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- W2016145731 endingPage "1459" @default.
- W2016145731 startingPage "1433" @default.
- W2016145731 abstract "Protein misfolding diseases have been classically understood as diffuse errors in protein folding, with misfolded protein arising autonomously throughout a tissue due to a pathologic stressor. The field of prion science has provided an alternative mechanism whereby a seed of pathologically misfolded protein, arising exogenously or through a rare endogenous structural fluctuation, yields a template to catalyze misfolding of the native protein. The misfolded protein may then spread intercellularly to communicate the misfold to adjacent areas and ultimately infect a whole tissue. Mounting evidence implicates a prion-like process in the propagation of several neurodegenerative diseases, including Alzheimer's, Parkinson's, Huntington's, amyotrophic lateral sclerosis, and the tauopathies. However, the parallels between the events observed in these conditions and those in prion disease are often incomplete. The aim of this review was to examine the current state of knowledge concerning the mechanisms of protein misfolding and aggregation for neurodegeneration-associated proteins. In addition, possible methods of intercellular spread are described that focus on the hypothesis that released microvesicles function as misfolded protein delivery vehicles, and the therapeutic options enabled by viewing these diseases from the prion perspective." @default.
- W2016145731 created "2016-06-24" @default.
- W2016145731 creator A5012764223 @default.
- W2016145731 creator A5024373195 @default.
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- W2016145731 creator A5066183867 @default.
- W2016145731 creator A5067205297 @default.
- W2016145731 creator A5087609900 @default.
- W2016145731 date "2011-11-15" @default.
- W2016145731 modified "2023-10-03" @default.
- W2016145731 title "Generalization of the Prion Hypothesis to Other Neurodegenerative Diseases: An Imperfect Fit" @default.
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