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Quantitative Characterization of protein post-translational modifications using mass spectrometry


EMSL Project ID
16725

Abstract

Post-translational protein modifications such as phosphorylation and oxidative modifications play essential roles in the regulation of a variety of biological processes. Increasing evidence suggests that changes in protein modifications over time correlate with particular phenotypes and disease states. However, quantitative characterization of protein modifications still presents a tremendous challenge for current analytical technologies due to the extremely low abundance of modified proteins among very complex proteome samples.

This project is directed towards developing global proteomic approaches for more sensitive and comprehensive characterization of modified proteins. Specifically, we will focus on the development of a quantitative proteomic approach for analyzing protein phosphorylation and oxidative protein modifications, including tyrosine nitration and methionine oxidation. Specific enrichment methodologies for these modified peptides will be one of the keys to the success for this project.

Project Details

Start Date
2006-02-02
End Date
2009-02-08
Status
Closed

Team

Principal Investigator

Weijun Qian
Institution
Pacific Northwest National Laboratory

Team Members

Shi-Jian Ding
Institution
University of Nebraska - Lincoln

Qibin Zhang
Institution
University of North Carolina Greensboro

Related Publications

Heibeck TH, SJ Ding, LK Opresko, R Zhao, AA Schepmoes, F Yang, AV Tolmachev, ME Monroe, DG Camp, II, RD Smith, HS Wiley, and W Qian. 2009. "An Extensive Survey of Tyrosine Phosphorylation Revealing New Sites in Human Mammary Epithelial Cells." Journal of Proteome Research 8(8):3852-3861.
Zhang X, ME Monroe, B Chen, MH Chin, TH Heibeck, AA Schepmoes, F Yang, BO Petritis, DG Camp, II, JG Pounds, JM Jacobs, DJ Smith, DJ Bigelow, RD Smith, and W Qian. 2010. "Endogenous 3, 4- Dihydroxyphenylalanine and Dopaquinone Modifications on Protein Tyrosine: links to mitochondrially derived oxidative stress via hydroxyl radical." Molecular & Cellular Proteomics. MCP 9(6):1199-1208.
Zhang, X.; Zhou, J.Y.; Chin, M.H.; Schepmoes, A.A.; Petyuk, V.A.; Weitz, K.K.; Petritis, B.O.; Monroe, M.E.; Camp, D.G.; Wood, S.A.; Melega, W.P.; Bigelow, D.J.; Smith, D.J.; Qian, W.J.- and Smith, R.D. Region-specific protein abundance changes in the brain of MPTP-induced Parkinsons disease mouse model. J Proteome Res, 2010, 9, 1496-1509