Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 291, Issue 30, Pages 15482-15490Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.R116.733428
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- Conselho Nacional de Desenvolvimento Cientifico e Tecnologico (CNPq)
- Conselho Nacional de Desenvolvimento Cientifico e Tecnologico (Instituto Nacional de Ciencia e Tecnologia (INCT) Program)
- Fundacao Carlos Chagas Filho de Amparo a Pesquisa do Estado do Rio de Janeiro (FAPERJ)
- Coordenacao de Aperfeicoamento de Pessoal de Nivel Superior (CAPES)
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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.
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