Structural mechanism for STI-571 inhibition of abelson tyrosine kinase.

By R. Sprengel, J. Bissonnette, W. Kaufmann, D. Pribnow, T. Neelands, T. Storck, M. Baetscher, Jasna Jerecic, J. Maylie, H. Knaus and 2 more. Science, 2000

1,840 citations recorded by the source corpus.

Subfields: Ecology, Evolution, Behavior and Systematics, Hematology, Organic Chemistry

View Paper: https://www.semanticscholar.org/paper/3c4ca6ac82d1b64dafa4e5c4ecabfe034a4cf452

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In Hematology

In Organic Chemistry

D. Barford

Citations in the corpus

Bcr-Abl kinase domain mutations, drug resistance, and the road to a cure for chronic myeloid leukemia. (2007, background): “Where do we stand on clinical development of a T315I inhibitor? Developing a T315I inhibitor is challenging, as most ATP-competitive inhibitors directly interact with threonine-315 via hydrogen bonding and with the specificity-imparting hydrophobic pocket for which this residue serves as a ‘gatekeep”
Modelling dynamics in protein crystal structures by ensemble refinement (2012, neutral): “These compounds bind the Abl kinase with high affinity, 37 nM (Schindler et al., 2000) and 100 nM respectively (Nagar et al.”
Features of selective kinase inhibitors. (2005, background): “A growing number of kinase inhibitors selectively c s target the inactive conformation [3, 21, 22], whereas other compounds bind to both conformations with sim- r m ilar affinity [23].”
Detection of BCR-ABL mutations in patients with CML treated with imatinib is virtually always accompanied by clinical resistance, and mutations in the ATP phosphate-binding loop (P-loop) are associated with a poor prognosis. (2003, background): “Met351Thr 9 CHR PHR Died from disease progression (12), acquired”
A Pharmacological Map of the PI3-K Family Defines a Role for p110α in Insulin Signaling (2006, neutral): “This insight should guide the design of selective PI3-K inhibitors, in the same way that structural studies of the gatekeeper pocket (Schindler et al., 1999) and the inactive conformation (Schindler et al., 2000) have guided the discovery of selective protein kinase inhibitors.”
In vitro activity of Bcr-Abl inhibitors AMN107 and BMS-354825 against clinically relevant imatinib-resistant Abl kinase domain mutants. (2005, background): “Imatinib selectively targets an inactive conformation of the Abl kinase domain in which the activation loop is in a nonphosphorylated, closed position that is incompatible with substrate binding (13).”