Matches in Nanopublications for { ?s ?p "We further demonstrate that cav-1-stimulated Akt activities lead to increased phosphorylation of multiple Akt substrates, including GSK3, FKHR, and MDM2. The results in Fig. 9 demonstrated that the expression of cav1 significantly increased the phosphorylation of GSK3 (Ser9/21) (134%), FKHRL1 (Thr32) (47 to 80%), and MDM2 (Ser166) (78 to 81%) and marginally increased phosphorylation of BAD (Ser112) and IkappaB kinase alpha (IKK{alpha}) (Ser180)/IKKb (Ser181) but did not significantly alter phosphorylation of CREB (Ser133) and AFX (Ser193) under these conditions" ?g. }
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- _5 value "We further demonstrate that cav-1-stimulated Akt activities lead to increased phosphorylation of multiple Akt substrates, including GSK3, FKHR, and MDM2. The results in Fig. 9 demonstrated that the expression of cav1 significantly increased the phosphorylation of GSK3 (Ser9/21) (134%), FKHRL1 (Thr32) (47 to 80%), and MDM2 (Ser166) (78 to 81%) and marginally increased phosphorylation of BAD (Ser112) and IkappaB kinase alpha (IKK{alpha}) (Ser180)/IKKb (Ser181) but did not significantly alter phosphorylation of CREB (Ser133) and AFX (Ser193) under these conditions" provenance.
- _5 value "We further demonstrate that cav-1-stimulated Akt activities lead to increased phosphorylation of multiple Akt substrates, including GSK3, FKHR, and MDM2. The results in Fig. 9 demonstrated that the expression of cav1 significantly increased the phosphorylation of GSK3 (Ser9/21) (134%), FKHRL1 (Thr32) (47 to 80%), and MDM2 (Ser166) (78 to 81%) and marginally increased phosphorylation of BAD (Ser112) and IkappaB kinase alpha (IKK{alpha}) (Ser180)/IKKb (Ser181) but did not significantly alter phosphorylation of CREB (Ser133) and AFX (Ser193) under these conditions" provenance.
- _5 value "We further demonstrate that cav-1-stimulated Akt activities lead to increased phosphorylation of multiple Akt substrates, including GSK3, FKHR, and MDM2. The results in Fig. 9 demonstrated that the expression of cav1 significantly increased the phosphorylation of GSK3 (Ser9/21) (134%), FKHRL1 (Thr32) (47 to 80%), and MDM2 (Ser166) (78 to 81%) and marginally increased phosphorylation of BAD (Ser112) and IkappaB kinase alpha (IKK{alpha}) (Ser180)/IKKb (Ser181) but did not significantly alter phosphorylation of CREB (Ser133) and AFX (Ser193) under these conditions" provenance.
- _5 value "We further demonstrate that cav-1-stimulated Akt activities lead to increased phosphorylation of multiple Akt substrates, including GSK3, FKHR, and MDM2. The results in Fig. 9 demonstrated that the expression of cav1 significantly increased the phosphorylation of GSK3 (Ser9/21) (134%), FKHRL1 (Thr32) (47 to 80%), and MDM2 (Ser166) (78 to 81%) and marginally increased phosphorylation of BAD (Ser112) and IkappaB kinase alpha (IKK{alpha}) (Ser180)/IKKb (Ser181) but did not significantly alter phosphorylation of CREB (Ser133) and AFX (Ser193) under these conditions" provenance.
- _5 value "We further demonstrate that cav-1-stimulated Akt activities lead to increased phosphorylation of multiple Akt substrates, including GSK3, FKHR, and MDM2. The results in Fig. 9 demonstrated that the expression of cav1 significantly increased the phosphorylation of GSK3 (Ser9/21) (134%), FKHRL1 (Thr32) (47 to 80%), and MDM2 (Ser166) (78 to 81%) and marginally increased phosphorylation of BAD (Ser112) and IkappaB kinase alpha (IKK{alpha}) (Ser180)/IKKb (Ser181) but did not significantly alter phosphorylation of CREB (Ser133) and AFX (Ser193) under these conditions" provenance.
- _5 value "We further demonstrate that cav-1-stimulated Akt activities lead to increased phosphorylation of multiple Akt substrates, including GSK3, FKHR, and MDM2. The results in Fig. 9 demonstrated that the expression of cav1 significantly increased the phosphorylation of GSK3 (Ser9/21) (134%), FKHRL1 (Thr32) (47 to 80%), and MDM2 (Ser166) (78 to 81%) and marginally increased phosphorylation of BAD (Ser112) and IkappaB kinase alpha (IKK{alpha}) (Ser180)/IKKb (Ser181) but did not significantly alter phosphorylation of CREB (Ser133) and AFX (Ser193) under these conditions" provenance.