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. 2015 Sep 1;26(17):3001–3012. doi: 10.1091/mbc.E14-10-1427

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© 2015 Haase, Zimmermann, et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0).

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FIGURE 6: — TgADF is more efficient in disassembling F-actin than PfADF1. (A, B) TIRF microscopy analysis of cofilin-mediated F-actin severing by wild-type and mutant ADF proteins. Filaments were assembled from 1 μM G-actin (10% Oregon green–labeled, 0.1% biotinylated) in flow chambers and attached to biotin-PEG (0.1%)–coated glass slides by streptavidin. Plots of the normalized severing rates (break μm^-1 s^-1) in the presence of different protein concentrations show the individual data points, as well as the mean ± SEM. (C, D) F-actin disassembly assays using pyrene-labeled actin, induced by vitamin D–binding protein. A range of wild-type and mutant ADF protein concentrations was tested on preassembled 1.5 μM F-actin (10% pyrene-actin; Chaudhry et al., 2013). Disassembly rates were determined by measuring the slope in the linear region of the original data set shown in Supplemental Figure S4.