Receptor- and heparin-binding domains of basic fibroblast growth factor.

@article{Baird1988ReceptorAH,
  title={Receptor- and heparin-binding domains of basic fibroblast growth factor.},
  author={Andrew Baird and David Crawford Schubert and Nicholas Chi-Kwan Ling and Renaud Guillemin},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1988},
  volume={85 7},
  pages={
          2324-8
        }
}
Two functional domains in the primary structure of basic fibroblast growth factor (FGF) have been identified on the basis of their ability to interact with the FGF receptor, bind radiolabeled heparin, and modulate the cellular response to FGF. Peptides derived from these two functional domains can act as partial agonists and antagonists in biological assays of FGF activity. Peptides related to the sequences of FGF-(24-68)-NH2 and FGF-(106-115)-NH2 inhibit thymidine incorporation into 3T3… CONTINUE READING
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