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Picomolar Amyloid-β Positively Modulates Synaptic Plasticity and Memory in Hippocampus
Open accessAbstract
Amyloid-β (Aβ) peptides are produced in high amounts during Alzheimer's disease, causing synaptic and memory dysfunction. However, they are also released in lower amounts in normal brains throughout life during synaptic activity. Here we show that low picomolar concentrations of a preparation containing both Aβ 42 monomers and oligomers cause a marked increase of hippocampal long-term potentiation, whereas high nanomolar concentrations lead to the well established reduction of potentiation. Picomolar levels of Aβ 42 also produce a pronounced enhancement of both reference and contextual fear memory. The mechanism of action of picomolar Aβ 42 on both synaptic plasticity and memory involves α7-containing nicotinic acetylcholine receptors. These findings strongly support a model for Aβ effects in which low concentrations play a novel positive, modulatory role on neurotransmission and memory, whereas high concentrations play the well known detrimental effect culminating in dementia.
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“studies that shed light on the physiological role of Aβ in non-diseased brains show that Aβ plays a role in synaptic transmission and is involved in learning and memory formation [18–22].”
From Amyloid-β interrupts canonical Sonic hedgehog signaling by distorting primary cilia structure (2018) · cites this paper as [22]
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“picomolar concentrations of Aβ are sufficient to stimulate nicotinic receptors and subsequently LTP and learning and memory in healthy rodents (Puzzo et al., 2008, 2012; Morley et al., 2010)”
From Emerging Alternative Proteinases in APP Metabolism and Alzheimer’s Disease Pathogenesis: A Focus on MT1-MMP and MT5-MMP (2019) · cites this paper as Puzzo et al., 2008
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“To address this concern, other studies injected picomolar concentrations of Aβ peptides into the mice, which also significantly enhanced synaptic plasticity and memory formation.394”
From Amyloid β-based therapy for Alzheimer’s disease: Challenges, successes and future (2023) · cites this paper as [394]
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“Remarkably, at sub-nanomolar doses, the effect on LTP is reversed, and Aβ markedly enhances LTP. Discovered by Arancio and colleagues in a detailed analysis (Puzzo et al., 2008), enhancement occurs over a narrow range of concentrations and is associated with presynaptic activation of alpha7 nicotinic receptors.”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Puzzo et al., 2008
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“and synaptic transmission (Puzzo et al., 2008, 2011)”
From Emerging Alternative Proteinases in APP Metabolism and Alzheimer’s Disease Pathogenesis: A Focus on MT1-MMP and MT5-MMP (2019) · cites this paper as Puzzo et al., 2008
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Citations
Cites
The Mouse Brain in Stereotaxic Coordinates
Paxinos, G. (2001) · Cited by 12,859
Short-Term Synaptic Plasticity
Zucker, R. S., & Regehr, W. G. (2002) · Annual Review of Physiology · doi:10.1146/annurev.physiol.64.092501.114547 · Cited by 5,068
Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide
Haass, C., & Selkoe, D. J. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2101 · Cited by 4,744
Differential contribution of amygdala and hippocampus to cued and contextual fear conditioning.
Phillips, R. G., & LeDoux, J. E. (1992) · Behavioral Neuroscience · doi:10.1037/0735-7044.106.2.274 · Cited by 3,292
mouse brain in stereotaxic coordinates
Franklin, K. B. J., & Paxinos, G. (1997) · Cited by 3,258
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
APP Processing and Synaptic Function
Kamenetz, F., Tomita, T., Hsieh, H., Seabrook, G., Borchelt, D., Iwatsubo, T., Sisodia, S., & Malinow, R. (2003) · Neuron · doi:10.1016/s0896-6273(03)00124-7 · Cited by 1,644
Citron, M., Westaway, D., Xia, W., Carlson, G., Diehl, T., Levesque, G., Johnson-wood, K., Lee, M., Seubert, P., Davis, A., et al. (1997) · Nature Medicine · doi:10.1038/nm0197-67 · Cited by 1,271
Synaptic Activity Regulates Interstitial Fluid Amyloid-β Levels In Vivo
Cirrito, J. R., Yamada, K. A., Finn, M. B., Sloviter, R. S., Bales, K. R., May, P. C., Schoepp, D. D., Paul, S. M., Mennerick, S., & Holtzman, D. M. (2005) · Neuron · doi:10.1016/j.neuron.2005.10.028 · Cited by 1,265
A Transcriptively Active Complex of APP with Fe65 and Histone Acetyltransferase Tip60
Cao, X., & Südhof, T. C. (2001) · Science · doi:10.1126/science.1058783 · Cited by 1,202
Research works printed but not linked: 2
- 1985, Exp Brain Res, 58, 11
- 2005, Methods Mol Biol, 299, 279
Cited by
Sorted by citations
Amyloid-β–induced neuronal dysfunction in Alzheimer's disease: from synapses toward neural networks
Palop, J. J., & Mucke, L. (2010) · Nature Neuroscience · doi:10.1038/nn.2583 · Cited by 1,651
Classification and basic pathology of Alzheimer disease
Duyckaerts, C., Delatour, B., & Potier, M.-C. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0532-1 · Cited by 1,031
Network abnormalities and interneuron dysfunction in Alzheimer disease
Palop, J. J., & Mucke, L. (2016) · Nature reviews. Neuroscience · doi:10.1038/nrn.2016.141 · Cited by 1,022
Neurotoxicity of Amyloid -Protein: Synaptic and Network Dysfunction
Mucke, L., & Selkoe, D. J. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006338 · Cited by 1,000
APP processing in Alzheimer’s disease.
