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- W2011467350 abstract "Alzheimer disease (AD) has traditionally been thought to involve the misfolding and aggregation of two different factors that contribute in parallel to pathogenesis: amyloid-β (Aβ) peptides, which represent proteolytic fragments of the transmembrane amyloid precursor protein, and tau, which normally functions as a neuronally enriched, microtubule-associated protein that predominantly accumulates in axons. Recent evidence has challenged this model, however, by revealing numerous functional interactions between Aβ and tau in the context of pathogenic mechanisms for AD. Moreover, the propagation of toxic, misfolded Aβ and tau bears a striking resemblance to the propagation of toxic, misfolded forms of the canonical prion protein, PrP, and misfolded Aβ has been shown to induce tau misfolding in vitro through direct, intermolecular interaction. In this review we discuss evidence for the prion-like properties of both Aβ and tau individually, as well as the intriguing possibility that misfolded Aβ acts as a template for tau misfolding in vivo." @default.
- W2011467350 created "2016-06-24" @default.
- W2011467350 creator A5005208190 @default.
- W2011467350 creator A5020053032 @default.
- W2011467350 creator A5052796696 @default.
- W2011467350 date "2013-01-01" @default.
- W2011467350 modified "2023-10-17" @default.
- W2011467350 title "Alzheimer disease" @default.
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- W2011467350 doi "https://doi.org/10.4161/pri.22118" @default.
- W2011467350 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3609044" @default.
- W2011467350 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/22965142" @default.
- W2011467350 hasPublicationYear "2013" @default.
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