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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.
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“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]
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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
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Yin, Z., Geng, X., Zhang, Z., Wang, Y., & Gao, X. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.746711 · Cited by 40
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Wang, D., Chen, S.-S., Lee, Y., & Chen, T. (2006) · Neuroscience Letters · doi:10.1016/j.neulet.2005.12.057 · Cited by 40
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Yam, A. Y.-W., Wang, X., Gao, C. M., Connolly, M. D., Zuckermann, R. N., Bleu, T., Hall, J., Fedynyshyn, J. P., Allauzen, S., Peretz, D., et al. (2011) · Biochemistry · doi:10.1021/bi200215j · Cited by 39
Olabarria, M., Pasini, S., Corona, C., Robador, P. A., Song, C., Patel, H., & Lefort, R. (2019) · Communications Biology · doi:10.1038/s42003-019-0350-5 · Cited by 41
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Leung, H.-W., Foo, G., & VanDongen, A. M. J. (2022) · Biomedicines · doi:10.3390/biomedicines10081946 · Cited by 41
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Rosi, S. (2011) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2011.02.003 · Cited by 40
Grinevich, V., Kolleker, A., Eliava, M., Takada, N., Takuma, H., Fukazawa, Y., Shigemoto, R., Kuhl, D., Waters, J., Seeburg, P. H., et al. (2009) · Journal of Neuroscience Methods · doi:10.1016/j.jneumeth.2009.07.015 · Cited by 40
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Farı́as, G. G., Godoy, J. A., Cerpa, W. F., Varela‐Nallar, L., & Inestrosa, N. C. (2009) · Developmental Dynamics · doi:10.1002/dvdy.22065 · Cited by 39
Zhong, Y., Zhu, Y., He, T., Li, W., Yan, H., & Miao, Y. (2015) · Neuroscience Letters · doi:10.1016/j.neulet.2015.09.023 · Cited by 39
Marcatti, M., Fracassi, A., Montalbano, M., Natarajan, C., Krishnan, B., Kayed, R., & Taglialatela, G. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04255-9 · Cited by 38
Senapati, S., Tripathi, K. K., Awad, K., & Rahimipour, S. (2024) · Small · doi:10.1002/smll.202311670 · Cited by 39
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He, Y., Wang, P., Wei, P., Feng, H., Ren, Y., Yang, J.-D., Rao, Y., Shi, J., & Tian, J. (2016) · International Journal of Immunopathology and Pharmacology · doi:10.1177/0394632016638099 · Cited by 38
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Self-citationEthanol protects cultured neurons against amyloid-β and α-synuclein-induced synapse damage
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Initiative, A. D. N., Bi, R., Kong, L., Xu, M., Li, G.-D., Zhang, D., Li, T., Fang, Y., Zhang, C., Zhang, B., et al. (2017) · Molecular Neurobiology · doi:10.1007/s12035-017-0397-6 · Cited by 39
Roselli, F., Livrea, P., & Almeida, O. F. X. (2011) · PLoS ONE · doi:10.1371/journal.pone.0023097 · Cited by 38
Musardo, S., & Marcello, E. E. (2017) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2017.06.018 · Cited by 37
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Fonte, V. G., Dostal, V., Roberts, C. M., Gonzales, P. K., Lacor, P. N., Magrané, J., Dingwell, N., Fan, E. Y., Silverman, M. A., Stein, G. H., et al. (2011) · Molecular Neurodegeneration · doi:10.1186/1750-1326-6-61 · Cited by 37
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Garcin, C. L., & Habib, S. J. (2017) · Results and problems in cell differentiation · doi:10.1007/978-3-319-53150-2_15 · Cited by 40
Bateman, D. A., McLaurin, J., & Chakrabartty, A. (2007) · BMC Neuroscience · doi:10.1186/1471-2202-8-29 · Cited by 36
Alpha7 neuronal nicotinic receptors: The missing link to understanding Alzheimer’s etiopathology?
