The DOI matches its Crossref record; 30 of the 31 references it cites were found in a registry or an index.
Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo
Abstract
Although extensive data support a central pathogenic role for amyloid beta protein (Abeta) in Alzheimer's disease, the amyloid hypothesis remains controversial, in part because a specific neurotoxic species of Abeta and the nature of its effects on synaptic function have not been defined in vivo. Here we report that natural oligomers of human Abeta are formed soon after generation of the peptide within specific intracellular vesicles and are subsequently secreted from the cell. Cerebral microinjection of cell medium containing these oligomers and abundant Abeta monomers but no amyloid fibrils markedly inhibited hippocampal long-term potentiation (LTP) in rats in vivo. Immunodepletion from the medium of all Abeta species completely abrogated this effect. Pretreatment of the medium with insulin-degrading enzyme, which degrades Abeta monomers but not oligomers, did not prevent the inhibition of LTP. Therefore, Abeta oligomers, in the absence of monomers and amyloid fibrils, disrupted synaptic plasticity in vivo at concentrations found in human brain and cerebrospinal fluid. Finally, treatment of cells with gamma-secretase inhibitors prevented oligomer formation at doses that allowed appreciable monomer production, and such medium no longer disrupted LTP, indicating that synaptotoxic Abeta oligomers can be targeted therapeutically.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“The cognitive decline, however, starts well before this stage, and there is growing evidence that one of the toxic protein species believed to be etiologically related to AD, soluble Ab oligomers, causes early memory problems by disrupting LTP and LTD mechanisms (Walsh et al. 2002;Tanzi 2005;Shankar et al. 2008;Cisse et al. 2011).”
From NMDA receptor-dependent long-term potentiation and long-term depression (LTP/LTD). (2012) · cites this paper as Walsh et al. 2002
In the citing paper
“While Aβ disrupts synaptic transmission 32,34,35 and induces synapse loss 17”
From NAD+ hydrolase Sarm1 is a key driver of synapse degeneration and memory loss in Alzheimer’s disease (2025) · cites this paper as [32]
In the citing paper
“When amyloid-β oligomers bind to PrPc, long-term potentiation and the formation of new memories are disrupted [129,130,131].”
From Sigma-2 Receptors—From Basic Biology to Therapeutic Target: A Focus on Age-Related Degenerative Diseases (2023) · cites this paper as [129]
In the citing paper
“As a result of these two mechanisms, activated GSK3β and increased calcineurin and STEP activation, Aβ oligomers reduce LTP [40].”
From ApoE, ApoE Receptors, and the Synapse in Alzheimer's Disease (2017) · cites this paper as [40]
In the citing paper
“This was followed by evidence indicating that soluble oligomeric Aβ mediates synaptic dysfunction and neuronal toxicity [31–33].”
From Systems-based proteomics to resolve the biology of Alzheimer’s disease beyond amyloid and tau (2021) · cites this paper as [32]
In the citing paper
“Many in vitro and in vivo studies have shown that exogenous application of Aβ alters synaptic plasticity [170, 198] and important synaptic proteins [3, 79, 177], although how precisely this occurs remains unclear.”
From Intraneuronal β-amyloid accumulation and synapse pathology in Alzheimer’s disease (2010) · cites this paper as [198]
Citations
Cites
Alzheimer's Disease: Genes, Proteins, and Therapy
Selkoe, D. J. (2001) · Physiological Reviews · doi:10.1152/physrev.2001.81.2.741 · Cited by 6,063
Self-citationTerry, R. D., Masliah, E., Salmon, D. P., Butters, N., DeTeresa, R., Hill, R., Hansen, L. A., & Katzman, R. (1991) · Annals of Neurology · doi:10.1002/ana.410300410 · Cited by 4,397
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
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
Enhanced neurofibrillary degeneration in transgenic mice expressing mutant tau and APP
Lewis, J., Dickson, D. W., Lin, W.-L., Chisholm, L., Corral, A., Jones, G., Yen, S.-H., Sahara, N., Skipper, L., Yager, D., et al. (2001) · Science · doi:10.1126/science.1058189 · Cited by 1,611
Soluble Amyloid β Peptide Concentration as a Predictor of Synaptic Change in Alzheimer's Disease
Lue, L.-F., Kuo, Y.-M., Roher, A. E., Brachova, L., Shen, Y., Sue, L., Beach, T., Kurth, J. H., Rydel, R. E., & Rogers, J. (1999) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)65184-x · Cited by 1,530
Beta-amyloid neurotoxicity requires fibril formation and is inhibited by congo red.
