Published in J Mol Biol on November 26, 2004
Formation of native prions from minimal components in vitro. Proc Natl Acad Sci U S A (2007) 5.94
Selective incorporation of polyanionic molecules into hamster prions. J Biol Chem (2007) 1.71
Prion protein complexed to N2a cellular RNAs through its N-terminal domain forms aggregates and is toxic to murine neuroblastoma cells. J Biol Chem (2008) 1.11
The amino-terminal PrP domain is crucial to modulate prion misfolding and aggregation. Biophys J (2005) 1.02
Defined DNA sequences promote the assembly of a bacterial protein into distinct amyloid nanostructures. Proc Natl Acad Sci U S A (2007) 1.01
Natively folded HypF-N and its early amyloid aggregates interact with phospholipid monolayers and destabilize supported phospholipid bilayers. Biophys J (2006) 0.95
Anti-bovine prion protein RNA aptamer containing tandem GGA repeat interacts both with recombinant bovine prion protein and its beta isoform with high affinity. Prion (2008) 0.94
Protein folding and misfolding on surfaces. Int J Mol Sci (2008) 0.88
Binding of sulphonated indigo derivatives to RepA-WH1 inhibits DNA-induced protein amyloidogenesis. Nucleic Acids Res (2008) 0.88
Bovine spongiform encephalopathy infection alters endogenous retrovirus expression in distinct brain regions of cynomolgus macaques (Macaca fascicularis). Mol Neurodegener (2011) 0.86
The peculiar interaction between mammalian prion protein and RNA. Prion (2008) 0.86
Glycosaminoglycan sulphation affects the seeded misfolding of a mutant prion protein. PLoS One (2010) 0.82
Amyloid-associated nucleic acid hybridisation. PLoS One (2011) 0.81
Binding of recombinant but not endogenous prion protein to DNA causes DNA internalization and expression in mammalian cells. J Biol Chem (2008) 0.80
Cross-talk between prion protein and quadruplex-forming nucleic acids: a dynamic complex formation. Nucleic Acids Res (2012) 0.78
Nucleic acid induced unfolding of recombinant prion protein globular fragment is pH dependent. Protein Sci (2014) 0.77
DNA-induced partial unfolding of prion protein leads to its polymerisation to amyloid. J Mol Biol (2002) 1.11
Unusual property of prion protein unfolding in neutral salt solution. Biochemistry (2002) 0.79
Prions at the crossroads: the need to identify the active TSE agent. Bioessays (2004) 0.75