia, A. C. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.1804-12.2012 · Cited by 23
Store depletion-induced h-channel plasticity rescues a channelopathy linked to Alzheimer’s disease
Musial, T. F., Molina-Campos, E., Bean, L. A., Ybarra, N., Borenstein, R., Russo, M. L., Buss, E. W., Justus, D., Neuman, K. M., Ayala, G. D., et al. (2018) · Neurobiology of Learning and Memory · doi:10.1016/j.nlm.2018.06.004 · Cited by 24
Globular and Protofibrillar Aβ Aggregates Impair Neurotransmission by Different Mechanisms
Moreth, J., Kroker, K. S., Schwanzar, D., Schnack, C., Arnim, C. A. F. V., Hengerer, B., Rosenbrock, H., & Kußmaul, L. (2013) · Biochemistry · doi:10.1021/bi3016444 · Cited by 24
Chaudhary, B. N., Kumari, S., Dhapola, R., Sharma, P., Paidlewar, M., Vellingiri, B., Medhi, B., & HariKrishnaReddy, D. (2025) · Biochemical Pharmacology · doi:10.1016/j.bcp.2025.117211 · Cited by 24
Molecular Factors Mediating Neural Cell Plasticity Changes in Dementia Brain Diseases
Kozubski, W. P., Ong, K. T., Waleszczyk, W. J., Zabel, M. K., & Dorszewska, J. (2021) · Neural Plasticity · doi:10.1155/2021/8834645 · Cited by 21
Martínez‐Mármol, R., Small, C., Jiang, A., Palliyaguru, T., Wallis, T. P., Gormal, R. S., Sibarita, J., Götz, J., & Meunier, F. A. (2022) · Molecular Psychiatry · doi:10.1038/s41380-022-01825-y · Cited by 21
O’Day, D. H. (2024) · Biomolecules · doi:10.3390/biom14020173 · Cited by 22
Glutamate Receptors in Human Caudate Nucleus in Normal Aging and Alzheimer’s Disease
Tsamis, K. I., Mytilinaios, D. G., Njau, S. N., & Balogiannis, S. (2013) · Current Alzheimer Research · doi:10.2174/1567205011310050002 · Cited by 21
Class A and C GPCR Dimers in Neurodegenerative Diseases
Moreira, I. S., Caniceiro, A. B., Bueschbell, B., & Schiedel, A. C. (2022) · Current Neuropharmacology · doi:10.2174/1570159x20666220327221830 · Cited by 18
Lipid rafts: linking prion protein to zinc transport and amyloid-β toxicity in Alzheimer's disease
Watt, N. T., Jarosz-Griffiths, H., & Hooper, N. M. (2014) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2014.00041 · Cited by 22
Presenilins, Deranged Calcium Homeostasis, Synaptic Loss and Dysfunction in Alzheimer's Disease
Александровна, П. Е., Supnet, C. B., & Борисович, Б. И. (2012) · Messenger · doi:10.1166/msr.2012.1002 · Cited by 20
CD4 T cells acquire Eomesodermin to modulate cellular senescence and aging
Elyahu, Y., Feygin, I., Eremenko, E., Pinkas, N., Zemer, A., Shicht, A., Berner, O., Avigdory-Meiri, R., Nemirovsky, A., Reshef, K., et al. (2025) · Nature Aging · doi:10.1038/s43587-025-00953-8 · Cited by 19
Molecular membrane dynamics: Insights into synaptic function and neuropathological disease
Bannai, H. (2017) · Neuroscience Research · doi:10.1016/j.neures.2017.07.007 · Cited by 18
Mitra, S., Dash, R., Sohel, M., Chowdhury, A., Munni, Y. A., Ali, M. C., Hannan, M. A., Islam, T., & Moon, I. S. (2022) · Current Neuropharmacology · doi:10.2174/1570159x20666220310115004 · Cited by 19
Ciappelloni, S., Murphy‐Royal, C., Dupuis, J. P., Oliet, S. H. R., & Groc, L. (2017) · Cell Calcium · doi:10.1016/j.ceca.2017.08.009 · Cited by 16
Szumlinski, K. K., Herbert, J. N., Espinoza, B. M., Madory, L. E., & Scudder, S. L. (2023) · Addiction Neuroscience · doi:10.1016/j.addicn.2023.100099 · Cited by 15
Privitera, L., Hogg, E. L., Lopes, M., Domingos, L. B., Gaestel, M., Müller, J., Wall, M. J., & Corrêa, S. A. L. (2022) · Aging Cell · doi:10.1111/acel.13717 · Cited by 17
Belfiore, M., Cariati, I., Matteucci, A., Gaddini, L., Macchia, G., Fioravanti, R., Frank, C., Tancredi, V., D’Arcangelo, G., & Diociaiuti, M. (2019) · Scientific Reports · doi:10.1038/s41598-019-41462-0 · Cited by 17
