The DOI matches its Crossref record; 52 of the 55 references it cites were found in a registry or an index.
Alzheimer's disease-affected brain: Presence of oligomeric Aβ ligands (ADDLs) suggests a molecular basis for reversible memory loss
Open accessAbstract
A molecular basis for memory failure in Alzheimer's disease (AD) has been recently hypothesized, in which a significant role is attributed to small, soluble oligomers of amyloid beta-peptide (A beta). A beta oligomeric ligands (also known as ADDLs) are known to be potent inhibitors of hippocampal long-term potentiation, which is a paradigm for synaptic plasticity, and have been linked to synapse loss and reversible memory failure in transgenic mouse AD models. If such oligomers were to build up in human brain, their neurological impact could provide the missing link that accounts for the poor correlation between AD dementia and amyloid plaques. This article, using antibodies raised against synthetic A beta oligomers, verifies the predicted accumulation of soluble oligomers in AD frontal cortex. Oligomers in AD reach levels up to 70-fold over control brains. Brain-derived and synthetic oligomers show structural equivalence with respect to mass, isoelectric point, and recognition by conformation-sensitive antibodies. Both oligomers, moreover, exhibit the same striking patterns of attachment to cultured hippocampal neurons, binding on dendrite surfaces in small clusters with ligand-like specificity. Binding assays using solubilized membranes show oligomers to be high-affinity ligands for a small number of nonabundant proteins. Current results confirm the prediction that soluble oligomeric A beta ligands are intrinsic to AD pathology, and validate their use in new approaches to therapeutic AD drugs and vaccines.
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“However, recent in vivo studies have shown that soluble Aβ oligomers are more neurotoxic than amyloid plaques and most likely responsible for synaptic dysfunction and memory loss in AD.7–11”
From The effect of Cu2+ and Zn2+ on the Aβ42 peptide aggregation and cellular toxicity (2013) · cites this paper as [11]
In the citing paper
“However, recent in vivo studies have shown that the soluble Aβ oligomers are possibly more neurotoxic than amyloid plaques,14–17 and are likely responsible for synaptic dysfunction and memory loss in AD patients and AD animal models.18–21”
From Bifunctional Compounds for Controlling Metal-Mediated Aggregation of the Aβ42Peptide (2012) · cites this paper as [18]
In the citing paper
“which was also shown to form neurotoxic soluble Aβ oligomers.18–20”
From Bifunctional Compounds for Controlling Metal-Mediated Aggregation of the Aβ42Peptide (2012) · cites this paper as [18]
In the citing paper
“recent studies have shown that the soluble Aβ oligomers are more neurotoxic both in vitro and in vivo.5−8”
From Small Bifunctional Chelators That Do Not Disaggregate Amyloid β Fibrils Exhibit Reduced Cellular Toxicity (2014) · cites this paper as [8]
In the citing paper
“the Aβ42 peptide was employed in these studies because it was shown to form neurotoxic soluble Aβ oligomers.5,8,48”
From Small Bifunctional Chelators That Do Not Disaggregate Amyloid β Fibrils Exhibit Reduced Cellular Toxicity (2014) · cites this paper as [8]
In the citing paper
“Dot immunoblots of soluble extracts from human brain show major increases in oligomers in AD-affected tissue (Gong et al., 2003; Kayed et al., 2003; Lambert et al., 2001).”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Gong et al., 2003
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 Gong et al., 2003
In the citing paper
“Cultured hippocampal neurons incubated with brain-derived oligomers show patterns that recapitulate the in situ distribution (Gong et al., 2003).”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Gong et al., 2003
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 Gong et al., 2003
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
Lipid rafts and signal transduction
Simons, K., & Toomre, D. (2000) · Nature Reviews Molecular Cell Biology · doi:10.1038/35036052 · Cited by 5,371
Goate, A., Chartier-Harlin, M.-C., Mullan, M., Brown, J., Crawford, F., Fidani, L., Giuffra, L., Haynes, A., Irving, N., James, L., et al. (1991) · Nature · doi:10.1038/349704a0 · Cited by 4,659
The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor
Kang, J., Lemaire, H.-G., Unterbeck, A., Salbaum, J. M., Masters, C. L., Grzeschik, K.-H., Multhaup, G., Beyreuther, K., & Müller-Hill, B. (1987) · Nature · doi:10.1038/325733a0 · Cited by 4,619
Amyloid plaque core protein in Alzheimer disease and Down syndrome.
