Gene interactions and pathways from curated databases and text-mining

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IFI44 — TNF

Text-mined interactions from Literome

Engelman et al., Mol Endocrinol 2000 (Insulin Resistance) : These activation kinetics suggest a mechanism of p42/44 action more complicated than a direct phosphorylation of IRS-1 triggered by the early spike of TNFalpha induced p42/44 activity
Schröder et al., J Biol Chem 2001 : Phosphorylation of p42/44 correlated with an increase of activity, and tumor necrosis factor-alpha levels were significantly reduced by addition of inhibitors of p42/44 and p38, PD 98059 and SB 203580, respectively
Saijonmaa et al., J Vasc Res 2001 : TNF-alpha and IL-1beta activated p44/42 and p38 mitogen activated protein kinases ( MAPKs ) in HUVECs ; this was inhibited by the specific inhibitors of these kinases, PD98059 and SB202190, respectively
Hideshima et al., Oncogene 2001 (MAP Kinase Signaling System...) : In this study we demonstrate that tumor necrosis factor alpha (TNFalpha) triggers only modest proliferation, as well as p44/p42 mitogen activated protein kinase ( MAPK ) and NF-kappaB activation, in MM.1S multiple myeloma ( MM ) cells
Hsu et al., Cell Signal 2001 (MAP Kinase Signaling System) : Furthermore, overexpression of dominant negative mutants, H-Ras-15A and Raf-N4, significantly suppressed p42/p44 mitogen activated protein kinase ( MAPK ) activation induced by TNF-alpha and PDGF-BB and attenuated the effect of TNF-alpha on BK-induced IP response, indicating that Ras and Raf may be required for activation of these kinases
Liu et al., Acta Pharmacol Sin 2001 : TNF-alpha simultaneously activates p38 CCDPK and p44/42 CCDPK, and these two CCDPK signaling pathways appeared to play opposing roles in TNF-alpha induced apoptosis in BAEC
Niwa et al., Eur J Pharmacol 2003 : TNF-alpha induced the phosphorylation of p44/p42 mitogen activated protein ( MAP ) kinase and p38 MAP kinase
Suo et al., J Biol Chem 2003 (MAP Kinase Signaling System) : Mechanistic studies indicated that, in comparison with PAR1 signaling, prolonged increase of [ Ca2+ ] i and phosphorylation of p44/42 mitogen activated protein kinases, as well as NFkappaB activation may be responsible for PAR4AP induced TNF-alpha production in microglia
Lin et al., Cell Signal 2004 : This hypothesis was further supported by that TNF-alpha induced a transient activation of p42/p44 and p38 MAPKs in a time-and concentration dependent manner
Takada et al., J Immunol 2004 : Overall, our results demonstrate that Syk activation plays an essential role in TNF induced activation of JNK, p38 MAPK, p44/p42 MAPK, NF-kappaB, and apoptosis
Takada et al., J Biol Chem 2004 : Deletion of GSK-3beta also abolished TNF induced c-Jun N-terminal kinase and p44/p42 mitogen activated kinase activation
Hernandez et al., Diabetologia 2004 (Insulin Resistance) : Rosiglitazone ameliorates insulin resistance in brown adipocytes of Wistar rats by impairing TNF-alpha induction of p38 and p42/p44 mitogen activated protein kinases
Kralisch et al., Mol Cell Endocrinol 2005 : Moreover, p44/42 mitogen activated protein kinase appears to partly mediate the negative effect of insulin but not TNFalpha on ATGL
Kishida et al., Exp Clin Endocrinol Diabetes 2005 (Diabetic Nephropathies) : TNF-alpha activated the phosphorylation of p44/42 MAPK, p38 MAPK, SAPK/JNK and Akt in mesangial cells
Yasui et al., Cancer Res 2005 (Multiple Myeloma) : Finally, it down-regulates interleukin-6 induced phosphorylation of Akt, signal transducers and activators of transcription 3, and p42/44 mitogen activated protein kinase ; insulin-like growth factor-I triggered Akt phosphorylation ; and tumor necrosis factor alpha induced IkappaBalpha and nuclear factor-kappaB p65 phosphorylation
Sandra et al., Oral Oncol 2006 (Ameloblastoma...) : These results suggested that TNFalpha induced both cell survival and apoptosis pathways in ameloblastoma and potential of TNFalpha in inducing apoptosis can be improved by inhibiting TNFalpha induced Akt and p44/42 mitogen activated protein kinase ( MAPK ) cell survival pathways