Lorenzo, A., & Yankner, B. A. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.25.12243 · Cited by 1,324
Plaque-independent disruption of neural circuits in Alzheimer’s disease mouse models
Hsia, A. Y., Masliah, E., McConlogue, L., Yu, G.-Q., Tatsuno, G., Hu, K., Kholodenko, D., Malenka, R. C., Nicoll, R. A., & Mucke, L. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.6.3228 · Cited by 1,123
Amyloid fibrillogenesis: themes and variations
Rochet, J., & Lansbury, P. T. (2000) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(99)00049-4 · Cited by 1,095
Amyloid β-Protein Fibrillogenesis
Walsh, D. M., Hartley, D. M., Kusumoto, Y., Fezoui, Y., Condron, M. M., Lomakin, A., Benedek, G. B., Selkoe, D. J., & Teplow, D. B. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.36.25945 · Cited by 1,046
Self-citation
Flagged first, then by citations
1 of the 31 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Items 601–700 of 1,069
The synaptic Aβ hypothesis of Alzheimer disease
Tanzi, R. E. (2005) · Nature Neuroscience · doi:10.1038/nn0805-977 · Cited by 206
Perez-Cruz, C., Nolte, M. W., van Gaalen, M. M., Rustay, N. R., Termont, A., Tanghe, A., Kirchhoff, F., & Ebert, U. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.6142-10.2011 · Cited by 172
Metal complexes designed to bind to amyloid-β for the diagnosis and treatment of Alzheimer's disease
Hayne, D. J., Lim, S., & Donnelly, P. S. (2014) · Chemical Society Reviews · doi:10.1039/c4cs00026a · Cited by 178
Single-channel Ca2+ imaging implicates Aβ1–42 amyloid pores in Alzheimer’s disease pathology
Demuro, A., Smith, M., & Parker, I. (2011) · The Journal of Cell Biology · doi:10.1083/jcb.201104133 · Cited by 179
Targeting Amyloid Aggregation: An Overview of Strategies and Mechanisms
Giorgetti, S., Greco, C., Tortora, P., & Aprile, F. A. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19092677 · Cited by 179
Behavioral phenotypes of amyloid‐based genetically modified mouse models of Alzheimer's disease
Kobayashi, D. T., & Chen, K. S. (2005) · Genes Brain & Behavior · doi:10.1111/j.1601-183x.2005.00124.x · Cited by 182
Deregulation of excitatory neurotransmission underlying synapse failure in Alzheimer's disease
Paula‐Lima, A. C., Brito‐Moreira, J., & Ferreira, S. T. (2013) · Journal of Neurochemistry · doi:10.1111/jnc.12304 · Cited by 170
PET amyloid-beta imaging in preclinical Alzheimer's disease
Vlassenko, A. G., Benzinger, T. L. S., & Morris, J. C. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.11.005 · Cited by 188
Villemagne, V. L., Ataka, S., Mizuno, T., Brooks, W. S., Wada, Y., Kondo, M., Jones, G. R., Watanabe, Y., Mulligan, R. S., Nakagawa, M., et al. (2009) · Archives of Neurology · doi:10.1001/archneurol.2009.285 · Cited by 176
Synaptic pathology: A shared mechanism in neurological disease
Henstridge, C. M., Pickett, E. K., & Spires‐Jones, T. L. (2016) · Ageing Research Reviews · doi:10.1016/j.arr.2016.04.005 · Cited by 176
ADF/Cofilin-Actin Rods in Neurodegenerative Diseases
