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dc.contributor.advisorGates, Kent S. (Kent Stephen), 1962-en_US
dc.contributor.authorLaButti, Jason N., 1972-en_US
dc.date.issued2009eng
dc.date.submitted2009 Springen_US
dc.descriptionVita.en_US
dc.descriptionTitle from PDF of title page (University of Missouri--Columbia, viewed on Feb 15, 2010).en_US
dc.descriptionThe entire thesis text is included in the research.pdf file; the official abstract appears in the short.pdf file; a non-technical public abstract appears in the public.pdf file.en_US
dc.descriptionDissertation advisor: Dr. Kent S. Gates.en_US
dc.descriptionDissertations, Academic -- University of Missouri--Columbia -- Chemistry.en_US
dc.descriptionPh. D. University of Missouri--Columbia 2009.en_US
dc.descriptionIncludes bibliographical references.en_US
dc.description.abstractTransmission of complex intracellular signals, such as those for glucose uptake or proliferation, is often accomplished through the reversible phosphorylation of specific protein tyrosine residues. This reversible phosphorylation serves as a biochemical "rheostat" that alters a protein's functional properties and leads to propagation of the signal. The phosphorylation status of these tyrosine residues, thus transmission of the cellular signal itself, is tightly controlled by the opposing actions of protein tyrosine kinases that catalyze the addition of phosphoryl groups and protein tyrosine phosphatases (PTPs) are cysteine based enzymes that catalyze their removal. Abstraction of these phosphoryl groups, in many cases, serves as an "off switch" to terminate the cellular responses to the extracellular stimulus. PTPs, therefore, play a central role in the regulation of diverse cellular processes including glucose metabolism, cell cycle control and immune responses. Accordingly, small molecules capable of inactivating PTPs through reversible oxidation of their active site cysteine thiolate may find use as therapeutic agents and/or tools for the study of diverse signal transduction pathways. In the body of work presented here we report the chemical properties of a novel PTP redox regulator and develop new methodologies for studying PTP redox regulation.en_US
dc.format.extentxiii, 148 pagesen_US
dc.identifier.oclc518020060en_US
dc.identifier.otherLabuttiJ-050709-D1305en_US
dc.identifier.urihttp://hdl.handle.net/10355/6158
dc.publisherUniversity of Missouri--Columbiaen_US
dc.relation.ispartof2009 Freely available dissertations (MU)en_US
dc.relation.ispartofcommunityUniversity of Missouri-Columbia. Graduate School. Theses and Dissertations. Dissertations. 2009 Dissertations
dc.subject.lcshPhosphorylationen_US
dc.subject.lcshOxidation-reduction reactionen_US
dc.subject.lcshCellular signal transductionen_US
dc.subject.lcshProtein-tyrosine phosphataseen_US
dc.titleInvestigations into the chemistry of protein tyrosine phosphatase redox regulationen_US
dc.typeThesisen_US
thesis.degree.disciplineChemistryeng
thesis.degree.grantorUniversity of Missouri--Columbiaeng
thesis.degree.levelDoctoralen_US
thesis.degree.namePh. D.en_US


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