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Tyrosine phosphorylation is a dynamic mechanism that has the potential to significantly alter the conformation, function and sub-cellular localizations of proteins. Identification of the site of post-translational modification and quantification of the levels of phosphorylation is essential to understand the functional significance of each phosphorylation site in biological systems. Increased sensitivity in mass spectrometry has recently allowed the quantification of hundreds of tyrosine phosphorylation sites across in vivo tissues and tumors. Furthermore, profiling phosphotyrosine signaling by mass spectrometry has led to greater insight into the function of tyrosine phosphorylation and, as such, it is clear that phosphotyrosine levels are significantly altered across many disease states. Thus, to gain a complete understanding of the mechanisms that lead to disease progression, it is important to identify deregulated proteins and genes and extend this to the identification of crucial changes at the signaling level. This chapter highlights the recent advances in quantitative phosphotyrosine analyses of relevant disease models and discusses the biological significance of these studies.

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