Zhang, Y.-W., Thompson, R., Zhang, H., & Xu, H. (2011) · Molecular Brain · doi:10.1186/1756-6606-4-3 · Cited by 983
Linking lipids to Alzheimer's disease: cholesterol and beyond
Di Paolo, G., & Kim, T.-W. (2011) · Nature Reviews Neuroscience · doi:10.1038/nrn3012 · Cited by 972
Amyloid β-based therapy for Alzheimer’s disease: Challenges, successes and future
Zhang, Y., Chen, H., Li, R., Sterling, K., & Song, W. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01484-7 · Cited by 988
“To address this concern, other studies injected picomolar concentrations of Aβ peptides into the mice, which also significantly enhanced synaptic plasticity and memory formation.(394) These findings suggest that physiological levels of Aβ monomers are crucial to maintain a normal synaptic function while only Aβ aggreg…”
BackgroundOxidative Stress and the Pathogenesis of Alzheimer's Disease
Zhao, Y., & Zhao, B. (2013) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2013/316523 · Cited by 855
Oxidative stress in Alzheimer’s disease
Chen, Z., & Zhong, C. (2014) · Neuroscience Bulletin · doi:10.1007/s12264-013-1423-y · Cited by 797
Apolipoprotein E and Apolipoprotein E Receptors: Normal Biology and Roles in Alzheimer Disease
Holtzman, D. M., Herz, J., & Bu, G. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006312 · Cited by 782
Basal Forebrain Cholinergic Circuits and Signaling in Cognition and Cognitive Decline
Ballinger, E. C., Ananth, M. R., Talmage, D. A., & Role, L. W. (2016) · Neuron · doi:10.1016/j.neuron.2016.09.006 · Cited by 763
Not just amyloid: physiological functions of the amyloid precursor protein family
Müller, U. C., Deller, T., & Korte, M. (2017) · Nature Reviews Neuroscience · doi:10.1038/nrn.2017.29 · Cited by 634
Cerebrospinal fluid secretion by the choroid plexus
Damkier, H. H., Brown, P. D., & Praetorius, J. (2013) · Physiological Reviews · doi:10.1152/physrev.00004.2013 · Cited by 606
Epileptic activity in Alzheimer’s disease: Causes and clinical relevance
Vossel, K. A., Tartaglia, M. C., Nygaard, H. B., Zeman, A. Z., & Miller, B. L. (2017) · The Lancet Neurology · doi:10.1016/s1474-4422(17)30044-3 · Cited by 590
Inflammation: the link between comorbidities, genetics, and Alzheimer’s disease
Newcombe, E. A., Camats-Perna, J., Silva, M. L., Valmas, N., Huat, T. J., & Medeiros, R. (2018) · Journal of Neuroinflammation · doi:10.1186/s12974-018-1313-3 · Cited by 532
The Role of NMDA Receptors in Alzheimer’s Disease
Liu, J., Chang, L., Song, Y., Li, H., & Wu, Y. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00043 · Cited by 535
Synaptic degeneration in Alzheimer's disease
Arendt, T. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0536-x · Cited by 517
Alzheimer's disease: synaptic dysfunction and Aβ
Shankar, G. M., & Walsh, D. M. (2009) · Molecular Neurodegeneration · doi:10.1186/1750-1326-4-48 · Cited by 486
Danysz, W., & Parsons, C. G. (2012) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2012.02057.x · Cited by 500
Amyloid-β as a positive endogenous regulator of release probability at hippocampal synapses
Abramov, E., Dolev, I., Fogel, H., Ciccotosto, G. D., Ruff, E., & Slutsky, I. (2009) · Nature Neuroscience · doi:10.1038/nn.2433 · Cited by 499
Biological metals and metal-targeting compounds in major neurodegenerative diseases
Barnham, K. J., & Bush, A. I. (2014) · Chem. Soc. Rev. · doi:10.1039/c4cs00138a · Cited by 497
Nicotinic ACh receptors as therapeutic targets in CNS disorders
Dineley, K. T., Pandya, A. A., & Yakel, J. L. (2015) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2014.12.002 · Cited by 460
