Specific binding of normal prion protein to the scrapie form via a localized domain initiates its conversion to the protease-resistant state.

@article{Horiuchi1999SpecificBO,
  title={Specific binding of normal prion protein to the scrapie form via a localized domain initiates its conversion to the protease-resistant state.},
  author={Miyuki Horiuchi and Byron Caughey},
  journal={The EMBO journal},
  year={1999},
  volume={18 12},
  pages={3193-203}
}
In the transmissible spongiform encephalopathies, normal prion protein (PrP-sen) is converted to a protease-resistant isoform, PrP-res, by an apparent self-propagating activity of the latter. Here we describe new, more physiological cell-free systems for analyzing the initial binding and subsequent conversion reactions between PrP-sen and PrP-res. These systems allowed the use of antibodies to map the sites of interaction between PrP-sen and PrP-res. Binding of antibodies (alpha219-232) to… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 67 extracted citations

References

Publications referenced by this paper.
Showing 1-10 of 53 references

Similar Papers

Loading similar papers…