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Response to Molecule–kinase interaction map

Nature Biotechnology volume 23, pages 1346–1348 (2005)Cite this article

Fabian et al. respond:

Buolamwini and Kamath suggest that the data presented in our manuscript lack statistical validation and are not sufficiently quantitative to justify some of our conclusions. In particular, they state that the validation of our technology, which included a detailed comparison of our measured binding (Kd) values to published IC50 values for kinase inhibition (Supplementary Table 2 online in our paper), is insufficient. We disagree with these assertions for several reasons. First, for every interaction identified in the manuscript, we report Kd values that were calculated from twelve-point competition curves. Average Kd values from at least two twelve-point curves were reported. We agree that more measurements would be better, particularly if our goal had been to obtain even more precise values to discern small differences (which it was not). Our data have been collected in a consistent, rigorous manner and are significantly more quantitative than data from other widely cited reports on kinase inhibitor selectivity that employ primarily 'percent inhibition' data collected at a single inhibitor concentration1,2.

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Authors and Affiliations

  1. Ambit Biosciences, 4215 Sorrento Valley Blvd., San Diego, 92121, CA, USA

    Miles A. Fabian, William H. Biggs III, Daniel K. Treiber, Patrick P. Zarrinkar & David J. Lockhart

Authors
  1. Miles A. Fabian
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  2. William H. Biggs III
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  3. Daniel K. Treiber
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  4. Patrick P. Zarrinkar
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  5. David J. Lockhart
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Fabian, M., Biggs, W., Treiber, D. et al. Response to Molecule–kinase interaction map. Nat Biotechnol 23, 1346–1348 (2005). https://doi.org/10.1038/nbt1105-1346b

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