The DOI matches its Crossref record; 64 of the 64 references it cites were found in a registry or an index.
Synaptic Targeting by Alzheimer's-Related Amyloid β Oligomers
Open accessAbstract
The cognitive hallmark of early Alzheimer's disease (AD) is an extraordinary inability to form new memories. For many years, this dementia was attributed to nerve-cell death induced by deposits of fibrillar amyloid beta (Abeta). A newer hypothesis has emerged, however, in which early memory loss is considered a synapse failure caused by soluble Abeta oligomers. Such oligomers rapidly block long-term potentiation, a classic experimental paradigm for synaptic plasticity, and they are strikingly elevated in AD brain tissue and transgenic-mouse AD models. The current work characterizes the manner in which Abeta oligomers attack neurons. Antibodies raised against synthetic oligomers applied to AD brain sections were found to give diffuse stain around neuronal cell bodies, suggestive of a dendritic pattern, whereas soluble brain extracts showed robust AD-dependent reactivity in dot immunoblots. Antigens in unfractionated AD extracts attached with specificity to cultured rat hippocampal neurons, binding within dendritic arbors at discrete puncta. Crude fractionation showed ligand size to be between 10 and 100 kDa. Synthetic Abeta oligomers of the same size gave identical punctate binding, which was highly selective for particular neurons. Image analysis by confocal double-label immunofluorescence established that >90% of the punctate oligomer binding sites colocalized with the synaptic marker PSD-95 (postsynaptic density protein 95). Synaptic binding was accompanied by ectopic induction of Arc, a synaptic immediate-early gene, the overexpression of which has been linked to dysfunctional learning. Results suggest the hypothesis that targeting and functional disruption of particular synapses by Abeta oligomers may provide a molecular basis for the specific loss of memory function in early AD.
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 source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Among these various forms, soluble Aβ aggregates are more toxic than monomers or insoluble fibrils; thus, reducing these soluble Aβ aggregates could represent a practical treatment approach in the early stages of AD [10,11,12].”
From Treatment of Alzheimer’s Disease: Beyond Symptomatic Therapies (2023) · cites this paper as [12]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Despite ongoing debate, Aβ accumulation, whether in the form of insoluble plaques, or smaller soluble oligomers does appear to be a primary driver of the disease process, particularly linked to synapse dysfunction [3].”
From Heterozygous expression of the Alzheimer’s disease-protective PLCγ2 P522R variant enhances Aβ clearance while preserving synapses (2022) · cites this paper as [3]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Conversely, overexpression of APP and its proteolytic product, Aβ, have been implicated in the synaptic losses seen early in the development of AD [27].”
From FMRP Mediates mGluR5-Dependent Translation of Amyloid Precursor Protein (2007) · cites this paper as [27]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Other suggested Aβ binding partners at synapses include the α7-nicotinic receptor [49], Ephrin A4 [73], PSD95 [35, 50, 52] and LilrB2 [32].”
From Transmembrane protein 97 is a potential synaptic amyloid beta receptor in human Alzheimer’s disease (2024) · cites this paper as [35]
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“Among these various forms, soluble Aβ aggregates are more toxic than monomers or insoluble fibrils; thus, reducing these soluble Aβ aggregates could represent a practical treatment approach in the early stages of AD [10,11,12].”
From Treatment of Alzheimer’s Disease: Beyond Symptomatic Therapies (2023) · cites this paper as [12]
The cited source says what the claim attributes to it.
In the citing paper
“As previously discussed, amyloid-β oligomers bind to synapses [144] and interfere with the normal process of neurotransmission, long-term potentiation, and thereby memory formation [145].”
