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. 2021 Mar 2;11:46. doi: 10.1186/s13578-021-00558-9

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© The Author(s) 2021

Open AccessThis 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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Fig. 5 — 0025A competitively replaces Bodipy-cyclopamine binding to wild-type Smo and mutant Smo-D473H. a Competitive binding of Bodipy-cyclopamine to wild-type Smo with different concentration of Smo antagonists: 0025A, GDC-0449 (GDC), cyclopamine (Cyc). The Bodipy-cyclopamine competitive assay was performed in HEK293 cells transiently transfected with human wild-type Smo. b Competitive binding of Bodipy-cyclopamine to mutant Smo with 10^–6 M (1 μM) Smo antagonists. The Bodipy-cyclopamine competitive assay was performed in HEK293 cells transiently transfected with human mutant Smo-D473H. The results of Bodipy-cyclopamine binding (green) were analyzed by flow-cytometry. All data are means ± SEM (student’s t-test). **P < 0.01, ***P < 0.001