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. 2011 Jun 21;105(2):212–220. doi: 10.1038/bjc.2011.200

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Copyright © 2011 Cancer Research UK

This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material.If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit https://creativecommons.org/licenses/by/4.0/.

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STAT3 phosphorylation of ALDH⁺/CD133⁺ subpopulation of colon cancer cells is higher than un-separated and the ALDH⁻/CD133⁻ subpopulations. (A) ALDH⁺/CD133⁺ and ALDH⁻/CD133⁻ subpopulations were separated from DLD-1, HCT-116, and SW480 colon cancer cells by flow cytometer. The percentage of ALDH⁺/CD133⁺ subpopulations was shown. (B) Phosphorylation of STAT3 (Y705), ERK 1/2 (T202/Y204), phospho-independent STAT3 of ALDH⁺/CD133⁺, and ALDH⁻/CD133⁻ subpopulations were detected by western blot. (C) Computer modelling of GO-Y030 binding to STAT3 SH2 domain. GO-Y030 is in Thick Stick-Ball (S-B) model and in grey colour. The native pTyr–Leu706 phospho-peptide binding of the partnering SH2 in homo-dimerisation is in green colour. GO-Y030 occupied both pTyr705- and Leu706-binding sites, which very effectively displaced the native pTyr705–Leu706 peptide with a stronger binding affinity than native peptide in the binding site of STAT3 SH2 domain. The colour reproduction of this figure is available at the British Journal of Cancer online.