From Sigma-2 Receptors—From Basic Biology to Therapeutic Target: A Focus on Age-Related Degenerative Diseases (2023) · cites this paper as [144]
In the citing paper
“Immunohistochemistry confirms that oligomers associate with neurons, accumulating very early in disease progression (Lacor et al., 2004), in loci distinct from amyloid deposits (Kayed et al., 2003).”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Lacor et al., 2004
In the citing paper
“as have the related predictions that oligomers cause dysfunctional trafficking of ionotropic glutamate receptors and metabotropic glutamate receptors (Gong et al., 2003; Lacor et al., 2004).”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Lacor et al., 2004
In the citing paper
“The possible source of extracellular oligomers and how they interact with neurons in human brain are suggested by their peri-somatic localization, observed in early-stage disease (Figure 1, left; (Lacor et al., 2004)).”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Lacor et al., 2004
In the citing paper
“The same binding specificity and punctate pattern is observed for synthetic oligomers, particularly those greater than 50 kDa (Lacor et al., 2004).”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Lacor et al., 2004
In the citing paper
“Oligomers show > 90% co-localization with the post-synaptic marker PSD-95 (Lacor et al., 2004).”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Lacor et al., 2004
In the citing paper
“This prediction was first confirmed for NMDA-Rs (Lacor et al., 2004; Lacor et al., 2007; Snyder et al., 2005).”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Lacor et al., 2004
In the citing paper
“One rapid consequence is an aberrant expression of Arc (Activity-Regulated Cytoskeletal associated protein; (Lacor et al., 2004)).”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Lacor et al., 2004
In the citing paper
“Because Arc is an actin binding protein, its aberrant expression was predicted to disrupt receptor trafficking (Lacor et al., 2004), which could consequently disrupt plasticity (Gong et al., 2003).”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Lacor et al., 2004
In the citing paper
“Coupled with the potential of dendrites for activity-stimulated exocytosis (Kennedy et al., 2010), such a phenomenon could account for the “perineuronal deposits” of oligomers seen in Figure 1 (Lacor et al., 2004).”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Lacor et al., 2004
In the citing paper
“All of these processes are affected by Aβ oligomers in vitro, using primary neuronal cultures (12, 15, 36, 37).”
From Synthetic amyloid-β oligomers impair long-term memory independently of cellular prion protein (2010) · cites this paper as [37]
In the citing paper
“Furthermore, extracellular Aβ1-42 oligomers preferentially target synapses when added to neurons [43, 91].”
From Intraneuronal β-amyloid accumulation and synapse pathology in Alzheimer’s disease (2010) · cites this paper as [91]
In the citing paper
“Other binding partners that have been suggested to bind Aβ include the α7-nicotinic receptor [49], Ephrin A4 (EphA4) [73], PSD95 [35, 50, 52] or LilrB2 [32].”
From Transmembrane protein 97 is a potential synaptic amyloid beta receptor in human Alzheimer’s disease (2024) · cites this paper as [35]
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
The Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics
Hardy, J., & Selkoe, D. J. (2002) · Science · doi:10.1126/science.1072994 · Cited by 13,864
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
Alzheimer's disease: the amyloid cascade hypothesis
Hardy, J. A., & Higgins, G. A. (1992) · Science · doi:10.1126/science.1566067 · Cited by 7,484
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
Triple-Transgenic Model of Alzheimer’s Disease with Plaques and Tangles
Oddo, S., Caccamo, A., Shepherd, J. D., Murphy, M. P., Golde, T. E., Kayed, R., Metherate, R., Mattson, M. P., Akbari, Y., & LaFerla, F. M. (2003) · Neuron · doi:10.1016/s0896-6273(03)00434-3 · Cited by 4,126
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
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-citationPathways towards and Away from Alzheimer’s Disease
Mattson, M. P. (2004) · Nature · doi:10.1038/nature02621 · Cited by 3,052
Mucke, L., Masliah, E., Yu, G.-Q., Mallory, M., Rockenstein, E. M., Tatsuno, G., Hu, K., Kholodenko, D., Johnson-Wood, K., & McConlogue, L. (2000) · The Journal of Neuroscience · doi:10.1523/jneurosci.20-11-04050.2000 · Cited by 1,856
Research works printed but not linked: 2
- Klein WL (2004) Cytotoxic intermediates in the fibrillation pathway: Aβ oligomers in Alzheimer's disease as a case study. In: Protein misfolding, aggregation and conformational diseases (Uversky V, ed). New York: Kluwer Academic/Plenum, in press.
- 2002, Nat Rev Neurosci, 3, 824
Cited by
Sorted by citations
Items 601–700 of 949
CSF-studies in neuropsychiatric disorders.
