Ontology highlight
ABSTRACT:
SUBMITTER: Hackl S
PROVIDER: S-EPMC6899880 | biostudies-literature | 2019 Oct
REPOSITORIES: biostudies-literature
Hackl Stefanie S Becker Christian F W CFW
Journal of peptide science : an official publication of the European Peptide Society 20191001 10
Deciphering the pathophysiologic events in prion diseases is challenging, and the role of posttranslational modifications (PTMs) such as glypidation and glycosylation remains elusive due to the lack of homogeneous protein preparations. So far, experimental studies have been limited in directly analyzing the earliest events of the conformational change of cellular prion protein (PrP<sup>C</sup> ) into scrapie prion protein (PrP<sup>Sc</sup> ) that further propagates PrP<sup>C</sup> misfolding and ...[more]