N-terminal truncation of prion protein affects both formation and conformation of abnormal protease-resistant prion protein generated in vitro.

@article{Lawson2001NterminalTO,
  title={N-terminal truncation of prion protein affects both formation and conformation of abnormal protease-resistant prion protein generated in vitro.},
  author={Victoria Lawson and Suzette A. Priola and Kathy Wehrly and Bruce Chesebro},
  journal={The Journal of biological chemistry},
  year={2001},
  volume={276 38},
  pages={35265-71}
}
Transmissible spongiform encephalopathy diseases are characterized by conversion of the normal protease-sensitive host prion protein, PrP-sen, to an abnormal protease-resistant form, PrP-res. In the current study, deletions were introduced into the flexible tail of PrP-sen (23) to determine if this region was required for formation of PrP-res in a cell-free assay. PrP-res formation was significantly reduced by deletion of residues 34-94 relative to full-length hamster PrP. Deletion of another… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 22 extracted citations

Prion processing: a double-edged sword?

Biochemical Society transactions • 2012

Similar Papers

Loading similar papers…