The DOI matches its Crossref record; 68 of the 68 references it cites were found in a registry or an index.
Diffusible, nonfibrillar ligands derived from Aβ 1–42 are potent central nervous system neurotoxins
Open accessAbstract
Abeta1-42 is a self-associating peptide whose neurotoxic derivatives are thought to play a role in Alzheimer's pathogenesis. Neurotoxicity of amyloid beta protein (Abeta) has been attributed to its fibrillar forms, but experiments presented here characterize neurotoxins that assemble when fibril formation is inhibited. These neurotoxins comprise small diffusible Abeta oligomers (referred to as ADDLs, for Abeta-derived diffusible ligands), which were found to kill mature neurons in organotypic central nervous system cultures at nanomolar concentrations. At cell surfaces, ADDLs bound to trypsin-sensitive sites and surface-derived tryptic peptides blocked binding and afforded neuroprotection. Germ-line knockout of Fyn, a protein tyrosine kinase linked to apoptosis and elevated in Alzheimer's disease, also was neuroprotective. Remarkably, neurological dysfunction evoked by ADDLs occurred well in advance of cellular degeneration. Without lag, and despite retention of evoked action potentials, ADDLs inhibited hippocampal long-term potentiation, indicating an immediate impact on signal transduction. We hypothesize that impaired synaptic plasticity and associated memory dysfunction during early stage Alzheimer's disease and severe cellular degeneration and dementia during end stage could be caused by the biphasic impact of Abeta-derived diffusible ligands acting upon particular neural signal transduction pathways.
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
“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 [10]
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 [14]
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 [7]
In the citing paper
“For the preformed Aβ42 fibrils, no significant cell toxicity was observed in either the absence or presence of Cu2+ (Figure 9, lanes 1 and 2), supporting the previously reported diminished toxicity of Aβ42 fibrils.5,7,54−56”
From Small Bifunctional Chelators That Do Not Disaggregate Amyloid β Fibrils Exhibit Reduced Cellular Toxicity (2014) · cites this paper as [7]
In the citing paper
“This function may be critical in controlling Aβ deposition as well as levels of potentially neurotoxic Aβ oligomers (Lambert et al., 1998).”
From CX3CR1 in Microglia Regulates Brain Amyloid Deposition through Selective Protofibrillar Amyloid-β Phagocytosis (2010) · cites this paper as Lambert et al., 1998
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 [34]
In the citing paper
“In vitro, apoE and apoJ form stable complexes with A (11, 16 -20), alter the aggregation of various A peptides (21)(22)(23), and affect A neurotoxicity (24 -27).”
From Apolipoprotein E Receptors Mediate the Effects of β-Amyloid on Astrocyte Cultures (2000) · cites this paper as [27]
In the citing paper
“A 1-42 aged according to this protocol is a mixture of fibrils and soluble globular aggregates, and is active to astrocytes (37,38) and toxic to neurons (26,27).”
From Apolipoprotein E Receptors Mediate the Effects of β-Amyloid on Astrocyte Cultures (2000) · cites this paper as [27]
In the citing paper
“ApoJ has been shown to potentiate the formation of a neurotoxic species of A (26,27).”
From Apolipoprotein E Receptors Mediate the Effects of β-Amyloid on Astrocyte Cultures (2000) · cites this paper as [27]
In the citing paper
“ApoE, apoJ, and most recently ␣ 2 -macroglobulin have been shown to form a complex with A that may facilitate clearance of the peptide (25-27, 50, 51).”
From Apolipoprotein E Receptors Mediate the Effects of β-Amyloid on Astrocyte Cultures (2000) · cites this paper as [27]
In the citing paper
“Evidence suggests that increased uptake of these neurotoxic Aβ42 peptides results in accumulation and aggregation within neurons eventually leading the formation of plaques and neuronal death [40, 41].”
