Department of Biochemistry

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W. Andy Tao

Biochemistry 

  • Professor of Biochemistry
765.494.9605
765.494.7897
HANS Room 434

Lab Members

Google Scholar Page

Area of Expertise: Proteomics and biological mass spectrometry

The mission of our research group is to bridge the gap between technology and biomedical/biochemical discovery. Mass spectrometry-based proteomics is the kind of research that is highly interdisciplinary, bringing together biology, chemistry, instrumentation, statistics, and bioinformatics. 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 novel chemistry and instrumentation.

Our group focuses on the development of novel strategies and reagents to efficiently target and discover proteins of important biological relevance as potential biomarkers. Such proteins of interest are typically low in abundance, dynamically expressed, and post-translationally modified. The subject, called targeted proteomics, therefore involves the integration of a number of technologies including the selective targeting of proteins with activities of interest, multi-step sample preparation, and mass spectrometry. Examining changes in these proteins 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.

Current projects in my group are: 1. Quantitative and functional proteomics in vitro and in living cells using soluble nanopolymers; 2. Phosphorylation imaging and detection; 3. Molecular signaling in cancer cells: phosphoproteomics. 4. Mapping protein-protein and protein-ligand interaction network.

Selected Publications

Wang, L., Yang, L., Pan, L., Kadasala, N. R., Xue, L., Schuster, R. J., . . . Tao, W. A. (2015). Time-Resolved Proteomic Visualization of Dendrimer Cellular Entry and Trafficking. Journal of the American Chemical Society, 137(40), 12772-5. doi:10.1021/jacs.5b07875

Lang, Z., Lei, M., Wang, X., Tang, K., Miki, D., Zhang, H., . . . Zhu, J. (2015). The methyl-CpG-binding protein MBD7 facilitates active DNA demethylation to limit DNA hyper-methylation and transcriptional gene silencing. Molecular Cell, 57(6), 971-83. doi:10.1016/j.molcel.2015.01.009

Amato, E., Bankemper, T., Kidney, R., Do, T., Onate, A., Thowfeik, F., . . . Ma, L. (2014). Investigation of fluorinated and bifunctionalized 3-phenylchroman-4-one (isoflavanone) aromatase inhibitors. Bioorg. Med. Chem, 22, 126-134. Retrieved from http://ac.els-cdn.com/S0968089613009851/1-s2.0-S0968089613009851-main.pdf?_tid=e55e8c3a-a654-11e4-bf74-00000aab0f6b&acdnat=1422384608_0c599b9ca45b80dd1c3484f2ea6bad20

Iliuk, A. B., & Tao, W. A. (2015). Universal non-antibody detection of protein phosphorylation using pIMAGO. Current protocols in chemical biology, 7(1), 17-25. doi:10.1002/9780470559277.ch140208

Wang, P., Du , Y., Hou, Y. J., Zhao, Y., Hsu, C., Yuan, F., . . . Zhu, J. (2015). Nitric oxide negatively regulates abscisic acid signaling in guard cells by S-nitrosylation of OST1. Proceedings of the National Academy of Sciences of the United States of America, 112(2), 613-8. doi:10.1073/pnas.1423481112

Xue, L., Wang, P., Cao, P., Zhu, J., & Tao, W. A. (2014). Identification of extracellular signal-regulated kinase 1 (ERK1) direct substrates using stable isotope labeled kinase assay-linked phosphoproteomics. Molecular & cellular proteomics : MCP, 13(11), 3199-210. doi:10.1074/mcp.O114.038588

Xue, L., Wang, W., Iliuk, A., Hu, L., Galan, J., Yu, S., . . . Geahlen, R. (2012). Sensitive kinase assay linked with phosphoproteomics for identifying direct kinase substrates. PNAS, 109, 5615-5620. Retrieved from http://www.pnas.org/content/109/15/5615.long

Xue, L., & Tao, W. (2013). Current technologies to identify protein kinase substrates in high throughput. Front. Biol, 8, 216-227. Retrieved from http://link.springer.com/article/10.1007/s11515-013-1257-z

Xue, L., Geahlen, R., & Tao, W. (2013). Identification of direct tyrosine kinase substrates based on protein kinase assay-linked phosphoproteomics. Mol. Cell Proteomics, 12, 2969-2980.

Awards & Honors

(2012) University Faculty Scholar 2011-2014. Purdue University.

(2011) Faculty Scholar. Purdue University.

(2007) Career Award (2007-2012). National Science Foundation.

(2007) Seed for Success. Purdue University.

(2006) Research Award. American Society for Mass Spectrometry.

(2002) Postdoctoral Fellowship. Damon Runyon Cancer Research Foundation.

Patents

Tao, W. A. Materials and methods for isolating phosphopeptides. U.S. Patent No. In pending. Filed on Oct 07, 2009. Washington, D.C.: U.S. Patent and Trademark Office.

Department of Biochemistry, 175 South University Street, West Lafayette, IN 47907-2063 USA, (765) 494-1600

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