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EphA4 Activation of c-Abl Mediates Synaptic Loss and LTP Blockade Caused by Amyloid-β Oligomers
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Other suggested Aβ binding partners at synapses include the α7-nicotinic receptor, Ephrin A4, PSD95 and LilrB2.
“Other suggested Aβ binding partners at synapses include the α7-nicotinic receptor [49], Ephrin A4 [73], PSD95 [35, 50, 52] and LilrB2 [32].”
From Transmembrane protein 97 is a potential synaptic amyloid beta receptor in human Alzheimer’s disease (2024) · cites this paper as [73]
Other binding partners that have been suggested to bind Aβ include the α7-nicotinic receptor, Ephrin A4 (EphA4), PSD95 or LilrB2.
“Other binding partners that have been suggested to bind Aβ include the α7-nicotinic receptor [49], Ephrin A4 (EphA4) [73], PSD95 [35, 50, 52] or LilrB2 [32].”
From Transmembrane protein 97 is a potential synaptic amyloid beta receptor in human Alzheimer’s disease (2024) · cites this paper as [73]
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Cellular prion protein mediates impairment of synaptic plasticity by amyloid-β oligomers
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Control of hippocampal dendritic spine morphology through ephrin-A3/EphA4 signaling
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Self-citationSynthetic amyloid-β oligomers impair long-term memory independently of cellular prion protein
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Reversing EphB2 depletion rescues cognitive functions in Alzheimer model
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c-Abl tyrosine kinase modulates tau pathology and Cdk5 phosphorylation in AD transgenic mice
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Metadata
- Authors
- M. Vargas, L., Leal, N., Estrada, L. D., González, A., Serrano, F., Araya, K., Gysling, K., Inestrosa, N. C., Pasquale, E. B., & Alvarez, A. R.
- Venue
- PLoS ONE
- Publisher
- Public Library of Science (PLoS)
- Published
- 2014-03-21
- Volume
- 9
- Issue
- 3
- Pages
- e92309
- ISSN
- 1932-6203
- PMC
- PMC3962387
- Cited by
- 85
- References
- 13
- Language
- en
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