Raedler, T. J., & Wiedemann, K. (2006) · PubMed · Cited by 25
Kokubo, H., Kayed, R., Glabe, C. G., Staufenbiel, M., Saido, T. C., Iwata, N., & Yamaguchi, H. (2009) · International Journal of Alzheimer s Disease · doi:10.4061/2009/689285 · Cited by 25
Espeseth, A. S., Huang, Q., Gates, A. T., Xu, M., Yu, Y., Simon, A. J., Shi, X., Zhang, X. D., Hodor, P. G., Stone, D. J., et al. (2006) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2006.07.003 · Cited by 25
Candidate anti-Aβ fluorene compounds selected from analogs of amyloid imaging agents
Hong, H., Maezawa, I., Budamagunta, M. S., Rana, S., Shi, A., Vassar, R. J., Liu, R., Lam, K. S., Cheng, R. H., Hua, D. H., et al. (2008) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2008.09.019 · Cited by 25
Intracerebroventricular passive immunization with anti‐oligoAβ antibody in TgCRND8
Chauhan, N. B. (2007) · Journal of Neuroscience Research · doi:10.1002/jnr.21110 · Cited by 24
Stefani, M. (2010) · Methods in molecular biology · doi:10.1007/978-1-60761-756-3_2 · Cited by 25
Neuroimmunomodulation by calcineurin in aging and Alzheimer's disease.
Reese, L. C., & Taglialatela, G. (2010) · Europe PMC (PubMed Central) · Cited by 26
β-amyloid and glutamate receptors
Gasparini, L., & Dityatev, A. E. (2008) · Experimental Neurology · doi:10.1016/j.expneurol.2008.03.005 · Cited by 24
Diabetes, Insulin and Alzheimer's Disease
Craft, S., & Christen, Y. (2010) · Research and perspectives in Alzheimer's disease · doi:10.1007/978-3-642-04300-0 · Cited by 24
Domínguez-Prieto, M., Velasco, A. L., Vega, L., Tabernero, A., & Medina, J. M. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-160346 · Cited by 24
Bories, C., Arsenault, D., Lemire, M., Tremblay, C., Koninck, Y. D., & Calon, F. (2017) · Aging · doi:10.18632/aging.101239 · Cited by 25
Melatonin in Synaptic Impairments of Alzheimer’s Disease
Shi, Y., Fang, Y., Wei, Y., Jiang, Q., Zeng, P. H., Tang, N., Lu, Y., & Tian, Q. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-171178 · Cited by 24
Puerariae Radix Prevents Anxiety and Cognitive Deficits in Mice Under Oligomeric Aβ-Induced Stress
Huang, H.-J., Huang, C.-Y., Lee, M., Lin, J., & Hsieh‐Li, H. M. (2019) · The American Journal of Chinese Medicine · doi:10.1142/s0192415x19500757 · Cited by 24
Cecchi, C., Pensalfini, A., Stefani, M., Baglioni, S., Fiorillo, C., Cappadona, S., Caporale, R., Nosi, D., Ruggiero, M., & Liguri, G. (2007) · Journal of Molecular Medicine · doi:10.1007/s00109-007-0265-3 · Cited by 24
Dequalinium-induced Protofibril Formation of α-Synuclein
Lee, C., Kim, H. J., Lee, J., Cho, H.-J., Kim, J., Chung, K. C., Jung, S., & Paik, S. R. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m505307200 · Cited by 24
Progressive Circuit Changes during Learning and Disease
Barth, A. L., & Ray, A. (2019) · Neuron · doi:10.1016/j.neuron.2019.09.032 · Cited by 24
Solórzano-Vargas, R. S., Vasilevko, V., Acero, G., Ugen, K. E., Martinez, R., Govezensky, T., Vázquez‐Ramírez, R., Kubli‐Garfias, C., Cribbs, D. H., Manoutcharian, K., et al. (2007) · Molecular Immunology · doi:10.1016/j.molimm.2007.08.008 · Cited by 24
Solomon, S., Sampathkumar, N. K., Carre, I., Mondal, M., Chennell, G., Vernon, A. C., Ruepp, M.-D., & Mitchell, J. C. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04473-1 · Cited by 23
McGeachan, R. I., Meftah, S., Taylor, L. W., Catterson, J. H., Negro, D., Bonthron, C., Holt, K., Tulloch, J., Rose, J. L., Gobbo, F., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-58879-z · Cited by 23
