IndraLab

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IGF1R activates IRS1. 10 / 44
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"Clemmons et al. have shown that, under normoglycemic conditions, stimulation of the IGF-IR expressed on vascular smooth muscle cells and vascular endothelial cells only activates IRS-1 leading to stimulation of the " metabolic " (phosphoinositide 3) PI-3 kinase pathway, but not to stimulation of the " mitogenic " (mitogen activated protein) MAP kinase pathway."
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"The knock-down of ARID1A increased IGF-1R levels, prevented IGF-1R and IRS1 suppression upon Bex+Carv and stimulated proliferation."
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"Binding of IGF1 to its receptor leads to activation of its intrinsic tyrosine kinase and autophosphorylation, thus generating docking sites for insulin receptor substrate (IRS), which is also phosphorylated by the IGF1 receptor."
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"This review discusses recently published data regarding the ability of hyperglycemia to sensitize cells that are capable of dedifferentiating to the growth promoting effects of IGF-I. Under normoglycemic conditions vascular smooth muscle and endothelial cells are cystostatic and stimulation of the IGF-I receptor activates the adaptor protein IRS-1 which leads to PI-3 kinase pathway activation."
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"Furthermore, IGF-1 stimulates tyrosine phosphorylation of insulin receptor substrate-1 (IRS-1) and IRS-2 and their association with the p85 subunit of phosphoinositide-3 kinase (PI3K)."
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"IGF-I binding to its receptor activates the kinase activity of the receptor, which then recruits the insulin response substrate-1, causing activation of phosphatidyl-inositol-3 kinase (PI3K) to phosphorylate Akt."
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"The inhibition of IGF-IR by siRNA and PPP downregulated pIRS-1, pAKT, and pSTAT3 and induced caspase-3 cleavage in MCL."
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"Furthermore, IGF-1 stimulates tyrosine phosphorylation of insulin receptor substrate-1 (IRS-1) and IRS-2 and their association with the p85 subunit of phosphoinositide-3 kinase (PI3K)."
17827393
signor
"Furthermore, IGF-1 stimulates tyrosine phosphorylation of insulin receptor substrate-1 (IRS-1) and IRS-2 and their association with the p85 subunit of phosphoinositide-3 kinase (PI3K)."
17827393
sparser
"Another study from the same group [ xref ] established that phosphorylation of AKT on Thr308 and Ser473 increases following treatment of ALL cells with AICAR and demonstrated that AKT phosphorylation on Thr 308 is mediated by AMPK-induced IGF-1R activation and phosphorylation of IRS-1."
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IGF1R phosphorylated on Y1166 activates IRS1. 1 / 1
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"We have studied the effect of double tyrosine mutations on IGF-I induced receptor autophosphorylation, activation of Shc and IRS-1 pathways, and cell proliferation and tumorigenicity. Substitution of tyrosines 1131/1135 blocks any detectable autophosphorylation, whereas substitution of tyrosines 1131/1136 or 1135/1136 only reduces autophosphorylation levels in some clones by approximately 50%. Nevertheless, all the cells expressing IGF-I receptors with double tyrosine substitutions demonstrated markedly reduced signaling through Shc and IRS-1 pathways. "
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IGF1R activates tyrosine-phosphorylated IRS1. 1 / 1
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"While tyrosine phosphorylated IRS-1 is activated by IGF-IR, phosphorylation of IRS-1 on serine/threonine by multiple kinases including JNK [37], IKK [38], Rho Kinase [39], PKC xi [40] and PI3K/Akt/mam[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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