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Targeted Functional Proteomics to Study Protein Post-translational Modifications and Protein-protein Interaction

Zhang, Zhe (2007) Targeted Functional Proteomics to Study Protein Post-translational Modifications and Protein-protein Interaction. Doctoral Dissertation, University of Pittsburgh. (Unpublished)

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The rapid development of proteomic techniques in the post-genomics era has allowedmuch attention to be paid to the understanding of molecular mechanisms of functional regulatoryproteins. This amazingly fast transformation from "know-how" to "know-why" has allowed thedetermination of if functional regulation is based on up- or down-regulation, or based on anyparticular chemical modification on the amino acid residues of protein targets.Here, different biologically important regulatory proteomes or protein targets wereinvestigated using comprehensive combinations of proteomics techniques. A large emphasis wasplaced on expression techniques suitable for protein and protein binding partner affinitypurification for targeted analysis of phospho-proteins. The main protein of interest in theseparticular studies was an important transcriptional factor in cardiac development, serum responsefactor-1. Several proteomics methods were examined and, along with the difficultiesencountered, the results are presented. Small molecule-protein interaction was examined with thecell cycle regulatory protein Cdc25B incubated with an inhibitor. Post-translationalmodification-related functional proteomics were also studied, first in a rodent early hemorrhagemodel wherein S-nitrosylation of plasma proteins were determined, then the phosphorylation ofserum response factor-1. Finally, top-down functional proteome mapping was represented by adetailed and very successful analysis of the proteins found enriched in brain tumor cellpseudopodia.This dissertation illustrates the vast range of potential of proteomics technologies instudying function-related biological systems. Meanwhile, some pioneering work using targetedfunctional proteomics strategies was achieved, and the results will help in part to advance thefield of "targeted functional proteomics", the combination of cell and molecular biologicaltechniques with chemical, affinity and mass spectrometric approaches to study regulation ofbiological systems.


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Item Type: University of Pittsburgh ETD
Status: Unpublished
CreatorsEmailPitt UsernameORCID
Zhang, Zhezhz16@pitt.eduZHZ16
ETD Committee:
TitleMemberEmail AddressPitt UsernameORCID
Committee ChairDay, Billy Wbday@pitt.eduBDAY
Committee MemberSepulveda, Jorge
Committee MemberZemaitis, Michael Amaz@pitt.eduMAZ
Committee MemberGibbs, Robert Bgibbsr@pitt.eduGIBBSR
Committee MemberJiang, Yuyuj5@pitt.eduYUJ5
Date: 22 June 2007
Date Type: Completion
Defense Date: 5 June 2007
Approval Date: 22 June 2007
Submission Date: 16 June 2007
Access Restriction: No restriction; Release the ETD for access worldwide immediately.
Institution: University of Pittsburgh
Schools and Programs: School of Pharmacy > Pharmaceutical Sciences
Degree: PhD - Doctor of Philosophy
Thesis Type: Doctoral Dissertation
Refereed: Yes
Uncontrolled Keywords: Phosphorylation; Protein-ligand Interaction; Proteomics; Pseudopod; S-Nitrosylation
Other ID:, etd-06162007-121003
Date Deposited: 10 Nov 2011 19:47
Last Modified: 15 Nov 2016 13:44


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