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. 2014 Feb 11;42(8):5234–5244. doi: 10.1093/nar/gku133

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© The Author(s) 2014. Published by Oxford University Press.

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

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Figure 3. — Structure probing of the NMSL. Denaturing PAGE analysis of RNAse 1 and RNAse V1 cleavage of 5′-[³²P]-end-labeled NMSL. Cleavages were assigned using a base hydrolysis ladder and an RNAse T1 sequencing reaction. Adenosines that are cleaved by both RNase 1 and V1 are indicated by gray triangles. The white triangles indicate positions that are not cleaved by either RNase. The predicted Watson–Crick base pairs A681:U705 and A687:U704 could not be confirmed by ribonuclease sensitivity. The asterisk indicates a nonribonuclease degradation product. 3′ heterogeneity of the low molecular weight cleavage products for positions A 682 and A 683 are visible.