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. 2017 Nov 16;8:1529. doi: 10.1038/s41467-017-01671-5

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© The Author(s) 2017

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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Fig. 4 — Carolacton effects on the human enzyme hsMTHFD2. a IC₅₀ determination for carolacton against DH and CYH activity of hsMTHFD2. Data are presented as means ± s.e.m. of three independent replicates. IC₅₀s were obtained via logistic dose–response fitting. The one-way ANOVA test was used for statistical analysis, P < 0.01. b SPR analysis of carolacton binding to hsMTHFD2. Carolacton shows strong binding to hsMTHFD2. The estimated K _D was obtained by fitting the association and dissociation signals with a 1:1 interacton model using the Biacore X 100 Evaluation Software