Ontology highlight
ABSTRACT:
SUBMITTER: Ritter C
PROVIDER: S-EPMC1567094 | biostudies-literature | 2005 Jun
REPOSITORIES: biostudies-literature
Ritter Christiane C Maddelein Marie-Lise ML Siemer Ansgar B AB Lührs Thorsten T Ernst Matthias M Meier Beat H BH Saupe Sven J SJ Riek Roland R
Nature 20050601 7043
Prions are believed to be infectious, self-propagating polymers of otherwise soluble, host-encoded proteins. This concept is now strongly supported by the recent findings that amyloid fibrils of recombinant prion proteins from yeast, Podospora anserina and mammals can induce prion phenotypes in the corresponding hosts. However, the structural basis of prion infectivity remains largely elusive because acquisition of atomic resolution structural properties of amyloid fibrils represents a largely u ...[more]