Fluorescent Biosensor for CrkII Phosphorylation by the Abl Tyrosine Kinase

  • Roseanne M. Hofmann
  • Graham J. Cotton
  • William Bornman
  • Emmanual Chang
  • Tom W. Muir
Part of the American Peptide Symposia book series (APSY, volume 7)

Abstract

Chronic myeloid leukemia (CML) causes the excessive proliferation of myeloid cells ADDIN ENRfu [1]. The majority of CML cases are caused by the reciprocal chromosomal translocation of the first exon of c-Abl on chromosome 9 and the breakpoint cluster region (Bcr) of chromosome 22. The c-Abl gene encodes a nonreceptor kinase that catalyzes the transfer of phosphate from ATP to tyrosine residues on protein substrates. The Bcr-Abl fusion protein produces an overactive kinase, and this deregulated tyrosine kinase activity is required for leukemic transformation.

Keywords

Hydrolysis Tyrosine Leukemia Carboxyl Fluores 

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Copyright information

© Springer Science+Business Media Dordrecht 2001

Authors and Affiliations

  • Roseanne M. Hofmann
    • 1
  • Graham J. Cotton
    • 1
  • William Bornman
    • 2
  • Emmanual Chang
    • 1
  • Tom W. Muir
    • 1
  1. 1.Laboratory of Synthetic Protein ChemistryRockefeller University of New YorkUSA
  2. 2.Laboratory of Bioorganic ChemistrySloan-Kettering InstituteNew YorkUSA

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