From The Sigma-2 Receptor/TMEM97, PGRMC1, and LDL Receptor Complex Are Responsible for the Cellular Uptake of Aβ42 and Its Protein Aggregates (2020) · cites this paper as [41]
In the citing paper
“Most importantly, these amyloid-free Aβ oligomers were potent CNS neurotoxins.”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Lambert et al., 1998
In the citing paper
“With chronic exposure, neurons ultimately were killed. Death was selective for subpopulations of vulnerable neurons and was prevented by knockout of Fyn, a protein tyrosine kinase linked to NMDA receptor signaling.”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Lambert et al., 1998
In the citing paper
“Investigation into the action of clusterin by Lambert, Klein and colleagues established that, concomitant with inhibition of amyloid formation, clusterin promotes accumulation of soluble Aβ oligomers (Lambert et al., 1998).”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Lambert et al., 1998
In the citing paper
“oligomers were found to inhibit functional synaptic plasticity (Lambert et al., 1998). Long-term potentiation (LTP) was inhibited within minutes. This rapid loss of LTP, measured in rat brain slices and in situ in mice, occurred without impact on baseline excitability, indicating impairment of signaling rather than degeneration.”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Lambert et al., 1998
In the citing paper
“In hippocampal slices, synthetic oligomers cause rapid LTP inhibition (Barghorn et al., 2005; Fa et al., 2010; Jurgensen et al., 2011; Lambert et al., 1998; Nimmrich et al., 2008; Rammes et al., 2011; Wang et al., 2002).”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Lambert et al., 1998
In the citing paper
“early studies showed that binding is lost upon controlled trypsin treatment of neurons (Lambert et al., 1998).”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Lambert et al., 1998
In the citing paper
“In vitro and in vivo studies have now indicated that soluble Aβ oligomers impair synaptic plasticity, inhibiting hippocampal long-term potentiation (LTP), the electrophysiological correlate of learning and memory (3 –6).”
From Synthetic amyloid-β oligomers impair long-term memory independently of cellular prion protein (2010) · cites this paper as [3]
Citations
Cites
Mass Spectrometric Sequencing of Proteins from Silver-Stained Polyacrylamide Gels
Shevchenko, A., Wilm, M. S., Vorm, O., & Mann, M. (1996) · Analytical Chemistry · doi:10.1021/ac950914h · Cited by 8,996
Terry, 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
Strittmatter, W. J., Saunders, A. M., Schmechel, D., Pericak-Vance, M., Enghild, J., Salvesen, G. S., & Roses, A. D. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.5.1977 · Cited by 4,268
Correlative Memory Deficits, Aβ Elevation, and Amyloid Plaques in Transgenic Mice
Hsiao, K., Chapman, P., Nilsen, S., Eckman, C., Harigaya, Y., Younkin, S., Yang, F., & Cole, G. (1996) · Science · doi:10.1126/science.274.5284.99 · Cited by 4,210
A simple method for organotypic cultures of nervous tissue
Stoppini, L., Buchs, P., & Muller, D. (1991) · Journal of Neuroscience Methods · doi:10.1016/0165-0270(91)90128-m · Cited by 3,096
Integrins and Signal Transduction Pathways: the Road Taken
Clark, E. A., & Brugge, J. S. (1995) · Science · doi:10.1126/science.7716514 · Cited by 2,911
Scheuner, D., Eckman, C., Jensen, M., Song, X., Citron, M., Suzuki, N., Bird, T. D., Hardy, J., Hutton, M., Kukull, W., et al. (1996) · Nature Medicine · doi:10.1038/nm0896-864 · Cited by 2,599
Jarrett, J. T., Berger, E. P., & Lansbury, P. T. (1993) · Biochemistry · doi:10.1021/bi00069a001 · Cited by 2,022
RAGE and amyloid-β peptide neurotoxicity in Alzheimer's disease
Yan, S. D., Chen, X., Fu, J., Chen, M., Zhu, H., Roher, A., Slattery, T., Zhao, L., Nagashima, M., Morser, J., et al. (1996) · Nature · doi:10.1038/382685a0 · Cited by 2,012
Neurotrophic and Neurotoxic Effects of Amyloid β Protein: Reversal by Tachykinin Neuropeptides
Yankner, B. A., Duffy, L. K., & Kirschner, D. A. (1990) · Science · doi:10.1126/science.2218531 · Cited by 1,975
Research works printed but not linked: 2
- B Leveugle, A Scanameo, W Ding, H Fillit NeuroReport 5, 1389–1392 (1994).