Prikhodko, O., Freund, R. K., Sullivan, E. M., Kennedy, M. J., & Dell’Acqua, M. L. (2024) · Journal of Neuroscience · doi:10.1523/jneurosci.0675-24.2024 · Cited by 16
Kalirin‐7 prevents dendritic spine dysgenesis induced by amyloid beta‐derived oligomers
Xie, Z., Shapiro, L. P., Cahill, M. E., Russell, T. A., Lacor, P. N., Klein, W. L., & Penzes, P. (2018) · European Journal of Neuroscience · doi:10.1111/ejn.14311 · Cited by 16
Self-citationMartín‐Belmonte, A., Aguado, C., Alfaro‐Ruiz, R., Albasanz, J. L., Martı́n, M., Moreno‐Martínez, A. E., Fukazawa, Y., & Luján, R. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22115867 · Cited by 17
Phosphoinositides: Two-Path Signaling in Neuronal Response to Oligomeric Amyloid β Peptide
Uranga, R. M., Alza, N. P., Conde, M. A., Antollini, S. S., & Salvador, G. A. (2016) · Molecular Neurobiology · doi:10.1007/s12035-016-9885-3 · Cited by 16
Dou, Y., Xie, J., Tan, Y., Zhang, M., Zhao, Y., & Liu, X. (2021) · Journal of Nanobiotechnology · doi:10.1186/s12951-021-01070-5 · Cited by 15
Toward a unified therapeutics approach targeting putative amyloid-β oligomer receptors
Overk, C., & Masliah, E. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1414554111 · Cited by 16
Regulation of Neuronal Na,K-ATPase by Extracellular Scaffolding Proteins
Liebmann, T., Fritz, N., Kruusmägi, M., Westin, L., Bernhem, K., Bondar, A. A., Aperia, A. C., & Brismar, H. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19082214 · Cited by 15
mGluR5 as a Potential Orchestrator of Astrocyte Interactions in Neurological Disorders
Kim, J., Lee, J., Song, H., Koo, J. W., & Kang, S. (2025) · Neural Plasticity · doi:10.1155/np/7259018 · Cited by 14
Sex differences and hormonal regulation of metabotropic glutamate receptor synaptic plasticity
Fabian, C. B., Seney, M. L., & Joffe, M. E. (2022) · International review of neurobiology · doi:10.1016/bs.irn.2022.10.002 · Cited by 14
Kwon, S. H., Parthiban, S., Tippani, M., Divecha, H. R., Eagles, N. J., Lobana, J. S., Williams, S. R., Mak, M., Bharadwaj, R. A., Kleinman, J. E., et al. (2023) · GEN Biotechnology · doi:10.1089/genbio.2023.0019 · Cited by 14
Pretreatment of chemically-synthesized Aβ42affects its biological activity in yeast
Porzoor, A., Caine, J. M., & Macreadie, I. G. (2014) · Prion · doi:10.4161/19336896.2014.992275 · Cited by 14
Involvement of ‘stress–response’ kinase pathways in Alzheimer's disease progression
Mairet‐Coello, G., & Polleux, F. (2014) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2014.03.011 · Cited by 16
Sánchez-Melgar, A., Albasanz, J. L., Pallàs, M., & Martı́n, M. (2020) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.0c00067 · Cited by 14
Eugenitol ameliorates memory impairments in 5XFAD mice by reducing Aβ plaques and neuroinflammation
Cho, E., Youn, K., Kwon, H., Jeon, J., Cho, W., Park, S. J., Son, S. H., Jang, D. S., Shin, C. Y., Moon, M., et al. (2022) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.112763 · Cited by 13
Effect of amyloids on the vesicular machinery: implications for somatic neurotransmission
Das, A. K., Pandit, R., & Maiti, S. (2015) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2014.0187 · Cited by 14
Yamamoto, K., Yamamoto, R., & Kato, N. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.660319 · Cited by 13
Durakoglugil, M. S., Wasser, C. R., Wong, C. H. Y., Pohlkamp, T., Xian, X., Lane‐Donovan, C., Fritschle, K., Nästle, L., & Herz, J. (2021) · Journal of Neuroscience · doi:10.1523/jneurosci.0388-21.2021 · Cited by 14
Adeoye, T., Shah, S. I., Demuro, A., Rabson, D. A., & Ullah, G. (2022) · Cells · doi:10.3390/cells11142167 · Cited by 15
