Tyrosine phosphorylation of CRKL in Philadelphia+ leukemia.

@article{tenHoeve1994TyrosinePO,
  title={Tyrosine phosphorylation of CRKL in Philadelphia+ leukemia.},
  author={Johanna ten Hoeve and Ralph B. Arlinghaus and J. Q. Guo and Nora Heisterkamp and John Groffen},
  journal={Blood},
  year={1994},
  volume={84 6},
  pages={
          1731-6
        }
}
The chimeric BCR/ABL protein is characteristic of Philadelphia (Ph)+ leukemia because it is the direct product of the Ph translocation and it has been shown to play a causal role in the genesis of leukemia. The BCR/ABL protein exhibits a deregulated tyrosine-kinase activity capable of phosphorylating different cellular substrates in vivo and in vitro. CRKL, an adaptor protein consisting of SH2 and SH3 domains in the absence of a catalytic domain, is one potential in vivo substrate of BCR/ABL… 

Figures and Tables from this paper

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Results indicate that the presence of the p210(bcr-abl) protein kinase within a cell is associated with phosphorylation of the JAK1 kinase and its substrate STAT1.
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