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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Ye, H., Jalini, S., Mylvaganam, S., & Carlen, P. L. (2008) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2008.05.012 · Cited by 63
Aggregation Prone Regions and Gatekeeping Residues in Protein Sequences
Beerten, J., Schymkowitz, J. W. H., & Rousseau, F. (2013) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026611212220003 · Cited by 63
Parthasarathy, S., Inoue, M., Xiao, Y., Matsumura, Y., Nabeshima, Y.-I., Hoshi, M. M., & Ishii, Y. (2015) · Journal of the American Chemical Society · doi:10.1021/jacs.5b03373 · Cited by 62
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Ahmed, S. A. A., Mahmood, Z., & Zahid, S. (2015) · Neurological Sciences · doi:10.1007/s10072-015-2352-5 · Cited by 65
Kaminari, A., Giannakas, N., Tzinia, A. K., & Tsilibary, E. C. (2017) · Scientific Reports · doi:10.1038/s41598-017-00794-5 · Cited by 62
Palavicini, J. P., Wang, C., Chen, L., HoSang, K. M., Wang, J., Tomiyama, T., Mori, H., & Han, X. (2017) · Acta Neuropathologica Communications · doi:10.1186/s40478-017-0460-6 · Cited by 62
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Jia, K., & Du, H. (2021) · Cells · doi:10.3390/cells10030649 · Cited by 63
Meli, G., Visintin, M., Cannistraci, I., & Cattaneo, A. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.01.061 · Cited by 64
Marcello, E. E., Epis, R., & Luca, M. D. (2008) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2007.11.083 · Cited by 63
Wang, X.-P., Zhang, J.-H., Wang, Y.-J., Feng, Y. N., Zhang, X., Sun, X.-X., Li, J.-L., Du, X.-T., Lambert, M. P., Yang, S.-G., et al. (2009) · FEBS Letters · doi:10.1016/j.febslet.2008.12.064 · Cited by 62
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Keating, C. D. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0500024102 · Cited by 61
Protease inhibitors as potential disease-modifying therapeutics for Alzheimer’s disease
Beher, D., & Graham, S. L. (2005) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.14.11.1385 · Cited by 61
Wang, H., Megill, A., He, K., Kirkwood, A., & Lee, H. (2012) · Neural Plasticity · doi:10.1155/2012/272374 · Cited by 66
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Messa, M., Colombo, L., Favero, E. D., Cantú, L., Stoilova, T., Cagnotto, A., Rossi, A., Morbin, M., Fede, G. D., Tagliavini, F., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.576256 · Cited by 59
Thomas, M. H., Pelleïeux, S., Vitale, N., & Olivier, J. L. (2016) · Biochimie · doi:10.1016/j.biochi.2016.07.013 · Cited by 60
Sharma, A. K., Schultz, J. W., Prior, J. T., Rath, N. P., & Mirica, L. M. (2017) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.7b01883 · Cited by 64
Zheng, X., Liu, D., Roychaudhuri, R., Teplow, D. B., & Bowers, M. T. (2015) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.5b00171 · Cited by 61
Hua, H., Munter, L. M., Harmeier, A., Georgiev, O., Multhaup, G., & Schaffner, W. (2011) · Biological Chemistry · doi:10.1515/bc.2011.084 · Cited by 58
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Huang, Y., Cho, H.-J., Bandara, N., Sun, L., Tran, D., Rogers, B. E., & Mirica, L. M. (2020) · Chemical Science · doi:10.1039/d0sc02641g · Cited by 62
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Stéphan, A., & Phillips, A. G. (2005) · Genes Brain & Behavior · doi:10.1111/j.1601-183x.2004.00113.x · Cited by 63
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Loureiro, J. A., Crespo, R., Börner, H. G., Martins, P. M., Rocha, F. A., Coelho, M. A. N., Pereira, M. D. C., & Rocha, S. (2014) · Journal of Materials Chemistry B · doi:10.1039/c3tb21483d · Cited by 57
Plasma amyloid-β oligomers level is a biomarker for Alzheimer’s disease diagnosis
Zhou, L., Chan, K. H., Chu, L., Kwan, J., Song, Y., Chen, L. H., Ho, P. W., Cheng, O., Ho, J. W.-M., & Lam, K. S. L. (2012) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2012.06.017 · Cited by 59
Sinnen, B. L., Bowen, A. B., Gibson, E. S., & Kennedy, M. J. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.1603-16.2016 · Cited by 59
Green, D. E., Bowen, M. L., Scott, L. E., Storr, T., Merkel, M., Böhmerle, K., Thompson, K. H., Patrick, B. O., Schugar, H. J., & Orvig, C. (2009) · Dalton Transactions · doi:10.1039/b918439b · Cited by 56
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Sorrentino, G., & Bonavita, V. (2007) · Neurological Sciences · doi:10.1007/s10072-007-0789-x · Cited by 56