Bencherif, M., & Lippiello, P. M. (2009) · Medical Hypotheses · doi:10.1016/j.mehy.2009.09.011 · Cited by 36
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Grutzendler, J., & Gan, W. (2006) · NeuroRx · doi:10.1016/j.nurx.2006.07.005 · Cited by 37
Costantini, C., Bianca, V. D., Formaggio, E., Chiamulera, C., Montresor, A., & Rossi, F. (2005) · Experimental Cell Research · doi:10.1016/j.yexcr.2005.09.004 · Cited by 36
Martinsson, I., Quintino, L., Garcia, M. G., Konings, S. C., Torres-Garcia, L., Svanbergsson, A., Stange, O., England, R., Deierborg, T., Li, J., et al. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.946297 · Cited by 35
Xu, S., Guilan, L., Bao, X., Wu, J., Li, S., Zheng, B., Anwyl, R., & Wang, Q. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-130680 · Cited by 35
Significant structural but not physiological changes in cortical neurons of 12-month-old Tg2576 mice
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Self-citationWilcox, K. C., Marunde, M. R., Das, A., Velasco, P. T., Kuhns, B. D., Marty, M. T., Haoming, J., Luan, C.-H., Sligar, S. G., & Klein, W. L. (2015) · PLoS ONE · doi:10.1371/journal.pone.0125263 · Cited by 37
Self-citationKulikova, A. A., Makarov, A. А., & Kozin, S. A. (2015) · Molecular Biology · doi:10.1134/s0026893315020065 · Cited by 35
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Landgren, S., von Otter, M., Palmér, M. S., Zetterström, C. E., Nilsson, S., Skoog, I. G., Gustafson, D., Minthon, L., Wallin, A., Andreasen, N., et al. (2012) · Journal of Neural Transmission · doi:10.1007/s00702-012-0823-x · Cited by 34
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Wang, J., Zhao, Z., Lin, E., Zhao, W., Qian, X., Freire, D., Bilski, A. E., Cheng, A., Vempati, P., Ho, L., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0065232 · Cited by 35
Takamura, A., Okamoto, Y., Kawarabayashi, T., Yokoseki, T., Shibata, M. S., Mouri, A., Nabeshima, T., Sun, H., Abe, K., Urisu, T., et al. (2011) · Molecular Neurodegeneration · doi:10.1186/1750-1326-6-20 · Cited by 34
Mahaman, Y. A. R., Huang, F., Salissou, M. T. M., Yacouba, M. B. M., Wang, J., Liu, R., Zhang, B., Li, H., Zhu, F., & Wang, X. (2023) · Neurotherapeutics · doi:10.1007/s13311-023-01356-6 · Cited by 34
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Takamura, A., Sato, Y., Watabe, D., Okamoto, Y., Nakata, T., Kawarabayashi, T., Oddo, S., LaFerla, F. M., Shoji, M., & Matsubara, E. (2012) · Life Sciences · doi:10.1016/j.lfs.2012.04.038 · Cited by 33
Mendes, N. D., Fernandes, A., de Almeida, G. M., Santos, L. E., Sellés, M. C., Silva, N. M. L. E., Machado, C. D. M., Horta‐Júnior, J. D. A. C., Louzada, P. R., Felice, F. G. D., et al. (2018) · Journal of Neuroscience Methods · doi:10.1016/j.jneumeth.2018.05.021 · Cited by 35
Self-citationRole of Striatal-Enriched Tyrosine Phosphatase in Neuronal Function
Kamceva, M., Benedict, J., Nairn, A. C., & Lombroso, P. J. (2016) · Neural Plasticity · doi:10.1155/2016/8136925 · Cited by 33
Rammes, G., Mattusch, C., Wulff, M., Seeser, F., Kreuzer, M., Zhu, K., Deussing, J. M., Herms, J. W., & Parsons, C. G. (2017) · Neuropharmacology · doi:10.1016/j.neuropharm.2017.02.003 · Cited by 37
Espeseth, A. S., Xu, M., Huang, Q., Coburn, C. A., Jones, K. L., Ferrer, M., Zuck, P. D., Strulovici, B., Price, E. A., Wu, G., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414331200 · Cited by 33
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Quiroz‐Baez, R., Ferrera, P., Rosendo‐Gutiérrez, R., Morán, J., Bermúdez‐Rattoni, F., & Arias, C. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-110326 · Cited by 32
