Investigations into the chemistry of protein tyrosine phosphatase redox regulation

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Investigations into the chemistry of protein tyrosine phosphatase redox regulation

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dc.contributor.advisor Gates, Kent S. (Kent Stephen), 1962- en_US
dc.contributor.author LaButti, Jason N., 1972- en_US
dc.date.accessioned 2010-02-25T17:47:17Z
dc.date.available 2010-02-25T17:47:17Z
dc.date.issued 2009 en_US
dc.date.submitted 2009 Spring en_US
dc.identifier.other LabuttiJ-050709-D1305 en_US
dc.identifier.uri http://hdl.handle.net/10355/6158
dc.description Vita. en_US
dc.description Title from PDF of title page (University of Missouri--Columbia, viewed on Feb 15, 2010). en_US
dc.description The 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.description Dissertation advisor: Dr. Kent S. Gates. en_US
dc.description Dissertations, Academic -- University of Missouri--Columbia -- Chemistry. en_US
dc.description Ph. D. University of Missouri--Columbia 2009. en_US
dc.description Includes bibliographical references. en_US
dc.description.abstract Transmission 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.extent xiii, 148 pages en_US
dc.language.iso en_US en_US
dc.publisher University of Missouri--Columbia en_US
dc.relation.ispartof 2009 Freely available dissertations (MU) en_US
dc.subject.lcsh Phosphorylation en_US
dc.subject.lcsh Oxidation-reduction reaction en_US
dc.subject.lcsh Cellular signal transduction en_US
dc.subject.lcsh Protein-tyrosine phosphatase en_US
dc.title Investigations into the chemistry of protein tyrosine phosphatase redox regulation en_US
dc.type Thesis en_US
thesis.degree.discipline Chemistry en_US
thesis.degree.grantor University of Missouri--Columbia en_US
thesis.degree.name Ph. D. en_US
thesis.degree.level Doctoral en_US
dc.identifier.oclc 518020060 en_US
dc.relation.ispartofcommunity University of Missouri-Columbia. Graduate School. Theses and Dissertations. Dissertations. 2009 Dissertations


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