The environmental dependency of protein folding best explains prion and amyloid diseases
نویسندگان
چکیده
منابع مشابه
Porcine prion protein amyloid
Mammalian prions are composed of misfolded aggregated prion protein (PrP) with amyloid-like features. Prions are zoonotic disease agents that infect a wide variety of mammalian species including humans. Mammals and by-products thereof which are frequently encountered in daily life are most important for human health. It is established that bovine prions (BSE) can infect humans while there is no...
متن کاملTwo amyloid States of the prion protein display significantly different folding patterns.
It has been well established that a single amino acid sequence can give rise to several conformationally distinct amyloid states. The extent to which amyloid structures formed within the same sequence are different, however, remains unclear. To address this question, we studied two amyloid states (referred to as R- and S-fibrils) produced in vitro from highly purified full-length recombinant pr...
متن کاملReview: prion protein and amyloid beta interactions
In 2009 it was discovered that prion protein (PrP) binds amyloid beta oligomers (Aβo), potentially acting as a receptor on the surface of neurons. PrP was additionally suggested to mediate at least some of the toxic effects of Aβo in Alzheimer’s disease (AD), a proposition which has proven enormously controversial. In the past three years, several studies have produced apparently strong evidenc...
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Mechanisms of prion protein assembly into amyloid.
The conversion of the alpha-helical, cellular isoform of the prion protein (PrP(C)) to the insoluble, beta-sheet-rich, infectious, disease-causing isoform (PrP(Sc)) is the key event in prion diseases. In an earlier study, several forms of PrP were converted into a fibrillar state by using an in vitro conversion system consisting of low concentrations of SDS and 250 mM NaCl. Here, we characteriz...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1998
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.95.3.930