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- _5 wasQuotedFrom 16621671 provenance.
- _5 value "Ligand binding to the extracellular subunits leads to activation of the intrinsic tyrosine kinases of the transmembrane subunits. The ATP-binding site at Lys1003 and the tyrosine kinase domain are required for all functions of the IGF-IR. Trans-phosphorylation between the subunits involves Tyr1131, 1135 and 1136 in the kinase domain and leads to full activation of kinase activity. Other tyrosine phosphorylated sites serve to recruit specific adaptor molecules via their SH2-binding domains. Phosphorylated Tyr950 in the juxtamembrane region serves as a docking site for the adaptor molecules insulin receptor substrate (IRS)-1 and Shc which are involved in activation of the phosphatidylinositol-3 kinase (PI3K) and MAPK/ERK kinase(MEK)-extracellular-regulated kinase (ERK)signaling pathways, respectively" provenance.