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Investigating the Role of the Prion Protein Polybasic Domain in PrPSc Formation and Neuroprotection
Date of Award
Doctor of Philosophy (PhD)
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.
Chair and Committee
Heather L. True-Krob, Kendall Blumer, David Holtzman, Jin-Moo Lee, Mark Sands
Turnbaugh, Jessie Aleksandra, "Investigating the Role of the Prion Protein Polybasic Domain in PrPSc Formation and Neuroprotection" (2011). Arts & Sciences Electronic Theses and Dissertations. 105.