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Systematic and standardized comparison of reported amyloid-β receptors for sufficiency, affinity, and Alzheimer's disease relevance
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Cellular prion protein (PrPc) is the most studied Aβ binding candidate at synapses, either alone or through a complex with mGluR5.
“Among the Aβ binding candidates, cellular prion protein (PrPc) represents the most studied, either alone or through a complex with mGluR5 [37, 62, 72, 79].”
From Transmembrane protein 97 is a potential synaptic amyloid beta receptor in human Alzheimer’s disease (2024) · cites this paper as [62]
The most studied binding partner of Aβ is PrPc, which through a cascade involving a complex with mGluR5 may lead to toxicity independently or via tau.
“The most studied binding partner is the PrPc, which through a cascade involving a complex with mGluR5 may lead to toxicity independently or via tau [37, 62, 72, 79].”
From Transmembrane protein 97 is a potential synaptic amyloid beta receptor in human Alzheimer’s disease (2024) · cites this paper as [62]
It is likely that Aβ is in fact interacting with more than one protein.
“It is likely that Aβ is in fact interacting with more than one protein [62].”
From Transmembrane protein 97 is a potential synaptic amyloid beta receptor in human Alzheimer’s disease (2024) · cites this paper as [62]
In post synapses, FRET was observed between Aβ and PrPc, between TMEM97 and PGRMC1, and between TMEM97 and PrPc.
“In post synapses, we also observed FRET between Aβ and PrPc—which has also been observed to bind Aβ in model systems[62]—and between TMEM97 and PGRMC1 which are known to be binding partners in vitro and in human cases [55], and between TMEM97 and PrPc (Fig. 3).”
From Transmembrane protein 97 is a potential synaptic amyloid beta receptor in human Alzheimer’s disease (2024) · cites this paper as [62]
Aβ oligomers have been shown to bind saturably to a single site, suggesting specific pharmacological interactions with receptors.
“Further, while Aβ fibrils bind non-specifically to a variety of surfaces, and Aβ monomers bind to several receptors when applied exogenously [5], Aβ oligomers have been shown to bind saturably to a single site[27, 62] suggesting specific pharmacological interactions with receptors.”
From Transmembrane protein 97 is a potential synaptic amyloid beta receptor in human Alzheimer’s disease (2024) · cites this paper as [62]
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The relationship between amyloid-beta and brain capillary endothelial cells in Alzheimer’s disease
Su, Q., Guo, J.-H., Zhang, Y.-L., Wang, J., & Zhang, Z.-N. (2022) · Neural Regeneration Research · doi:10.4103/1673-5374.335829 · Cited by 91
LILRB2-mediated TREM2 signaling inhibition suppresses microglia functions
Zhao, P., Xu, Y., Jiang, L.-L., Fan, X., Ku, Z., Li, L., Liu, X., Deng, M., Arase, H., Zhu, J.-J., et al. (2022) · Molecular Neurodegeneration · doi:10.1186/s13024-022-00550-y · Cited by 54
Transmembrane protein 97 is a potential synaptic amyloid beta receptor in human Alzheimer’s disease
Colom-Cadena, M., Toombs, J., Simzer, E., Holt, K., McGeachan, R., Tulloch, J., Jackson, R. J., Catterson, J. H., Spires-Jones, M. P., Rose, J., et al. (2024) · Acta Neuropathologica · doi:10.1007/s00401-023-02679-6 · Cited by 44
Metadata
- Authors
- Smith, L. M., Kostylev, M. A., Lee, S., & Strittmatter, S. M.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2019-04
- Volume
- 294
- Issue
- 15
- Pages
- 6042-6053
- ISSN
- 0021-9258
- Cited by
- 73
- References
- 17
- Language
- en
- Funders
- HHS | NIH | National Institute on Aging (R01AG034924, P50AG047270, RF1AG05300)
- HHS | NIH | National Institute of Neurological Disorders and Stroke (R35NS097283)
- Dr. Ralph and Marian Falk Medical Research Trust (Transformative Award)
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