Castillo, C. A., Ballesteros‐Yáñez, I., León, D., Albasanz, J. L., & Martı́n, M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22126577 · Cited by 12
AD molecular: Molecular imaging of Alzheimer's disease: PET imaging of neurotransmitter systems
Mecca, A. P. (2019) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2019.04.003 · Cited by 13
Sánchez-Melgar, A., Albasanz, J. L., Griñán‐Ferré, C., Pallàs, M., & Martı́n, M. (2020) · Cells · doi:10.3390/cells9071628 · Cited by 12
Surface Traffic in Synaptic Membranes
Heine, M. (2012) · Advances in experimental medicine and biology · doi:10.1007/978-3-7091-0932-8_9 · Cited by 13
Cellular prion protein and Alzheimer disease
Kudo, W., Petersen, R. B., & Lee, H. (2013) · Prion · doi:10.4161/pri.22848 · Cited by 12
mGluR-dependent plasticity in rodent models of Alzheimer’s disease
Valdivia, G., Ardiles, Á. O., Idowu, A., Salazar, C., Lee, H., Gallagher, M., Palacios, A. G., & Kirkwood, A. (2023) · Frontiers in Synaptic Neuroscience · doi:10.3389/fnsyn.2023.1123294 · Cited by 11
Li, J., Liu, Y., Yin, C., Zeng, Y., & Mei, Y. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102468 · Cited by 13
Choquet, D., Opazo, P., & Zhang, H. (2025) · Translational Neurodegeneration · doi:10.1186/s40035-025-00470-z · Cited by 11
Actor-Engel, H. S., Schwartz, S. L., Crosby, K. C., Sinnen, B. L., Prikhodko, O., Ramsay, H. J., Bourne, J. N., Winborn, C. S., Lucas, A., Smith, K. R., et al. (2021) · eNeuro · doi:10.1523/eneuro.0416-21.2021 · Cited by 11
Alteration of scaffold: Possible role of MACF1 in Alzheimer’s disease pathogenesis
Wang, X., Qi, Y., Zhou, X., Zhang, G., & Fu, C. (2019) · Medical Hypotheses · doi:10.1016/j.mehy.2019.109259 · Cited by 12
Ammassari‐Teule, M. (2020) · Frontiers in Synaptic Neuroscience · doi:10.3389/fnsyn.2020.566615 · Cited by 12
Behroozi, Z., Askarpour, H., & Baghcheghi, Y. (2026) · Journal of Alzheimer s Disease Reports · doi:10.1177/25424823261415807 · Cited by 10
Chou, Q.-L., Alik, A., Marquier, F., Melki, R., Treussart, F., & Simonneau, M. (2022) · eNeuro · doi:10.1523/eneuro.0227-21.2022 · Cited by 12
Hu, S., Xian, Y., Fan, Y., Mak, S., Wang, J., Tang, J., Pang, Y., Pi, R., Tsim, K. W. K., Liu, F., et al. (2020) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2020.173065 · Cited by 10
Involvement of IL-10R/STAT3 pathway in amyloid β clearance by microlgia in Alzheimer's disease
Liu, H., Zhou, Y., & Song, W. (2021) · International Immunopharmacology · doi:10.1016/j.intimp.2021.108263 · Cited by 9
Salardini, E., O’Dell, R. S., Tchorz, E., Nabulsi, N., Huang, Y. H., Carson, R. E., van Dyck, C. H., & Mecca, A. P. (2025) · Alzheimer s Research & Therapy · doi:10.1186/s13195-025-01739-1 · Cited by 8
Fioriti, L., Wijesekara, N., Argyrousi, E. K., Matsuzaki, S., Takamura, H., Satoh, K., Han, K., Yamauchi, H., Staniszewski, A., Acquarone, E., et al. (2025) · Alzheimer s & Dementia · doi:10.1002/alz.70030 · Cited by 8
Laurén, J., Gimbel, D. A., Nygaard, H. B., Gilbert, J. W., & Strittmatter, S. M. (2010) · Nature · doi:10.1038/nature09218 · Cited by 8
Maladie d’Alzheimer, peptide β-amyloïde et synapses
Hémar, A., & Mulle, C. (2011) · médecine/sciences · doi:10.1051/medsci/2011278015 · Cited by 14
Developing BACE-1 inhibitors for FXS
Westmark, C. J., Berry‐Kravis, E., Ikonomidou, C., Yin, J. C. P., & Puglielli, L. (2013) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2013.00077 · Cited by 8
Nong, Y., Kim, J. S., Jia, L., Arancio, O., & Wang, Q. (2025) · Journal of Alzheimer s Disease · doi:10.1177/13872877251342273 · Cited by 8
West, E., Osborne, C., Nolan, W., & Bate, C. (2015) · Biology · doi:10.3390/biology4020367 · Cited by 7
