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. 2016 Dec 9;45(3):1307–1318. doi: 10.1093/nar/gkw1239

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© The Author(s) 2016. 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-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com

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Figure 5. — DDX19B activity in translation termination in the presence of eRFs variants. Relative quantitative analysis of the stop codon binding efficiency of (A) eRF1(AGQ), eRF1(AGQ)+eRF3c+GTP, eRF1+eRF3c+GMPPNP and (B) eRF1(K83N), hydroxylated eRF1 (eRF1-OH) in the presence of DDX19B. Stop codon binding efficiency of eRF1 alone was set as 100% (n = 3). (C) ATPase activity of DDX19B mutants E243Q, R372G and R429Q (n = 3). (D) Relative quantitative analysis of the stop codon binding efficiency of eRF1, eRF1+eRF3c+GTP and DDX19B mutants in the presence of ATP or AMPPNP. Stop codon binding efficiency of eRF1 alone was set as 100% (n = 3). The error bars represent the standard deviation.