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- W2998692653 endingPage "545" @default.
- W2998692653 startingPage "522" @default.
- W2998692653 abstract "The prototype of transmissible neurodegenerative proteinopathies is prion diseases, characterized by aggregation of abnormally folded conformers of the native prion protein. A wealth of mechanisms has been proposed to explain the conformational conversion from physiological protein into misfolded, pathological form, mode of toxicity, propagation from cell-to-cell and regional spread. There is increasing evidence that other neurodegenerative diseases, most notably Alzheimer's disease (Aβ and tau), Parkinson's disease (α-synuclein), frontotemporal dementia (TDP43, tau or FUS) and motor neurone disease (TDP43), exhibit at least some of the misfolded prion protein properties. In this review, we will discuss to what extent each of the properties of misfolded prion protein is known to occur for Aβ, tau, α-synuclein and TDP43, with particular focus on self-propagation through seeding, conformational strains, selective cellular and regional vulnerability, stability and resistance to inactivation, oligomers, toxicity and summarize the most recent literature on transmissibility of neurodegenerative disorders." @default.
- W2998692653 created "2020-01-10" @default.
- W2998692653 creator A5005354758 @default.
- W2998692653 creator A5063134863 @default.
- W2998692653 date "2020-02-11" @default.
- W2998692653 modified "2023-10-13" @default.
- W2998692653 title "Invited Review: The role of prion‐like mechanisms in neurodegenerative diseases" @default.
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