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dc.contributor.authorCornish, Steven
dc.date.accessioned2020-04-30T10:00:17Z
dc.date.available2020-04-30T10:00:17Z
dc.date.issued2015-04-01
dc.identifier.urihttps://scholars.carroll.edu/handle/20.500.12647/2761
dc.description.abstractPrion diseases are very rare, neurodegenerative diseases caused by misfolding of the Prion protein. The pathologies created by the misfolded protein are remarkably similar to those of Alzheimer’s disease. This paper provides a comprehensive study of the genomic and proteomic similarities between Prion proteins and several proteins implicated in Alzheimer’s disease (AD). While genomic similarity has been proven, studies are unclear as to whether any genomic mutations in PRNP affect the progression of AD. Studies have definitively proven that Prion protein interacts on a molecular level with several proteins implicated in AD. These interactions require further study to definitively prove whether they speed or slow AD progression, but current evidence indicates that Prion protein interaction will lead to faster progression of AD in vitro.
dc.subjectPrion, Alzheimer's
dc.titleInvestigating the Role of PrP and Amyloid Beta Proteins in AD and Other Protein-Misfolding Diseases
dc.typethesis
carrollscholars.object.degreeBachelor's
carrollscholars.object.departmentLife & Environmental Sciences
carrollscholars.object.disciplinesBiochemistry; Biochemistry, Biophysics, and Structural Biology; Diseases; Life Sciences; Molecular Biology; Nervous System Diseases
carrollscholars.legacy.itemurlhttps://scholars.carroll.edu/lifesci_theses/18
carrollscholars.legacy.contextkey10918183
carrollscholars.object.seasonSpring
dc.date.embargo12/31/1899 0:00


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