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• W2565431933 endingPage "a030718" @default.
• W2565431933 startingPage "a030718" @default.
• W2565431933 abstract "Prions are self-propagating protein conformations that are traditionally regarded as agents of neurodegenerative disease in animals. However, it has become evident that prion-like aggregation of endogenous proteins can also occur under normal physiological conditions (e.g., during memory storage or activation of the immune response). In this review, we focus on the functional prion-related protein TIA-1, an RNA-binding protein that is involved in multiple aspects of RNA metabolism but is best understood in terms of its role in stress granule assembly during the cellular stress response. We propose that stress granule formation provides a useful conceptual framework with which to address the positive role of TIA-1 prion-like aggregation. Elucidating the function of TIA-1 prion-like aggregation will advance our understanding of how prion-based molecular switches are used in normal physiological settings." @default.
• W2565431933 created "2017-01-06" @default.
• W2565431933 creator A5034071817 @default.
• W2565431933 creator A5091766299 @default.
• W2565431933 date "2016-12-21" @default.
• W2565431933 modified "2023-10-14" @default.
• W2565431933 title "TIA-1 Is a Functional Prion-Like Protein" @default.
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• W2565431933 doi "https://doi.org/10.1101/cshperspect.a030718" @default.
• W2565431933 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5411700" @default.
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• W2565431933 hasPublicationYear "2016" @default.
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