- 10.1146/annurev.bi.63.070194.003125 · DOI
Cited by
Sorted by citations
Items 601–700 of 1,060
Anti-Amyloid Immunotherapies for Alzheimer's Disease: A 2023 Clinical Update
Yadollahikhales, G., & Rojas, J. C. (2023) · Neurotherapeutics · doi:10.1007/s13311-023-01405-0 · Cited by 165
Modarresi, F., Faghihi, M. A., Patel, N. S., Sahagan, B. G., Wahlestedt, C., & López-Toledano, M. A. (2011) · International Journal of Alzheimer s Disease · doi:10.4061/2011/929042 · Cited by 154
Conformation-dependent antibodies target diseases of protein misfolding
Glabe, C. C. (2004) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2004.08.009 · Cited by 154
Kinetics of amyloid formation and membrane interaction with amyloidogenic proteins
Murphy, R. M. (2007) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2006.12.014 · Cited by 157
Soong, R., Brender, J., Macdonald, P. M., & Ramamoorthy, A. (2009) · Journal of the American Chemical Society · doi:10.1021/ja900285z · Cited by 157
Reelin signaling antagonizes β-amyloid at the synapse
Durakoglugil, M. S., Chen, Y., White, C. L., Kavalali, E. T., & Herz, J. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0908176106 · Cited by 153
Dementia of the eye: the role of amyloid beta in retinal degeneration
Ratnayaka, J. A., Serpell, L. C., & Lotery, A. J. (2015) · Eye · doi:10.1038/eye.2015.100 · Cited by 160
Transmembrane Structures for Alzheimer’s Aβ 1−42 Oligomers
Strodel, B., Lee, J. W. L., Whittleston, C. S., & Wales, D. J. (2010) · Journal of the American Chemical Society · doi:10.1021/ja103725c · Cited by 155
Synaptic memory mechanisms: Alzheimer's disease amyloid β-peptide-induced dysfunction
Rowan, M. J., Klyubin, I. V., Wang, Q., Hu, N., & Anwyl, R. (2007) · Biochemical Society Transactions · doi:10.1042/bst0351219 · Cited by 154
Nanodiscs as a New Tool to Examine Lipid–Protein Interactions
Schuler, M. A., Denisov, I. G., & Sligar, S. G. (2012) · Methods in molecular biology · doi:10.1007/978-1-62703-275-9_18 · Cited by 153
Rushworth, J. V., Jarosz-Griffiths, H., Watt, N. T., & Hooper, N. M. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.400358 · Cited by 157
Alifragis, P., & Marsh, J. (2018) · Neural Regeneration Research · doi:10.4103/1673-5374.230276 · Cited by 156
GluT4: A central player in hippocampal memory and brain insulin resistance
McNay, E. C., & Pearson-Leary, J. (2019) · Experimental Neurology · doi:10.1016/j.expneurol.2019.113076 · Cited by 159
Ward, R. V., JENNINGS, K. H., Jepras, R., Neville, W. A., OWEN, D. E., HAWKINS, J., Christie, G., Davis, J. B., George, A. R., Karran, E. H., et al. (2000) · Biochemical Journal · doi:10.1042/bj3480137 · Cited by 153
Fawzi, N. L., Phillips, A. H., Ruscio, J. Z., Doucleff, M., Wemmer, D. E., & Head-Gordon, T. L. (2008) · Journal of the American Chemical Society · doi:10.1021/ja710366c · Cited by 154
Kriem, B., Sponne, I., Fifre, A., Malaplate, C., Lozac'h‐Pillot, K., Koziel, V., Yen, F. T., Bihain, B. E., Oster, T., Olivier, J. L., et al. (2004) · The FASEB Journal · doi:10.1096/fj.04-1807fje · Cited by 157
Sarroukh, R., Cerf, E., Derclaye, S., Dufrêne, Y. F., Goormaghtigh, E., Ruysschaert, J., & Raussens, V. (2010) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-010-0529-x · Cited by 160
Alzheimer’s disease: How metal ions define β-amyloid function
Kepp, K. P. (2017) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2017.05.007 · Cited by 154
Human Amylin Oligomer Growth and Fibril Elongation Define Two Distinct Phases in Amyloid Formation
Green, J. D., Goldsbury, C. S., Kistler, J., Cooper, G. J. S., & Aebi, U. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312452200 · Cited by 151
Sehlin, D., Englund, H., Simu, B., Karlsson, M., Ingelsson, M., Nikolajeff, F. K., Lannfelt, L., & Pettersson, F. E. (2012) · PLoS ONE · doi:10.1371/journal.pone.0032014 · Cited by 150
