Inhibition of FGF-stimulated phosphatidylinositol hydrolysis and neurite outgrowth by a cell-membrane permeable phosphopeptide

@article{Hall1996InhibitionOF,
  title={Inhibition of FGF-stimulated phosphatidylinositol hydrolysis and neurite outgrowth by a cell-membrane permeable phosphopeptide},
  author={Heike Hall and Emma J. Williams and Stephen E. Moore and Frank S. Walsh and Alain Prochiantz and Patrick Doherty},
  journal={Current Biology},
  year={1996},
  volume={6},
  pages={580-587}
}
BACKGROUND Activated receptor tyrosine kinases bind downstream effector molecules with high affinity. Provided that they can be introduced into cells, peptides corresponding to these high-affinity sites should be able to compete for the interaction and thereby inhibit specific signal transduction cascades. The high-affinity binding site for phospholipase C gamma (PLCgamma) on the activated fibroblast growth factor receptor (FGFR) is centred around the tyrosine at position 766 (766Tyr), and… CONTINUE READING

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