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. 2012 May 9;40(15):7347–7357. doi: 10.1093/nar/gks353

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© The Author(s) 2012. Published by Oxford University Press.

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 2. — RI-1 inhibits human RAD51 in biochemical assays. (A) Chemical structure of RI-1 is displayed. (B) Human RAD51 protein was allowed to bind fluorescently-tagged ssDNA following a pre-incubation in various concentrations of RI-1. DNA binding is reported as a function of fluorescence polarization as described in the ‘Materials and Methods’ section. (C) HsRAD51 was allowed to generate joint molecules (‘D-loops’) in the presence of RI-1. A representative phosphorimage of an agarose gel is displayed, and the positions of free oligo and oligo associated with D-loops are indicated.