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ach_2.11.1.3.2.source-code.input_example.csv Maven / Gradle / Ivy

PMC_ID,Sent_ID,Sentence,Paragraph
PMC2900437,1,"Lysates of U2OS cells transfected with HA-tagged B56γ3 or F395C were immunoprecipitated with anti-HA antibody, then analyzed by western blot against p53, Cyclin G, ERK, Sgo, PP2A A, HA, and vinculin (vinc) antibodies.","Mutant B56γ3 is unable to promote p53 Thr55 dephosphorylation. (A) Lysates of U2OS cells transfected with HA-tagged B56γ3, F395C, or Q392G/C398L (QC) mutant B56γ3, were either immunoprecipitated with anti-HA antibody, then analyzed by western blot against p53, PP2A A and C, HA, and vinculin (vinc) (left); or analyzed for p53 Thr55 phosphorylation, p21 protein levels, HA, p53, and vinculin (vinc) (right). Amino acid sequence of the p53-interaction domain of B56γ showing the cancer-derived F395C mutation is present on the top. (B) Lysates of U2OS cells transfected with empty vector control (EV), HA-tagged B56γ3, Q392G, C398L, Q392G/C398L (QC), or Q400S/Q401S (QQ) mutant B56γ3 were analyzed for p53 Thr55 phosphorylation, p21 protein levels, HA, p53, and vinculin (vinc). (C) Lysates of U2OS cells transfected with empty vector control (EV), HA-tagged B56γ3, or F395C mutant B56γ3 and either mock treated (M) or treated with ionizing radiation (IR) were analyzed for p53 Thr55 phosphorylation, HA, p53, and vinculin (vinc). (D) Lysates of U2OS cells transfected with varying amounts of HA-tagged F395C mutant B56γ3, were either mock (M) treated or treated with ionizing radiation (IR), then analyzed by western blot against endogenous (endo) and exogenous (exo) B56γ, as well as p53 and Thr55 phosphorylation. (E) Lysates of U2OS cells transfected with HA-tagged B56γ3 or F395C were immunoprecipitated with anti-HA antibody, then analyzed by western blot against p53, Cyclin G, ERK, Sgo, PP2A A, HA, and vinculin (vinc) antibodies."
PMC2920914,2,"Therefore, we checked Akt (Ser473) phosphorylation during myoblast differentiation. As2O3 (0.1–0.5 μM) significantly decreased the phosphorylation of Akt (Figure 5B) and its downstream targets, mTOR and p70s6k proteins, during myogenic differentiation in a dose-dependent manner Figure 6B).","Akt can substitute for PI3K in the stimulation of myogenesis, and it may be an essential downstream component of PI3K-induced muscle differentiation (Jiang et al. 1999). Therefore, we investigated the effects of As2O3 on the phosphorylation of Akt and its downstream signals, mTOR and p70s6k, during myogenic differentiation. Moreover, Gonzalez et al. (2004) demonstrated that, during myoblast differentiation, Akt kinase activity correlated with Ser473 but not Thr308 phosphorylation. Therefore, we checked Akt (Ser473) phosphorylation during myoblast differentiation. As shown in Figure 5B, Akt protein phosphorylation was gradually activated during myogenic differentiation. As2O3 (0.1–0.5 μM) significantly decreased the phosphorylation of Akt (Figure 5B) and its downstream targets, mTOR and p70s6k proteins, during myogenic differentiation in a dose-dependent manner Figure 6B). These results imply that As2O3 inhibits myogenic differentiation by inhibiting an Akt-related pathway."