Ontology highlight
ABSTRACT:
SUBMITTER: Ghaemmaghami S
PROVIDER: S-EPMC2856248 | biostudies-literature | 2010 Apr
REPOSITORIES: biostudies-literature
Ghaemmaghami Sina S Ullman Julie J Ahn Misol M St Martin Susan S Prusiner Stanley B SB
The Journal of biological chemistry 20091202 14
Prion-infected cells accumulate a heterogeneous population of aberrantly folded PrP conformers, including the disease-causing isoform (PrP(Sc)). We found that specific chemicals can modulate the levels of various PrP conformers in cultured cells. Positively charged polyamidoamines (dendrimers) eliminated protease-resistant (r) PrP(Sc) from prion-infected cells and induced the formation of insoluble, protease-sensitive PrP aggregates (designated PrP(A)). Larger, positively charged polyamidoamines ...[more]