Ontology highlight
ABSTRACT:
SUBMITTER: Dinkel KD
PROVIDER: S-EPMC5771472 | biostudies-literature | 2017 Aug
REPOSITORIES: biostudies-literature
Dinkel Kelcey D KD Schneider David A DA Muñoz-Gutiérrez Juan F JF McElliott Valerie R VR Stanton James B JB
Virus research 20170725
Prion diseases are fatal neurodegenerative disorders by which the native cellular prion protein (PrP<sup>C</sup>) is misfolded into an accumulating, disease-associated isoform (PrP<sup>D</sup>). To improve the understanding of prion pathogenesis and develop effective treatments, it is essential to elucidate factors contributing to cellular permissiveness. We previously isolated five clones from an immortalized subline of ovine microglia, two of which had demonstrated differential permissiveness ...[more]