Fig 2: IPA-3 treatment reduces p38 phosphorylation during Mabs and C2C12 differentiation. Representative western blot revealing total p38, p-p38, and myogenin expression in crude protein extracts from IPA-3 treated or control Mabs (A) and C2C12 (D) during 5 days of myogenic differentiation. ß-Tubulin, vinculin, or actin are used as loading controls. The bar graphs illustrate the ratio between p-p38 and total p38 signals during Mabs (B) or C2C12 (E) differentiation, as determined by the densitometric quantitation of western blots such as the one in panel A and D. The bar graphs represent the densitometric quantitation of myogenin expression for Mabs (C) and C2C12 (F). The values are mean of at least three independent experiments + SEM. Statistical significance was evaluated by the unpaired t-test, *P = 0.05, **P = 0.01, ****P = 0.0001. Mabs, mesoangioblasts.

Fig 3: ARRDC4 enhances EV71-triggered activation of NF-?B and MAPK pathway. The t-MØ were transfected with ARRDC4-specific siRNA or the negative control siRNA. After 48 h, the cells were infected with EV71 for indicated time, then total and phosphor-JNK, -ERK, -p38, -p65, -IRF3 and total I?Ba were detected with immunoblot, the expression of EV71-VP1 and ß-actin were detected as well. Data are representative of three independent experiments with similar results

Fig 4: Expression of EphA5, IGFBP5 and H2BK in cultured human non-stem GBM cell lines and primary cultures, and analysis of a Temozolomide (TMZ)-induced cellular dormant state in different GBM cultures(A) Cultured human glioma cell lines and primary cultures were analysed by qRT-PCR and Western Blot regarding the mRNA and protein expression of EphA5, IGFBP5 and H2BK (?CT 3.3 = 10-fold expression difference; black highlighted primary cultures correspond to solid GBM samples in Figure 1A). (B and C) GBM cells were stimulated with 500 µM TMZ or 0.2% DMSO (control) for 10 days, and the dormant state was analysed by monitoring dye retention at day 10 using combined transmitted-light and fluorescence microscopy (B), and determination of phospho-p38 / phospho-p42/44 ratios by Western Blot and subsequent densitometric analysis comparing DMSO and TMZ treated samples (C).

Fig 5: Kinases activation mediates cisplatin-induced Bmal1 expression.a Western blot analyses of AKT, ERK1/2, P38, and JNK phosphorylation in HK-2 cells treated with 20 µM cisplatin for 24 h. b Quantitative analyses of a. n = 3, **P < 0.01 vs. CTL group. c, d RT-qPCR and western blot analyses of BMAL1 expression in HK-2 cells treated with 20 µM cisplatin alone or in combinations of various signaling pathway inhibitors for 24 h. n = 3, **P < 0.01 vs. vehicle group, #P < 0.05 and ##P < 0.01 vs. cisplatin alone group. e Quantitative analysis of panel d. n = 3, **P < 0.01 vs. vehicle group, ##P < 0.01 cisplatin + inhibitor vs. cisplatin alone group. All values are presented as the mean ± SD. Concentrations: U0126, 10 µM; SB203580, 10 µM; SP600125, 10 µM.