| Literature DB >> 27288413 |
Jerson L Silva1, Yraima Cordeiro2.
Abstract
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.Entities:
Keywords: cancer; functional amyloid; functional amyloids; neurodegenerative disease; nucleic acid; p53; prion; prions; protein aggregation; protein misfolding
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Year: 2016 PMID: 27288413 PMCID: PMC4957035 DOI: 10.1074/jbc.R116.733428
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157