Design, synthesis, and biological characterization of a peptide-mimetic antagonist for a tethered-ligand receptor.

@article{AndradeGordon1999DesignSA,
  title={Design, synthesis, and biological characterization of a peptide-mimetic antagonist for a tethered-ligand receptor.},
  author={Patricia Andrade-Gordon and Bruce E Maryanoff and Claudia K. Derian and Han Cheng Zhang and Michael F Addo and Andrew L Darrow and Annette J Eckardt and William J. Hoekstra and David F McComsey and Donna Oksenberg and E E Reynolds and Rosemary J Santulli and Robert Murry Scarborough and C. I. Edvard Smith and Kimberly B White},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1999},
  volume={96 22},
  pages={12257-62}
}
Protease-activated receptors (PARs) represent a unique family of seven-transmembrane G protein-coupled receptors, which are enzymatically cleaved to expose a truncated extracellular N terminus that acts as a tethered activating ligand. PAR-1 is cleaved and activated by the serine protease alpha-thrombin, is expressed in various tissues (e.g., platelets and vascular cells), and is involved in cellular responses associated with hemostasis, proliferation, and tissue injury. We have discovered a… CONTINUE READING
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Peptide Chemistry, ed

  • T. Fujita, T. Nose, M. Nakajima, Y. Inoue, Y. Shimohigashi, M. Ohno
  • 1997

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