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- W2000481487 abstract "Prefibrillar oligomers of the β-amyloid peptide (Aβ) are recognized as potential mediators of Alzheimer’s disease (AD) pathophysiology. Deficits in synaptic function, neurotoxicity, and the progression of AD have all been linked to the oligomeric Aβ assemblies rather than to Aβ monomers or to amyloid plaques. However, the molecular sites of Aβ oligomer action have remained largely unknown. Recently, the cellular prion protein (PrPC) has been shown to act as a functional receptor for Aβ oligomers in brain slices. Because PrPC serves as the substrate for Creutzfeldt–Jakob Disease (CJD), these data suggest mechanistic similarities between the two neurodegenerative diseases. Here, we review the importance of Aβ oligomers in AD, commonalities between AD and CJD, and the newly emergent role of PrPC as a receptor for Aβ oligomers." @default.
- W2000481487 created "2016-06-24" @default.
- W2000481487 creator A5026147594 @default.
- W2000481487 creator A5063261204 @default.
- W2000481487 date "2009-12-04" @default.
- W2000481487 modified "2023-10-18" @default.
- W2000481487 title "β-amyloid oligomers and cellular prion protein in Alzheimer’s disease" @default.
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- W2000481487 doi "https://doi.org/10.1007/s00109-009-0568-7" @default.
- W2000481487 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2846635" @default.
- W2000481487 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/19960174" @default.
- W2000481487 hasPublicationYear "2009" @default.
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