Crystal structure of the T315I Abl mutant in complex with the aurora kinases inhibitor PHA-739358.

@article{Modugno2007CrystalSO,
  title={Crystal structure of the T315I Abl mutant in complex with the aurora kinases inhibitor PHA-739358.},
  author={Michele Modugno and Elena Casale and Chiara Soncini and Pamela Rosettani and Riccardo Colombo and Rosita Lupi and Luisa Rusconi and Daniele Fancelli and Patrizia Carpinelli and Alexander D Cameron and Antonella Isacchi and J{\"u}rgen Moll},
  journal={Cancer research},
  year={2007},
  volume={67 17},
  pages={7987-90}
}
Mutations in the kinase domain of Bcr-Abl are the most common cause of resistance to therapy with imatinib in patients with chronic myelogenous leukemia (CML). Second-generation Bcr-Abl inhibitors are able to overcome most imatinib-resistant mutants, with the exception of the frequent T315I substitution, which is emerging as a major cause of resistance to these drugs in CML patients. Structural studies could be used to support the drug design process for the development of inhibitors able to… CONTINUE READING

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