Wang, Y., Zheng, A., Yang, H., Wang, Q., Ren, B. X., Guo, T., Qiang, J., Cao, H., Gao, Y., Xu, L., et al. (2021) · Journal of Integrative Neuroscience · doi:10.31083/j.jin.2021.01.224 · Cited by 23
Targeting soluble amyloid-beta oligomers with a novel nanobody
Haynes, J. R., Whitmore, C. A., Behof, W. J., Landman, C. A., Ong, H. H., Feld, A. P., Suero, I. C., Greer, C. B., Gore, J. C., Wijesinghe, P., et al. (2024) · Scientific Reports · doi:10.1038/s41598-024-66970-6 · Cited by 23
Early inflammation and immune response mRNAs in the brain of AD11 anti-NGF mice
D’Onofrio, M., Arisi, I., Brandi, R., Mambro, A. D., Felsani, A., Capsoni, S., & Cattaneo, A. (2009) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2009.05.023 · Cited by 23
Fragile X mental retardation protein: from autism to neurodegenerative disease
Wang, H. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00043 · Cited by 26
Sell, G. L., Schaffer, T. B., & Margolis, S. S. (2017) · Journal of Clinical Investigation · doi:10.1172/jci85504 · Cited by 25
Klein, W. L., Lacor, P. N., Felice, F. G. D., & Ferreira, S. T. (2007) · Research and perspectives in neurosciences · doi:10.1007/978-3-540-45702-2_11 · Cited by 23
Self-citationParsons, C. G. (2019) · Neuropharmacology · doi:10.1016/j.neuropharm.2018.08.027 · Cited by 22
Cell size effects in the molecular dynamics of the intrinsically disordered Aβ peptide
Mehra, R., & Kepp, K. P. (2019) · The Journal of Chemical Physics · doi:10.1063/1.5115085 · Cited by 22
Specific binding of DNA to aggregated forms of Alzheimer's disease amyloid peptides
Camero, S., Ayuso, J. M., Barrantes, A., Benítez, M. J., & Jiménez, J. S. (2013) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2013.01.007 · Cited by 22
Orbán, G., Völgyi, K., Juhász, G. D., Penke, B., Kékesi, K. A., Kardos, J., & Czurkó, A. (2010) · Brain Research · doi:10.1016/j.brainres.2010.07.061 · Cited by 22
Bate, C., & Williams, A. (2015) · Biology · doi:10.3390/biology4030591 · Cited by 22
Sevlever, D., Zou, F., Ma, L., Carrasquillo, S., Crump, M., Culley, O. J., Hunter, T. A., Bisceglio, G. D., Younkin, L. H., Allen, M., et al. (2015) · Molecular Neurodegeneration · doi:10.1186/s13024-015-0015-x · Cited by 22
Morin, J., Cerón-Solano, G., Velázquez-Campos, G., Pacheco‐López, G., Bermúdez‐Rattoni, F., & Díaz-Cintra, S. Y. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-150975 · Cited by 22
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
Cai, H., Wang, Y., He, J., Cai, T., Wu, J., Fang, J., Zhang, R., Guo, Z., Guan, L., Zhan, Q., et al. (2017) · Oncotarget · doi:10.18632/oncotarget.21515 · Cited by 22
Li, W., Jin, L., Li, Y.-P., Feng, Q., Ren, L., Wang, F., & Bo, G.-J. (2018) · Neural Regeneration Research · doi:10.4103/1673-5374.239448 · Cited by 22
Mahaman, Y. A. R., Huang, F., Embaye, K. S., Wang, X., & Zhu, F. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.680118 · Cited by 22
Chapter 8 The Molecular and Cellular Pathogenesis of Dementia of the Alzheimer's Type
Luque, F. A., & Jaffe, S. L. (2009) · International review of neurobiology · doi:10.1016/s0074-7742(09)00408-5 · Cited by 22
Hong, H.-S., Maezawa, I., Petrlova, J., Zhao, X.-Y., C. Voss, J., & Jin, L.-W. (2015) · Journal of Alzheimer's Disease · doi:10.3233/jad-150318 · Cited by 23
Widespread γ-secretase activity in the cell, but do we need it at the mitochondria?