Peripheral Amyloid Precursor Protein Derivative Expression in Fragile X Syndrome
McLane, R. D., Schmitt, L., Pedapati, E. V., Shaffer, R. C., Dominick, K. C., Horn, P. S., Groß, C., & Erickson, C. A. (2019) · Frontiers in Integrative Neuroscience · doi:10.3389/fnint.2019.00049 · Cited by 7
Bouvet, P., Gea, P. D., Aimard, M., Chounlamountri, N., Honnorat, J., Delcros, J., Salin, P. A., & Meissirel, C. (2023) · Aging Cell · doi:10.1111/acel.13907 · Cited by 9
Kaar, A., Weir, M. P., & Rae, M. G. (2024) · Neuroscience Letters · doi:10.1016/j.neulet.2024.137664 · Cited by 8
Imaging organelle transport in primary hippocampal neurons treated with amyloid-β oligomers
Gan, K. J., & Silverman, M. A. (2015) · Methods in cell biology · doi:10.1016/bs.mcb.2015.06.012 · Cited by 7
Li, Y., & Yang, X. (2024) · Cognitive Neurodynamics · doi:10.1007/s11571-024-10064-6 · Cited by 7
Hadžibegović, S., Bontempi, B., & Nicole, O. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26041737 · Cited by 6
Yang, T., Zhang, D., Huang, H., Liu, F., Wu, J., Ma, X., Liu, S., Huang, M., Zhou, Y., & Shen, Y. (2025) · Brain · doi:10.1093/brain/awaf186 · Cited by 10
β-Adrenergic Receptor, Amyloid β-Peptide, and Alzheimer's Disease
Wang, D., & Xiang, Y. K. (2011) · Current topics in membranes · doi:10.1016/b978-0-12-384921-2.00010-0 · Cited by 6
Sex-Specific Multiparameter Blood Test for the Early Diagnosis of Alzheimer’s Disease
Cho, H. J., Schulz, P., Venkataraman, L., Caselli, R. J., & Sierks, M. R. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232415670 · Cited by 6
Zhao, D. Y., Zhang, S., Meng, Y., Xiongwei, D., Zhang, D., Liang, Y., Wang, L., & Liu, C. (2014) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.24691 · Cited by 6
Synaptic Function and Neuropathological Disease Revealed by Quantum Dot-Single-Particle Tracking
Bannai, H., Inoue, T., Hirose, M., Niwa, F., & Mikoshiba, K. (2020) · Neuromethods · doi:10.1007/978-1-0716-0532-5_7 · Cited by 6
Yang, S.-T., Wang, M., Galvin, V. C., Yang, Y., & Arnsten, A. F. T. (2020) · Psychopharmacology · doi:10.1007/s00213-020-05661-2 · Cited by 6
Ovsepian, S. V., Horáček, J., O’Leary, V. B., & Höschl, C. (2020) · The Neuroscientist · doi:10.1177/1073858420940943 · Cited by 8
Long-term dynamics of aberrant neuronal activity in Alzheimer’s diseasePreprint
Korzhova, V., Marinković, P., Goltstein, P. M., Herms, J. W., & Liebscher, S. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/801902 · Cited by 6
Palomares, D., Vanparys, A., Jorgji, J., Paître, E., Kienlen‐Campard, P., & Suelves, N. (2025) · Acta Neuropathologica Communications · doi:10.1186/s40478-025-02118-5 · Cited by 7
CaV2.1 mediates presynaptic dysfunction induced by amyloid β oligomers
Jeans, A. F., Padamsey, Z., Collins, H., Foster, W., Allison, S., Dierksmeier, S. E., Klein, W. L., van den Maagdenberg, A. M. J. M., & Emptage, N. J. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.115451 · Cited by 5
Self-citationAlzheimer’s Disease, β-Amyloid Peptides, and Ubiquitin-Proteasome System: Nutritherapeutic Insights
Simon, P. Y. R., & David, R. (2025) · Neurodegenerative Diseases · doi:10.1159/000545170 · Cited by 5
Анатольевич, П. И., & Pinelis, V. G. (2021) · F1000Research · doi:10.12688/f1000research.24558.2 · Cited by 5
Adeoye, T., Shah, S. I., Demuro, A., Rabson, D. A., & Ullah, G. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.04.21.489060 · Cited by 5
The role of amyloid beta 4-42 in the etiology of Alzheimer's disease
Bouter, Y. (2015) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-4849 · Cited by 5
Current trends in advanced imaging modalities for the early diagnosis of Alzheimer's disease
