The consequences of pathogenic mutations to the human prion protein.
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ABSTRACT:
SUBMITTER: van der Kamp MW
PROVIDER: S-EPMC2719504 | biostudies-literature | 2009 Aug
REPOSITORIES: biostudies-literature
Publications
The consequences of pathogenic mutations to the human prion protein.
van der Kamp Marc W MW Daggett Valerie V
Protein engineering, design & selection : PEDS 20090714 8
Prion diseases, in which the conformational transition of the native prion protein (PrP) to a misfolded form causes aggregation and subsequent neurodegeneration, have fascinated the scientific community as this transmissible disease appears to be purely protein-based. Disease can arise due to genetic factors only. At least 30 single point mutations have been indicated to cause disease in humans. Somehow, these mutations must influence the stability, processing and/or cellular interactions of PrP ...[more]
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