Kent, S. A., Spires-Jones, T. L., & Durrant, C. S. (2020) · Acta Neuropathologica · doi:10.1007/s00401-020-02196-w · Cited by 446
The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease
Ferreira, S. T., & Klein, W. L. (2011) · Neurobiology of Learning and Memory · doi:10.1016/j.nlm.2011.08.003 · Cited by 442
Resolving controversies on the path to Alzheimer's therapeutics
Selkoe, D. J. (2011) · Nature Medicine · doi:10.1038/nm.2460 · Cited by 494
Molecular Pathogenesis of Alzheimer's Disease: An Update
Sanabria‐Castro, A., Echeverría, I. A., & Bonilla, C. M. (2017) · Annals of Neurosciences · doi:10.1159/000464422 · Cited by 427
Spatial correlation between brain aerobic glycolysis and amyloid-β (Aβ) deposition
Vlassenko, A. G., Vaishnavi, S. N., Couture, L., Sacco, D., Shannon, B. J., Mach, R. H., Morris, J. C., Raichle, M. E., & Mintun, M. A. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1010461107 · Cited by 404
Activity Dependent Degeneration Explains Hub Vulnerability in Alzheimer's Disease
de Haan, W., Mott, K. K., van Straaten, E. C. W., Scheltens, P., & Stam, C. J. (2012) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1002582 · Cited by 400
Calabrese, E. J. (2013) · Critical Reviews in Toxicology · doi:10.3109/10408444.2013.808172 · Cited by 391
The Amyloid Cascade Hypothesis in Alzheimer’s Disease: It’s Time to Change Our Mind
Ricciarelli, R., & Fedele, E. (2017) · Current Neuropharmacology · doi:10.2174/1570159x15666170116143743 · Cited by 380
Ferreira, S. T., Lourenco, M. V., Oliveira, M. M., & De Felice, F. G. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00191 · Cited by 373
Intraneuronal β-amyloid accumulation and synapse pathology in Alzheimer’s disease
Gouras, G. K., Tampellini, D., Takahashi, R. H., & Capetillo-Zarate, E. (2010) · Acta Neuropathologica · doi:10.1007/s00401-010-0679-9 · Cited by 372
Amyloid Beta in Aging and Alzheimer’s Disease
Sehar, U., Rawat, P., Reddy, A. P., Kopel, J. J., & Reddy, P. H. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232112924 · Cited by 409
Soluble Aβ oligomer production and toxicity
Larson, M. E., & Lesné, S. E. (2012) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07478.x · Cited by 356
Proteolytic processing of Alzheimer’s β‐amyloid precursor protein
Zhang, H., Ma, Q., Zhang, Y., & Xu, H. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07519.x · Cited by 344
Endogenous amyloid‐β is necessary for hippocampal synaptic plasticity and memory
Puzzo, D., Privitera, L., Fa', M., Staniszewski, A., Hashimoto, G., Aziz, F., Sakurai, M., Ribe, E. M., Troy, C. M., Mercken, M., et al. (2011) · Annals of Neurology · doi:10.1002/ana.22313 · Cited by 278
Self-citationAlzheimer's disease: synapses gone cold
Koffie, R. M., Hyman, B. T., & Spires‐Jones, T. L. (2011) · Molecular Neurodegeneration · doi:10.1186/1750-1326-6-63 · Cited by 316
Synaptic changes in Alzheimer’s disease and its models
Pozueta, J., Lefort, R., & Shelanski, M. L. (2012) · Neuroscience · doi:10.1016/j.neuroscience.2012.05.050 · Cited by 319
Role of Amyloid-β and Tau Proteins in Alzheimer’s Disease: Confuting the Amyloid Cascade
Gulisano, W., Maugeri, D., Baltrons, M. A., Fà, M., Amato, A., Palmeri, A., D’Adamio, L., Grassi, C., Devanand, D. P., Honig, L. S., et al. (2018) · Journal of Alzheimer's Disease · doi:10.3233/jad-179935 · Cited by 313
Self-citationBiron, K. E., Dickstein, D. L., Gopaul, R., & Jefferies, W. A. (2011) · PLoS ONE · doi:10.1371/journal.pone.0023789 · Cited by 300
Role of the nicotinic acetylcholine receptor in Alzheimer's disease pathology and treatment.
