Improved coiled-coil design enhances interaction with Bcr-Abl and induces apoptosis.

  title={Improved coiled-coil design enhances interaction with Bcr-Abl and induces apoptosis.},
  author={Andrew S. Dixon and Geoffrey D. Miller and Benjamin J. Bruno and Jonathan E. Constance and David W. Woessner and Trevor P. Fidler and James C. Robertson and Thomas E. Cheatham and Carol S Lim},
  journal={Molecular pharmaceutics},
  volume={9 1},
The oncoprotein Bcr-Abl drives aberrant downstream activity through trans-autophosphorylation of homo-oligomers in chronic myelogenous leukemia (CML).(1, 2) The formation of Bcr-Abl oligomers is achieved through the coiled-coil domain at the N-terminus of Bcr.(3, 4) We have previously reported a modified version of this coiled-coil domain, CCmut2, which exhibits disruption of Bcr-Abl oligomeric complexes and results in decreased proliferation of CML cells and induction of apoptosis.(5) A major… CONTINUE READING


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Chronic myeloid leukemia: a historical perspective

J. M. Goldman
Semin. Hematol. 2011, • 2011

: where are we now and where can we go ?

C. Pavlovsky, H. Kantarjian, J. E. Cortes
Hematology • 2010

Chronic myeloid leukemia 2010: where are we now and where can we go?

Hematology. American Society of Hematology. Education Program • 2010

Controlling subcellular localization to alter function: Sending oncogenic Bcr-Abl to the nucleus causes apoptosis.

Journal of controlled release : official journal of the Controlled Release Society • 2009

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