Gene interactions and pathways from curated databases and text-mining

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AKT1 — TNFSF11

Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

Text-mined interactions from Literome

Wong et al., Mol Cell 1999 : TRANCE , a TNF family member, activates Akt/PKB through a signaling complex involving TRAF6 and c-Src ... Here, we demonstrate that TRANCE activates the antiapoptotic serine/threonine kinase Akt/PKB through a signaling complex involving c-Src and TRAF6 ... A deficiency in c-Src or addition of Src family kinase inhibitors blocks TRANCE mediated PKB activation in osteoclasts
Lee et al., Bone 2002 : The RANKL stimulated phosphorylation of Akt , a downstream target of PI 3-kinase, and that of ERK were observed
Zhang et al., J Immunol 2003 : In addition, SHP-1 regulated RANKL stimulated tyrosine phosphorylation of p85 subunit of phosphatidylinositol 3 kinase and the phosphorylation of Akt
Saito et al., J Biol Chem 2004 (Bacterial Infections...) : r4-1BB showed no effects on M-CSF- or RANKL induced phosphorylation of I-kappaB, ERK1/2, p38, or JNK, whereas RANKL induced phosphorylation of Akt , a downstream target of phosphatidylinositol 3-kinase (PI3K), was completely abolished by r4-1BB, suggesting that 4-1BB/4-1BBL reverse signaling may interfere with PI3K/Akt pathway
Kwak et al., Biochem Pharmacol 2004 (Bone Resorption) : M-CSF and RANKL activate the ERK, Akt , and NF-kappaB signal transduction pathways, and SCOH suppressed this activation
Kim et al., Biochem Pharmacol 2004 (Bone Resorption) : RANKL activated the ERK, Akt , and NF-kappaB signal transduction pathways in osteoclast precursor cells, and tanshinone IIA suppressed this activation
Wang et al., J Clin Invest 2004 : In particular, ritonavir is found to inhibit RANKL induced Akt signaling by disrupting the recruitment of TNF receptor associated factor 6/c-Src complex to lipid rafts
Ha et al., Exp Cell Res 2004 : Pretreatment of osteoclasts with the antioxidants N-acetyl-l-cystein and glutathione reduced RANKL induced Akt , NF-kappaB, and ERK activation
Min et al., Blood 2007 (Neovascularization, Pathologic) : RANKL also led to the activation of Akt and eNOS and to NO production in endothelial cells ( ECs )
Kim et al., Mol Pharmacol 2007 (Calcium Signaling) : On the other hand, DMS strongly inhibited two separate signaling pathways, the RANKL induced activation of ERK and Akt , which eventually converged on the transcription factors c-Fos and NFATc1
Li et al., J Ethnopharmacol 2007 (Bone Resorption) : CE-C suppressed the activation of extracellular signal regulated kinase ( ERK ), protein kinase B ( PKB/Akt ) and inhibitor of kappa B ( I-kappaB ) by RANKL in osteoclast precursor cells
Mozar et al., J Cell Physiol 2008 (Bone Resorption) : Pi was found to specifically inhibit the RANKL induced JNK and Akt activation , while RANKL induced p38 and ERK 1/2 phosphorylation were not significantly affected
Hu et al., Eur J Pharmacol 2008 : RANKL induced Akt phosphorylation was strongly inhibited by berberine ; however, neither monocyte/macrophage-colony stimulating factor ( M-CSF ) -induced nor insulin induced Akt activation was inhibited by the drug
McGonigle et al., Angiogenesis 2009 : Signaling studies showed that OPG induced ERK1/2 and Akt phosphorylation in HUVECs while RANKL had no effect
Fumimoto et al., J Pharmacol Sci 2012 : Kahweol completely abolished RANKL stimulated phosphorylation of extracellular signal regulated kinase and impaired phosphorylation of Akt
Hemingway et al., Exp Mol Pathol 2013 : We found that both RANKL and LIGHT strongly induced phosphorylation of Akt and NF?B but not JNK in mouse osteoclast precursor cells
Li et al., Biochem Biophys Res Commun 2013 : AG490 had no effects on RANKL induced activation of Akt , ERK1/2
Hwang et al., Life Sci 2013 : We observed suppression of ERK, JNK, AKT , and p38 mitogen activated protein kinases induced by RANKL in Western blotting after BPA treatment in RAW 264.7 cells