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. 2015 Oct 10;43(18):8790–8800. doi: 10.1093/nar/gkv764

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© The Author(s) 2015. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 6. — The spatial location of RPA1N affects the stimulation of WRN's helicase activity. (A) A gel showing recombinant Xenopus wild-type RPA and two mutant RPAs. Proteins were separated by a 4–12% NUPAGE MES gel (Invitrogen, CA, USA) and stained by Coomassie brilliant blue. (B) An agarose gel showing the binding activity of the wild-type and mutant RPAs to ss-m13 DNA. (C) Effect of wild-type RPA and mutant RPAs on the unwinding activity of WRN. The substrate was a ³²P-labeled 56mer oligonucleotide annealed to m13 ss-DNA. (D) Quantitaton of the unwinding activity in the presence of wild-type RPA or mutant RPAs. The percentages of the oligonucleotide dissociated were quantitated and the averages and standard deviations were calculated from three sets of data and plotted.