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. 2010 Dec 2;286(8):6201–6210. doi: 10.1074/jbc.M110.154989

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© 2011 by The American Society for Biochemistry and Molecular Biology, Inc.

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FIGURE 3. — Normalized MT-stimulated rates of ATP hydrolysis for wild type HsEg5 and D. melanogaster homologue Klp61F as a function of allosteric effector concentration. Steady-state, MT-ATPase rates (ADP/motor/s) for wild type Drosophila Klp61F (A), HsEg5 (B), Klp61F-L5 (C), and Klp61F-L5-α3 (D) were measured in the presence of either STC (open squares) or monastrol (filled black triangles). 4 μm taxol-stabilized microtubules were present in each assay. The averages of 3–10 measurements and S.E. are normalized against the parent kinesin motor, which has a rate of 100%. All the inhibition curves exhibited by the Klp61F chimeras are significantly different from the corresponding traces exhibited by Klp61F-WT (Wilcoxon signed rank test (α = 0.05).