Masters, C. L., Simms, G., Weinman, N. A., Multhaup, G., McDonald, B. L., & Beyreuther, K. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.12.4245 · Cited by 4,431
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
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-citation
Research works printed but not linked: 2
- Terry R. D. (1999) in Alzheimer Disease eds. Terry R. D. Katzman R. Bick K. L. & Sisodia S. S. (Lippincott Williams & Wilkins Philadelphia) pp. 187-206.
- Chang L. Gong Y. Bakhos L. Yu J. Venton D. L. & Klein W. L. (2003) J. Mol. Neurosci. in press.
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Picone, P., Carrotta, R., Montana, G., Nobile, M. R., Biagio, P. L. S., & Carlo, M. D. (2009) · Biophysical Journal · doi:10.1016/j.bpj.2008.11.056 · Cited by 97
Disruption of glutamate receptors at Shank-postsynaptic platform in Alzheimer's disease
Gong, Y., Lippa, C. F., Zhu, J., Lin, Q., & Rosso, A. L. (2009) · Brain Research · doi:10.1016/j.brainres.2009.07.056 · Cited by 102
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Li, Y.-Y., Fang, J. Y., & Ao, G. (2016) · Expert Opinion on Therapeutic Patents · doi:10.1080/13543776.2017.1272572 · Cited by 97
BACE1 Structure and Function in Health and Alzheimers Disease
Cole, S., & Vassar, R. (2008) · Current Alzheimer Research · doi:10.2174/156720508783954758 · Cited by 98
Why Alzheimer's is a disease of memory: The attack on synapses by Aß oligomers (ADDLs)
Viola, K. L., Velasco, P. T., & Klein, W. L. (2008) · The journal of nutrition health & aging · doi:10.1007/bf02982587 · Cited by 97
Self-citationBhattarai, K., Ku, Z., Silva, S., Jeon, J., Kim, J. O., Lee, S. J., Urbas, A. M., & Zhou, J. (2015) · Advanced Optical Materials · doi:10.1002/adom.201500231 · Cited by 96
Kaczorowski, C. C., Sametsky, E. A., Shah, S., Vassar, R. J., & Disterhoft, J. F. (2009) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2009.09.003 · Cited by 96
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Brito‐Moreira, J., Paula-Lima, A. C., Bomfim, T. R., de Oliveira, F. F., Sepúlveda, F. J., Mello, F. G. D., Aguayo, L. G., Panizzutti, R., & Ferreira, S. T. (2011) · Current Alzheimer Research · doi:10.2174/156720511796391917 · Cited by 111
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Bishop, G. M., & Robinson, S. R. (2004) · Drugs & Aging · doi:10.2165/00002512-200421100-00001 · Cited by 94
Role of Amyloid- Glycine 33 in Oligomerization, Toxicity, and Neuronal Plasticity
Harmeier, A., Wozny, C., Rost, B. R., Munter, L. M., Hua, H., Georgiev, O., Beyermann, M., Hildebrand, P. W., Weise, C., Schaffner, W., et al. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.1336-09.2009 · Cited by 97
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Zameer, A., Kasturirangan, S., Emadi, S., Nimmagadda, S. V., & Sierks, M. R. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.09.068 · Cited by 96
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Ugalde, C. L., Finkelstein, D. I., Lawson, V. A., & Hill, A. F. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13772 · Cited by 92
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Giuffrida, M. L., Caraci, F., Bona, P. D., Pappalardo, G., Nicoletti, F., Rizzarelli, E., & Copani, A. (2010) · Reviews in the Neurosciences · doi:10.1515/revneuro.2010.21.2.83 · Cited by 94
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Wu, C.-C., Chawla, F., Games, D., Rydel, R. E., Freedman, S. B., Schenk, D., Young, W. G., Morrison, J. H., & Bloom, F. E. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0402147101 · Cited by 91
