Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.

@article{Daub2008KinaseselectiveEE,
  title={Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.},
  author={Henrik Daub and Jesper V. Olsen and Michaela Bairlein and Florian Gnad and Felix S Oppermann and Roman K{\"o}rner and Zolt{\'a}n Greff and Gy{\"o}rgy K{\'e}ri and Olaf Stemmann and Matthias Mann},
  journal={Molecular cell},
  year={2008},
  volume={31 3},
  pages={438-48}
}
Protein kinases are pivotal regulators of cell signaling that modulate each other's functions and activities through site-specific phosphorylation events. These key regulatory modifications have not been studied comprehensively, because low cellular abundance of kinases has resulted in their underrepresentation in previous phosphoproteome studies. Here, we combine kinase-selective affinity purification with quantitative mass spectrometry to analyze the cell-cycle regulation of protein kinases… CONTINUE READING
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