Matches in SemOpenAlex for { <https://semopenalex.org/work/W2577234665> ?p ?o ?g. }
- W2577234665 endingPage "a024257" @default.
- W2577234665 startingPage "a024257" @default.
- W2577234665 abstract "Transmissible spongiform encephalopathies are infectious neurodegenerative diseases caused by the conversion of prion protein (PrP) into a self-replicating conformation that spreads via templated conversion of natively folded PrP molecules within or between cells. Recent studies provide compelling evidence that prion-like behavior is a general property of most protein aggregates associated with neurodegenerative diseases. Many of these disorders are associated with spontaneous protein aggregation, but genetic mutations can increase the aggregation propensity of specific proteins, including expansion of polyglutamine (polyQ) tracts, which is causative of nine inherited neurodegenerative diseases. Aggregates formed by polyQ-expanded huntingtin (Htt) in Huntington's disease can transfer between cells and seed the aggregation of cytoplasmic wild-type Htt in a prion-like manner. Additionally, prion-like properties of glutamine-rich proteins underlie nonpathological processes in yeast and higher eukaryotes. Here, we review current evidence supporting prion-like characteristics of polyQ and glutamine-rich proteins." @default.
- W2577234665 created "2017-01-26" @default.
- W2577234665 creator A5050586961 @default.
- W2577234665 creator A5058767055 @default.
- W2577234665 date "2017-01-17" @default.
- W2577234665 modified "2023-10-11" @default.
- W2577234665 title "Prion-Like Characteristics of Polyglutamine-Containing Proteins" @default.
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