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. 2020 Mar 30;35(1):880–896. doi: 10.1080/14756366.2020.1740692

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© 2020 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group.

This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial License (http://creativecommons.org/licenses/by-nc/4.0/), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 4. — The antagonist effect of 6A by reporter gene assay (A,B) and the physical binding of 6A to RXRα-LBD (C), ERα-LBD (D), PPARγ-LBD (E), and TR3-LBD (F) by SPR assay. (A) Dose-dependent effect of 6A on inhibiting RXRα transactivation. HEK293T cells transfected with p-BIND-RXRα-LBD and pG5-luc were treated with indicated concentrations of 6A in the presence of 9-cis-RA (0.10 μM). (B) Inhibition of 9-cis-RA-induced RXRE-luciferase reporter activation by 6A. HEK293T cells transfected with RXRE (50 ng), full-length RXRα (50 ng), Renilla (1 ng) were treated with 9-cis-RA in the presence of indicated concentrations of 6A or UVI3003 (1 μM). (C) Surface plasmon resonance of 6A binding to RXRα-LBD. D. Surface plasmon resonance of 6A binding to ERα-LBD. E. Surface plasmon resonance of 6A binding to PPARγ-LBD. F. Surface plasmon resonance of 6A binding to TR3-LBD. (C–F) Gradient concentrations of 6A were respectively injected through chips immobilised with RXRα-LBD, ERα-LBD, PPARγ-LBD, and TR3-LBD.