Charge Neutralization of the Central Lysine Cluster in Prion Protein (PrP) Promotes PrPSc-like Folding of Recombinant PrP Amyloids-Reference-Cited by-同舟云学术

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Charge Neutralization of the Central Lysine Cluster in Prion Protein (PrP) Promotes PrPSc-like Folding of Recombinant PrP Amyloids

Published:2015-01 Issue:2 Volume:290 Page:1119-1128
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Groveman Bradley R.,Kraus Allison,Raymond Lynne D.,Dolan Michael A.,Anson Kelsie J.,Dorward David W.,Caughey Byron

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference57 articles.

1. Prions and the potential transmissibility of protein misfolding diseases;Kraus;Annu. Rev. Microbiol,2013

2. A protease-resistant protein is a structural component of the scrapie prion;McKinley;Cell,1983

3. Secondary structure analysis of the scrapie-associated protein PrP 27–30 in water by infrared spectroscopy;Caughey;Biochemistry,1991

4. Conformational transitions, dissociation, and unfolding of scrapie amyloid (prion) protein;Safar;J. Biol. Chem,1993

5. Conversion of α-helices into β-sheets features in the formation of the scrapie prion protein;Pan;Proc. Natl. Acad. Sci. U.S.A,1993

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