Purification and identification of protein-tyrosine kinase-binding proteins using synthetic phosphopeptides as affinity reagents.

@article{Wilhelmsen2004PurificationAI,
  title={Purification and identification of protein-tyrosine kinase-binding proteins using synthetic phosphopeptides as affinity reagents.},
  author={Kevin Wilhelmsen and Jeremy Copp and Gary Glenn and Ross C Hoffman and Philip T Tucker and Peter van der Geer},
  journal={Molecular & cellular proteomics : MCP},
  year={2004},
  volume={3 9},
  pages={887-95}
}
Protein-tyrosine kinases are known regulators of cell division that have been implicated in the onset of a variety of malignancies. They act through cellular signaling proteins that bind to specific autophosphorylation sites. To find out whether these autophosphorylation sites can be used to identify downstream signaling proteins, synthetic peptides based on an autophosphorylation site in the colony-stimulating factor-1 (CSF-1) receptor were linked to agarose beads and incubated with lysates… CONTINUE READING