Journal article
Pathogenic mechanisms of prion protein, amyloid-β and α-synuclein misfolding: the prion concept and neurotoxicity of protein oligomers
CL Ugalde, DI Finkelstein, VA Lawson, AF Hill
Journal of Neurochemistry | WILEY | Published : 2016
DOI: 10.1111/jnc.13772
Abstract
Proteinopathies represent a group of diseases characterized by the unregulated misfolding and aggregation of proteins. Accumulation of misfolded protein in the central nervous system (CNS) is associated with neurodegenerative diseases, such as the transmissible spongiform encephalopathies (or prion diseases), Alzheimer's disease, and the synucleinopathies (the most common of which is Parkinson's disease). Of these, the pathogenic mechanisms of prion diseases are particularly striking where the transmissible, causative agent of disease is the prion, or proteinaceous infectious particle. Prions are composed almost exclusively of PrPSc; a misfolded isoform of the normal cellular protein, PrPC, ..
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Awarded by National Health and Medical Research Council