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. 2013 Feb 21;41(7):4295–4306. doi: 10.1093/nar/gkt082

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© The Author(s) 2013. 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 1. — (a) The predicted domain boundaries of vIRF-1: DBD and the IAD (30). Below are the different domain boundary truncations of our four vIRF-1 protein constructs. (b) A TSSA was performed for all the four vIRF-1 protein constructs with several dsDNA, including the PRDIII-I sequence from the human IRF operator (PRDIII-I), a two times repeat of S0 (S0_x2), two sequences from the viral operator region that contains sequences that are highly similar to S0 (v1 and v2) and a random DNA sequence that contains 25 bp (N25). The TSSA shows that only vIRF-1^88–196 is stabilized by the various dsDNA. (c) A dose–response experiment results of vIRF-1^88–196 with varying concentrations of the aforementioned dsDNA. A dose–responsive stabilization of vIRF-1^88–196 by the different dsDNA was observed.