Zhang, X., & Xue, P. (2025) · Chinese Chemical Letters · doi:10.1016/j.cclet.2025.111628 · Cited by 4
Basli, A., & Bounaas, J. (2022) · Nutrition and Health · doi:10.1177/02601060221137104 · Cited by 4
Yan, Y., Su, J., Xie, M., Kong, Y., Wang, C., Yuan, G., Fang, Y., Hwang, K., Kim, C., Han, H. S., et al. (2025) · Brain stimulation · doi:10.1016/j.brs.2025.103015 · Cited by 6
Ginsenosides Decrease β-Amyloid Production via Potentiating Capacitative Calcium Entry
Cho, Y. Y., Park, J. H., Lee, J. H., & Chung, S. (2024) · Biomolecules & Therapeutics · doi:10.4062/biomolther.2023.172 · Cited by 4
Super-resolution microscopy as a drug discovery tool
Toms, L., FitzPatrick, L., & Auckland, P. (2025) · SLAS DISCOVERY · doi:10.1016/j.slasd.2025.100209 · Cited by 4
Lee, J., & Kwag, J. (2021) · Alzheimer s Research & Therapy · doi:10.1186/s13195-021-00901-9 · Cited by 4
Colacurcio, D. J., Zyskind, J. W., Jordan‐Sciutto, K. L., & Akay, C. (2015) · Neuroscience Letters · doi:10.1016/j.neulet.2015.10.031 · Cited by 4
Spectroscopic Investigations of Pentobarbital Interaction with Transthyretin
Darwish, S. M., Ghithan, J., Abuteir, M. M., Faroun, M., & Abu-hadid, M. M. (2012) · Journal of Spectroscopy · doi:10.1155/2013/927962 · Cited by 4
Simulation of Ca 2+ oscillations in astrocytes mediated by amyloid beta in Alzheimer’s diseasePreprint
Gao, H., Liu, L., & Chen, S. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.03.18.996843 · Cited by 5
Rueda‐Carrasco, J., Sokolova, D., Lee, S., Childs, T., Jurčáková, N., Schepper, S. D., Ge, J. Z., Lachica, J., Toomey, C. E., Freeman, O. J., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.04.04.486424 · Cited by 4
Chen, H., Cao, J., Zhang, Y., Su, X., Kang, Y., Gao, L., & Jing, Y. (2025) · The FASEB Journal · doi:10.1096/fj.202501545rr · Cited by 4
Group I metabotropic glutamate receptors (mGluR1/5) and neurodegenerative diseases
Solntseva, E. I., Rogozin, P. D., & Skrebitsky, V. G. (2019) · Annals of Clinical and Experimental Neurology · doi:10.25692/acen.2019.4.8 · Cited by 3
Addressing the Complex Etiology of Alzheimer‘s Disease: the Role of P25/Cdk5
Mungenast, A. E., & Tsai, L. (2011) · Future Neurology · doi:10.2217/fnl.11.22 · Cited by 3
The multitude of therapeutic targets in neurodegenerative proteinopathies
Melki, R. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-805120-7.00001-4 · Cited by 3
Abd‐Elrahman, K. S., Albaker, A. B., de Souza, J. M., Ribeiro, F. M., Schlossmacher, M. G., Tiberi, M., Hamilton, A., & Ferguson, S. S. G. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/803262 · Cited by 3
Small, C., Martínez‐Mármol, R., Wallis, T. P., Gormal, R. S., Götz, J., & Meunier, F. A. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.09.04.282855 · Cited by 3
NCAM2 promotes targeting of APP from the cell surface to BACE1-containing recycling endosomes
Pfundstein, G., Keable, R., Hu, S., Al-Hadi, M., Baker, M., Schachner, M., Leshchyns’ka, I., & Sytnyk, V. (2025) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2025.102807 · Cited by 2
Neurochemical Aspects of Alzheimer Disease
Farooqui, A. A. (2016) · Springer eBooks · doi:10.1007/978-3-319-15889-1_1 · Cited by 2
Yalçın, A., Turunç, E., Kaplan, M. M., Uyanıkgil, Y., Erzurumlu, Y., Gavini, E., & Kanıt, L. (2024) · Drug and Chemical Toxicology · doi:10.1080/01480545.2024.2349951 · Cited by 2
Inorganic, Organic and Polymer-Based Nanomaterials
Singh, P., Manori, S., Raina, K. K., & Shukla, R. K. (2024) · Smart nanomaterials technology · doi:10.1007/978-981-97-0308-1_2 · Cited by 2
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
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