Bamburg, J. R., Bernstein, B. W., Davis, R. C., Flynn, K. C., Goldsbury, C., Jensen, J. R., Maloney, M. T., Marsden, I. T., Minamide, L. S., Pak, C. W., et al. (2010) · Current Alzheimer Research · doi:10.2174/156720510791050902 · Cited by 173
Caccamo, A., Maldonado, M. A., Majumder, S., Medina, D. X., Holbein, W. W., Magrì, A., & Oddo, S. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.180638 · Cited by 186
Noguchi, A., Matsumura, S., Dezawa, M., Tada, M., Yanazawa, M., Ito, A., Akioka, M., Kikuchi, S., Sato, M., Ideno, S., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.000208 · Cited by 173
Calcium signalling and Alzheimer's disease
Berridge, M. J. (2011) · Neurochemical Research · doi:10.1007/s11064-010-0371-4 · Cited by 167
Thermodynamics and Kinetics of Aggregation for the GNNQQNY Peptide
Strodel, B., Whittleston, C. S., & Wales, D. J. (2007) · Journal of the American Chemical Society · doi:10.1021/ja075346p · Cited by 176
Withanoside IV and its active metabolite, sominone, attenuate Aβ(25–35)‐induced neurodegeneration
Kuboyama, T., Tohda, C., & Komatsu, K. (2006) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2006.04664.x · Cited by 171
Cytoskeletal pathologies of Alzheimer disease
Bamburg, J. R., & Bloom, G. S. (2009) · Cell Motility and the Cytoskeleton · doi:10.1002/cm.20388 · Cited by 175
Interactions between APP secretases and inflammatory mediators
Sastre, M., Walter, J., & Gentleman, S. (2008) · Journal of Neuroinflammation · doi:10.1186/1742-2094-5-25 · Cited by 178
McKeever, P. M., Schneider, R., Taghdiri, F., Weichert, A., Multani, N., Brown, R. A., Boxer, A. L., Karydas, A., Miller, B., Robertson, J., et al. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-1032-x · Cited by 166
Neuroplasticity in Alzheimer's disease
Teter, B., & Ashford, J. W. (2002) · Journal of Neuroscience Research · doi:10.1002/jnr.10441 · Cited by 170
Rival, T., Page, R. M., Chandraratna, D. S., Sendall, T. J., Ryder, E. J., Liu, B., Lewis, H. D., Rosahl, T. W., Hider, R. C., Camargo, L. M., et al. (2009) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2009.06701.x · Cited by 171
The Role of the Tripartite Glutamatergic Synapse in the Pathophysiology of Alzheimer’s Disease
Rudy, C. C., Hunsberger, H. C., Weitzner, D. S., & Reed, M. N. (2015) · Aging and Disease · doi:10.14336/ad.2014.0423 · Cited by 187
γ-secretases: from cell biology to therapeutic strategies
Bergmans, B. A., & Strooper, B. D. (2010) · The Lancet Neurology · doi:10.1016/s1474-4422(09)70332-1 · Cited by 179
Matsuzaki, K. (2014) · Accounts of Chemical Research · doi:10.1021/ar500127z · Cited by 173
Secretase inhibitors for the treatment of Alzheimer's disease: Long road ahead
Kumar, D., Ganeshpurkar, A., Kumar, D., Modi, G. P., Gupta, S., & Singh, S. K. (2018) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2018.02.035 · Cited by 170
Integrins in synapse regulation
Park, Y. K., & Goda, Y. (2016) · Nature Reviews Neuroscience · doi:10.1038/nrn.2016.138 · Cited by 167