Pahnke, J., Fröhlich, C., Krohn, M., Schumacher, T., & Paarmann, K. (2013) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2013.08.007 · Cited by 35
Lipid microdomain modification sustains neuronal viability in models of Alzheimer’s disease
Herzer, S., Meldner, S., Rehder, K. F., Gröne, H., & Nordström, V. (2016) · Acta Neuropathologica Communications · doi:10.1186/s40478-016-0354-z · Cited by 33
Wang, X., Kastanenka, K. V., Arbel‐Ornath, M., Commins, C., Kuzuya, A., Lariviere, A., Krafft, G. A., Hefti, F. F., Jerecìć, J., & Bacskai, B. J. (2018) · Scientific Reports · doi:10.1038/s41598-018-22979-2 · Cited by 32
Self-citationTransdermal Delivery of Treatment for Alzheimer’s Disease
Chan, A. L. F., Chien, Y. W., & Lin, S. J. (2008) · Drugs & Aging · doi:10.2165/00002512-200825090-00003 · Cited by 32
Protective effect of new S-acylglutathione derivatives against amyloid-induced oxidative stress
Pensalfini, A., Cecchi, C., Zampagni, M., Becatti, M., Favilli, F., Paoli, P., Catarzi, S., Bagnoli, S., Nacmias, B., Sorbi, S., et al. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.01.025 · Cited by 32
Amyloid-β oligomer synaptotoxicity is mimicked by oligomers of the model protein HypF-N
Tatini, F., Pugliese, A. M., Traini, C., Niccoli, S., Maraula, G., Dami, T. E., Mannini, B., Scartabelli, T., Pedata, F., Casamenti, F., et al. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2013.03.020 · Cited by 33
Suram, A., Hegde, M. L., & Rao, K. S. J. (2007) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2007.03.015 · Cited by 32
Molecular Mechanisms of AMPA Receptor Trafficking in the Nervous System
Cao, Y., Ling-Ling, W., Li, X., Yuan, Y.-L., Zhao, W., Qi, J., Zhao, X.-Y., Ward, N., & Wang, J. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms25010111 · Cited by 36
Reelin-mediated Signaling during Normal and Pathological Forms of Aging.
Doehner, J., & Knuesel, I. (2010) · Europe PMC (PubMed Central) · Cited by 32
Yang, R., Zhao, G., Wang, D., Pang, X.-C., Wang, S., Fang, J., Li, C., Liu, A., Wu, S., & Du, G. (2015) · Pharmacology Biochemistry and Behavior · doi:10.1016/j.pbb.2015.10.009 · Cited by 31
Fang, X. T., Eriksson, J., Antoni, G., Yngve, U., Cato, L., Lannfelt, L., Sehlin, D., & Syvänen, S. (2016) · Neuropharmacology · doi:10.1016/j.neuropharm.2016.10.009 · Cited by 31
Development of grape polyphenols as multi-targeting strategies for Alzheimer's disease
Gaamouch, F. E., Liu, K., Lin, H., Wu, C., & Wang, J. (2021) · Neurochemistry International · doi:10.1016/j.neuint.2021.105046 · Cited by 31
Song, C., Zhang, T., & Zhang, Y. (2022) · Molecules · doi:10.3390/molecules27196751 · Cited by 33
Mahaman, Y. A. R., Feng, J., Huang, F., Salissou, M. T. M., Wang, J., Liu, R., Zhang, B., Li, H., Zhu, F., & Wang, X. (2022) · Nutrients · doi:10.3390/nu14204284 · Cited by 31
Differentiation Increases the Resistance of Neuronal Cells to Amyloid Toxicity
Cecchi, C., Pensalfini, A., Liguri, G., Baglioni, S., Fiorillo, C., Guadagna, S., Zampagni, M., Formigli, L., Nosi, D., & Stefani, M. (2008) · Neurochemical Research · doi:10.1007/s11064-008-9627-7 · Cited by 31
Wang, S., Yu, X., Cheng, L., Ren, W., Wen, G., Wu, X., Lou, H., Ren, X., Lu, L., Hermenean, A. O., et al. (2024) · Cell Death and Disease · doi:10.1038/s41419-024-06845-w · Cited by 30
Karasawa, T., & Lombroso, P. J. (2014) · Neuroscience Research · doi:10.1016/j.neures.2014.08.018 · Cited by 30
Aβ pathology downregulates brain mGluR5 density in a mouse model of Alzheimer