Lombardo, S., & Maskos, U. (2015) · Neuropharmacology · doi:10.1016/j.neuropharm.2014.11.018 · Cited by 281
Olfactory Dysfunction Correlates with Amyloid-β Burden in an Alzheimer's Disease Mouse Model
Wesson, D. W., Levy, E., Nixon, R. A., & Wilson, D. A. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.4622-09.2010 · Cited by 290
Immunotherapeutic Approaches for Alzheimer’s Disease
Wisniewski, T., & Goñi, F. (2015) · Neuron · doi:10.1016/j.neuron.2014.12.064 · Cited by 284
“Is dopamine involved in Alzheimer's disease?”
Martorana, A., & Koch, G. (2014) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00252 · Cited by 276
Recent advances in our understanding of neurodegeneration
Jellinger, K. A. (2009) · Journal of Neural Transmission · doi:10.1007/s00702-009-0240-y · Cited by 274
Extracellular Tau Oligomers Produce An Immediate Impairment of LTP and Memory
Fà, M., Puzzo, D., Piacentini, R., Staniszewski, A., Zhang, H., Baltrons, M. A., Puma, D. D. L., Chatterjee, I., Li, J., Saeed, F., et al. (2016) · Scientific Reports · doi:10.1038/srep19393 · Cited by 290
Self-citationSynaptic dysfunction in Alzheimer's disease: Mechanisms and therapeutic strategies
Chen, Y., Fu, A. K. Y., & Ip, N. Y. (2019) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2018.11.006 · Cited by 258
Amyloid-β Receptors: The Good, the Bad, and the Prion Protein
Jarosz-Griffiths, H. H., Noble, E., Rushworth, J. V., & Hooper, N. M. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.r115.702704 · Cited by 256
Amyloid-β as a Modulator of Synaptic Plasticity
Parihar, M. S., & Brewer, G. J. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-101020 · Cited by 264
Kandalepas, P. C., Sadleir, K. R., Eimer, W. A., Zhao, J., Nicholson, D. A., & Vassar, R. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1152-3 · Cited by 240
Barry, A. E., Klyubin, I., Mc Donald, J. M., Mably, A. J., Farrell, M. A., Scott, M., Walsh, D. M., & Rowan, M. J. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.6500-10.2011 · Cited by 237
Singh, B., Day, C. M., Abdella, S., & Garg, S. (2024) · Journal of Controlled Release · doi:10.1016/j.jconrel.2024.01.047 · Cited by 256
What Happens with the Circuit in Alzheimer's Disease in Mice and Humans?