Limbocker, R., Chia, S., Ruggeri, F. S., Perni, M., Cascella, R., Heller, G. T., Meisl, G., Mannini, B., Habchi, J., Michaels, T. C. T., et al. (2019) · Nature Communications · doi:10.1038/s41467-018-07699-5 · Cited by 154
Shea, D. W., Hsu, C.-C., Bi, T., Paranjapye, N., Childers, M. C., Cochran, J., Tomberlin, C., Wang, L., Paris, D., Zonderman, J. A., et al. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1820585116 · Cited by 152
Oliveira, M. M., Lourenco, M. V., Longo, F., Kasica, N. P., Yang, W., Ureta, G., Ferreira, D. D. P., Mendonça, P. H. J., Bernales, S., Ma, T., et al. (2021) · Science Signaling · doi:10.1126/scisignal.abc5429 · Cited by 149
Nazem, A., & Mansoori, G. A. (2008) · Journal of Alzheimer s Disease · doi:10.3233/jad-2008-13210 · Cited by 150
PTEN recruitment controls synaptic and cognitive function in Alzheimer's models
Knafo, S., Sánchez‐Puelles, C., Palomer, E., Delgado, I., Draffin, J. E., Mingo, J., Wahle, T., Kaleka, K. S., Mou, L., Pereda-Pérez, I., et al. (2016) · Nature Neuroscience · doi:10.1038/nn.4225 · Cited by 149
Multi-Target Directed Donepezil-Like Ligands for Alzheimer's Disease
Unzeta, M., Esteban, G., Bolea, I., Fogel, W. A., Ramsay, R. R., Youdim, M. B. H., Tipton, K. F., & Marco, J. L. (2016) · Frontiers in Neuroscience · doi:10.3389/fnins.2016.00205 · Cited by 154
Amyloid β oligomers (AβOs) in Alzheimer’s disease
Mroczko, B., Groblewska, M., Litman‐Zawadzka, A., Kornhuber, J., & Lewczuk, P. (2017) · Journal of Neural Transmission · doi:10.1007/s00702-017-1820-x · Cited by 150
Neuronal Production of Transthyretin in Human and Murine Alzheimer's Disease: Is It Protective?
Li, X., Masliah, E., Reixach, N., & Buxbaum, J. N. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.2417-11.2011 · Cited by 147
Spatial relationship between synapse loss and β‐amyloid deposition in Tg2576 mice
Dong, H., Martin, M. V., Chambers, S., & Csernansky, J. G. (2006) · The Journal of Comparative Neurology · doi:10.1002/cne.21176 · Cited by 149
Characterization of the dipeptide repeat protein in the molecular pathogenesis of c9FTD/ALS
Yamakawa, M., Ito, D., Honda, T., Kubo, K., Noda, M., Nakajima, K., & Suzuki, N. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu576 · Cited by 154
Long-term neprilysin inhibition — implications for ARNIs
Campbell, D. J. (2016) · Nature Reviews Cardiology · doi:10.1038/nrcardio.2016.200 · Cited by 152
Metals and Neuronal Metal Binding Proteins Implicated in Alzheimer’s Disease
Cristóvão, J. S., Santos, R., & Gomes, C. M. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/9812178 · Cited by 146
Aβ aggregation and possible implications in Alzheimer's disease pathogenesis
Bharadwaj, P. R., Dubey, A. K., Masters, C. L., Martins, R. N., & Macreadie, I. G. (2008) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2009.00609.x · Cited by 155
Alzheimer's disease amyloid β-protein and synaptic function
Ondrejcak, T., Klyubin, I., Hu, N.-W., Barry, A. E., Cullen, W. K., & Rowan, M. J. (2010) · NeuroMolecular Medicine · doi:10.1007/s12017-009-8091-0 · Cited by 146
Haas, L. T., Salazar, S. V., Kostylev, M. A., Um, J. W., Kaufman, A. C., & Strittmatter, S. M. (2015) · Brain · doi:10.1093/brain/awv356 · Cited by 145
THE GENETICS AND MOLECULAR PATHOLOGY OF ALZHEIMER'S DISEASE
Selkoe, D. J. (2000) · Neurologic Clinics · doi:10.1016/s0733-8619(05)70232-2 · Cited by 146
Axonal transport, tau protein, and neurodegeneration in Alzheimer's disease
Terwel, D., Dewachter, I., & Van Leuven, F. (2002) · NeuroMolecular Medicine · doi:10.1385/nmm:2:2:151 · Cited by 146
Protecting Motor Neurons from Toxic Insult by Antagonism of Adenosine A2a and Trk Receptors
Mojsilovic‐Petrovic, J., Jeong, G., Crocker, A. J., Arneja, A., David, S., Russell, D., & Kalb, R. G. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.1856-06.2006 · Cited by 145
Is aging part of Alzheimer's disease, or is Alzheimer's disease part of aging?
