Gene interactions and pathways from curated databases and text-mining

◀ Back to EPHB2

CPD — EPHB2

Text-mined interactions from Literome

Wang et al., J Cell Physiol 2000 : Both EGF and Cpd 5 caused an induction of phospho-extracellular response kinase (ERK) , which was also more sustained with Cpd 5 ... Moreover, whereas Cpd 5 induced a striking translocation of phosphorylated ERK from cytosol to the nucleus, no significant nuclear translocation occurred after stimulation with EGF
Kar et al., J Cell Physiol 2002 : U0126 and PD 098059, specific inhibitors of MEK1/2, the ERK1/2 kinases, antagonized both cell growth inhibition and ERK1/2 phosphorylation mediated by Cpd5
Adachi et al., J Cell Physiol 2002 : Furthermore, Cpd 5 action caused a strong nuclear phospho-ERK signal and induced phospho-Elk-1, a nuclear target of ERK activation, in contrast to the weak effects of EGF ... The MEK inhibitors PD098056 and U0126 abrogated both the induction by Cpd 5 of phospho-ERK , its nuclear translocation and phospho-Elk-1 and also antagonized its growth inhibitory effects
Carr et al., J Cell Physiol 2002 (Carcinoma, Hepatocellular) : Cpd 5 could activate ERK1/2 either by signaling from an activated EGFR, which is upstream in the signaling cascade, or by direct inhibition of ERK1/2 phosphatase ( s ) ... The growth inhibitory effect during liver regeneration and transplantable tumor growth is also correlated with ERK1/2 phosphorylation induced by Cpd 5
Wang et al., J Cell Physiol 2005 : We now report that Cpd 5 can directly cause ERK phosphorylation by inhibiting Cdc25A activity independently of the EGFR pathway ... In EGFR-devoid NR6 fibroblasts and MEK ( ERK kinase ) mutated MCF7 cells, Cpd 5 treatment also resulted in ERK phosphorylation, providing support for the idea that Cpd 5 can directly act on ERK phosphorylation by inhibiting Cdc25A activity
Wang et al., J Cell Physiol 2006 (Carcinoma, Hepatocellular...) : We previously showed that prolonged and strong ERK phosphorylation induced by Compound 5 (Cpd 5) , a Cdc25A protein phosphatase inhibitor, was involved in its mechanism of cell growth inhibition