Met/Val129 polymorphism of the full-length human prion protein dictates distinct pathways of amyloid formation-Reference-Cited by-同舟云学术

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Met/Val129 polymorphism of the full-length human prion protein dictates distinct pathways of amyloid formation

Published:2022-10 Issue:10 Volume:298 Page:102430
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Pauly Thomas^ORCID,Bolakhrif Najoua,Kaiser Jesko,Nagel-Steger Luitgard,Gremer Lothar^ORCID,Gohlke Holger,Willbold Dieter

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference47 articles.

1. Scrapie agent contains a hydrophobic protein;Prusiner;Proc. Natl. Acad. Sci.,1981

2. Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins;Pan;Proc. Natl. Acad. Sci.,1993

3. Thermal stability and conformational transitions of scrapie amyloid (prion) protein correlate with infectivity;Safar;Protein Sci.,1993

4. Novel proteinaceous infectious particles cause scrapie;Prusiner;Science,1982

5. Amyloid-type protein aggregation and prion-like properties of amyloids;Willbold;Chem. Rev.,2021

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