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Marchini F.K.,Functional Genomics Laboratory FiocruzParana | de Godoy L.M.F.,Functional Genomics Laboratory FiocruzParana | Batista M.,Functional Genomics Laboratory FiocruzParana | Kugeratski F.G.,Functional Genomics Laboratory FiocruzParana | Krieger M.A.,Functional Genomics Laboratory FiocruzParana
Sub-Cellular Biochemistry | Year: 2014

The identification and localization of protein phosphorylation sites provide clues to what proteins or pathways might be activated in a given condition, helping to improve our understanding about signaling networks. Advances in strategies for enrichment of phosphorylated peptides/proteins, mass spectrometry (MS) instrumentation, and specifi c MS techniques for identifi cation and quantification of post-translational modifi cations have allowed for large-scale mapping of phos-phorylation sites, promoting the field of phosphoproteomics. The great promise of phosphoproteomics is to unravel the dynamics of signaling networks, a layer of the emerging field of systems biology. Until a few years ago only a small number of phosphorylation sites had been described. Following large-scale trends, recent phos-phoproteomic studies have reported the mapping of thousands of phosphorylation sites in trypanosomatids. However, quantitative information about the regulation of such sites in different conditions is still lacking. In this chapter, we provide a historical overview of phosphoproteomic studies for trypanosomatids and discuss some challenges and perspectives in the field. © Springer Science+Business Media Dordrecht 2014. Source

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