Teng, F. Y. H., & Tang, B. L. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.12.131 · Cited by 21
Chiang, H., Mudar, R. A., Pudhiyidath, A., Spence, J. S., Womack, K. B., Cullum, C. M., Tanner, J. A., Eroh, J., Kraut, M. A., & Hart, J. (2015) · Journal of Alzheimer s Disease · doi:10.3233/jad-142781 · Cited by 21
Mezias, C., & Raj, A. (2017) · Frontiers in Neurology · doi:10.3389/fneur.2017.00653 · Cited by 21
Rahman, K. A., Orlando, M., Boulos, A., Andrzejak, E., Schmitz, D., Ziv, N. E., Prüß, H., Garner, C. C., & Ichkova, A. (2023) · Glia · doi:10.1002/glia.24369 · Cited by 21
Ma, K., Lv, J., Yang, W., Chang, K.-W., Hu, X., Shi, L., Zhai, W.-Y., Zong, H.-F., & Qian, Y. (2017) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2017.11.006 · Cited by 21
Chatterjee, M., Kwon, J., Benedict, J., Kamceva, M., Kurup, P. K., & Lombroso, P. J. (2021) · Experimental Brain Research · doi:10.1007/s00221-020-06028-x · Cited by 21
Inhibition of heme synthesis alters Amyloid Precursor Protein processing
Gatta, L. B., Vitali, M. A., Verardi, R., Arosio, P., & Finazzi, D. (2008) · Journal of Neural Transmission · doi:10.1007/s00702-008-0147-z · Cited by 21
Microglia-Synapse Pathways: Promising Therapeutic Strategy for Alzheimer’s Disease
Xie, J., Wang, H., Lin, T., & Bi, B. (2017) · BioMed Research International · doi:10.1155/2017/2986460 · Cited by 22
Mandell, A. M., & Green, R. C. (2011) · Wiley eBooks · doi:10.1002/9781444344110.ch1 · Cited by 22
Borbély, E., Horváth, J., Furdan, S., Bozsó, Z., Penke, B., & Fülöp, L. (2014) · BioMed Research International · doi:10.1155/2014/345305 · Cited by 21
Santin, M. D., Vandenberghe, M. E., Herard, A.-S., Pradier, L., Cohen, C., Debeir, T., Delzescaux, T., Rooney, T., & Dhenain, M. (2016) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2016.00055 · Cited by 20
Snapshots of a protein folding intermediate
Yamada, S., Ford, N. B., Keller, G. E., Ford, W. C., Gray, H. B., & Winkler, J. R. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1221832110 · Cited by 20
Morrissey, J. A., Mockett, B. G., Singh, A., Kweon, D., Ohline, S. M., Tate, W. P., Hughes, S. M., & Abraham, W. C. (2019) · Neuropharmacology · doi:10.1016/j.neuropharm.2019.107670 · Cited by 24
Chang, K.-W., Zong, H.-F., Rizvi, M. Y., Ma, K., Zhai, W., Wang, M., Yang, W., Ji, S., & Qian, Y. (2020) · Neurobiology of Learning and Memory · doi:10.1016/j.nlm.2019.107154 · Cited by 20
Khan, Z. U., Carretero‐Rey, M., de León-López, C. A. M., & Navarro‐Lobato, I. (2025) · Molecular Neurobiology · doi:10.1007/s12035-025-05203-x · Cited by 28
Copper(ii) and zinc(ii) dependent effects on Aβ42 aggregation: a CD, Th-T and SFM study
Attanasio, F., Bona, P. D., Cataldo, S., Sciacca, M. F. M., Milardi, D., Pignataro, B., & Pappalardo, G. (2013) · New Journal of Chemistry · doi:10.1039/c3nj40999f · Cited by 20
Parodí, J., Ormeño, D., & la Paz, L. D. O.-D. (2015) · BMB Reports · doi:10.5483/bmbrep.2015.48.1.125 · Cited by 19
Two Distinct Conformations of Aβ Aggregates on the Surface of Living PC12 Cells
Bateman, D. A., & Chakrabartty, A. (2009) · Biophysical Journal · doi:10.1016/j.bpj.2009.01.056 · Cited by 19
Perlecan domain V inhibits α2 integrin-mediated amyloid-β neurotoxicity
Wright, S., Parham, C. L., Lee, B., Clarke, D. N., Auckland, L. D., Johnston, J. A., Lawrence, A. L., Dickeson, S. K., Santoro, S. A., Griswold‐Prenner, I., et al. (2010) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2010.10.018 · Cited by 19