Lee, M., Lee, H., Park, I. S., Park, J. A., Kwon, Y., Ryu, Y. H., Kim, C. H., Kang, J. H., Hyun, I. Y., Lee, K. C., et al. (2018) · Neuropharmacology · doi:10.1016/j.neuropharm.2018.02.003 · Cited by 30
Nutraceutical based SIRT3 activators as therapeutic targets in Alzheimer's disease
Govindarajulu, M., Ramesh, S., Neel, L. T., Fabbrini, M., Buabeid, M. A., Fujihashi, A., Dwyer, D., Lynd, T. O., Shah, K., Mohanakumar, K. P., et al. (2021) · Neurochemistry International · doi:10.1016/j.neuint.2021.104958 · Cited by 31
Tau hyperphosphorylation affects Smad 2/3 translocation
Baig, S., Helmond, Z. V., & Love, S. (2009) · Neuroscience · doi:10.1016/j.neuroscience.2009.06.045 · Cited by 30
Ha, C., & Park, C. B. (2006) · Langmuir · doi:10.1021/la0601511 · Cited by 30
Warner, C. J. A., Dutta, S., Foley, A. R., & Raskatov, J. A. (2016) · Chemistry - A European Journal · doi:10.1002/chem.201601763 · Cited by 30
Rammes, G., Seeser, F., Mattusch, K., Zhu, K., Haas, L. T., Kummer, M. P., Heneka, M. T., Herms, J. W., & Parsons, C. G. (2018) · Neuropharmacology · doi:10.1016/j.neuropharm.2018.07.021 · Cited by 30
Lambert, M., Velasco, P., Viola, K., & Klein, W. (2009) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/187152709787601876 · Cited by 29
Self-citationAPP depletion alters selective pre- and post-synaptic proteins
Martinsson, I., Capetillo-Zarate, E., Faideau, M., Willén, K., Esteras, N., Frykman, S., Tjernberg, L. O., & Gouras, G. K. (2019) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2019.02.003 · Cited by 29
Polymorphism of Oligomers of a Peptide from β-Amyloid
Pham, J. D., Demeler, B., & Nowick, J. S. (2014) · Journal of the American Chemical Society · doi:10.1021/ja500996d · Cited by 29
Johnson, R. D., Steel, D. G., & Gafni, A. (2014) · Protein Science · doi:10.1002/pro.2479 · Cited by 29
EL-ASWAD, A. F., ALY, M. I., Fouad, M. R., & Badawy, M. E. I. (2019) · Journal of Environmental Science and Health Part B · doi:10.1080/03601234.2019.1595893 · Cited by 29
Viola, K. L., Bicca, M. A., Bebenek, A. M., Kranz, D. L., Nandwana, V., Waters, E. A., Haney, C. R., Lee, M. Y., Gupta, A., Brahmbhatt, Z., et al. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.768646 · Cited by 29
Self-citationCyclooxygenase-Dependent Lipid-Modification of Brain Proteins
Boutaud, O. G., Andreasson, K. I., Zagol-Ikapitte, I. A., & Oates, J. A. (2006) · Brain Pathology · doi:10.1111/j.1750-3639.2005.tb00510.x · Cited by 29
Promising Therapies for Alzheimer';s Disease
Confaloni, A., Tosto, G., & Tata, A. M. (2016) · Current Pharmaceutical Design · doi:10.2174/1381612822666160215154218 · Cited by 29
Parsons, C. G., & Rammes, G. (2017) · Expert Opinion on Investigational Drugs · doi:10.1080/13543784.2017.1313832 · Cited by 29
Poejo, J., Salazar, J., Mata, A. M., & Gutiérrez‐Merino, C. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094976 · Cited by 28
Ethanol Reduces Amyloid Aggregation In Vitro and Prevents Toxicity in Cell Lines
Ormeño, D., Romero, F., Fenner, J. L., Ávila, A. I., Martínez‐Torres, A., & Parodí, J. (2013) · Archives of Medical Research · doi:10.1016/j.arcmed.2012.12.004 · Cited by 29
Wang, X., Yang, W., Hölscher, C., Wang, Z., Cai, H., Li, Q., & Qi, J. (2013) · Journal of Neuroscience Research · doi:10.1002/jnr.23181 · Cited by 28
The elusive nature and diagnostics of misfolded Aβ oligomers
Cerasoli, E., Ryadnov, M. G., & Austen, B. (2015) · Frontiers in Chemistry · doi:10.3389/fchem.2015.00017 · Cited by 30
Legleiter, J. A., Fryer, J. D., Holtzman, D. M., & Kowalewski, T. (2011) · ACS Chemical Neuroscience · doi:10.1021/cn2000475 · Cited by 28
