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. 2019 Nov 25;9:17496. doi: 10.1038/s41598-019-53695-0

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© The Author(s) 2019

Open Access 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 http://creativecommons.org/licenses/by/4.0/.

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The potentiation of cisplatin by perifosine and H89 was mediated by the functional inhibition of BAD protein. CellTiter96, MTS cell survival assays showing siRNA depletion of BAD protein did not affect the sensitivity of TNBC cells to cisplatin but reduced the sensitivity of (a) BT549 and (b) MDA468 to the AKT inhibitor, perifosine as well as the sensitivity of (c) BT549, and (d) MDA436 to the PKA inhibitor, H89. Western blots show depletion of BAD protein by siRNA. Histone H3 and GAPDH were used as loading controls.