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STAT3 phosphorylated on Y705 is transcriptionally active. 19 / 19
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"We found that the Tyr701 phosphorylation kinetics of Stat1 mediated by IFN stimulation was higher when cells were incubated with IFN-alpha5 than when using IFN-alpha2. Similarly, Tyr(1054/1055) phosphorylation kinetics of Tyk2 were more intense after exposure to IFN-alpha5 than when using IFN-alpha2. Concomitantly, Tyr705 phosphorylation of Stat3 was higher after stimulation with IFN-alpha5 than with IFN-alpha2."

"Signal transducer and activator of transcription 3 (STAT3) is activated by the IL-6 family of cytokines and growth factors. STAT3 requires phosphorylation on Ser-727, in addition to tyrosine phosphorylation on Tyr-705, to be transcriptionally active."

"We found that the Tyr701 phosphorylation kinetics of Stat1 mediated by IFN stimulation was higher when cells were incubated with IFN-alpha5 than when using IFN-alpha2. Similarly, Tyr(1054/1055) phosphorylation kinetics of Tyk2 were more intense after exposure to IFN-alpha5 than when using IFN-alpha2. Concomitantly, Tyr705 phosphorylation of Stat3 was higher after stimulation with IFN-alpha5 than with IFN-alpha2."

"activated form of STAT3, Tyr-705 phospho-stat3, was found in the nucleus of cancer cells in 11 of 40 (27.5%) human gastric cancer specimens."

"Here, we report identification of signal transducer and activator of transcription 3 (STAT3) as a substrate of PTPRT. Phosphorylation of a tyrosine at amino acid Y705 is essential for the function of STAT3, and PTPRT specifically dephosphorylated STAT3 at this position. Accordingly, overexpression of normal PTPRT in colorectal cancer cells reduced the expression of STAT3 target genes."

"Stat3 is activated by phosphorylation on Tyr-705, which leads to dimer formation, nuclear translocation, and regulation of gene expression."

". Furthermore, the bFGF-induced activation of ERK1/2 seems to enhance the transcriptional activity of STAT3. Co-stimulation of KMS-11 with bFGF and IL-6 leads to marked expression of STAT3 target genes, such as c-myc and bcl-2, further suggesting the relevance of STAT3 phosphorylated at both Tyr705 and Ser727 for the full activation as a transcription factor (Fig. 5). In addition, the"

" . Furthermore, the bFGF-induced activation of ERK1/2 seems to enhance the transcriptional activity of STAT3. Co-stimulation of KMS-11 with bFGF and IL-6 leads to marked expression of STAT3 target genes, such as c-myc and bcl-2, further suggesting the relevance of STAT3 phosphorylated at both Tyr705 and Ser727 for the full activation as a transcription factor (Fig. 5). In addition, the"

"activated form of STAT3, Tyr-705 phospho-stat3, was found in the nucleus of cancer cells in 11 of 40 (27.5%) human gastric cancer specimens."

"Signal transducer and activator of transcription 3 (STAT3) is activated by the IL-6 family of cytokines and growth factors. STAT3 requires phosphorylation on Ser-727, in addition to tyrosine phosphorylation on Tyr-705, to be transcriptionally active."

"LIGHT, a member of tumor necrosis factor superfamily, activates Stat3 in cancer cells. LIGHT induces dose-dependent activation of Stat3 by phosphorylation at both the tyrosine 705 and serine 727 residues."

"In this paper, we present a comprehensive pathway map of EGFR signaling and other related pathways."

"LIGHT, a member of tumor necrosis factor superfamily, activates Stat3 in cancer cells. LIGHT induces dose-dependent activation of Stat3 by phosphorylation at both the tyrosine 705 and serine 727 residues."

"Stat3 is activated by phosphorylation on Tyr-705, which leads to dimer formation, nuclear translocation, and regulation of gene expression."

"leads to phosphorylation of MITF at S73 and of STAT3 at both tyrosine 705 and S727. This phosphorylation increases the transcriptional activity of MITF and STAT3 as indicated by mRNA accumulation of their target genes such as Bcl-2, granzyme B, and c-Myc"

"A dramatic reduction of the phosphorylation of the Stat3 protein at Tyr residue 705 was observed in cells infected with adenovirus Wild type p53. Co-transfection of cells with wild type p53 along with Stat3 luciferase reporter, inhibited Stat3 dependent luciferase activity."

"A dramatic reduction of the phosphorylation of the Stat3 protein at Tyr residue 705 was observed in cells infected with adenovirus Wild type p53. Co-transfection of cells with wild type p53 along with Stat3 luciferase reporter, inhibited Stat3 dependent luciferase activity."

"Here, we report identification of signal transducer and activator of transcription 3 (STAT3) as a substrate of PTPRT. Phosphorylation of a tyrosine at amino acid Y705 is essential for the function of STAT3, and PTPRT specifically dephosphorylated STAT3 at this position. Accordingly, overexpression of normal PTPRT in colorectal cancer cells reduced the expression of STAT3 target genes."

"leads to phosphorylation of MITF at S73 and of STAT3 at both tyrosine 705 and S727. This phosphorylation increases the transcriptional activity of MITF and STAT3 as indicated by mRNA accumulation of their target genes such as Bcl-2, granzyme B, and c-Myc"