Nature Biotechnology
23, 329 - 336 (2005)
Published online: 13 February 2005; | doi:10.1038/nbt1068
A small molecule−kinase interaction map for clinical kinase inhibitorsMiles A Fabian, William H Biggs III, Daniel K Treiber, Corey E Atteridge, Mihai D Azimioara, Michael G Benedetti, Todd A Carter, Pietro Ciceri, Philip T Edeen, Mark Floyd, Julia M Ford, Margaret Galvin, Jay L Gerlach, Robert M Grotzfeld, Sanna Herrgard, Darren E Insko, Michael A Insko, Andiliy G Lai, Jean-Michel Lélias, Shamal A Mehta, Zdravko V Milanov, Anne Marie Velasco, Lisa M Wodicka, Hitesh K Patel, Patrick P Zarrinkar
& David J LockhartSupplementary Table 1 (pdf 36K)
Kinase inhibitors for which specificity profiles were determined Supplementary Table 2 (pdf 20K)
Comparison of binding constants measured in the competition binding assays to published results. Supplementary Table 3 (pdf 12K)
Comparison of the results of cell-based assays and binding assays for FLT3 and EGFR inhibitors. Supplementary Table 4 (pdf 32K)
Complete quantitative results of screening twenty kinase inhibitors against 119 protein kinases. Supplementary Table 5 (pdf 12K)
Binding constants for eight small molecules binding to ten EGFR variants. Binding constant values are in nanomolar. Supplementary Table 6 (pdf 20K)
List of clone type used for each kinase assay. Domain clones include the complete kinase catalytic
domain along with flanking sequences. Supplementary Notes (pdf 32K)
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