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. 2016 Feb 11;7(2):e2094. doi: 10.1038/cddis.2016.11

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Copyright © 2016 Macmillan Publishers Limited

Cell Death and Disease is an open-access journal published by Nature Publishing Group. This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article's Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/

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Structural simulation of ANP by the combined drugs competitively targets phosphorylation of JNK/Erk. (Aa–c) The two-dimensional chemical structural formulas of PL, ZA and ANP. (d and e) The three-dimensional chemical structural formulas of PL, ZA and ANP. (B) Molecular docking of the combination of PL and ZA with JNK-1 or Erk-1 kinases. (C) Optimization of reaction conditions for enzymatic activity of the JNK-1/Erk-1 proteases. (D) HTRF assay of competitiveness of PL and ZA alone against ANP binding to JNK/Erk. (E) HTRF assay of competitiveness of the combined drugs against ANP binding to JNK/Erk. (F) BMMs were cultured with 30 ng/ml MCSF and 50 ng/ml RANKL with or without the combined drugs. The downstream expression of c-Jun/c-Fos/NFATc-1 was investigated via western blotting. The data are presented as the means±S.D. All experiments were repeated at least three times (**significant difference at P<0.05)