The DOI matches its Crossref record; 186 of the 189 references it cites were found in a registry or an index.
Alzheimer's disease amyloid β-protein and synaptic function
Abstract
Alzheimer's disease (AD) is characterized neuropathologically by the deposition of different forms of amyloid beta-protein (A beta) including variable amounts of soluble species that correlate with severity of dementia. The extent of synaptic loss in the brain provides the best morphological correlate of cognitive impairment in clinical AD. Animal research on the pathophysiology of AD has therefore focussed on how soluble A beta disrupts synaptic mechanisms in vulnerable brain regions such as the hippocampus. Synaptic plasticity in the form of persistent activity-dependent increases or decreases in synaptic strength provide a neurophysiological substrate for hippocampal-dependent learning and memory. Acute treatment with human-derived or chemically prepared soluble A beta that contains certain oligomeric assemblies, potently and selectively disrupts synaptic plasticity causing inhibition of long-term potentiation (LTP) and enhancement of long-term depression (LTD) of glutamatergic transmission. Over time these and related actions of A beta have been implicated in reducing synaptic integrity. This review addresses the involvement of neurotransmitter intercellular signaling in mediating or modulating the synaptic plasticity disrupting actions of soluble A beta, with particular emphasis on the different roles of glutamatergic and cholinergic mechanisms. There is growing evidence to support the view that NMDA and possibly nicotinic receptors are critically involved in mediating t…
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“Previous reports consistently show that Aβ inhibits long-term potentiation (LTP) in the hippocampus (Ondrejcak et al., 2010), a widely accepted cellular model for learning and memory (Bliss and Collingridge, 1993)”
From Wild-Type, but Not Mutant N296H, Human Tau Restores Aβ-Mediated Inhibition of LTP in Tau−/− mice (2017) · cites this paper as Ondrejcak et al., 2010
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1 retracted
RETRACTED ARTICLE: A specific amyloid-β protein assembly in the brain impairs memory
Lesné, S., Koh, M. T., Kotilinek, L., Kayed, R., Glabe, C. G., Yang, A., Gallagher, M., & Ashe, K. H. (2006) · Nature · doi:10.1038/nature04533 · Cited by 2,769 · cited 1×
“…that certain forms of soluble Ab can trigger synaptic pruning in cultured neurons and brain slices in vitro (Roselli et al. 2005; Shankar et al. 2007) and cause cognitive impairment in the absence of neurodegeneration in animals (Cleary et al. 2005; Lesne et al. 2006; Haass and Selkoe 2007).”
BackgroundRetractedPhilosophical transactions of the Royal Society of London. B
Press, H. (1886) · Cited by 10,087
A JOURNAL OF PHARMACOLOGY AND EXPERIMENTAL THERAPEUTICS
Lindemann, L., Jaeschke, G., Michalon, A., Vieira, E., Honer, M., Spooren, W., Porter, R., Hartung, T., Kolczewski, S., Büttelmann, B., et al. (1909) · JAMA · doi:10.1001/jama.1909.02550020033007 · Cited by 7,889
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
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
Self-citationShankar, G. M., Li, S., Mehta, T. H., Garcia-Munoz, A., Shepardson, N. E., Smith, I., Brett, F. M., Farrell, M. A., Rowan, M. J., Lemere, C. A., et al. (2008) · Nature Medicine · doi:10.1038/nm1782 · Cited by 3,685
Self-citationDiffusible, 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
Long-Term Potentiation and Memory
Lynch, M. A. (2004) · Physiological Reviews · doi:10.1152/physrev.00014.2003 · Cited by 2,074
Natural oligomers of the amyloid-β protein specifically disrupt cognitive function
Cleary, J. P., Walsh, D. M., Hofmeister, J. J., Shankar, G. M., Kuskowski, M. A., Selkoe, D. J., & Ashe, K. H. (2004) · Nature Neuroscience · doi:10.1038/nn1372 · Cited by 1,722
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
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- Wang, Q., Klyubin, I., Wright, S., Griswold-Prenner, I., Rowan, M. J., & Anwyl, R. (2008b). Alpha v integrins mediate beta-amyloid induced inhibition of long-term potentiation. Neurobiology of Aging, 29, 1485–1493. · DOI · Paper page
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Wei, C., Liu, J., Wu, B., Shen, T., Fan, J. J., Lin, Y., Li, L., Guo, Y., Shang, Y., Zhou, B., et al. (2025) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2025.04.034 · Cited by 9
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Metadata
- Authors
- Ondrejcak, T., Klyubin, I., Hu, N.-W., Barry, A. E., Cullen, W. K., & Rowan, M. J.
- Affiliations
- Trinity College Dublin (IE)
- Corresponding author
- Rowan, Michael J.
- Venue
- NeuroMolecular Medicine
- Published
- 2009-09-16
- Volume
- 12
- Issue
- 1
- Pages
- 13-26
- ISSN
- 1535-1084 (ISSN-L)
- 1559-1174
- OpenAlex
- W2150302044
- Cited by
- 146
- References
- 189
- Citations by year
- 2026: 3 · 2025: 6 · 2024: 7 · 2023: 2 · 2022: 7 · 2021: 6 · 2020: 5 · 2019: 5 · 2018: 7 · 2017: 16 · 2016: 5 · 2015: 7 · 2014: 10 · 2013: 13 · 2012: 18
- FWCI
- 10.26
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- NeuroMolecular Medicine (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Health Research Board
- Science Foundation Ireland
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- Alzheimer's disease, amyloid-beta, soluble amyloid-beta oligomers, synaptic plasticity, long-term potentiation, long-term depression, glutamatergic neurotransmission, cholinergic mechanisms, NMDA receptor, nicotinic acetylcholine receptors, muscarinic receptors, hippocampus, synaptic loss, neurotransmitter signaling
- MeSH terms
- Acetylcholine, Alzheimer Disease, Animals, Humans, Synaptic Transmission, Receptors, Cholinergic, Synapses, Receptors, N-Methyl-D-Aspartate, Amyloid beta-Peptides, Long-Term Potentiation, Glutamic Acid, Long-Term Synaptic Depression
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