Prion Protein of 106 Residues Creates an Artificial Transmission Barrier for Prion Replication in Transgenic Mice

This publication has 45 references indexed in Scilit:

• Structure of the recombinant full-length hamster prion protein PrP(29–231): The N terminus is highly flexible
  Proceedings of the National Academy of Sciences, 1997
• Evidence for protein X binding to a discontinuous epitope on the cellular prion protein during scrapie prion propagation
  Proceedings of the National Academy of Sciences, 1997
• Solution structure of a 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform
  Proceedings of the National Academy of Sciences, 1997
• Proposed three-dimensional structure for the cellular prion protein.
  Proceedings of the National Academy of Sciences, 1994
• Prion isolate specified allotypic interactions between the cellular and scrapie prion proteins in congenic and transgenic mice.
  Proceedings of the National Academy of Sciences, 1994
• Perturbation of the secondary structure of the scrapie prion protein under conditions that alter infectivity.
  Proceedings of the National Academy of Sciences, 1993
• Linkage of prion protein and scrapie incubation time genes
  Cell, 1986
• Scrapie and cellular PrP isoforms are encoded by the same chromosomal gene
  Cell, 1986
• Examination of the secondary structure of proteins by deconvolved FTIR spectra
  Biopolymers, 1986
• ENCEPHALOPATHY IN MICE PRODUCED BY INOCULATION WITH SCRAPIE BRAIN MATERIAL
  The Lancet, 1961