Matches in Nanopublications for { ?s ?p "The best characterized of the AGC kinases is phosphoinositide-dependent kinase 1 (PDK1), one of the serine kinases that phosphorylates and activates the serine/threonine kinase Akt/PKB37. Akt possesses a PH domain that also interacts directly with PtdIns(3,4,5)P3, promoting membrane targeting of the protein and catalytic activation. Akt has been suggested to be important in transmission of the insulin signal, by phosphorylation of the enzyme GSK-3 (see below), the forkhead transcription factors and cAMP response element-binding protein" ?g. }
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- _5 value "The best characterized of the AGC kinases is phosphoinositide-dependent kinase 1 (PDK1), one of the serine kinases that phosphorylates and activates the serine/threonine kinase Akt/PKB37. Akt possesses a PH domain that also interacts directly with PtdIns(3,4,5)P3, promoting membrane targeting of the protein and catalytic activation. Akt has been suggested to be important in transmission of the insulin signal, by phosphorylation of the enzyme GSK-3 (see below), the forkhead transcription factors and cAMP response element-binding protein" provenance.
- _5 value "The best characterized of the AGC kinases is phosphoinositide-dependent kinase 1 (PDK1), one of the serine kinases that phosphorylates and activates the serine/threonine kinase Akt/PKB37. Akt possesses a PH domain that also interacts directly with PtdIns(3,4,5)P3, promoting membrane targeting of the protein and catalytic activation. Akt has been suggested to be important in transmission of the insulin signal, by phosphorylation of the enzyme GSK-3 (see below), the forkhead transcription factors and cAMP response element-binding protein" provenance.
- _5 value "The best characterized of the AGC kinases is phosphoinositide-dependent kinase 1 (PDK1), one of the serine kinases that phosphorylates and activates the serine/threonine kinase Akt/PKB37. Akt possesses a PH domain that also interacts directly with PtdIns(3,4,5)P3, promoting membrane targeting of the protein and catalytic activation. Akt has been suggested to be important in transmission of the insulin signal, by phosphorylation of the enzyme GSK-3 (see below), the forkhead transcription factors and cAMP response element-binding protein" provenance.
- _5 value "The best characterized of the AGC kinases is phosphoinositide-dependent kinase 1 (PDK1), one of the serine kinases that phosphorylates and activates the serine/threonine kinase Akt/PKB37. Akt possesses a PH domain that also interacts directly with PtdIns(3,4,5)P3, promoting membrane targeting of the protein and catalytic activation. Akt has been suggested to be important in transmission of the insulin signal, by phosphorylation of the enzyme GSK-3 (see below), the forkhead transcription factors and cAMP response element-binding protein" provenance.