Article
Kinase domain mutants of Bcr-Abl exhibit altered transformation potency, kinase activity, and substrate utilization, irrespective of sensitivity to imatinib.
Molecular and cellular biology - 1 Aug 2006
Griswold Ian J, MacPartlin Mary, Bumm Thomas, Goss Valerie L, O'Hare Thomas, Lee Kimberly A, Corbin Amie S, Stoffregen Eric P, Smith Caitlyn, Johnson Kara, Moseson Erika M, Wood Lisa J, Polakiewicz Roberto D, Druker Brian J, Deininger Michael W
Abstract excerpt
Kinase domain (KD) mutations of Bcr-Abl interfering with imatinib binding are the major mechanism of acquired imatinib resistance in patients with Philadelphia chromosome-positive leukemia. Mutations of the ATP binding loop (p-loop) have been associated with a poor prognosis. We compared the transformation potency of five common KD mutants in various biological assays. Relative to unmutated (native) Bcr-Abl, the...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.