Swerdlow, R. H. (2006) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2006.06.021 · Cited by 154
Inhibiting, promoting, and preserving stability of functional proteinfibrils
Jones, O. G., & Mezzenga, R. (2011) · Soft Matter · doi:10.1039/c1sm06643a · Cited by 143
Schützmann, M. P., Hasecke, F., Bachmann, S., Zielinski, M., Hänsch, S., Schroeder, G. F., Zempel, H., & Hoyer, W. (2021) · Nature Communications · doi:10.1038/s41467-021-24900-4 · Cited by 152
Alzheimer's Disease and the Amyloid β Protein
Small, D. H., & McLean, C. (1999) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1999.0730443.x · Cited by 146
Bieschke, J., Zhang, Q., Powers, E. T., Lerner, R. A., & Kelly, J. W. (2005) · Biochemistry · doi:10.1021/bi0501030 · Cited by 145
TREM2 promotes Aβ phagocytosis by upregulating C/EBPα-dependent CD36 expression in microglia
Kim, S.-M., Mun, B.-R., Lee, S.-J., Joh, Y., Lee, H.-Y., Ji, K.-Y., Choi, H.-R., Lee, E.-H., Kim, E.-M., Jang, J.-H., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-11634-x · Cited by 143
Klein, W. L. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-129039 · Cited by 145
Self-citationMechanisms of Transthyretin Inhibition of β-Amyloid AggregationIn Vitro
Li, X., Zhang, X., Ladiwala, A. R. A., Du, D., Yadav, J. K., Tessier, P. M., Wright, P. E., Kelly, J. W., & Buxbaum, J. N. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.2561-13.2013 · Cited by 143
Acceleration of Amyloid β-Peptide Aggregation by Physiological Concentrations of Calcium
Isaacs, A. M., Senn, D. B., Yuan, M., Shine, J. P., & Yankner, B. A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602061200 · Cited by 149
The Biological Function of the Prion Protein: A Cell Surface Scaffold of Signaling Modules
Linden, R. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00077 · Cited by 151
Pathways of Amyloid-β Aggregation Depend on Oligomer Shape
Barz, B., Liao, Q., & Strodel, B. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.7b10343 · Cited by 144
Roberts, B. R., Lind, M., Wagen, A. Z., Rembach, A., Frugier, T., Li, Q.-X., Ryan, T. M., McLean, C. A., Doecke, J. D., Rowe, C. C., et al. (2017) · Brain · doi:10.1093/brain/awx057 · Cited by 143
ER stress is involved in Aβ‐induced GSK‐3β activation and tau phosphorylation
Resende, R., Ferreiro, E. B., Pereira, C., & Oliveira, C. R. (2008) · Journal of Neuroscience Research · doi:10.1002/jnr.21648 · Cited by 142
Effect of AZD0530 on Cerebral Metabolic Decline in Alzheimer Disease
van Dyck, C. H., Nygaard, H. B., Chen, K., Donohue, M., Raman, R., Rissman, R. A., Brewer, J. B., Koeppe, R. A., Chow, T. W., Rafii, M. S., et al. (2019) · JAMA Neurology · doi:10.1001/jamaneurol.2019.2050 · Cited by 150
New Class of Inhibitors of Amyloid-β Fibril Formation
Lashuel, H. A., Hartley, D. M., Balakhaneh, D., Aggarwal, A. K., Teichberg, S., & Callaway, D. J. E. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m206593200 · Cited by 146
Masters, C. L., & Beyreuther, K. (2006) · Brain · doi:10.1093/brain/awl251 · Cited by 145
Ile-Phe Dipeptide Self-Assembly: Clues to Amyloid Formation
de Groot, N. S., Parella, T., Avilés, F. X., Vendrell, J., & Ventura, S. (2006) · Biophysical Journal · doi:10.1529/biophysj.106.096677 · Cited by 141