Zheng, X., Wu, C. F., Liu, D., Li, H., Bitan, G., Shea, J., & Bowers, M. T. (2015) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.5b08177 · Cited by 57
Caraci, F., Tascedda, F., Merlo, S., Benatti, C., Spampinato, S. F., Munafò, A., Leggio, G. M., Nicoletti, F., Brunello, N., Drago, F., et al. (2016) · Frontiers in Pharmacology · doi:10.3389/fphar.2016.00389 · Cited by 58
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Thatcher, G. R. J., Bennett, B. M., & Reynolds, J. N. (2005) · Current Alzheimer Research · doi:10.2174/1567205053585945 · Cited by 56
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Michalski, B., Corrada, M. M., Kawas, C. H., & Fahnestock, M. L. (2015) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2015.08.022 · Cited by 57
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Self-citationAlzheimer Disease and Its Management
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Ariga, T., Wakade, C. G., & Yu, R. K. (2011) · International Journal of Alzheimer s Disease · doi:10.4061/2011/193618 · Cited by 53
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Wang, P., Su, C., Feng, H., Chen, X., Dong, Y., Rao, Y., Ren, Y., Yang, J.-D., Shi, J., Tian, J., et al. (2017) · International Journal of Immunopathology and Pharmacology · doi:10.1177/0394632016688025 · Cited by 54
Choi, J., Choi, H. J., Jung, D. C., Lee, J.-H., & Cheon, J. (2008) · Chemical Communications · doi:10.1039/b803294g · Cited by 53
Murakami, K. (2014) · Bioscience Biotechnology and Biochemistry · doi:10.1080/09168451.2014.940275 · Cited by 53
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Carlo, M. D. (2009) · European Biophysics Journal · doi:10.1007/s00249-009-0439-8 · Cited by 56
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LoPachin, R. M., Gavin, T., & Barber, D. S. (2008) · NeuroToxicology · doi:10.1016/j.neuro.2008.04.016 · Cited by 53
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Self-citationStereospecific interactions are necessary for Alzheimer disease amyloid-β toxicity.
Ciccotosto, G., Tew, D., Drew, S., Smith, D. G., Johanssen, T., Lal, V., Lau, T., Perez, K., Curtain, C., Wade, J., et al. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2009.02.018 · Cited by 48
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Wang, L., Yang, H., Zhao, S., Sato, H., Konishi, Y., Beach, T. G., Abdelalim, E. M., Bisem, N. J., & Tooyama, I. (2011) · PLoS ONE · doi:10.1371/journal.pone.0022325 · Cited by 51
Rózga, M., & Bal, W. (2009) · Chemical Research in Toxicology · doi:10.1021/tx900358j · Cited by 54
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Patel, A. N., & Jhamandas, J. H. (2012) · Expert Reviews in Molecular Medicine · doi:10.1017/s1462399411002134 · Cited by 51
Urbanc, B., Betnel, M., Cruz, L., Li, H., Fradinger, E. A., Monien, B. H., & Bitan, G. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.05.021 · Cited by 51
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Sensi, S. L., Rapposelli, I. G., Frazzini, V., & Mascetra, N. (2007) · Experimental Gerontology · doi:10.1016/j.exger.2007.10.018 · Cited by 49
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Caruso, G., Grasso, M., Fidilio, A., Torrisi, S. A., Musso, N., Geraci, F., Tropea, M. R., Privitera, A., Tascedda, F., Puzzo, D., et al. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.809541 · Cited by 53
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Truong, A. P., Tóth, G., Probst, G., Sealy, J., Bowers, S., Wone, D. W. G., Dressen, D., Hom, R. K., Konradi, A., Sham, H., et al. (2010) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2010.08.102 · Cited by 49
Anker, J. N., Hall, W. P., Lambert, M. P., Velasco, P. T., Mrksich, M., Klein, W. L., & Duyne, R. P. V. (2009) · The Journal of Physical Chemistry C · doi:10.1021/jp900266k · Cited by 48
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Yi, X., Feng, C., Hu, S., Li, H., & Wang, J. (2015) · The Analyst · doi:10.1039/c5an01864a · Cited by 52
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Rush, T., & Buisson, A. (2014) · Cell and Tissue Research · doi:10.1007/s00441-013-1789-1 · Cited by 48
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Kreiser, R. P., Wright, A. K., Block, N. R., Hollows, J. E., Nguyen, L. T., LeForte, K., Mannini, B., Vendruscolo, M., & Limbocker, R. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21228651 · Cited by 48
