Investigating the Role of the Prion Protein Polybasic Domain in PrPSc Formation and Neuroprotection

Date of Award

Summer 8-15-2011

Author's School

Graduate School of Arts and Sciences

Author's Department

Biology & Biomedical Sciences (Molecular Cell Biology)

Degree Name

Doctor of Philosophy (PhD)

Degree Type



Prion diseases are characterized by the conformational conversion of the cellular prion protein (PrPC ) into the misfolded PrPSc isoform. However, both the normal, physiological function of PrPC and the mechanism of its conversion into PrPSc remain undefined. Several lines of evidence suggest that the expression of PrP can be neuroprotective, including its ability to abrogate the neurotoxic activity of PrP deletion mutants. In my thesis work, I characterized the role of the polybasic domain (residues 23-31) in the neuroprotective effect of WT PrP and examined the role of these residues in the formation of the infectious PrPSc protein.


English (en)

Chair and Committee

David Harris

Committee Members

Heather L. True-Krob, Kendall Blumer, David Holtzman, Jin-Moo Lee, Mark Sands


Permanent URL: https://doi.org/10.7936/K7639MPZ

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