Phosphorylation of prion protein at serine 43 induces prion protein conformational change.

@article{Giannopoulos2009PhosphorylationOP,
  title={Phosphorylation of prion protein at serine 43 induces prion protein conformational change.},
  author={Paresa N. Giannopoulos and Catherine Robertson and Julie Jodoin and Hemant K. Paudel and Stephanie A Booth and Andr{\'e}a C LeBlanc},
  journal={The Journal of neuroscience : the official journal of the Society for Neuroscience},
  year={2009},
  volume={29 27},
  pages={8743-51}
}
The cause of the conformational change of normal cellular prion protein (PrP) into its disease-associated form is unknown. Posttranslational modifications, such as glycosylation, acetylation, S-nitrosylation, and phosphorylation, are known to induce protein conformational changes. Here, we investigated whether phosphorylation could induce the conformational change of PrP because PrP contains several kinase motifs and has been found recently in the cytosol, in which kinases generally reside… CONTINUE READING
9 Citations
54 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-9 of 9 extracted citations

References

Publications referenced by this paper.
Showing 1-10 of 54 references

Similar Papers

Loading similar papers…