A High-Throughput Screen for Compounds That Inhibit Aggregation of the Alzheimer’s Peptide
Kim, W., Kim, Y., Min, J., Kim, D. J., Chang, Y., & Hecht, M. H. (2006) · ACS Chemical Biology · doi:10.1021/cb600135w · Cited by 169
Amyloid formation as a protein phase transition
Michaels, T. C. T., Qian, D., Šarić, A., Vendruscolo, M., Linse, S. S., & Knowles, T. P. J. (2023) · Nature Reviews Physics · doi:10.1038/s42254-023-00598-9 · Cited by 164
Hu, Y., Xu, P., Pigino, G. F., Brady, S. T., Larson, J., & Lazarov, O. (2010) · The FASEB Journal · doi:10.1096/fj.09-136945 · Cited by 176
Henley, D. B., May, P. C., Dean, R. A., & Siemers, E. (2009) · Expert Opinion on Pharmacotherapy · doi:10.1517/14656560903044982 · Cited by 168
Chami, L., & Checler, F. (2012) · Molecular Neurodegeneration · doi:10.1186/1750-1326-7-52 · Cited by 168
Broersen, K., Rousseau, F., & Schymkowitz, J. (2010) · Alzheimer's Research & Therapy · doi:10.1186/alzrt36 · Cited by 168
A polymer physics perspective on driving forces and mechanisms for protein aggregation
Pappu, R. V., Wang, X., Vitalis, A., & Crick, S. L. (2007) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2007.08.033 · Cited by 170
Decker, H., Jürgensen, S., Adrover, M. F., Brito‐Moreira, J., Bomfim, T. R., Klein, W. L., Epstein, A. L., Felice, F. G. D., Jerusalinsky, D. A., & Ferreira, S. T. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.07058.x · Cited by 172
Volianskis, A., Køstner, R., Mølgaard, M., Hass, S., & Jensen, M. S. (2008) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2008.08.005 · Cited by 179
Sadowski, M. J., Pankiewicz, J., Scholtzova, H., Mehta, P. D., Prelli, F., Quartermain, D., & Wisniewski, T. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0604011103 · Cited by 167
Orally available compound prevents deficits in memory caused by the Alzheimer amyloid‐β oligomers
Townsend, M., Cleary, J. P., Mehta, T., Hofmeister, J. J., Lesné, S., O‘Hare, E., Walsh, D. M., & Selkoe, D. J. (2006) · Annals of Neurology · doi:10.1002/ana.21051 · Cited by 169
Self-citationSanchez‐Ramos, J., Song, S., Sava, V. M., Catlow, B. J., Lin, X., Mori, T., Cao, C., & Arendash, G. W. (2009) · Neuroscience · doi:10.1016/j.neuroscience.2009.05.071 · Cited by 165
Berson, A., Barbash, S., Shaltiel, G., Goll, Y., Hanin, G., Greenberg, D., Ketzef, M., Becker, A. J., Friedman, A., & Soreq, H. (2012) · EMBO Molecular Medicine · doi:10.1002/emmm.201100995 · Cited by 166
Residues 17–20 and 30–35 of beta‐amyloid play critical roles in aggregation
Liu, R., McAllister, C., Lyubchenko, Y. L., & Sierks, M. R. (2003) · Journal of Neuroscience Research · doi:10.1002/jnr.10859 · Cited by 166
ApoE, ApoE Receptors, and the Synapse in Alzheimer's Disease
Lane-Donovan, C., & Herz, J. (2017) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2016.12.001 · Cited by 157
“Jo J, et al. Abeta(1-42) inhibition of LTP is mediated by a signaling pathway involving caspase-3, Akt1 and GSK-3beta.”