Branched KLVFF Tetramers Strongly Potentiate Inhibition of β‐Amyloid Aggregation
Chafekar, S. M., Malda, H., Merkx, M., Meijer, E. W., Viertl, D., Lashuel, H. A., Baas, F., & Scheper, W. (2007) · ChemBioChem · doi:10.1002/cbic.200700338 · Cited by 145
α-Helix targeting reduces amyloid-β peptide toxicity
Nerelius, C., Sandegren, A., Sargsyan, H., Raunak, R., Leijonmarck, H., Chatterjee, U., Fisahn, A., Imarisio, S., Lomas, D. A., Crowther, D. C., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0810364106 · Cited by 141
New structures help the modeling of toxic amyloidß ion channels
Jang, H., Zheng, J., Lal, R., & Nussinov, R. (2008) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2007.10.007 · Cited by 144
Na, K-ATPase α3 is a death target of Alzheimer patient amyloid-β assembly
Ohnishi, T., Yanazawa, M., Sasahara, T., Kitamura, Y., Hiroaki, H., Fukazawa, Y., Kii, I., Nishiyama, T., Kakita, A., Takeda, H., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1421182112 · Cited by 141
Palmitoylation in Alzheimers disease and other neurodegenerative diseases
Cho, E., & Park, M. (2016) · Pharmacological Research · doi:10.1016/j.phrs.2016.06.008 · Cited by 151
Lee, M., Yu, W., Shih, Y., Chen, C., Guo, Z., Huang, S., Chan, J. C. C., & Chen, Y. (2018) · Scientific Reports · doi:10.1038/s41598-018-23122-x · Cited by 141
Prion recognition elements govern nucleation, strain specificity and species barriers
Tessier, P. M., & Lindquist, S. L. (2007) · Nature · doi:10.1038/nature05848 · Cited by 141
Nimmrich, V., & Ebert, U. (2009) · Reviews in the Neurosciences · doi:10.1515/revneuro.2009.20.1.1 · Cited by 139
Aβ Oligomers Induce Neuronal Cell Cycle Events in Alzheimer's Disease
Varvel, N. H., Bhaskar, K., Patil, A. R., Pimplikar, S. W., Herrup, K., & Lamb, B. T. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.2441-08.2008 · Cited by 141
Why is the amyloid beta peptide of Alzheimer’s disease neurotoxic?
Rauk, A. (2008) · Dalton Transactions · doi:10.1039/b718601k · Cited by 139
Glial cell dysregulation: a new perspective on Alzheimer disease
Rommy von Bernhardi, M. (2007) · Neurotoxicity Research · doi:10.1007/bf03033906 · Cited by 141
Re, F., Airoldi, C., Zona, C., Masserini, M., Ferla, B. L., Quattrocchi, N., & Nicotra, F. (2010) · Current Medicinal Chemistry · doi:10.2174/092986710791959729 · Cited by 142
Ostapchenko, V. G., Chen, M., Guzmán, M. S., Xie, Y., Lavine, N. E., Fan, J., Beraldo, F. H., Martyn, A. C., Belrose, J. C., Mori, Y., et al. (2015) · Journal of Neuroscience · doi:10.1523/jneurosci.4081-14.2015 · Cited by 143
Ledo, J. H., Azevedo, E. P., Beckman, D., Ribeiro, F. C., Santos, L. E., Razolli, D. S., Kincheski, G. C., Melo, H. M., Bellio, M., Teixeira, A. L., et al. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.1269-16.2016 · Cited by 138
Thal, D. R., Capetillo-Zarate, E., Larionov, S., Staufenbiel, M., Zurbruegg, S., & Beckmann, N. (2009) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2008.01.017 · Cited by 138
Human apoE4-targeted replacement mice display synaptic deficits in the absence of neuropathology.
