Functional analysis of discoidin domain receptor 1: effect of adhesion on DDR1 phosphorylation.

@article{Lhte2002FunctionalAO,
  title={Functional analysis of discoidin domain receptor 1: effect of adhesion on DDR1 phosphorylation.},
  author={Corine G M L'h{\^o}te and Peter D. Thomas and Trivadi Sundaram Ganesan},
  journal={FASEB journal : official publication of the Federation of American Societies for Experimental Biology},
  year={2002},
  volume={16 2},
  pages={234-6}
}
Discoidin domain receptor 1 (DDR1), a receptor tyrosine kinase (RTK), has been shown to be activated mainly by soluble fibrillar collagen. Unusually, the kinetics of phosphorylation of the receptor is slow, with maximal phosphorylation observed after 90 min. To understand the reasons for slow phosphorylation of the receptor, we examined several cell lines under different conditions. We confirm that endogenous DDR1 is phosphorylated slowly by collagen in adherent T47D and HCT116 cells. In… CONTINUE READING
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