[-] Show simple item record

dc.contributor.advisorGates, Kent S. (Kent Stephen), 1962-eng
dc.contributor.authorLaButti, Jason N., 1972-eng
dc.date.issued2009eng
dc.date.submitted2009 Springeng
dc.descriptionVita.eng
dc.descriptionTitle from PDF of title page (University of Missouri--Columbia, viewed on Feb 15, 2010).eng
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.eng
dc.descriptionDissertation advisor: Dr. Kent S. Gates.eng
dc.descriptionDissertations, Academic -- University of Missouri--Columbia -- Chemistry.eng
dc.descriptionPh. D. University of Missouri--Columbia 2009.eng
dc.descriptionIncludes bibliographical references.eng
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.eng
dc.format.extentxiii, 148 pageseng
dc.identifier.oclc518020060eng
dc.identifier.otherLabuttiJ-050709-D1305eng
dc.identifier.urihttp://hdl.handle.net/10355/6158eng
dc.publisherUniversity of Missouri--Columbiaeng
dc.relation.ispartof2009 Freely available dissertations (MU)eng
dc.relation.ispartofcommunityUniversity of Missouri-Columbia. Graduate School. Theses and Dissertations. Dissertations. 2009 Dissertationseng
dc.subject.lcshPhosphorylationeng
dc.subject.lcshOxidation-reduction reactioneng
dc.subject.lcshCellular signal transductioneng
dc.subject.lcshProtein-tyrosine phosphataseeng
dc.titleInvestigations into the chemistry of protein tyrosine phosphatase redox regulationeng
dc.typeThesiseng
thesis.degree.disciplineChemistry (MU)eng
thesis.degree.grantorUniversity of Missouri--Columbiaeng
thesis.degree.levelDoctoraleng
thesis.degree.namePh. D.eng


Files in this item

[PDF]
[PDF]
[PDF]

This item appears in the following Collection(s)

[-] Show simple item record