Chen,H., Ma, J., Li, W., Eliseenkova, A., Xu, C., Neubert, T., Miller, W., and Mohammadi, M. A Molecular Brake in the Kinase Hinge Region Regulates the Activity of Receptor Tyrosine Kinases. United States: N. p., 2007.
Web. doi:10.1016/j.molcel.2007.06.028.
Chen,H., Ma, J., Li, W., Eliseenkova, A., Xu, C., Neubert, T., Miller, W., & Mohammadi, M. A Molecular Brake in the Kinase Hinge Region Regulates the Activity of Receptor Tyrosine Kinases. United States. doi:10.1016/j.molcel.2007.06.028.
Chen,H., Ma, J., Li, W., Eliseenkova, A., Xu, C., Neubert, T., Miller, W., and Mohammadi, M. Mon .
"A Molecular Brake in the Kinase Hinge Region Regulates the Activity of Receptor Tyrosine Kinases". United States.
doi:10.1016/j.molcel.2007.06.028.
@article{osti_930014,
title = {A Molecular Brake in the Kinase Hinge Region Regulates the Activity of Receptor Tyrosine Kinases},
author = {Chen,H. and Ma, J. and Li, W. and Eliseenkova, A. and Xu, C. and Neubert, T. and Miller, W. and Mohammadi, M.},
abstractNote = {Activating mutations in the tyrosine kinase domain of receptor tyrosine kinases (RTKs) cause cancer and skeletal disorders. Comparison of the crystal structures of unphosphorylated and phosphorylated wild-type FGFR2 kinase domains with those of seven unphosphorylated pathogenic mutants reveals an autoinhibitory 'molecular brake' mediated by a triad of residues in the kinase hinge region of all FGFRs. Structural analysis shows that many other RTKs, including PDGFRs, VEGFRs, KIT, CSF1R, FLT3, TEK, and TIE, are also subject to regulation by this brake. Pathogenic mutations activate FGFRs and other RTKs by disengaging the brake either directly or indirectly.},
doi = {10.1016/j.molcel.2007.06.028},
journal = {Molecular Cell},
number = 5,
volume = 27,
place = {United States},
year = {Mon Jan 01 00:00:00 EST 2007},
month = {Mon Jan 01 00:00:00 EST 2007}
}