Rahimi, F., Shanmugam, A., & Bitan, G. (2008) · Current Alzheimer Research · doi:10.2174/156720508784533358 · Cited by 88
Moir, R. D., Tseitlin, K. A., Soscia, S. J., Hyman, B. T., Irizarry, M. C., & Tanzi, R. E. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414176200 · Cited by 88
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Self-citationWalker, D. G., & Lue, L.-F. (2005) · Journal of Neuroscience Research · doi:10.1002/jnr.20484 · Cited by 89
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Prangkio, P., Yusko, E. C., Sept, D., Yang, J., & Mayer, M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0047261 · Cited by 88
Torrisi, S. A., Geraci, F., Tropea, M. R., Grasso, M., Caruso, G., Fidilio, A., Musso, N., Sanfilippo, G., Tascedda, F., Palmeri, A., et al. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.00693 · Cited by 90
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Yanagisawa, D., Taguchi, H., Yamamoto, A., Shirai, N., Hirao, K., & Tooyama, I. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-102100 · Cited by 85
Evangelisti, E., Cecchi, C., Cascella, R., Sgromo, C., Becatti, M., Dobson, C. M., Chiti, F., & Stefani, M. (2012) · Journal of Cell Science · doi:10.1242/jcs.098434 · Cited by 84
Brody, D. L., Jiang, H., Wildburger, N. C., & Esparza, T. J. (2017) · Alzheimer s Research & Therapy · doi:10.1186/s13195-017-0293-3 · Cited by 86
Imbimbo, B. P., Giudice, E. D., Colavito, D., D’Arrigo, A., Carbonare, M. D., Villetti, G., Facchinetti, F., Volta, R., Pietrini, V., Baroc, M. F., et al. (2007) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.107.129007 · Cited by 84
Cai, W., Li, L., Sang, S., Pan, X., & Zhong, C. (2023) · Neuroscience Bulletin · doi:10.1007/s12264-022-00985-9 · Cited by 83
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Brody, A. H., & Strittmatter, S. M. (2017) · Advances in pharmacology · doi:10.1016/bs.apha.2017.09.007 · Cited by 89
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Hölscher, C. (2005) · Reviews in the Neurosciences · doi:10.1515/revneuro.2005.16.3.181 · Cited by 83
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Leary, S. P., Liu, C. Y., & Apuzzo, M. L. J. (2006) · Neurosurgery · doi:10.1227/01.neu.0000216793.45952.ed · Cited by 81
Smith, L. M., Kostylev, M. A., Lee, S., & Strittmatter, S. M. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.006252 · Cited by 73
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Truong, L. T. N., Takamura, Y., Tamiya, E., & Vestergaard, M. C. M. (2015) · Analytica Chimica Acta · doi:10.1016/j.aca.2015.08.036 · Cited by 79
Veloso, A. J., Chow, A. M., Ganesh, H. V. S., Li, N., Dhar, D., Wu, D. C. H., Mikhaylichenko, S. N., Brown, I. R., & Kerman, K. (2014) · Analytical Chemistry · doi:10.1021/ac500424t · Cited by 79
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Bitel, C. L., Kasinathan, C., Kaswala, R. H., Klein, W. L., & Frederikse, P. H. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-120571 · Cited by 78
Self-citationStefani, M. (2007) · The Neuroscientist · doi:10.1177/1073858407303428 · Cited by 77
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Zheng, X., Liu, D., Klärner, F., Schrader, T. H., Bitan, G., & Bowers, M. T. (2015) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.5b00692 · Cited by 79
Foss, T. R., Kelker, M. S., Wiseman, R. L., Wilson, I. A., & Kelly, J. W. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.01.050 · Cited by 79
Batista, A. F., Bodart‐Santos, V., Felice, F. G. D., & Ferreira, S. T. (2018) · CNS Drugs · doi:10.1007/s40263-018-0593-6 · Cited by 78
