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Matches in Nanopublications for { ?s ?p "identified four sites (Ser-124, Thr-308, Thr-450, and Ser-473) on Akt1 that are phosphorylated in vivo. Thr-308 and Ser-473 are inducibly phosphorylated after treatment of cells with extracellular stimuli, whereas Ser-124 and Thr-450 appear to be basally phosphorylated The third mechanism by which 3'-phosphorylated phosphoinositides regulate Akt activity is by controlling the accessibility of Akt as a substrate for PDKs. In in vitro reconstitution assays, the binding of PI3,4,5P to the Akt PH domain is required for PDK-1 to phosphorylate Akt In addition, PDK-1 complexed with either a fragment of PRK2, PRK2, or a PRK2-related peptide may be regulated by increased phospholipid concentrations" ?g. }

• _5 value "identified four sites (Ser-124, Thr-308, Thr-450, and Ser-473) on Akt1 that are phosphorylated in vivo. Thr-308 and Ser-473 are inducibly phosphorylated after treatment of cells with extracellular stimuli, whereas Ser-124 and Thr-450 appear to be basally phosphorylated The third mechanism by which 3'-phosphorylated phosphoinositides regulate Akt activity is by controlling the accessibility of Akt as a substrate for PDKs. In in vitro reconstitution assays, the binding of PI3,4,5P to the Akt PH domain is required for PDK-1 to phosphorylate Akt In addition, PDK-1 complexed with either a fragment of PRK2, PRK2, or a PRK2-related peptide may be regulated by increased phospholipid concentrations" provenance.
• _6 value "identified four sites (Ser-124, Thr-308, Thr-450, and Ser-473) on Akt1 that are phosphorylated in vivo. Thr-308 and Ser-473 are inducibly phosphorylated after treatment of cells with extracellular stimuli, whereas Ser-124 and Thr-450 appear to be basally phosphorylated The third mechanism by which 3'-phosphorylated phosphoinositides regulate Akt activity is by controlling the accessibility of Akt as a substrate for PDKs. In in vitro reconstitution assays, the binding of PI3,4,5P to the Akt PH domain is required for PDK-1 to phosphorylate Akt In addition, PDK-1 complexed with either a fragment of PRK2, PRK2, or a PRK2-related peptide may be regulated by increased phospholipid concentrations" provenance.
• _6 value "identified four sites (Ser-124, Thr-308, Thr-450, and Ser-473) on Akt1 that are phosphorylated in vivo. Thr-308 and Ser-473 are inducibly phosphorylated after treatment of cells with extracellular stimuli, whereas Ser-124 and Thr-450 appear to be basally phosphorylated The third mechanism by which 3'-phosphorylated phosphoinositides regulate Akt activity is by controlling the accessibility of Akt as a substrate for PDKs. In in vitro reconstitution assays, the binding of PI3,4,5P to the Akt PH domain is required for PDK-1 to phosphorylate Akt In addition, PDK-1 complexed with either a fragment of PRK2, PRK2, or a PRK2-related peptide may be regulated by increased phospholipid concentrations" provenance.
• _6 value "identified four sites (Ser-124, Thr-308, Thr-450, and Ser-473) on Akt1 that are phosphorylated in vivo. Thr-308 and Ser-473 are inducibly phosphorylated after treatment of cells with extracellular stimuli, whereas Ser-124 and Thr-450 appear to be basally phosphorylated The third mechanism by which 3'-phosphorylated phosphoinositides regulate Akt activity is by controlling the accessibility of Akt as a substrate for PDKs. In in vitro reconstitution assays, the binding of PI3,4,5P to the Akt PH domain is required for PDK-1 to phosphorylate Akt In addition, PDK-1 complexed with either a fragment of PRK2, PRK2, or a PRK2-related peptide may be regulated by increased phospholipid concentrations" provenance.
• _6 value "identified four sites (Ser-124, Thr-308, Thr-450, and Ser-473) on Akt1 that are phosphorylated in vivo. Thr-308 and Ser-473 are inducibly phosphorylated after treatment of cells with extracellular stimuli, whereas Ser-124 and Thr-450 appear to be basally phosphorylated The third mechanism by which 3'-phosphorylated phosphoinositides regulate Akt activity is by controlling the accessibility of Akt as a substrate for PDKs. In in vitro reconstitution assays, the binding of PI3,4,5P to the Akt PH domain is required for PDK-1 to phosphorylate Akt In addition, PDK-1 complexed with either a fragment of PRK2, PRK2, or a PRK2-related peptide may be regulated by increased phospholipid concentrations" provenance.
• _6 value "identified four sites (Ser-124, Thr-308, Thr-450, and Ser-473) on Akt1 that are phosphorylated in vivo. Thr-308 and Ser-473 are inducibly phosphorylated after treatment of cells with extracellular stimuli, whereas Ser-124 and Thr-450 appear to be basally phosphorylated The third mechanism by which 3'-phosphorylated phosphoinositides regulate Akt activity is by controlling the accessibility of Akt as a substrate for PDKs. In in vitro reconstitution assays, the binding of PI3,4,5P to the Akt PH domain is required for PDK-1 to phosphorylate Akt In addition, PDK-1 complexed with either a fragment of PRK2, PRK2, or a PRK2-related peptide may be regulated by increased phospholipid concentrations" provenance.
• _5 value "identified four sites (Ser-124, Thr-308, Thr-450, and Ser-473) on Akt1 that are phosphorylated in vivo. Thr-308 and Ser-473 are inducibly phosphorylated after treatment of cells with extracellular stimuli, whereas Ser-124 and Thr-450 appear to be basally phosphorylated The third mechanism by which 3'-phosphorylated phosphoinositides regulate Akt activity is by controlling the accessibility of Akt as a substrate for PDKs. In in vitro reconstitution assays, the binding of PI3,4,5P to the Akt PH domain is required for PDK-1 to phosphorylate Akt In addition, PDK-1 complexed with either a fragment of PRK2, PRK2, or a PRK2-related peptide may be regulated by increased phospholipid concentrations" provenance.
• _6 value "identified four sites (Ser-124, Thr-308, Thr-450, and Ser-473) on Akt1 that are phosphorylated in vivo. Thr-308 and Ser-473 are inducibly phosphorylated after treatment of cells with extracellular stimuli, whereas Ser-124 and Thr-450 appear to be basally phosphorylated The third mechanism by which 3'-phosphorylated phosphoinositides regulate Akt activity is by controlling the accessibility of Akt as a substrate for PDKs. In in vitro reconstitution assays, the binding of PI3,4,5P to the Akt PH domain is required for PDK-1 to phosphorylate Akt In addition, PDK-1 complexed with either a fragment of PRK2, PRK2, or a PRK2-related peptide may be regulated by increased phospholipid concentrations" provenance.