Norvin, D., Kım, G., Baker‐Nigh, A., & Geula, C. (2015) · Neuroscience · doi:10.1016/j.neuroscience.2015.04.011 · Cited by 19
Biological Membranes as Protein Aggregation Matrices and Targets of Amyloid Toxicity
Bucciantini, M., & Cecchi, C. (2010) · Methods in molecular biology · doi:10.1007/978-1-60761-756-3_15 · Cited by 19
Lombroso, P. J., Ogren, M. P., Kurup, P. K., & Nairn, A. C. (2016) · F1000Research · doi:10.12688/f1000research.8571.1 · Cited by 19
Is Dementia More Fatal Than Previously Estimated? A Population-based Prospective Cohort Study
Bae, J. B., Han, J. W., Kwak, K. P., Kim, B., Kim, S. G., Kim, J. L., Kim, T. H., Ryu, S., Moon, S. W., Park, J. H., et al. (2018) · Aging and Disease · doi:10.14336/ad.2018.0123 · Cited by 19
Early mechanisms of amyloid fibril nucleation in model and disease-related proteins
Morel, B., & Conejero‐Lara, F. (2019) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2019.140264 · Cited by 19
Assessing the Effects of Acute Amyloid β Oligomer Exposure in the Rat
Wong, R., Cechetto, D. F., & Whitehead, S. N. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17091390 · Cited by 19
Xue, C., Tran, J., Wang, H., Park, G., Hsu, F., & Guo, Z. (2019) · Royal Society Open Science · doi:10.1098/rsos.190179 · Cited by 19
Proteomics of the astrocyte secretome reveals changes in their response to soluble oligomeric Aβ
Matafora, V., Gorb, A., Yang, F., Noble, W. J., Bachi, A., Perez‐Nievas, B. G., & Jiménez-Sánchez, M. (2023) · Journal of Neurochemistry · doi:10.1111/jnc.15875 · Cited by 19
Review of triazole scaffolds for treatment and diagnosis of Alzheimer's disease
Li, Q., Qi, S., Liang, J., Tian, Y., He, S., Liao, Q., Xing, S., Han, L., & Chen, X. (2023) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2023.110623 · Cited by 19
Wang, S., Kang, D. W., Um, Y. H., Kim, S., Lee, C. U., Scheltens, P., & Lim, H. K. (2024) · Alzheimer s Research & Therapy · doi:10.1186/s13195-024-01400-3 · Cited by 20
Synaptic and Sub-Synaptic Localization of Amyloid-β Protein Precursor in the Rat Hippocampus
Rodrigues, D. I., Gutierres, J. M., Pliássova, A., Oliveira, C. R., Cunha, R. A., & Agostinho, P. M. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-132030 · Cited by 18
Nakanishi, N., Ryan, S. D., Zhang, X., Khan, A. U., Holland, T., Cho, E.-G., Huang, X., Liao, F., Xu, H., Lipton, S. A., et al. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.4646-10.2013 · Cited by 18
Roy, M., Cardoso, C., Dorieux, O., Malgorn, C., Epelbaum, S., Petit, F., Kraska, A., Brouillet, E., Delatour, B., Perret, M., et al. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.07.017 · Cited by 21
Perspectives for treating Alzheimer's disease: a review on promising pharmacological substances
Cazarim, M. D. S., Moriguti, J. C., Ogunjimi, A. T., & Pereira, L. R. L. (2016) · Sao Paulo Medical Journal · doi:10.1590/1516-3180.2015.01980112 · Cited by 19
Drebrin and cognitive impairment
Ma, L., Li, Y., & Wang, R. (2015) · Clinica Chimica Acta · doi:10.1016/j.cca.2015.06.021 · Cited by 18
Alzheimer Disease: The Role of Aβ in the Glutamatergic System
Campos‐Peña, V., & Antônio, M. (2014) · InTech eBooks · doi:10.5772/57367 · Cited by 24
Alzheimer β-amyloid blocks epileptiform activity in hippocampal neurons
