Ph.D., Purdue University, 2001; Postdoctoral, Institute for Systems Biology, 2002-2004.

The Tao research group focuses on the development and applications of biological mass spectrometry for functional proteomics. Examining changes in proteins of interest and their modifications within cells under different physiological conditions will offer insights into understanding cellular and molecular mechanisms that cannot currently be obtained through traditional biological studies that usually focus on the detailed analysis of individual biomolecules. Functional proteomics thus holds significant promise for the discovery of diagnostic or prognostic protein markers, for the detection of new therapeutic targets, and as a powerful tool to further our understanding of basic biological processes and mechanisms. The realization of these expectations relies on the development of robust and highly sensitive and specific methods to identify and quantify important proteins and their specific modifications.

Current projects in the Tao Group are: 1. Molecular signaling in cancer cells: phosphoproteomics 2. Identification of biomarkers for early detection of diseases 3. Tracing virus infection pathways

Walls CD, Iliuk A, Bai Y, Wang M, Tao WA, Zhang ZY. (2013). Phosphatase of Regenerating Liver 3 (PRL3) provokes a tyrosine phosphoproteome to drive pro-metastatic signal transduction. "Mol Cell Proteomics.", doi: 10.1074/mcp.M113.028886

Huang R, Oh H, Arrendale A, Martin VA, Galan J, Workman EJ, Stout JR, Walczak CE, Tao WA, Borch RF, Geahlen RL. (2013). Intracellular targets for a phosphotyrosine peptidomimetic include the mitotic kinesin, MCAK. "Biochem Pharmacol.", doi: 10.1016/j.bcp.2013.06.024

Xue L, Geahlen RL, Tao WA. (2013). Identification of Direct Tyrosine Kinase Substrates Based on Protein Kinase Assay-Linked Phosphoproteomics. Mol Cell Proteomics., doi: 10.1074/mcp.O113.027722

Radu M, Rawat SJ, Beeser A, Iliuk A, Tao WA, Chernoff J. (2013). ArhGAP15, a Rac-Specific GTPase Activating Protein, Plays a Dual Role in Inhibiting Small GTPase Signaling. J Biol Chem., doi: 10.1074/jbc.M113.459719

Wang P, Xue L, Batelli G, Lee S, Hou YJ, Van Oosten MJ, Zhang H, Tao WA, Zhu JK (2013). Quantitative phosphoproteomics identifies SnRK2 protein kinase substrates and reveals the effectors of abscisic acid action. Proc Natl Acad Sci USA., doi:10.1073/pnas.1308974110

Xue L, Wang P, Wang L, Renzi E, Radivojac P, Tang H, Arnold R, Zhu JK, Tao WA (2013). Quantitative measurement of phosphoproteome response to osmotic stress in Arabidopsis based on Library-Assisted eXtracted Ion Chromatogram (LAXIC). Mol Cell Proteomics., doi:10.1074/mcp.O113.027284

Iliuk AB, Tao WA (2013). Is phosphoproteomics ready for clinical research? Clin Chim Acta. , doi:10.1016/j.cca.2012.10.063

Hu L, Yang L, Lipchik AM, Geahlen RL, Parker LL, Tao WA (2013). A Quantitative Proteomics-Based Competition Binding Assay to Characterize pITAM–Protein Interactions. Anal Chem., doi:10.1021/ac400359t

Yu S, Huang H, Iliuk A, Wang WH, Jayasundera KB, Tao WA, Post CB, Geahlen RL (2012). Syk inhibits the activity of protein kinase a by phosphorylating tyrosine 330 of the catalytic subunit. J Biol Chem., doi:10.1074/jbc.M112.426130

Tao WA, Coon J (2013). 2012 ASMS Fall Workshop: Mass Spectrometry-Based Phosphorylation Analysis and Phosphoproteomics. Journal of The American Society for Mass Spectrometry.

Xue L, Tao WA (2013). Current technologies to identify protein kinase substrates in high throughput. Frontiers in Biology., doi:10.1007/s11515-013-1257-z

Puchulu-Campanella E, Chu H, Anstee DJ, Galan JA, Tao WA, Low PS (2012). Identification of the Components of a Glycolytic Enzyme Metabolon on the Human Red Blood Cell Membrane. J Biol Chem. , doi:10.1074/jbc.M112.428573

Pan L, Iliuk A, Yu S, Geahlen RL, Tao WA (2012). Multiplexed quantitation of protein expression and phosphorylation based on functionalized soluble nanopolymers. J Am Chem Soc. 134(44):18201-4, doi:10.1021/ja308453m

Chu H, Puchulu-Campanella E, Galan JA, Tao WA, Low PS, Hoffman JF (2012). Identification of cytoskeletal elements enclosing the ATP pools that fuel human red blood cell membrane cation pumps. Proc Natl Acad Sci U S A. 109(31):12794-9, doi:10.1073/pnas.1209014109

Iliuk A, Liu XS, Xue L, Liu X, Tao WA (2012). Chemical visualization of phosphoproteomes on membrane. Mol Cell Proteomics. 11(9):629-39, doi:10.1074/mcp.O112.018010

Xue L, Wang WH, Iliuk A, Hu L, Galan JA, Yu S, Hans M, Geahlen RL, Tao WA (2012). Sensitive kinase assay linked with phosphoproteomics for identifying direct kinase substrates. Proc Natl Acad Sci U S A. 109(15):5615-20, doi:10.1073/pnas.1119418109

Choo YS, Vogler G, Wang D, Kalvakuri S, Iliuk A, Tao WA, Bodmer R, Zhang Z (2012). Regulation of parkin and PINK1 by neddylation. Hum Mol Genet. 21(11):2514-23, doi:10.1093/hmg/dds070

Hu L, Tao WA (2012). Chemical enrichment of tyrosine phosphopeptides. Se Pu. 29(9):869-75.

Burnside K, Lembo A, Harrell MI, Gurney M, Xue L, BinhTran NT, Connelly JE, Jewell KA, Schmidt BZ, de los Reyes M, Tao WA, Doran KS, Rajagopal L (2011). Serine/threonine phosphatase Stp1 mediates post-transcriptional regulation of hemolysin, autolysis, and virulence of group B Streptococcus. J Biol Chem. 286(51):44197-210, doi:10.1074/jbc.M111.313486

Iliuk A, Jayasundera K, Schluttenhofer R, Tao WA (2011). Functionalized soluble nanopolymers for phosphoproteome analysis. Methods Mol Biol. 790(5): 277-85, doi:10.1007/978-1-61779-319-6_21