Wang, C., Wilson, W. A., Moore, S. D., Mace, B. E., Maeda, N., Schmechel, D. E., & Sullivan, P. M. (2005) · Neurobiology of Disease · doi:10.1016/j.nbd.2004.10.013 · Cited by 138
In Vivo Effects of ApoE and Clusterin on Amyloid-β Metabolism and Neuropathology
Holtzman, D. M. (2004) · Journal of Molecular Neuroscience · doi:10.1385/jmn:23:3:247 · Cited by 139
Biochemistry and Molecular Biology of Amyloid β‐Protein and the Mechanism of Alzheimer's Disease
(2008) · Handbook of Clinical Neurology · doi:10.1016/s0072-9752(07)01223-7 · Cited by 137
Protective Role of Methylene Blue in Alzheimer's Disease via Mitochondria and Cytochrome c Oxidase
Atamna, H., & Kumar, R. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100414 · Cited by 142
Paula-Lima, A. C., Adasme, T., SanMartín, C. D., Sebollela, A. S., Hetz, C. A., Carrasco, M. A., Ferreira, S. T., & Hidalgo, C. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3287 · Cited by 141
Strategies for the Inhibition of Protein Aggregation in Human Diseases
Bartolini, M., & Andrisano, V. (2010) · ChemBioChem · doi:10.1002/cbic.200900666 · Cited by 140
Schmidt, C., Lepsverdize, E., L, S., Das, A. M., Pizzo, S. V., Dityatev, A. E., & Schachner, M. (2007) · Molecular Psychiatry · doi:10.1038/sj.mp.4002077 · Cited by 139
Molecular tweezers for lysine and arginine – powerful inhibitors of pathologic protein aggregation
Schrader, T. H., Bitan, G., & Klärner, F. (2016) · Chemical Communications · doi:10.1039/c6cc04640a · Cited by 138
Neuronal RNA oxidation is a prominent feature of familial Alzheimer's disease
Nunomura, A., Chiba, S., Lippa, C. F., Cras, P. P., Kalaria, R. N., Takeda, A., Honda, K., Smith, M. A., & Perry, G. L. (2004) · Neurobiology of Disease · doi:10.1016/j.nbd.2004.06.003 · Cited by 136
Structure and function of amyloid in Alzheimer's disease
Morgan, C., Colombres, M., Núñez, M. T., & Inestrosa, N. C. (2004) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2004.10.004 · Cited by 146
Kheterpal, I., Chen, M., Cook, K. D., & Wetzel, R. B. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.06.066 · Cited by 135
Ognibene, E., Middei, S., Daniele, S., Adriani, W., Ghirardi, O., Caprioli, A., & Laviola, G. (2004) · Behavioural Brain Research · doi:10.1016/j.bbr.2004.05.028 · Cited by 140
YAZAWA, H., YU, Z.-X., TAKEDA, K., LE, Y., GONG, W., FERRANS, V. J., OPPENHEIM, J. J., LI, C. C. H., & WANG, J. M. (2001) · The FASEB Journal · doi:10.1096/fj.01-0251com · Cited by 105
The effect of Cu2+ and Zn2+ on the Aβ42 peptide aggregation and cellular toxicity
Sharma, A. K., Pavlova, S. T., Kim, J., Kim, J., & Mirica, L. M. (2013) · Metallomics · doi:10.1039/c3mt00161j · Cited by 135
Metal exposure and Alzheimer’s pathogenesis
Liu, G., Huang, W., Moir, R. D., Vanderburg, C. R., Lai, B. C. H., Peng, Z., Tanzi, R. E., Rogers, J. T., & Huang, X. (2006) · Journal of Structural Biology · doi:10.1016/j.jsb.2005.12.011 · Cited by 135
Acidic pH promotes the formation of toxic fibrils from β-amyloid peptide
Su, Y., & Chang, P.-T. (2001) · Brain Research · doi:10.1016/s0006-8993(00)03322-9 · Cited by 135
Communication breaks-Down: From neurodevelopment defects to cognitive disabilities in Down syndrome
Contestabile, A., Benfenati, F., & Gasparini, L. (2010) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2010.01.003 · Cited by 134
Pitt, J., Roth, W., Lacor, P., Smith, A. B., Blankenship, M., Velasco, P., De Felice, F., Breslin, P., & Klein, W. L. (2009) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2009.07.018 · Cited by 134
