Purification of G4 Resolvase1 : a protein entangled in many cellular functions

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dc.contributor.advisor Smaldino, Philip J.
dc.contributor.author Beerbower, Peter Edward
dc.date.accessioned 2019-04-08T13:33:29Z
dc.date.available 2019-04-08T13:33:29Z
dc.date.issued 2018-05
dc.identifier.other A-390
dc.identifier.uri http://cardinalscholar.bsu.edu/handle/123456789/201559
dc.description.abstract G-quadruplexes are supersecondary structures that form in guanine-rich regions of DNA and RNA. These structures are extremely thermally stable, likely to form in ~750,000 locations in the human genome and are enriched in the promoter regions of proto-oncogenes and developmental genes, non-coding regions, and within telomeres. Due to the prevalence of these structures in key genomic locations, these structures are cable of regulating a large fraction of cellular processes. Within humans, the enzyme G4 Resolvase 1 (G4R1) is responsible for the majority of Gquadruplex resolving activity. This places G4R1 at the forefront of regulating all functions involved with G-quadruplexes. Despite regulating G-quadruplexes, a nearly ubiquitous structure throughout the human genome, G4R1 is relatively understudied. Within this thesis, I present a method for producing highly pure and selectively catalytically active samples of rG4R1 and discuss the potential involvement of G4R1 with the pathology of Amyotrophic Lateral Sclerosis. en_US
dc.description.sponsorship Honors College
dc.subject.lcsh Cytology.
dc.title Purification of G4 Resolvase1 : a protein entangled in many cellular functions en_US
dc.type Undergraduate senior honors thesis.
dc.description.degree Thesis (B.?) en_US

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  • Undergraduate Honors Theses [5614]
    Honors theses submitted to the Honors College by Ball State University undergraduate students in partial fulfillment of degree requirements.

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