Sehlin, D., Hedlund, M., Lord, A., Englund, H., Gellerfors, P., Paulie, S., Lannfelt, L., & Pettersson, F. E. (2010) · Neurodegenerative Diseases · doi:10.1159/000316530 · Cited by 47
Synthetic dityrosine-linked β-amyloid dimers form stable, soluble, neurotoxic oligomers
Kok, W. M., Cottam, J. M., Ciccotosto, G. D., Miles, L. A., Karas, J. A., Scanlon, D. B., Roberts, B. R., Parker, M. W., Cappai, R., Barnham, K. J., et al. (2013) · Chemical Science · doi:10.1039/c3sc22295k · Cited by 46
Metabolic Abnormalities of Erythrocytes as a Risk Factor for Alzheimer's Disease
Kosenko, E. A., Tikhonova, L. A., Montoliu, C., Barreto, G. E., Aliev, G., & Kaminsky, Y. G. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2017.00728 · Cited by 47
Systematic Review on the Efficacy and Safety of Herbal Medicines for Alzheimer's Disease
Man, S. C., Durairajan, S. S. K., Kum, W. F., Lu, J., Huang, J. D., Cheng, C. F., Chung, V. C., Xu, M., & Li, M. (2008) · Journal of Alzheimer s Disease · doi:10.3233/jad-2008-14209 · Cited by 46
Design and biological activity of β-sheet breaker peptide conjugates
Rocha, S., Cardoso, I., Börner, H. G., Pereira, M. D. C., Saraiva, M. J., & Coelho, M. A. N. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.01.090 · Cited by 46
Surfactant-induced conformational transition of amyloid β-peptide
Sureshbabu, N., Kirubagaran, R., & Rajadas, J. (2008) · European Biophysics Journal · doi:10.1007/s00249-008-0379-8 · Cited by 49
Amyloid-Mediated Mechanisms of Membrane Disruption
Sciacca, M. F. M., Rosa, C. L., & Milardi, D. (2021) · Biophysica · doi:10.3390/biophysica1020011 · Cited by 45
Morphological and Molecular Profiling of Amyloid-β Species in Alzheimer’s Pathogenesis
Almeida, Z. L., Vaz, D. C., & Brito, R. M. M. (2024) · Molecular Neurobiology · doi:10.1007/s12035-024-04543-4 · Cited by 49
Basi, G. S., Feinberg, H., Oshidari, F., Anderson, J., Barbour, R., Baker, J., Comery, T. A., Diep, L., Gill, D. S., Johnson‐Wood, K., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.045187 · Cited by 45
TGF-β1 prevents rat retinal insult induced by amyloid-β (1–42) oligomers
Fisichella, V., Giurdanella, G., Platania, C. B. M., Romano, G. L., Leggio, G. M., Salomone, S., Drago, F., Caraci, F., & Bucolo, C. (2016) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2016.02.002 · Cited by 45
Down syndrome, beta-amyloid and neuroimaging
Head, E., Helman, A. M., Powell, D. K., & Schmitt, F. A. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.09.013 · Cited by 49
Sun, L., Sharma, A. K., Han, B.-H., & Mirica, L. M. (2020) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.0c00376 · Cited by 46
Rishton, G. M., Look, G. C., Ni, Z., Zhang, J. Y., Wang, Y., Huang, Y., Wu, X., Izzo, N. J., Mozzoni, K., Limegrover, C. S., et al. (2021) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.1c00048 · Cited by 45
Probing the origins, diagnosis and treatment of amyloid diseases using antibodies
Dumoulin, M., & Dobson, C. M. (2004) · Biochimie · doi:10.1016/j.biochi.2004.09.012 · Cited by 45
Wasilewska‐Sampaio, A. P., Silveira, M. S., Holub, O., Goecking, R., Gomes, F. C. A., Moura‐Neto, V., Linden, R., Ferreira, S. T., & Felice, F. G. D. (2005) · The FASEB Journal · doi:10.1096/fj.05-3812com · Cited by 45
Jensen, L. E., Bultynck, G., Luyten, T., Amijee, H., Bootman, M. D., & Roderick, H. L. (2013) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2013.00036 · Cited by 46
Helmond, Z. V., Heesom, K. J., & Love, S. (2008) · Journal of Neuroscience Methods · doi:10.1016/j.jneumeth.2008.09.002 · Cited by 44
The Role of β-Amyloid Protein in Synaptic Function: Implications for Alzheimers Disease Therapy
Peña‐Ortega, F., Gutiérrez-Lerma, A. I., Quiroz‐Baez, R., & Arias, C. (2006) · Current Neuropharmacology · doi:10.2174/157015906776359531 · Cited by 45
Wang, X., Li, J., Ma, C., Huang, C., & Li, Z. (2019) · Biochemical Pharmacology · doi:10.1016/j.bcp.2019.113674 · Cited by 45
Vosough, F., & Barth, A. (2021) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.0c00642 · Cited by 44
Apoptosis is secondary to non-apoptotic axonal degeneration in neurons exposed to Aβ in distal axons
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PGH2‐derived levuglandin adducts increase the neurotoxicity of amyloid β1–42
Boutaud, O. G., Montine, T. J., Chang, L., Klein, W. L., & Oates, J. A. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03586.x · Cited by 44
Self-citation
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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