W. Andy TaoAssistant Professor of Biochemistry Investigators: Area: Proteomics and biological mass spectrometry |
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Proteomics research is highly interdisciplinary, bringing together biology, chemistry, instrumentation, statistics, and computer science. A typical proteomic research starts with an important biological problem and therefore the very first step is to extract the sample from biological matrices for efficient downstream analysis. The sample is separated and then analyzed by mass spectrometry, typically online micro-capillary liquid chromatography-tandem mass spectrometry (mLC-MS/MS). MS data are then searched against protein database to obtain sequencing information of proteins. Proteins are finally validated using traditional biological methods. Our group focuses on the first step, i.e., how to efficiently target and isolate samples of interest among complex biological matrices. 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. Targeted 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 proteins of interest. |
Selected Publications:
- Timmer JC, Enoksson M, Wildfang E, Zhu W, Igarashi Y, Denault JB, Ma Y, Dummitt B, Chang YH, Mast AE, Eroshkin A, Smith JW, Tao WA, Salvesen GS. Profiling constitutive proteolytic events in vivo. Biochem J. 407(1): 41-8 (2007).
- Enoksson M, Li J, Ivancic MM, Timmer J, Wildfang E, Eroshkin A, Salvesen GS and Tao WA. Identification of proteolytic cleavage sites by quantitative proteomics. J. Proteome Res. 6(7): 2850-8 (2007).
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Song Y, Talaty N, Tao WA, Pan Z, Cooks RG. Rapid ambient mass spectrometric profiling of intact, unteated bacteria desorption electrospray ionization. Chem. Commun. 61-63 (2007).
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Guo M, Galan J. and Tao WA. Soluble nanopolymer-based phosphoproteomics for studying protein phosphatase. Methods 42(3): 289-297 (2007).
- Bodenmiller B, Mueller LN, Pedrioli PGA, Pflieger D, Jünger MA, Eng JK, Aebersold R, and Tao WA. An integrated chemical, mass spectrometric and computational strategy for (quantitative) phosphoproteomics: Application to Drosophila melanogaster Kc167 Cells. Mol. Biosys. 3: 275-286 (2007).
- He XC, Yin T, Grindley JC, Tian Q, Sato T, Tao WA, Dirisina R, Porter-Westpfahl KS, Hembree M, Johnson T, Wiedemann LM., Barrett TA, Hood L, Wu H, Li L. PTEN-deficient intestinal stem cells initiate intestinal polyposis. Nature Genetics 39(2): 189-198 (2007).
- Guo M, Galan J, Tao WA (2007). A novel quantitative proteomics reagent based on soluble nanopolymers. Chem. Commun. 1251-1253, DOI:10.1039/ B614926J (2007).
- Zhou F, Galan J, Geahlen RL, Tao WA. A Novel quantitative proteomics strategy to study phosphorylation-dependent peptide-protein interactions. J. Proteome Res.6: 133-40 (2007).
- Cooks RG, Chen H, Eberlin MN, Zheng X, Tao WA. Polar acetalization and transacetalization in the gas phase: the Eberlin Reaction. Chem. Rev. 106: 188-211 (2006).
- Tao WA, Wollscheid B, O'Brien R, Eng, Li X, Bodenmiller B, Watts J, Hood L, Aebersold R. Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and mass spectrometry. Nature Methods 2(8): 591-598 (2005).