BackgroundInfluentialDesigning Peptide Inhibitors for Oligomerization and Toxicity of Alzheimer's β-Amyloid Peptide
Austen, B., Paleologou, K. E., Ali, S. A. E., Qureshi, M. M., Allsop, D., & El‐Agnaf, O. M. A. (2008) · Biochemistry · doi:10.1021/bi701415b · Cited by 170
Falker‐Gieske, C., Hartmann, A., Guett, I., Dohler, F., Altmeppen, H. C., Betzel, C., Schubert, R., Thurm, D., Wegwitz, F., Joshi, P., et al. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.13514 · Cited by 166
Bode, D. C., Freeley, M., Nield, J., Palma, M., & Viles, J. H. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ac118.007195 · Cited by 166
The complement cascade: Yin-Yang in neuroinflammation—neuro-protection and -degeneration
Alexander, J. J., Anderson, A. J., Barnum, S. R., Stevens, B., & Tenner, A. J. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05668.x · Cited by 177
Li, Q., Zhao, H., Zhang, Z. F., Liu, Z. G., Pei, X., Wang, J. B., & Li, Y. (2009) · Neuroscience · doi:10.1016/j.neuroscience.2009.07.014 · Cited by 165
Nygaard, H. B., Wagner, A. F., Bowen, G. S., Good, S. P., MacAvoy, M. G., Strittmatter, K. A., Kaufman, A. C., Rosenberg, B. J., Sekine-Konno, T., Varma, P., et al. (2015) · Alzheimer s Research & Therapy · doi:10.1186/s13195-015-0119-0 · Cited by 168
Hellström‐Lindahl, E., Ravid, R., & Nordberg, A. K. (2006) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2006.10.010 · Cited by 167
Hoey, S. E., Williams, R. J., & Perkinton, M. S. (2009) · The Journal of Neuroscience · doi:10.1523/jneurosci.6017-08.2009 · Cited by 178
Alzheimer's disease and acetylcholine receptors
Kihara, T., & Shimohama, S. (2004) · Acta Neurobiologiae Experimentalis · doi:10.55782/ane-2004-1495 · Cited by 166
Rammes, G., Hasenjäger, A., Sroka-Saidi, K., Deussing, J. M., & Parsons, C. G. (2011) · Neuropharmacology · doi:10.1016/j.neuropharm.2011.01.051 · Cited by 163
Tchantchou, F., Lacor, P. N., Cao, Z., Lao, L., Hou, Y., Cui, C., Klein, W. L., & Luo, Y. (2009) · Journal of Alzheimer s Disease · doi:10.3233/jad-2009-1189 · Cited by 164
Crimins, J. L., Pooler, A. M., Polydoro, M., Luebke, J. I., & Spires‐Jones, T. L. (2013) · Ageing Research Reviews · doi:10.1016/j.arr.2013.03.002 · Cited by 173
Taylor, M., Moore, S., Mayes, J., Parkin, E. T., Beeg, M., Canovi, M., Gobbi, M., Mann, D. M. A., & Allsop, D. (2010) · Biochemistry · doi:10.1021/bi100144m · Cited by 166
Protein‐folding kinetics and mechanisms studied by pulse‐labeling and mass spectrometry
Konermann, L., & Simmons, D. A. (2003) · Mass Spectrometry Reviews · doi:10.1002/mas.10044 · Cited by 162
H UMAN N EURODEGENERATIVE D ISEASE M ODELING U SING D ROSOPHILA
Bonini, N. M., & Fortini, M. (2003) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.26.041002.131425 · Cited by 169
Fernando, W. M. A. D. B., Martins, I. J., Morici, M., Bharadwaj, P., Rainey-Smith, S. R., Lim, W. L. F., & Martins, R. N. (2020) · Journal of Alzheimer's Disease · doi:10.3233/jad-190120 · Cited by 164
Targeting Fyn Kinase in Alzheimer’s Disease
Nygaard, H. B. (2018) · Biological Psychiatry · doi:10.1016/j.biopsych.2017.06.004 · Cited by 162
γ-Secretase Modulators as Potential Disease Modifying Anti-Alzheimer’s Drugs
Oehlrich, D., Berthelot, D., & Gijsen, H. J. M. (2010) · Journal of Medicinal Chemistry · doi:10.1021/jm101168r · Cited by 163
