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. 2017 Nov 3;15(4-5):649–658. doi: 10.1080/15476286.2017.1377868

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© 2018 The Author(s). Published with license by Taylor & Francis Group, LLC

This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivatives License (http://creativecommons.org/licenses/by-nc-nd/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited, and is not altered, transformed, or built upon in any way.

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Figure 6. — H130R substitution enhances the interaction between T2-TrpRS and VE-cadherin. (A) The fitted sensorgram of the binding between wild-type (WT) T2-TrpRS and EC1-2 domain of VE-cadherin by surface plasmon resonance. The response unit is plotted over 400 s that illustrates the association and dissociation of the complex. The concentration of WT T2-TrpRS is 2-fold increased from 12.5 nM to 200 nM. (B) The fitted sensorgram of the binding between H130R T2-TrpRS and EC1-2 domain of VE-cadherin. The response unit of H130R T2-TrpRS at concentration from 0.78 nM to 25 nM is plotted over 400 s. (C) In vitro pull down assay to test the interaction between TrpRS and endogenous VE-cadherin. The melanoma C8161 cells expressed VE-cadherin was pulled down by 6xHis tagged FL- and T2-TrpRS (WT and H130R), and immune-blotted by rabbit anti VE-cadherin. The TrpRS variants are blotted with HRP-conjugated 6xHis antibodies.