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New Progress in Large Scale Protein Phosphorylation Analysis of Human Livers
  English.dicp.cas.cn    Posted:2012-10-24

The DICP research team led by Prof. Hanfa Zou has made a new progress in large scale protein phosphorylation analysis of human livers, and the results have been published in the recent issue of Mol. Cell. Proteomics (Mol. Cell. Proteomics2012111070-1083, http://www.mcponline.org/content/11/10/1070.full).

In this study, phosphopeptides in tryptic lysates of human livers were enriched by Ti-IMAC materials, and then separated by a reversed phase-reversed phase (RP-RP) multidimensional separation approach with high orthogonality. A total of 9719 protein phosphorylation sites, corresponding to 2998 phosphoproteins, were identified, and it has been the largest data set in phosphoproteomics of human liver tissues up to now. On the basis of this data set, a novel software package of iGPS was used to construct a human liver protein phosphorylation network containing 12,819 potential site-specific kinase-substrate correlations among 350 PKs and 962 substrates for 2633 p-sites.

As one of the most important post-translational modifications, protein phosphorylation plays a crucial role in diverse biological processes such as signal transduction and cell cycle. The research group of “Novel Technology and Materials for Separation and Detection of Biomolecules” of DICP focuses their investigations on the development of new technologies and methods based on mass spectrometry for phosphoproteomics analysis. A series of research studies have been published in Mol. Cell. ProteomicsAnal. Chem. and J. Proteome Res.. In 2011, Prof. Hanfa Zou has been invited to write a perspective review on phosphorylation analysis for Anal. Chem.




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