Ontology highlight
ABSTRACT:
SUBMITTER: Riemschoss K
PROVIDER: S-EPMC6607448 | biostudies-literature | 2019 Aug
REPOSITORIES: biostudies-literature
Riemschoss Katrin K Arndt Verena V Bolognesi Benedetta B von Eisenhart-Rothe Philipp P Liu Shu S Buravlova Oleksandra O Duernberger Yvonne Y Paulsen Lydia L Hornberger Annika A Hossinger André A Lorenzo-Gotor Nieves N Hogl Sebastian S Müller Stephan A SA Tartaglia Gian G Lichtenthaler Stefan F SF Vorberg Ina M IM
Life science alliance 20190702 4
Prions of lower eukaryotes are self-templating protein aggregates that replicate by converting homotypic proteins into stable, tightly packed beta-sheet-rich protein assemblies. Propagation is mediated by prion domains, low-complexity regions enriched in polar and devoid of charged amino acid residues. In mammals, compositionally similar domains modulate the assembly of dynamic stress granules (SGs) that associate via multivalent weak interactions. Dysregulation of SGs composed of proteins with ...[more]