Structural Properties of EGCG-Induced, Nontoxic Alzheimer's Disease Aβ Oligomers
del Amo, J. M. L., Fink, U., Dasari, M., Grelle, G., Wanker, E. E., Bieschke, J., & Reif, B. (2012) · Journal of Molecular Biology · doi:10.1016/j.jmb.2012.01.013 · Cited by 160
Clearance of Amyloid-β Peptides By Microglia and Macrophages: the Issue of What, When and Where
Lai, A. Y., & McLaurin, J. (2012) · Future Neurology · doi:10.2217/fnl.12.6 · Cited by 166
Genetic modulation of polyglutamine toxicity by protein conjugation pathways in Drosophila
Chan, H. Y. E. (2002) · Human Molecular Genetics · doi:10.1093/hmg/11.23.2895 · Cited by 165
Harris, S. S., Wolf, F., De Strooper, B., & Busche, M. A. (2020) · Neuron · doi:10.1016/j.neuron.2020.06.005 · Cited by 161
Leroy, K., Ando, K., Laporte, V., Dedecker, R., Suain, V., Authelet, M., Héraud, C., Pierrot, N., Yilmaz, Z., Octave, J.-N., et al. (2012) · The American Journal of Pathology · doi:10.1016/j.ajpath.2012.08.012 · Cited by 161
Soluble Aβ oligomers impair hippocampal LTP by disrupting glutamatergic/GABAergic balance
Lei, M., Xu, H., Li, Z., Wang, Z., O’Malley, T. T., Zhang, D., Walsh, D. M., Xu, P., Selkoe, D. J., & Li, S. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.10.019 · Cited by 162
Self-citationMurakami, K., Irie, K., Ohigashi, H., Hara, H., Nagao, M., Shimizu, T., & Shirasawa, T. (2005) · Journal of the American Chemical Society · doi:10.1021/ja054041c · Cited by 161
Peric, A., & Annaert, W. G. (2015) · Acta Neuropathologica · doi:10.1007/s00401-014-1379-7 · Cited by 172
Yan, L., Velkova, A., Tatarek‐Nossol, M., Andreetto, E., & Kapurniotu, A. (2007) · Angewandte Chemie International Edition · doi:10.1002/anie.200604056 · Cited by 164
Green, J. D., Kreplak, L., Goldsbury, C. S., Li‐Blatter, X., Stolz, M., Cooper, G. J. S., Seelig, A., Kistler, J., & Aebi, U. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.07.052 · Cited by 161
A Molecular Switch in Amyloid Assembly: Met35and Amyloid β-Protein Oligomerization
Bitan, G., Tarus, B., Vollers, S. S., Lashuel, H. A., Condron, M. M., Straub, J. E., & Teplow, D. B. (2003) · Journal of the American Chemical Society · doi:10.1021/ja0349296 · Cited by 158
Ellis, R. J., & Pinheiro, T. J. T. (2002) · Nature · doi:10.1038/416483a · Cited by 162
Alzheimer's disease and post-operative cognitive dysfunction
Xie, Z., & Tanzi, R. E. (2006) · Experimental Gerontology · doi:10.1016/j.exger.2006.01.014 · Cited by 159
Mahmoudi, M., Quinlan-Pluck, F., Monopoli, M. P., Sheibani, S., Vali, H., Dawson, K. A., & Lynch, I. (2012) · ACS Chemical Neuroscience · doi:10.1021/cn300196n · Cited by 162
Localization and Processing of the Amyloid-β Protein Precursor in Mitochondria-Associated Membranes
Prete, D. D., Suski, J. M., Oulès, B., Debayle, D., Gay, A.-S., Lacas‐Gervais, S., Bussiere, R., Bauer, C., Pinton, P., Paterlini-Bréchot, P., et al. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-160953 · Cited by 167
Distinct thermodynamic signatures of oligomer generation in the aggregation of the amyloid-β peptide
Cohen, S. I. A., Cukalevski, R., Michaels, T. C. T., Šarić, A., Törnquist, M., Vendruscolo, M., Dobson, C. M., Buell, A. K., Knowles, T. P. J., & Linse, S. S. (2018) · Nature Chemistry · doi:10.1038/s41557-018-0023-x · Cited by 161
