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. 2005 Jan 7;33(1):114–125. doi: 10.1093/nar/gki155

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© 2005, the authors Nucleic Acids Research, Vol. 33 No. 1 © Oxford University Press 2005; all rights reserved

The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use permissions, please contact journals.permissions@oupjournals.org.

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Stable 3′ mRNA cleavage fragments are translated with moderate efficiency. (A) Translation of stable 3′ mRNA cleavage fragments was quantified using a preS luciferase fusion construct. The binding sites for different ASO and labeled probes are shown. The drawing is not to scale. (B) Northern-blot analysis with probes discriminating RNA cleavage fragments upon cotransfection of preS-Luc with different ASO. Faint bands consistent with 5′ cleavage fragments are indicated by arrows. (C) Immunoblotting of luciferase fusion proteins upon cotransfection with different ASO is depicted (top). Equal amounts of protein were loaded. Quantification of protein yield by luciferase activity (bottom). Values are given in percent compared to luciferase activity obtained after cotransfection of control ASO. The number of observations is given in brackets. Asterisks indicate a statistically significant difference compared with control ASO treated cells, whereas, the section mark symbol indicates a statistically significant difference between cells cotransfected with ASO DHBV795 and DHBV874.