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. 2019 May 13;47(16):8375–8387. doi: 10.1093/nar/gkz381

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© The Author(s) 2019. 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 Non-Commercial 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 2. — Electrophoretic mobility shift assay of TCF4 bHLH protein binding to oligos containing a single E-box. (A) Schematic of chemical reactions of DNA cytosine methylation by DNMT and 5mC oxidations by Tet enzymes. (B) The central CpG dinucleotides are unmodified (C/C) or fully modified (M/M, H/H, F/F; where M = 5mC, H = 5hmC, and F = 5fC). (C) The central CpG dinucleotides are hemi-modified (M/C, H/C, F/C or 5caC/C; where 5caC = 5-carboxyC). (D) The two outer CpA dinucleotides are unmodified (C/C), fully modified (M/M, H/H, F/F) or hemi-modified (5caC/C). The protein concentrations used were a maximum of 7 μM (the right most lane 15 of each panel) followed by serial 2-fold dilutions (from right to left). The arrows indicated a reference point where the shift was observed for the unmodified oligo. The same samples were quantified by fluorescence polarization (Supplementary Figure S1).