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dc.contributor.authorKutlik, Robert Alan
dc.date.accessioned2014-03-04T18:28:31Z
dc.date.available2014-03-04T18:28:31Z
dc.date.issued2010-05
dc.identifier.otherkutlik_robert_a_201005_ms
dc.identifier.urihttp://purl.galileo.usg.edu/uga_etd/kutlik_robert_a_201005_ms
dc.identifier.urihttp://hdl.handle.net/10724/26381
dc.description.abstractRas converting enzyme (Rce1p) has been the focus of research due to the prevalence of Ras mutants in cancerous tissues. In vivo studies have shown inactivation of Rce1p causes the mislocalization of Ras; therefore inhibition of Rce1p might have applications in cancer treatment. Several inhibitors of Rce1p have been identified, including 4-((8-hydroxyquinolin-7-yl)(phenyl)methylamino)benzoic acid. The 8-hydroxyquinoline motif found in this molecule has been used extensively for its metal binding properties. The mechanism of Rce1p has been the subject of some debate, although, it is likely a zinc metalloprotease. Described here are several analogous molecules that display stronger Rce1p inhibition and looser zinc binding.
dc.languageeng
dc.publisheruga
dc.rightspublic
dc.subjectRas converting enzyme
dc.subjectRce1
dc.subject8-hydroxyquinoline
dc.subjectsmall molecule inhibition
dc.title8-hydroxyquinoline based small molecule inhibitors of the endoprotease Ras converting enzyme
dc.typeThesis
dc.description.degreeMS
dc.description.departmentChemistry
dc.description.majorChemistry
dc.description.advisorTimothy Dore
dc.description.committeeTimothy Dore
dc.description.committeeWalter Schmidt
dc.description.committeeRobert Phillips


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