Nanopublications LDF server

Matches in Nanopublications for { ?s ?p "enhanced proliferation of KMS-11. bFGF but not IL-6 stimu- lation induces the phosphorylation of Ser727 in STAT3, and a selective MEK1/2 inhibitor abolishes the serine- but not tyrosine-phosphorylation of STAT3 in response to bFGF and IL-6 stimulations, supportingthe notion that two independent signaling pathways converge on STAT3 to regulate its func- tion in the cell. Thus, the bFGF-induced activation of ERK1/ 2 pathway is involved in the phosphorylation of the critical serine residue of STAT3 " ?g. }

• _4 value "enhanced proliferation of KMS-11. bFGF but not IL-6 stimu- lation induces the phosphorylation of Ser727 in STAT3, and a selective MEK1/2 inhibitor abolishes the serine- but not tyrosine-phosphorylation of STAT3 in response to bFGF and IL-6 stimulations, supportingthe notion that two independent signaling pathways converge on STAT3 to regulate its func- tion in the cell. Thus, the bFGF-induced activation of ERK1/ 2 pathway is involved in the phosphorylation of the critical serine residue of STAT3 " provenance.
• _5 value "enhanced proliferation of KMS-11. bFGF but not IL-6 stimu- lation induces the phosphorylation of Ser727 in STAT3, and a selective MEK1/2 inhibitor abolishes the serine- but not tyrosine-phosphorylation of STAT3 in response to bFGF and IL-6 stimulations, supportingthe notion that two independent signaling pathways converge on STAT3 to regulate its func- tion in the cell. Thus, the bFGF-induced activation of ERK1/ 2 pathway is involved in the phosphorylation of the critical serine residue of STAT3 " provenance.
• _5 value "enhanced proliferation of KMS-11. bFGF but not IL-6 stimu- lation induces the phosphorylation of Ser727 in STAT3, and a selective MEK1/2 inhibitor abolishes the serine- but not tyrosine-phosphorylation of STAT3 in response to bFGF and IL-6 stimulations, supportingthe notion that two independent signaling pathways converge on STAT3 to regulate its func- tion in the cell. Thus, the bFGF-induced activation of ERK1/ 2 pathway is involved in the phosphorylation of the critical serine residue of STAT3 " provenance.
• _5 value "enhanced proliferation of KMS-11. bFGF but not IL-6 stimu- lation induces the phosphorylation of Ser727 in STAT3, and a selective MEK1/2 inhibitor abolishes the serine- but not tyrosine-phosphorylation of STAT3 in response to bFGF and IL-6 stimulations, supportingthe notion that two independent signaling pathways converge on STAT3 to regulate its func- tion in the cell. Thus, the bFGF-induced activation of ERK1/ 2 pathway is involved in the phosphorylation of the critical serine residue of STAT3 " provenance.
• _5 value "enhanced proliferation of KMS-11. bFGF but not IL-6 stimu- lation induces the phosphorylation of Ser727 in STAT3, and a selective MEK1/2 inhibitor abolishes the serine- but not tyrosine-phosphorylation of STAT3 in response to bFGF and IL-6 stimulations, supportingthe notion that two independent signaling pathways converge on STAT3 to regulate its func- tion in the cell. Thus, the bFGF-induced activation of ERK1/ 2 pathway is involved in the phosphorylation of the critical serine residue of STAT3 " provenance.
• _5 value "enhanced proliferation of KMS-11. bFGF but not IL-6 stimu- lation induces the phosphorylation of Ser727 in STAT3, and a selective MEK1/2 inhibitor abolishes the serine- but not tyrosine-phosphorylation of STAT3 in response to bFGF and IL-6 stimulations, supportingthe notion that two independent signaling pathways converge on STAT3 to regulate its func- tion in the cell. Thus, the bFGF-induced activation of ERK1/ 2 pathway is involved in the phosphorylation of the critical serine residue of STAT3 " provenance.
• _5 value "enhanced proliferation of KMS-11. bFGF but not IL-6 stimu- lation induces the phosphorylation of Ser727 in STAT3, and a selective MEK1/2 inhibitor abolishes the serine- but not tyrosine-phosphorylation of STAT3 in response to bFGF and IL-6 stimulations, supportingthe notion that two independent signaling pathways converge on STAT3 to regulate its func- tion in the cell. Thus, the bFGF-induced activation of ERK1/ 2 pathway is involved in the phosphorylation of the critical serine residue of STAT3 " provenance.
• _4 value "enhanced proliferation of KMS-11. bFGF but not IL-6 stimu- lation induces the phosphorylation of Ser727 in STAT3, and a selective MEK1/2 inhibitor abolishes the serine- but not tyrosine-phosphorylation of STAT3 in response to bFGF and IL-6 stimulations, supportingthe notion that two independent signaling pathways converge on STAT3 to regulate its func- tion in the cell. Thus, the bFGF-induced activation of ERK1/ 2 pathway is involved in the phosphorylation of the critical serine residue of STAT3 " provenance.