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IFI44 — IGF1

Text-mined interactions from Literome

Misawa et al., Cancer Res 2000 (Neuroblastoma) : Exogenous IGF-I induced phosphorylation and activation of extracellular signal regulated kinases p44/42 ( ERK1 and ERK2 ), with a maximal level 30 min after the stimulation ... The MEK1 inhibitor PD98059 reduced IGF-I mediated p44/42 MAPKs phosphorylation and produced a parallel reduction of IGF-I stimulated N-Myc induction
Flint et al., Domest Anim Endocrinol 2002 : But since IGF-I did not activate p42/p44 , a different MAP kinase, not detected by the antibody used here, is implicated
Li et al., Mol Cell Biochem 2002 (MAP Kinase Signaling System) : In both skeletal and cardiac muscle, des IGF-I increased the phosphorylation of Akt-1 at Ser 473 ( p < 0.01 ) with no change in the phosphorylation of p44 and p42 MAP kinases at Thr202/Tyr204
Boehm et al., Arthritis Rheum 2007 : Inhibition of Hsp90 with 100 nM or 500 nM geldanamycin blocked IGF-1 induced cell proliferation, Akt and p42/44 activation, and COL2A1 expression
Harwood et al., J Biol Chem 2008 (MAP Kinase Signaling System) : The effect of rapamycin on IGF-I or insulin activation of p44/42 was recapitulated by amino acid deprivation
Chenal et al., Eur J Neurosci 2008 : Investigation of the putative signalling pathways leading to translation activation revealed that insulin and IGF-1 induced p44- and p42 MAPK, Akt and mTOR phosphorylation
Madhala-Levy et al., J Cell Physiol 2012 (MAP Kinase Signaling System) : In cultures derived from Smo ( mut ) ( MCre ; Smo ( flox/flox ) ) mice lacking Smo expression specifically in hindlimb muscles, IGF-I induced Akt and p42/44 phosphorylation was significantly reduced compared to IGF-I 's effect on Smo ( cont ) cells ... In cultures derived from Smo ( mut ) ( MCre ; Smo ( flox/flox ) ) mice lacking Smo expression specifically in hindlimb muscles, IGF-I induced Akt and p42/44 phosphorylation was significantly reduced compared to IGF-I 's effect on Smo ( cont ) cells
Mendivil et al., Reprod Sci 2011 (Endometrial Neoplasms...) : Treatment with AMG 479 rapidly blocked IGF-1 induced phosphorylation of IFG-1-R, Akt, and p44/42
Blakesley et al., J Biol Chem 1998 : In addition, these mutant IGF-I receptors do not affect IGF-I stimulated p42/p44 mitogen activated protein kinase activation or phosphatidylinositol (PI) 3'-kinase activity