Zott, B., Busche, M. A., Sperling, R. A., & Konnerth, A. (2018) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-080317-061725 · Cited by 221
Rodent models for Alzheimer’s disease drug discovery
Puzzo, D., Gulisano, W., Palmeri, A., & Arancio, O. (2015) · Expert Opinion on Drug Discovery · doi:10.1517/17460441.2015.1041913 · Cited by 222
Self-citationBehavioral assays with mouse models of Alzheimer's disease: Practical considerations and guidelines
Puzzo, D., Lee, L. S., Palmeri, A., Calabrese, G., & Arancio, O. (2014) · Biochemical Pharmacology · doi:10.1016/j.bcp.2014.01.011 · Cited by 226
Self-citationNimgampalle, M., Chakravarthy, H., Sharma, S., Shree, S., Bhat, A. R., Pradeepkiran, J. A., & Devanathan, V. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.101994 · Cited by 207
The senescence accelerated mouse (SAMP8) as a model for oxidative stress and Alzheimer's disease
Morley, J. E., Armbrecht, H. J., Farr, S. A., & Kumar, V. B. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.11.015 · Cited by 205
The Cholinergic System, the Adrenergic System and the Neuropathology of Alzheimer’s Disease
Bekdash, R. A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22031273 · Cited by 222
Dziewczapolski, G., Głogowski, M., Masliah, E., & Heinemann, S. F. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.6159-08.2009 · Cited by 199
Research update: Alpha7 nicotinic acetylcholine receptor mechanisms in Alzheimer's disease
Parri, H. R., Hernandez, C. M., & Dineley, K. T. (2011) · Biochemical Pharmacology · doi:10.1016/j.bcp.2011.06.039 · Cited by 187
Imbimbo, B. P., & Giardina, G. A. M. (2011) · Current Topics in Medicinal Chemistry · doi:10.2174/156802611795860942 · Cited by 196
Meftah, S., & Gan, J. (2023) · Frontiers in Synaptic Neuroscience · doi:10.3389/fnsyn.2023.1129036 · Cited by 205
The duality of amyloid-β: its role in normal and Alzheimer’s disease states
Azargoonjahromi, A. (2024) · Molecular Brain · doi:10.1186/s13041-024-01118-1 · Cited by 214
Molecular mechanisms of neuropathological changes in Alzheimer’s disease: a review
Šerý, O., Povová, J., Mı́šek, I., Pešák, L., & Janout, V. (2013) · Folia Neuropathologica · doi:10.5114/fn.2013.34190 · Cited by 198
Goure, W. F., Krafft, G. A., Jerecic, J., & Hefti, F. (2014) · Alzheimer's Research & Therapy · doi:10.1186/alzrt272 · Cited by 190
Exosomes neutralize synaptic-plasticity-disrupting activity of Aβ assemblies in vivo
An, K., Klyubin, I. V., Kim, Y., Jung, J. H., Mably, A. J., O’Dowd, S., Lynch, T., Kanmert, D., Lemere, C. A., Finan, G. M., et al. (2013) · Molecular Brain · doi:10.1186/1756-6606-6-47 · Cited by 196
Acute function of secreted amyloid precursor protein fragment APPsα in synaptic plasticity
Hick, M., Herrmann, U., Weyer, S. W., Mallm, J.-P., Tschäpe, J.-A., Borgers, M., Mercken, M., Roth, F. C., Draguhn, A., Slomianka, L., et al. (2015) · Acta Neuropathologica · doi:10.1007/s00401-014-1368-x · Cited by 191
Singh, S. K., Srivastav, S., Yadav, A. K., Srikrishna, S., & Perry, G. L. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/7361613 · Cited by 196
Amyloid Beta: Multiple Mechanisms of Toxicity and Only Some Protective Effects?
Carrillo‐Mora, P., Luna, R., & Colín-Barenque, L. (2014) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2014/795375 · Cited by 187
Alzheimer’s Disease: The Link Between Amyloid-β and Neurovascular Dysfunction
Solis, E., Hascup, K. N., & Hascup, E. R. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-200473 · Cited by 192
Izzo, N. J., Staniszewski, A., To, L., Fa, M., Teich, A. F., Saeed, F., Wostein, H., Walko, T., Vaswani, A., Wardius, M., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0111898 · Cited by 180
Self-citationHu, N., Klyubin, I. V., Anwyl, R., & Rowan, M. J. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0908083106 · Cited by 176
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
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
Ligand-Gated Ion Channels: New Insights into Neurological Disorders and Ligand Recognition
Lemoine, D., Jiang, R., Taly, A., Chataigneau, T., Specht, A., & Grütter, T. (2012) · Chemical Reviews · doi:10.1021/cr3000829 · Cited by 176
Harris, S. S., Wolf, F., De Strooper, B., & Busche, M. A. (2020) · Neuron · doi:10.1016/j.neuron.2020.06.005 · Cited by 161
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
He, Y., Wei, M., Wu, Y., Qin, H., Li, W., Ma, X., Cheng, J., Ren, J., Shen, Y., Chen, Z., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-09114-z · Cited by 159
Fabiani, C., & Antollini, S. S. (2019) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2019.00309 · Cited by 158
Alifragis, P., & Marsh, J. (2018) · Neural Regeneration Research · doi:10.4103/1673-5374.230276 · Cited by 156
A role for tau in learning, memory and synaptic plasticity
Biundo, F., Prete, D. D., Zhang, H., Arancio, O., & D'adamio, L. (2018) · Scientific Reports · doi:10.1038/s41598-018-21596-3 · Cited by 159
Self-citationOxidative Stress and Metabolic Syndrome: Cause or Consequence of Alzheimer's Disease?