Cheng et al., Environ Health Perspect 2006 : We examined the cells responsible for the excess production of Pb-increased LPS induced TNF-alpha and liver injury, and the roles of protein kinase C ( PKC ) and p42/44 mitogen activated protein kinase ( MAPK ) in the induction of TNF-alpha
Ahn et al., J Biol Chem 2006 : Further, the deletion of NQO1 abolished TNF induced c-Jun N-terminal kinase, Akt, p38, and p44/p42 mitogen activated protein kinase activation
Shi et al., Osteoarthritis Cartilage 2007 (Osteoarthritis) : Upon examination of the signaling components, we found that TNFalpha was a potent activator of p38, p44/42 , p54/46 MAPK, and IkappaBalpha ( IkappaBalpha )
Kesherwani et al., Cytokine 2007 : Quantitative role of p42/44 and p38 in the production and regulation of cytokines TNF-alpha , IL-1beta and IL-12 by murine peritoneal macrophages in vitro by concanavalin A ... In the present study the quantitative role of p42/44 and p38 in the production of TNF-alpha , IL-1beta and IL-12 by murine peritoneal macrophages, in vitro, on treatment with Concanavalin A ( ConA ) has been investigated ... The expression of TNF-alpha, IL-1beta and IL-12 was down regulated in the presence of PD98059 and SB202190 in a dose dependent manner, suggesting the involvement of p42/44 and p38 in ConA induced production of TNF-alpha , IL-1beta and IL-12 by macrophages
Sodhi et al., Glycoconj J 2007 : Pharmacological inhibitor of tyrosine kinase, PI3 kinase, protein kinase C, p42/44 , p38, JNK and intracellular calcium immobilizing agent down regulated the WGA induced expression of cytokines TNF-alpha , IL-1beta, IL-12 and IFN-gamma
Ahn et al., Cancer Res 2007 (Skin Neoplasms) : Deletion of NQO2 also abolished TNF induced c-Jun NH2-terminal kinase, Akt, p38, and p44/p42 mitogen activated protein kinase activation
Fakhrzadeh et al., Toxicol Appl Pharmacol 2008 (Pneumonia) : TNFalpha signaling involves PI-3-kinase (PI3K)/protein kinase B (PKB), and p44/42 MAP kinase (MAPK) which are important in NF-kappaB activation
Jiang et al., Infect Immun 2008 : It was shown that these three proteins could ( i ) induce expression of tumor necrosis factor alpha (TNF-alpha) and tissue factor and ( ii ) induce phosphorylation of p44/42 mitogen activated protein kinases ( MAPK ) and activation of early growth response factor 1 (Egr-1)
Zeng et al., J Hepatol 2009 (Reperfusion Injury) : In contrast, RAGE stimulated Egr-1 independent pathways regulate TNF-alpha production and apoptosis in response to I/R. Consistent with these findings, phospho-p44/42 and phospho-JNK MAPK and c-Jun were strikingly suppressed in RAGE ( -/- ) versus WT mice, but not in Egr-1 ( -/- ) mice
Eda et al., Rheumatol Int 2011 (MAP Kinase Signaling System) : IL-1ß and TNF-a activated the intracellular mitogen activated protein kinases ( MAPKs ) : p44/42 MAPK, p38, and c-Jun N-terminal kinase (JNK) as well as nuclear factor-?B ( NF-?B ) in osteoblasts
Waterman et al., Biochem Biophys Res Commun 1995 : Since we recently found that TNF-alpha stimulation of neutrophils does not increase the tyrosine phosphorylation or activation of the p42erk2 and p44erk1 mitogen activated protein kinases ( MAPKs ), the present studies demonstrate the involvement of a MAPK independent pathway in the phosphorylation and activation of cPLA2
Schwenger et al., J Biol Chem 1996 : Inhibition of tumor necrosis factor induced p42/p44 mitogen activated protein kinase activation by sodium salicylate ... Tumor necrosis factor (TNF) activates both p42 and p44 mitogen activated protein kinases ( MAPK ) in human FS-4 fibroblasts, cells for which TNF is mitogenic
Schwenger et al., Proc Natl Acad Sci U S A 1997 : In a previous study, we demonstrated that sodium salicylate ( NaSal ) selectively inhibits tumor necrosis factor (TNF) induced activation of the p42 and p44 mitogen activated protein kinases ( MAPKs ) ( known as extracellular signal regulated kinases )
Boone et al., FEBS Lett 1998 (Fibrosarcoma) : Activation of p42/p44 mitogen activated protein kinases ( MAPK ) and p38 MAPK by tumor necrosis factor (TNF) is mediated through the death domain of the 55-kDa TNF receptor