Gene interactions and pathways from curated databases and text-mining

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EPHB2 — NFKBIA

Text-mined interactions from Literome

Savkovic et al., Am J Physiol Gastrointest Liver Physiol 2001 (Inflammation...) : ERK1/2 inhibitors attenuated IkappaBalpha degradation and IL-8 expression
Jiang et al., J Biol Chem 2004 : Inhibition of ERK did not affect interleukin-1beta induced I-kappaBalpha phosphorylation and degradation but attenuated I-kappaBbeta degradation
Yeh et al., J Biol Chem 2004 : However, results of immunoblotting analysis showed that neither cisplatin nor MEK/ERK inhibitors induced marked IkappaBalpha degradation, suggesting that suppression of the MEK/ERK signaling pathway may enhance cisplatin induced NF-kappaB activation via mechanisms other than the conventional pathway
Matsubara et al., Biochem Pharmacol 2005 (MAP Kinase Signaling System) : PD98059, a MEK inhibitor, and BAY 11-8702, an I kappa B-alpha inhibitor, reduced ERK and NF-kappa B cascade activation, respectively, with little effect on PKC phosphorylation
Lubin et al., Neuroscience 2005 : Interestingly, inhibition of ERK but not PI3K blocked the kainate mediated increase in phospho-IkappaBalpha
Maeng et al., Cell Signal 2006 : Consistently, inhibition of ERK significantly increased IkappaB kinase (IKK) activity, IkappaBalpha phosphorylation, and nuclear translocation of NF-kappaB induced by VEGF, whereas overexpression of ERK resulted in the loss of these responses to VEGF
Singleton et al., Shock 2005 (MAP Kinase Signaling System...) : GLN given 1 h postsepsis led to inhibition of lung tissue NF-kappaB activation ( P < 0.001 vs. SP ), attenuated degradation of IKBalpha , and inhibited phosphorylation of p38 MAPK, and ERK , pathways critical for cytokine release
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
Kanayama et al., J Endotoxin Res 2007 : Here, we show that bikunin : ( i ) blocks LPS induced secretion of pro-inflammatory cytokines, including TNF-alpha and IL-1beta, in a dose dependent manner ; ( ii ) has an inhibitory effect on cytokine production at a concentration of 0.2 microM, reaching 65 % inhibition at the highest doses of bikunin tested ( 5 microM ) ; ( iii ) has the suppressive capacity of ERK1/2 and p38 signaling pathways ; and ( iv ) inhibited sequentially the LPS induced phosphorylation of IkappaB-alpha , degradation of IkappaB-alpha, and nuclear translocation of NF-kappaB
Adhikary et al., J Leukoc Biol 2008 (Corneal Diseases...) : We found that S. aureus and Pam3Cys stimulate phosphorylation of JNK, p38 MAPK, and ERK within 4 h and that blockade of JNK, but not p38 or ERK phosphorylation, had an inhibitory effect on IkBalpha degradation and CXC chemokine production
Thanislass et al., Vet Res Commun 2009 : Activation of ERK resulted in phosphorylation of IkappaB-alpha which lead to its degradation which in turn followed by nuclear translocation of NF-kappaB, which is also supported by the western blot analysis
Min et al., Int Immunopharmacol 2009 : 5-Hydroxyzerumbone, however, did not affect the degradation of IkappaB-alpha and the activation of p38 and ERK in LPS treated cells
Siggs et al., Proc Natl Acad Sci U S A 2010 (Immunologic Deficiency Syndromes) : Degradation of IkappaB alpha , which is considered a primary requirement for NEMO mediated immune signaling, occurred normally in response to Toll-like receptor stimulation, yet ERK phosphorylation and NF-kappaB p65 nuclear translocation were severely impaired
Chen et al., TheScientificWorldJournal 2010 : Blocking phosphorylation of ERK1/2 by MAPK inhibitors U0126 and PD98059, and inhibiting activation of NF-?B by IkappaB ( I?B ) kinase inhibitors wedelolactone or IMD-0354, abolished the DSP effects
Sonoda et al., J Biol Chem 1997 : Since OA-activated Erk1 phosphorylated recombinant IkappaB-alpha in vitro, we assumed that Erk1 is involved in the phosphorylation and subsequent degradation of IkappaB-alpha , thus leading to the activation of IL-8 gene transcription
Lee et al., Proc Natl Acad Sci U S A 1998 : We have previously shown that mitogen activated protein kinase/ERK kinase kinase 1 ( MEKK1 ) can induce both this site-specific phosphorylation of IkappaB alpha at Ser-32 and Ser-36 in vivo and the activity of a high molecular weight IkappaB kinase complex in vitro