Phosphorylation of the fibronectin receptor complex in cells transformed by oncogenes that encode tyrosine kinases.

@article{Hirst1986PhosphorylationOT,
  title={Phosphorylation of the fibronectin receptor complex in cells transformed by oncogenes that encode tyrosine kinases.},
  author={Robert Hirst and Alan E Horwitz and Clayton Buck and Larry R. Rohrschneider},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1986},
  volume={83 17},
  pages={6470-4}
}
The fibronectin (FN) receptor in avian cells has been characterized previously as a complex of three membrane glycoproteins of about Mr 160,000, Mr 140,000, and Mr 120,000 (simply termed protein band 1, band 2, and band 3, respectively). Monoclonal antibodies to the band 3 protein of the complex prevent FN and laminin binding both in vivo and in vitro and enable the detection of the receptor proteins in the plasma membrane and in adhesion plaques. Association of the FN receptor proteins with… CONTINUE READING
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