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. 2011 Sep 2;39(22):9779–9788. doi: 10.1093/nar/gkr667

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© The Author(s) 2011. 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 5. — Influence of acidic residues on the p56 inhibition activity. The inhibition ability of two triple mutants (D5A/D8A/D11A and D18A/D19A/D20A) and two single mutants, E26A(A) and E37A(B) of p56 was assayed. Different doses of the mutant proteins (from 0.2 to 18.8 ng for the triple mutants and the E26A mutant and from 0.25 to 16 ng for the E37A mutant) were incubated with 5 pg of UDG. Then, the DNA substrate was added and incubated for 20 min at 37°C and the product was analysed in 8 M urea-20% polyacrylamide gels. (C) After quantification by densitometry, the percentage of inhibition for the mutants was calculated with respect to the wild-type protein. Data are depicted in a bar chart and average values of three independent experiments with standard deviations are represented.