Ontology highlight
ABSTRACT:
SUBMITTER: Cheng CJ
PROVIDER: S-EPMC5500178 | biostudies-literature | 2017 Jul
REPOSITORIES: biostudies-literature
Journal of neurochemistry 20170522 1
Prion diseases are associated with the misfolding of the prion protein (PrP) from its normal cellular form (PrP<sup>C</sup> ) to its infectious scrapie form (PrP<sup>S</sup><sup>c</sup> ). Post-translational modifications in PrP in vivo can play an important role in modulating the process of misfolding. To gain more insight into the effects of post-translational modifications in PrP structure and dynamics and to test the hypothesis that such modifications can interact with the protein, we have p ...[more]