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EPHB2 — SYT1

Text-mined interactions from Literome

Hu et al., Carcinogenesis 2004 (Cell Transformation, Neoplastic) : Here we show that TNF-alpha induces greater ERK dependent p65 phosphorylation at S536 in transformation sensitive ( P+ ) cells than in P- cells
Ha et al., J Immunol 2007 : Moreover, IkappaB kinase (IKK) alpha and IKKbeta are distinctly involved in MUC5AC induction via an ERK1 dependent , but IkappaBalpha-p65- and p100-p52 independent, mechanism, thereby revealing novel roles for IKKs in mediating up-regulation of MUC5AC mucin by S. pneumoniae
Chen et al., J Cell Biochem 2008 (Hypertrophy...) : Furthermore, ERK inhibitors ( U0126 and PD98059 ) suppressed LPA stimulated activation of NF-kappaB and p65 phosphorylation whereas wortmannin showed no effect on NF-kappaB activation
Joo et al., J Biol Chem 2008 (Lung Neoplasms) : Our results indicate that the induction of inflammatory genes by farnesol is mediated by the activation of the NF-kappaB pathway and involves MEK1/2-ERK1/2-MSK1 dependent phosphorylation of p65/RelA ( Ser ( 276 ) )
Wiesner et al., Circ Res 2010 (Atherosclerosis...) : In a nuclear factor-DNA binding assay, the cooperative effect of mmLDL and LPS costimulation on c-Jun and c-Fos DNA binding, but not on p65 or p50, was dependent on mmLDL induced activation of extracellular signal regulated kinase ( ERK ) 1/2
Peirce et al., PloS one 2010 : Moreover, LPS induced activation of the MAP kinases ERK and p38 was enhanced in cells over expressing Themis2 whereas the activation of JNK, IRF3 or NF-kappaB p65 , was unaffected
Choi et al., J Biol Chem 2010 : Both primary intestinal epithelial cells from TRIF-KO mice and TRIF silenced NCM460 cells significantly reduced flagellin induced NF?B ( p105 and p65 ), JNK1/2, and ERK1/2 activation compared with control cells
Qi et al., Front Biosci (Elite Ed) 2012 (Reperfusion Injury) : Moreover, the phosphorylation of AKT and ERK1/2 in the liver was enhanced , while the phosphorylation of JNK, p38 and p65 was suppressed
Liu et al., Hum Immunol 2012 (Inflammation...) : ERK inhibitor blocked the interaction of PARP-1 with ERK1/2, phosphorylation of PARP-1, and poly ( ADP-ribosyl ) ation of p65 , suggesting that ERK dependent phosphorylation of PARP-1 regulates PARP-1 activity and NF-?B activation
Qing et al., Arch Toxicol 2013 (MAP Kinase Signaling System...) : JNK and ERK inhibition also induced I?Ba degradation and NF-?B p65 translocation, leading to expression of Bcl-2 and XIAP