Sepúlveda, F. J., Opazo, C., & Aguayo, L. G. (2009) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2009.04.012 · Cited by 18
Probing differences among Aβ oligomers with two triangular trimers derived from Aβ
Kreutzer, A. G., Guaglianone, G., Yoo, S., Parrocha, C. M. T., Ruttenberg, S. M., Malonis, R. J., Tong, K., Lin, Y.-F., Nguyen, J. T., Howitz, W. J., et al. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2219216120 · Cited by 18
Amyloid solutions: lecanemab, gantenerumab, and donanemab in the treatment of Alzheimer's disease
Ameen, T. B., Ali, U., Salma, O., Samee, M. A., Abbas, S. M. I., Kashif, S. N., Arifi, M. A., Ali, M., Khowaja, M., Ali, S. M. S., et al. (2025) · The Egyptian Journal of Neurology Psychiatry and Neurosurgery · doi:10.1186/s41983-025-00968-3 · Cited by 20
Venkataramani, V., Wirths, O., Budka, H., Härtig, W., Kovács, G. G., & Bayer, T. A. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-111379 · Cited by 17
Quantitation and Mapping of Cerebral Detergent‐Insoluble Proteins in the Elderly
Woltjer, R. L., Sonnen, J. A., Sokal, I., Rung, L. G., Yang, W. J., Kjerulf, J. D., Klingert, D., Johnson, C., Rhew, I. C., Tsuang, D. W., et al. (2008) · Brain Pathology · doi:10.1111/j.1750-3639.2008.00190.x · Cited by 17
Amyloid Oligomer Structures and Toxicity
Glabe, C. G. (2009) · The Open Biology Journal · doi:10.2174/1874196700902010222 · Cited by 18
Terol, P. A., Kumita, J. R., Hook, S., Dobson, C. M., & Esbjörner, E. K. (2015) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2015.11.018 · Cited by 18
Insights into the Structure of Amyloid Fibrils
Marshall, K. E., & Serpell, L. C. (2009) · The Open Biology Journal · doi:10.2174/1874196700902010185 · Cited by 17
Szögi, T., Schuster, I., Borbély, E., Gyebrovszki, A., Bozsó, Z., Gera, J., Rajkó, R., Sántha, M., Penke, B., & Fülöp, L. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20123050 · Cited by 18
Alzheimer's amyloid story finds its star
Cole, G. M., & Frautschy, S. A. (2006) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2006.07.002 · Cited by 17
Izumi, H., Ishimoto, T., Yamamoto, H., Nishijo, H., & Mori, H. (2010) · Brain Structure and Function · doi:10.1007/s00429-010-0297-2 · Cited by 17
Aβ Infusion and Related Models of Alzheimer Dementia
Lawlor, P. A., & Young, D. (2010) · Neuromethods · doi:10.1007/978-1-60761-898-0_17 · Cited by 19
Analysis of DNA variations in promoter region of HCNP gene with Alzheimer’s disease
Okita, K., Matsukawa, N., Maki, M., Nakazawa, H., Katada, E., Hattori, M., Akatsu, H., Borlongan, C. V., & Ojika, K. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.12.037 · Cited by 17
Mouse models of neurodegenerative disease: preclinical imaging and neurovascular component
Albanese, S., Greco, A., Auletta, L., & Mancini, M. (2018) · Brain Imaging and Behavior · doi:10.1007/s11682-017-9770-3 · Cited by 16
Durell, S. R., Kayed, R., & Guy, H. R. (2022) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.26301 · Cited by 16
Preparation of α-Synuclein Amyloid Assemblies for Toxicity Experiments
Chen, S. W., & Cremades, N. (2018) · Methods in molecular biology · doi:10.1007/978-1-4939-7816-8_4 · 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-citationMembrane Remodeling by Arc/Arg3.1
Hedde, P. N., Malacrida, L. S., Baryłko, B., Binns, D. D., Albanesi, J. P., & Jameson, D. M. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.630625 · Cited by 16
