Protein misfolding results in devastating degenerative diseases and cancer. Among the culprits involved in these illnesses are prions and prion-like proteins, which can propagate by converting normal proteins to the wrong conformation. For spongiform encephalopathies, a real prion can be transmitted among individuals. In other disorders, the bona fide prion characteristics are still under investigation. Besides inducing misfolding of native proteins, prions bind nucleic acids and other polyanions. Here, we discuss how nucleic acid binding might influence protein misfolding for both disease-related and benign, functional prions and why the line between bad and good amyloids might be more subtle than previously thought.
The “Jekyll and Hyde” Actions of Nucleic Acids on the Prion-like Aggregation of Proteins*
Published 2016 in Journal of Biological Chemistry
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- Publication year
2016
- Venue
Journal of Biological Chemistry
- Publication date
2016-06-10
- Fields of study
Biology, Medicine, Chemistry
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- Source metadata
Semantic Scholar, PubMed
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