Gong, Y., & Lippa, C. F. (2010) · American Journal of Alzheimer's Disease & Other Dementias® · doi:10.1177/1533317510382893 · Cited by 76
Self-citationSmall-molecule BACE1 inhibitors: a patent literature review (2006 – 2011)
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Päiviö, A., Jarvet, J., Gräslund, A., Lannfelt, L., & Westlind‐Danielsson, A. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.03.028 · Cited by 77
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Bandara, N., Sharma, A. K., Krieger, S., Schultz, J. W., Han, B. H., Rogers, B. E., & Mirica, L. M. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.7b05937 · Cited by 82
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Caetano, F. A., Beraldo, F. H., Hajj, G. N. M., Guimaraes, A. L., Jürgensen, S., Wasilewska-Sampaio, A. P., Hirata, P. H. F., Souza, I., Machado, C. F., Wong, D. Y.-L., et al. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07225.x · Cited by 74
Mališauskas, M., Östman, J., Darinskas, A., Zamotin, V., Liutkevičius, E., Lundgren, E., & Morozova‐Roche, L. A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407273200 · Cited by 75
Johnson, E. C. B., Ho, K., Yu, G.-Q., Das, M., Sanchez, P. E., Djukic, B., Lopez, I., Yu, X., Gill, M., Zhang, W., et al. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-00393-5 · Cited by 73
Reddy, P. H., & McWeeney, S. K. (2005) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.04.014 · Cited by 73
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Lourenco, M. V., Ferreira, S. T., & Felice, F. G. D. (2015) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2015.03.003 · Cited by 74
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Hamilton, A., Zamponi, G. W., & Ferguson, S. S. G. (2015) · Molecular Brain · doi:10.1186/s13041-015-0107-0 · Cited by 72
Kitazawa, M., Green, K. N., Caccamo, A., & LaFerla, F. M. (2006) · American Journal Of Pathology · doi:10.2353/ajpath.2006.051232 · Cited by 73
Moretto, N., Bolchi, A., Rivetti, C., Imbimbo, B. P., Villetti, G., Pietrini, V., Polonelli, L., Signore, S. J. D., Smith, K. M., Ferrante, R. J., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m609690200 · Cited by 69
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Metadata
- Authors
- Gong, Y., Chang, L., Viola, K. L., Lacor, P. N., Lambert, M. P., Finch, C. E., Krafft, G. A., & Klein, W. L.
- Affiliations
- Northwestern University (US)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2003-08-18
- Volume
- 100
- Issue
- 18
- Pages
- 10417-10422
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC193576
- OpenAlex
- W2040721710
- Cited by
- 1,061
- References
- 55
- Citations by year
- 2026: 21 · 2025: 15 · 2024: 19 · 2023: 32 · 2022: 24 · 2021: 33 · 2020: 35 · 2019: 38 · 2018: 44 · 2017: 45 · 2016: 32 · 2015: 42 · 2014: 52 · 2013: 49 · 2012: 53
- FWCI
- 35.26
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Northwestern University
- National Institutes of Health (1p01ag015501-01)
- National Institute on Aging (P01-AG15501, R01-AG18877, R01AG018877)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- Alzheimer's disease, amyloid-beta oligomers, memory loss, hippocampal long-term potentiation, synaptic plasticity, synaptic loss, frontal cortex, dendrites, protein-ligand binding, amyloid plaques, therapeutic vaccines
- MeSH terms
- Alzheimer Disease, Animals, Binding Sites, Brain Chemistry, Cells, Cultured, Cerebral Cortex, Ligands, Neurons, Oligopeptides, Peptide Fragments, Tissue Extracts, Immunoblotting, Amyloid beta-Peptides, Rats, Sprague-Dawley, Long-Term Potentiation, Rats
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