Chronic dietary α-lipoic acid reduces deficits in hippocampal memory of aged Tg2576 mice
Quinn, J. F., Bussiere, J. R., Hammond, R., Montine, T. J., Henson, E., Jones, R. E., & Stackman, R. W. (2006) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.12.014 · Cited by 161
Mizuno, T., Doi, Y., Mizoguchi, H., Jin, S., Noda, M., Sonobe, Y., Takeuchi, H., & Suzumura, A. (2011) · The American Journal of Pathology · doi:10.1016/j.ajpath.2011.06.011 · Cited by 159
Oxidative Stress and Cell Membranes in the Pathogenesis of Alzheimer's Disease
Axelsen, P. H., Komatsu, H., & Murray, I. V. J. (2011) · Physiology · doi:10.1152/physiol.00024.2010 · Cited by 159
More than cholesterol transporters: lipoprotein receptors in CNS function and neurodegeneration
Lane-Donovan, C., Philips, G. T., & Herz, J. (2014) · Neuron · doi:10.1016/j.neuron.2014.08.005 · Cited by 158
Faraco, G., Park, L., Zhou, P., Luo, W., Paul, S. M., Anrather, J., & Iadecola, C. (2016) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.2015.79 · Cited by 158
Balducci, C., Mancini, S., Minniti, S., La Vitola, P., Zotti, M., Sancini, G., Mauri, M., Cagnotto, A., Colombo, L., Fiordaliso, F., et al. (2014) · The Journal of Neuroscience · doi:10.1523/jneurosci.0284-14.2014 · Cited by 162
Wu, J., Breydo, L., Isas, J. M., Lee, J., Kuznetsov, Y. G., Langen, R., & Glabe, C. G. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.069542 · Cited by 163
Lesné, S., Kotilinek, L., & Ashe, K. H. (2007) · Neuroscience · doi:10.1016/j.neuroscience.2007.10.054 · Cited by 159
The synapse as a treatment avenue for Alzheimer’s Disease
Peng, L., Bestard‐Lorigados, I., & Song, W. (2022) · Molecular Psychiatry · doi:10.1038/s41380-022-01565-z · Cited by 162
Immunotherapy for Alzheimer's disease
Gélinas, D. S., Silva, K. D., Fenili, D., George‐Hyslop, P. S., & McLaurin, J. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0404866101 · Cited by 161
Amyloid‐ß‐directed immunotherapy for Alzheimer's disease
Lannfelt, L., Relkin, N. R., & Siemers, E. (2014) · Journal of Internal Medicine · doi:10.1111/joim.12168 · Cited by 161
The molecular mechanism of fullerene-inhibited aggregation of Alzheimer's β-amyloid peptide fragment
Xie, L., Luo, Y., Lin, D., Xi, W., Yang, X., & Wei, G. (2014) · Nanoscale · doi:10.1039/c4nr01005a · Cited by 157
Monomer-dependent secondary nucleation in amyloid formation
Linse, S. S. (2017) · Biophysical Reviews · doi:10.1007/s12551-017-0289-z · Cited by 158
Wang, Z., Jackson, R. J., Hong, W., Taylor, W. M., Corbett, G. T., Moreno, A. J., Liu, W., Li, S., Frosch, M. P., Slutsky, I., et al. (2017) · Journal of Neuroscience · doi:10.1523/jneurosci.2009-17.2017 · Cited by 157
Self-citationAβ Oligomer-Induced Synapse Degeneration in Alzheimer’s Disease
Wilcox, K. C., Lacor, P. N., Pitt, J. E., & Klein, W. L. (2011) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-011-9691-4 · Cited by 159
Viayna, E., Sola, I., Bartolini, M., Simone, A. D., Tapia‐Rojas, C., Serrano, F. G., Sabaté, R., Juárez‐Jiménez, J., Pérez, B., Luque, F. J., et al. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm401824w · Cited by 156
Experimental investigation of protein folding and misfolding
