Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry.

@article{Salomon2003ProfilingOT,
  title={Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry.},
  author={Arthur R. Salomon and Scott B. Ficarro and Laurence M. Brill and Achim Brinker and Qui T. Phung and Christer Ericson and K. Morgan Sauer and Ansgar Brock and David Micha Horn and Peter G. Schultz and Eric C. Peters},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2003},
  volume={100 2},
  pages={443-8}
}
The reversible phosphorylation of tyrosine residues is an important mechanism for modulating biological processes such as cellular signaling, differentiation, and growth, and if deregulated, can result in various types of cancer. Therefore, an understanding of these dynamic cellular processes at the molecular level requires the ability to assess changes in the sites of tyrosine phosphorylation across numerous proteins simultaneously as well as over time. Here we describe a sensitive approach… CONTINUE READING