Biochemical characterization of the binding of echistatin to integrin alphavbeta3 receptor.

@article{Kumar1997BiochemicalCO,
  title={Biochemical characterization of the binding of echistatin to integrin alphavbeta3 receptor.},
  author={C. Promod Chandra Kumar and Hui Nie and C P Rogers and Michael Malkowski and Eugene Maxwell and Joseph J. Catino and Lydia Armstrong},
  journal={The Journal of pharmacology and experimental therapeutics},
  year={1997},
  volume={283 2},
  pages={
          843-53
        }
}
Echistatin is a 49-amino-acid peptide belonging to the family of disintegrins that are derived from snake venoms and are potent inhibitors of platelet aggregation and cell adhesion. Integrin alphavbeta3 receptor plays a critical role in several physiological processes such as tumor-induced angiogenesis, tumor cell metastasis, osteoporosis and wound repair. In this study, we have characterized the binding of echistatin to purified integrin alphavbeta3 receptor and the form expressed on human… CONTINUE READING
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