Williams, R. S. B., & Bate, C. (2015) · Neuropharmacology · doi:10.1016/j.neuropharm.2015.06.013 · Cited by 30
Structure-Selective Anisotropy Assay for Amyloid Beta Oligomers
Matveeva, E. G., Rudolph, A. S., Moll, J. R., & Thompson, R. B. (2012) · ACS Chemical Neuroscience · doi:10.1021/cn3001262 · Cited by 28
Aß Pathology and Neuron–Glia Interactions: A Synaptocentric View
Huffels, C. F. M., Middeldorp, J., & Hol, E. M. (2022) · Neurochemical Research · doi:10.1007/s11064-022-03699-6 · Cited by 29
Epelbaum, S., Youssef, I., Lacor, P. N., Chaurand, P., Duplus, E., Brugg, B., Duyckaerts, C. J., & Delatour, B. (2015) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2015.03.005 · Cited by 30
Self-citationWillén, K. I., Sroka-Oleksiak, A., Takahashi, R. H., & Gouras, G. K. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170262 · Cited by 28
Jaye, S., Sandau, U. S., & Saugstad, J. A. (2024) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2024.1378576 · Cited by 26
Ghatak, S., Nakamura, T., & Lipton, S. A. (2023) · Frontiers in Neural Circuits · doi:10.3389/fncir.2023.1099467 · Cited by 26
Dias, B. D. C., Jovanovic, K., Gonsalves, D., Moodley, K., Reusch, U., Knackmuss, S. H. J., Penny, C. B., Weinberg, M. S., Little, M., & Weiss, S. F. T. (2013) · Scientific Reports · doi:10.1038/srep02702 · Cited by 26
Kumar, A., Pate, K. M., Moss, M. A., Dean, D. N., & Rangachari, V. (2014) · PLoS ONE · doi:10.1371/journal.pone.0111492 · Cited by 26
Methods and models in neurodegenerative and systemic protein aggregation diseases.
Brorsson, A., Kumita, J. R., Ian, M., Bolognesi, B., Speretta, E., Luheshi, L. M., Knowles, T. P. J., Dobson, C. M., & Crowther, D. C. (2010) · PubMed · doi:10.2741/3626 · Cited by 26
Sandberg, A., Berenjeno‐Correa, E., Rodriguez, R. C., Axenhus, M., Weiss, S. S., Batenburg, K. L., Hoozemans, J. J. M., Tjernberg, L. O., & Scheper, W. (2022) · Alzheimer s Research & Therapy · doi:10.1186/s13195-022-01141-1 · Cited by 29
Chen, Y., Wang, X., Xiao, B., Luo, Z., & Long, H. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03442-4 · Cited by 26
Elucidating Molecular Mass and Shape of a Neurotoxic Aβ Oligomer
Sebollela, A. S., Mustata, G.-M., Luo, K., Velasco, P. T., Viola, K. L., Cline, E. N., Shekhawat, G. S., Wilcox, K. C., Dravid, V. P., & Klein, W. L. (2014) · ACS Chemical Neuroscience · doi:10.1021/cn500156r · Cited by 25
Self-citationDiChiara, T., DiNunno, N., Clark, J. R., Bu, R. L., Cline, E. N., Rollins, M. G., Gong, Y., Brody, D. L., Sligar, S. G., Velasco, P. T., et al. (2017) · PubMed · Cited by 25
Self-citationCline, E. N., Das, A., Bicca, M. A., Mohammad, S. N., Schachner, L. F., Kamel, J. M., DiNunno, N., Weng, A., Paschall, J. D., Bu, R. L., et al. (2018) · Journal of Neurochemistry · doi:10.1111/jnc.14647 · Cited by 25
Self-citationMuscone Ameliorates Synaptic Dysfunction and Cognitive Deficits in APP/PS1 Mice
Liu, Y., Bian, H., Xu, S., Shu, S., Jia, J., Chen, J., Cao, X., Bao, X., Gu, Y., Xia, S., et al. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-200188 · Cited by 26
Morales-Zavala, F., Jara-Guajardo, P., Chamorro, D., Riveros, A. L., Chandía-Cristi, A., Salgado, N., Pismante, P., Giralt, E., Sánchez‐Navarro, M., Araya, E., et al. (2021) · Biomaterials Science · doi:10.1039/d0bm01825b · Cited by 25
Melatonin: Regulation of Prion Protein Phase Separation in Cancer Multidrug Resistance
Loh, D., & Reiter, R. J. (2022) · Molecules · doi:10.3390/molecules27030705 · Cited by 25
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
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