Contreras, D. L., Carvajal, K., Toral-Ríos, D., Franco-Bocanegra, D., & Campos‐Peña, V. (2014) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2014/497802 · Cited by 155
Why Pleiotropic Interventions are Needed for Alzheimer's Disease
Frautschy, S. A., & Cole, G. M. (2010) · Molecular Neurobiology · doi:10.1007/s12035-010-8137-1 · Cited by 152
Synaptic Therapy in Alzheimer's Disease: A CREB-centric Approach
Teich, A. F., Nicholls, R. E., Puzzo, D., Fiorito, J., Purgatorio, R., Fà, M., & Arancio, O. (2015) · Neurotherapeutics · doi:10.1007/s13311-014-0327-5 · Cited by 151
Self-citationAlzheimer'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
Therapeutic Strategies Targeting Amyloid-β in Alzheimer’s Disease
Pinheiro, L. M. V., & Faustino, C. M. C. (2019) · Current Alzheimer Research · doi:10.2174/1567205016666190321163438 · Cited by 144
Klein, W. L. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-129039 · Cited by 145
Alpha 7 nicotinic acetylcholine receptor and its effects on Alzheimer's disease
Ma, K., & Qian, Y. (2018) · Neuropeptides · doi:10.1016/j.npep.2018.12.003 · Cited by 147
Tamayev, R., Matsuda, S., Arancio, O., & D'Adamio, L. (2012) · EMBO Molecular Medicine · doi:10.1002/emmm.201100195 · Cited by 142
Self-citationBuchholz, S., & Zempel, H. (2024) · Alzheimer s & Dementia · doi:10.1002/alz.13784 · Cited by 154
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Metadata
- Authors
- Puzzo, D., Privitera, L., Leznik, E., Fà, M., Staniszewski, A., Palmeri, A., & Arancio, O.
- Affiliations
- Columbia University Irving Medical Center (US)
- University of Catania (IT)
- Columbia University (US)
- Corresponding author
- Arancio, Ottavio
- ORCID
- Venue
- The Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 2008-12-31
- Volume
- 28
- Issue
- 53
- Pages
- 14537-14545
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- PMC
- PMC2673049
- OpenAlex
- W2078917784
- Cited by
- 740
- References
- 56
- Citations by year
- 2026: 17 · 2025: 23 · 2024: 41 · 2023: 38 · 2022: 40 · 2021: 45 · 2020: 49 · 2019: 44 · 2018: 38 · 2017: 46 · 2016: 46 · 2015: 50 · 2014: 51 · 2013: 42 · 2012: 44
- FWCI
- 28.04
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Neuroscience (publishedVersion, cc-by-nc-sa)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- UNICA IRIS Institutional Research Information System (University of Cagliari) (submittedVersion)
- Funders
- Alzheimer's Association (NIRG-07-59597)
- National Institutes of Health
- National Institute of Neurological Disorders and Stroke (R01NS040045, R01NS049442, NS049442)
- 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 › Cognitive Neuroscience › Memory and Neural Mechanisms
- Keywords
- amyloid-beta, synaptic plasticity, long-term potentiation, hippocampus, memory, fear memory, contextual fear, alpha7 nicotinic acetylcholine receptor, Alzheimer's disease, amyloid-beta oligomers, neurotransmission
- MeSH terms
- Analysis of Variance, Animals, Bungarotoxins, Dose-Response Relationship, Drug, Electric Stimulation, Hippocampus, Humans, Male, Mecamylamine, Memory, Mice, Inbred C57BL, Neuronal Plasticity, Peptide Fragments, Receptors, Nicotinic, Synapses, 2-Amino-5-phosphonovalerate, Amyloid beta-Peptides, Mice, Knockout, Patch-Clamp Techniques, Excitatory Amino Acid Antagonists, Nicotinic Antagonists, Maze Learning, Excitatory Postsynaptic Potentials, Mice, alpha7 Nicotinic Acetylcholine Receptor, In Vitro Techniques
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