Han, F., Zhao, J., & Zhao, G. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-210374 · Cited by 16
Gilson, V., Mbebi, C., Sellal, F., & de Barry, J. (2015) · Journal of Alzheimer s Disease · doi:10.3233/jad-142529 · Cited by 17
Lin, C., Nicol, C. J. B., Cheng, Y., Chen, S., Yen, C., Huang, R., & Chiang, M. (2018) · Experimental Cell Research · doi:10.1016/j.yexcr.2018.06.033 · Cited by 16
Translational considerations for CNS gene therapy
Ryan, D. A., & Federoff, H. J. (2007) · Expert Opinion on Biological Therapy · doi:10.1517/14712598.7.3.305 · Cited by 16
Emergence of Barrel Motif in Amyloid-β Trimer: A Computational Study
Nguyen, H. L., Linh, H. Q., Matteini, P., Penna, G. L., & Li, M. S. (2020) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.0c05508 · Cited by 15
Biasetti, L., Rey, S. A., Fowler, M. W., Ratnayaka, J. A., Fennell, K., Smith, C. A., Marshall, K. E., Hall, C. N., Vargas‐Caballero, M., Serpell, L. C., et al. (2022) · Cerebral Cortex · doi:10.1093/cercor/bhac134 · Cited by 15
Hydrogen Peroxide Modifies Aβ–Membrane Interactions with Implications for Aβ40 Aggregation
Pilkington, A. W., Donohoe, G. C., Akhmedov, N. G., Ferrebee, T., Valentine, S. J., & Legleiter, J. A. (2019) · Biochemistry · doi:10.1021/acs.biochem.9b00233 · Cited by 15
Ashe, K. H. (2007) · New England Journal of Medicine · doi:10.1056/nejmcibr073552 · Cited by 15
Niidome, T., Ishikawa, Y., Ogawa, T., Nakagawa, M., & Nakamura, Y. (2024) · Folia Pharmacologica Japonica · doi:10.1254/fpj.24005 · Cited by 14
Metadata
- Authors
- 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., Krafft, G. A., & Klein, W. L.
- Affiliations
- Northwestern University (US)
- University of Southern California (US)
- Acumen Pharmaceuticals (United States) (US)
- Corresponding author
- Klein, William L.
- Venue
- The Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 2004-11-10
- Volume
- 24
- Issue
- 45
- Pages
- 10191-10200
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- PMC
- PMC6730194
- OpenAlex
- W2162807572
- Cited by
- 954
- References
- 64
- Citations by year
- 2026: 14 · 2025: 18 · 2024: 24 · 2023: 41 · 2022: 35 · 2021: 28 · 2020: 26 · 2019: 32 · 2018: 41 · 2017: 50 · 2016: 51 · 2015: 50 · 2014: 54 · 2013: 65 · 2012: 59
- FWCI
- 25.08
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Neuroscience (publishedVersion, cc-by-nc-sa)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Illinois Department of Public Health
- Northwestern University
- National Institutes of Health (AG11385)
- National Institute on Aging (R01 AG11385, P30AG13854, R01AG022547, R01-AG22547, R01AG011385, R03AG022237, R01-AG18877, P30AG013854, R01AG018877)
- 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
- Alzheimer's disease, amyloid-beta oligomers, synaptic targeting, long-term potentiation, synaptic plasticity, PSD-95, Arc, hippocampal neurons, memory loss, early Alzheimer's disease
- MeSH terms
- Aged, Aged, 80 and over, Alzheimer Disease, Animals, Binding Sites, Cerebral Cortex, Cerebrospinal Fluid Proteins, Chromatography, High Pressure Liquid, Cytoskeletal Proteins, Female, Hippocampus, Humans, Male, Nerve Tissue Proteins, Neurons, Peptide Fragments, Protein Binding, Synapses, Tissue Extracts, Amyloid beta-Peptides, 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