Dobson, C. M. (2004) · Methods · doi:10.1016/j.ymeth.2004.03.002 · Cited by 156
Stereoselective Interactions of Peptide Inhibitors with the β-Amyloid Peptide
Chalifour, R. J., McLaughlin, R. W., Lavoie, L., Morissette, C., Tremblay, N., Boulé, M., Sarazin, P., Stéa, D., Lacombe, D., Tremblay, P., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212694200 · Cited by 156
Alzheimer’s disease, cerebrovascular disease, and the β-amyloid cascade
Honjo, K., Black, S. E., & Verhoeff, N. P. L. G. (2012) · Canadian Journal of Neurological Sciences / Journal Canadien des Sciences Neurologiques · doi:10.1017/s0317167100015547 · Cited by 152
Calcium channel blockers and dementia
Nimmrich, V., & Eckert, A. (2013) · British Journal of Pharmacology · doi:10.1111/bph.12240 · Cited by 156
Zou, K., Kim, D. S., Kakio, A., Byun, K., Gong, J., Kim, J. W., Kim, M. J., Sawamura, N., Nishimoto, S., Matsuzaki, K., et al. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.02018.x · Cited by 160
Wong, P. T., Schauerte, J. A., Wisser, K. C., Ding, H., Lee, E. L., Steel, D. G., & Gafni, A. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.11.060 · Cited by 158
Rad, S. K., Arya, A., Karimian, H., Madhavan, P., Rizwan, F., Koshy, S., & Prabhu, G. (2018) · Drug Design Development and Therapy · doi:10.2147/dddt.s173970 · Cited by 167
AMPA receptors as drug targets in neurological disease—advantages, caveats, and future outlook
Chang, P. K. ‐., Verbich, D., & McKinney, R. A. (2012) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2012.08165.x · Cited by 155
Altered aggregation properties of mutant γ‐crystallins cause inherited cataract
Sandilands, A., Hutcheson, A. M., Long, H. A., Prescott, A. R., Vrensen, G. F. J. M., Löster, J., Klopp, N., Lutz, R. B., Graw, J., Masaki, S., et al. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf609 · Cited by 155
Metadata
- Authors
- Walsh, D. M., Klyubin, I., Fadeeva, J. V., Cullen, W. K., Anwyl, R., Wolfe, M. S., Rowan, M. J., & Selkoe, D. J.
- Affiliations
- Brigham and Women's Hospital (US)
- Trinity College Dublin (IE)
- Corresponding author
- Selkoe, Dennis J.
- Venue
- Nature
- Published
- 2002-04
- Volume
- 416
- Issue
- 6880
- Pages
- 535-539
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2150999725
- Cited by
- 4,291
- References
- 31
- Citations by year
- 2026: 83 · 2025: 83 · 2024: 115 · 2023: 120 · 2022: 110 · 2021: 135 · 2020: 162 · 2019: 148 · 2018: 161 · 2017: 194 · 2016: 196 · 2015: 196 · 2014: 215 · 2013: 227 · 2012: 270
- FWCI
- 101.91
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- 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, amyloid-beta oligomers, Alzheimer's disease, amyloid hypothesis, hippocampal long-term potentiation, synaptic plasticity, synaptotoxicity, intracellular vesicles, gamma-secretase inhibitors, insulin-degrading enzyme, cerebrospinal fluid, neurotoxicity
- MeSH terms
- Alzheimer Disease, Animals, Cricetinae, Hippocampus, Humans, Insulysin, Microsomes, Endopeptidases, Protease Inhibitors, Recombinant Proteins, Amyloid beta-Peptides, Aspartic Acid Endopeptidases, CHO Cells, Culture Media, Conditioned, Long-Term Potentiation, Rats, Amyloid Precursor Protein Secretases, Plaque, Amyloid
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