Ontology highlight
ABSTRACT:
SUBMITTER: Ohhashi Y
PROVIDER: S-EPMC3277852 | biostudies-literature | 2010 Mar
REPOSITORIES: biostudies-literature
Ohhashi Yumiko Y Ito Kazuki K Toyama Brandon H BH Weissman Jonathan S JS Tanaka Motomasa M
Nature chemical biology 20100117 3
Aggregation-prone proteins often misfold into multiple distinct amyloid conformations that dictate different physiological impacts. Although amyloid formation is triggered by a transient nucleus, the mechanism by which an initial nucleus is formed and allows the protein to form a specific amyloid conformation has been unclear. Here we show that, before fiber formation, the prion domain (Sup35NM, consisting of residues 1-254) of yeast prion Sup35, the [PSI(+)] protein determinant, forms oligomers ...[more]