Self-citationβ‐amyloid inhibition of long‐term potentiation is mediated via tumor necrosis factor
Wang, Q., Wu, J., Rowan, M. J., & Anwyl, R. (2005) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2005.04457.x · Cited by 134
Cholesterol in Alzheimers Disease: Unresolved Questions
Stefani, M., & Liguri, G. (2009) · Current Alzheimer Research · doi:10.2174/156720509787313899 · Cited by 136
Oligomerization of Amyloid Aβ16–22 Peptides Using Hydrogen Bonds and Hydrophobicity Forces
Favrin, G., Irbäck, A., & Mohanty, S. (2004) · Biophysical Journal · doi:10.1529/biophysj.104.046839 · Cited by 134
The Molecular Basis of Functional Bacterial Amyloid Polymerization and Nucleation
Wang, X., Hammer, N. D., & Chapman, M. R. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m800466200 · Cited by 137
Siman, R., Reaume, A. G., Savage, M. J., Trusko, S., Lin, Y.-G., Scott, R. W., & Flood, D. G. (2000) · The Journal of Neuroscience · doi:10.1523/jneurosci.20-23-08717.2000 · Cited by 133
LRP in Amyloid‐β Production and Metabolism
Bu, G., Cam, J. A., & Zerbinatti, C. (2006) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1377.005 · Cited by 141
Spines, plasticity, and cognition in Alzheimer's model mice
Spires-Jones, T., & Knafo, S. (2012) · Neural Plasticity · doi:10.1155/2012/319836 · Cited by 133
NSAID and Antioxidant Prevention of Alzheimer's Disease: Lessons from In Vitro and Animal Models
COLE, G. M., MORIHARA, T., LIM, G. P., YANG, F., BEGUM, A., & FRAUTSCHY, S. A. (2004) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1332.005 · Cited by 129
New developments on the role of NMDA receptors in Alzheimer's disease
Malinow, R. (2012) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2011.09.001 · Cited by 132
RETRACTED: Cognitive effects of cell-derived and synthetically derived Aβ oligomers
Reed, M. N., Hofmeister, J. J., Jungbauer, L. M., Welzel, A. T., Yu, C., Sherman, M. A., Lesné, S., LaDu, M. J., Walsh, D. M., Ashe, K. H., et al. (2010) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2009.11.007 · Cited by 135
RetractedStructural properties of Aβ protofibrils stabilized by a small molecule
Williams, A. D., Sega, M., Chen, M., Kheterpal, I., Geva, M., Berthelier, V., Kaleta, D. T., Cook, K. D., & Wetzel, R. B. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0408582102 · Cited by 133
Amyloid-β detection with saccharide immobilized gold nanoparticle on carbon electrode
Chikae, M., Fukuda, T., Kerman, K., Idegami, K., Miura, Y., & Tamiya, E. (2008) · Bioelectrochemistry · doi:10.1016/j.bioelechem.2008.06.005 · Cited by 132
Metadata
- Authors
- 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., Wals, P., Zhang, C., 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
- 1998-05-26
- Volume
- 95
- Issue
- 11
- Pages
- 6448-6453
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC27787
- OpenAlex
- W2165021720
- Cited by
- 3,506
- References
- 68
- Citations by year
- 2026: 61 · 2025: 69 · 2024: 82 · 2023: 81 · 2022: 101 · 2021: 115 · 2020: 137 · 2019: 105 · 2018: 127 · 2017: 138 · 2016: 139 · 2015: 152 · 2014: 171 · 2013: 188 · 2012: 196
- FWCI
- 29.85
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- amyloid-beta 42, neurotoxicity, Alzheimer's disease, Fyn tyrosine kinase, neuroprotection, hippocampal long-term potentiation, synaptic plasticity, signal transduction, organotypic brain cultures
- MeSH terms
- Alzheimer Disease, Animals, Brain, Cell Membrane, Cells, Cultured, Ligands, Neurotoxins, Amyloid beta-Peptides, Cell Death, Mice
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
