Crystal structures of the kinase domain of c-Abl in complex with the small molecule inhibitors PD173955 and imatinib (STI-571).

By B. Nagar, W. Bornmann, P. Pellicena, T. Schindler, D. Veach, W. Miller, B. Clarkson, J. Kuriyan. Cancer Research, 2002

949 citations recorded by the source corpus.

View Paper: https://www.semanticscholar.org/paper/fb3d4b790d85cdf4cfbcc363182333b7126fec32

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Citations in the corpus

In vitro activity of Bcr-Abl inhibitors AMN107 and BMS-354825 against clinically relevant imatinib-resistant Abl kinase domain mutants. (2005, background): “The Abl and Src active conformations are more similar and many inhibitors that bind to the active conformation of Src are also capable of inhibiting Abl (11).”
A small molecule–kinase interaction map for clinical kinase inhibitors (2005, background): “SRC, FRK, FYN and LCK are closely related, and the fact that imatinib can discriminate between them presents an interesting subject for molecular recognition studie”
Discovery and development of sorafenib: a multikinase inhibitor for treating cancer (2006, background): “Interestingly, the interaction between sorafenib and Raf1–wild-type B-Raf turned out to show some similarity with the interaction between c-Abl and its inhibitor, imatini”
The structure of Dasatinib (BMS-354825) bound to activated ABL kinase domain elucidates its inhibitory activity against imatinib-resistant ABL mutants. (2006, background): “inhibitors as reported previously (12) with minor modifications.”
Modelling dynamics in protein crystal structures by ensemble refinement (2012, unknown): “Moreover, the ordered water network between Glu286, Lys271 and the pyrimidine moiety of Imatinib ( Nagar et al., 2002 ) was reproduced in the ensemble model ( Figure 12B ).”
Identification of RIP1 kinase as a specific cellular target of necrostatins. (2008, unknown): “Similar to our data, mutations destabilizing the inactive conformation, such as H396P in the activation loop, have been found to eliminate sensitivity of Bcr-Abl to imatini”
A glimpse of structural biology through X-ray crystallography. (2014, background): “…20, 2014 ª2014 Elsevier Inc. tures reveal the precise interactions of an imatinib variant with surrounding residues in the ATP-binding pocket of BCRABL and explain how patient-derived mutations (such as T315I) inactivate imatinib binding (Figure 3D) (Nagar et al., 2002; Schindler et al., 2000).”