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Fig. 6 Coumestrol reduces tau phosphorylation levels and restores microtubule assembly in cell-free systems. (A) Turbidity increased over time (gray) when treated with the tau protein. Turbidity was reduced when co-treated with DYRK1A (green dashed line). Concomitant coumestrol treatment rescued the effect of DYRK1A treatment. (B) Phosphorylated (p)-tau levels were detected by Western blotting, and relative quantification was performed by normalizing p-tau to total tau. Coumestrol dose-dependently reduced p-tau levels.
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Reprinted from International journal of biological macromolecules, 282(Pt 4), Peng, C.H., Hwang, T.L., Hung, S.C., Tu, H.J., Tseng, Y.T., Lin, T.E., Lee, C.C., Tseng, Y.C., Ko, C.Y., Yen, S.C., Hsu, K.C., Pan, S.L., HuangFu, W.C., Identification, biological evaluation, and crystallographic analysis of coumestrol as a novel dual-specificity tyrosine-phosphorylation-regulated kinase 1A inhibitor, 136860, Copyright (2024) with permission from Elsevier. Full text @ Int. J. Biol. Macromol.