Id |
Subject |
Object |
Predicate |
Lexical cue |
TextSentencer_T1 |
0-158 |
Sentence |
denotes |
Phosphoproteomic profiling of NSCLC cells reveals that ephrin B3 regulates pro-survival signaling through Akt1-mediated phosphorylation of the EphA2 receptor. |
T1 |
0-158 |
Sentence |
denotes |
Phosphoproteomic profiling of NSCLC cells reveals that ephrin B3 regulates pro-survival signaling through Akt1-mediated phosphorylation of the EphA2 receptor. |
TextSentencer_T2 |
159-300 |
Sentence |
denotes |
The ephrin and Eph signaling circuit has been reported as deregulated in a number of tumor types including nonsmall cell lung cancer (NSCLC). |
T2 |
159-300 |
Sentence |
denotes |
The ephrin and Eph signaling circuit has been reported as deregulated in a number of tumor types including nonsmall cell lung cancer (NSCLC). |
TextSentencer_T3 |
301-449 |
Sentence |
denotes |
Here we show that suppression of the ephrin-familly member ephrin B3 decreases NSCLC cell proliferation and has profound effects on cell morphology. |
T3 |
301-449 |
Sentence |
denotes |
Here we show that suppression of the ephrin-familly member ephrin B3 decreases NSCLC cell proliferation and has profound effects on cell morphology. |
TextSentencer_T4 |
450-648 |
Sentence |
denotes |
To reveal which signaling networks ephrin B3 utilize to regulate such effects on growth and morphology, differential regulation of phosphorylated proteins was analyzed in the NSCLC cell line U-1810. |
T4 |
450-648 |
Sentence |
denotes |
To reveal which signaling networks ephrin B3 utilize to regulate such effects on growth and morphology, differential regulation of phosphorylated proteins was analyzed in the NSCLC cell line U-1810. |
TextSentencer_T5 |
649-818 |
Sentence |
denotes |
Using strong cat ion exchange (SCX) and TiO(2)-based fractionation followed by nano-LC and mass spectrometry analysis, we identified 1083 unique phosphorylated proteins. |
T5 |
649-818 |
Sentence |
denotes |
Using strong cat ion exchange (SCX) and TiO(2)-based fractionation followed by nano-LC and mass spectrometry analysis, we identified 1083 unique phosphorylated proteins. |
TextSentencer_T6 |
819-974 |
Sentence |
denotes |
Out of these, 150 proteins were found only when ephrin B3 is expressed, whereas 66 proteins were found exclusively in U-1810 cells with silenced ephrin B3. |
T6 |
819-974 |
Sentence |
denotes |
Out of these, 150 proteins were found only when ephrin B3 is expressed, whereas 66 proteins were found exclusively in U-1810 cells with silenced ephrin B3. |
TextSentencer_T7 |
975-1304 |
Sentence |
denotes |
Network analysis of changes in the phosphoproteome with regard to the presence or absence of ephrin B3 expression generated a hypothesis that the site specific phosphorylation on Ser-897 detected on the erythropoietin-producing hepatocellular receptor tyrosine kinase class A2 (EphA2) is critical for the survival of NSCLC cells. |
T7 |
975-1304 |
Sentence |
denotes |
Network analysis of changes in the phosphoproteome with regard to the presence or absence of ephrin B3 expression generated a hypothesis that the site specific phosphorylation on Ser-897 detected on the erythropoietin-producing hepatocellular receptor tyrosine kinase class A2 (EphA2) is critical for the survival of NSCLC cells. |
TextSentencer_T8 |
1305-1444 |
Sentence |
denotes |
Upstream of the EphA2 phosphorylation, activation of Akt1 on Ser 129 was also revealed as part of the ephrin B3-mediated signaling pathway. |
T8 |
1305-1444 |
Sentence |
denotes |
Upstream of the EphA2 phosphorylation, activation of Akt1 on Ser 129 was also revealed as part of the ephrin B3-mediated signaling pathway. |
TextSentencer_T9 |
1445-1563 |
Sentence |
denotes |
Phosphorylation of these sites was further confirmed by immune-based strategies in combination with mass spectrometry. |
T9 |
1445-1563 |
Sentence |
denotes |
Phosphorylation of these sites was further confirmed by immune-based strategies in combination with mass spectrometry. |
TextSentencer_T10 |
1564-1835 |
Sentence |
denotes |
Moreover, by further stepwise pathway walking, annotating the phosphorylated sites and their corresponding kinases upstream, our data support the process in which a Heat shock protein 90 isoform (HSP90AA1) acts as a protector of EphA2, thereby saving it from degradation. |
T10 |
1564-1835 |
Sentence |
denotes |
Moreover, by further stepwise pathway walking, annotating the phosphorylated sites and their corresponding kinases upstream, our data support the process in which a Heat shock protein 90 isoform (HSP90AA1) acts as a protector of EphA2, thereby saving it from degradation. |
TextSentencer_T11 |
1836-2004 |
Sentence |
denotes |
In addition, protein kinase CK2 (CK2) is suggested as a dominant kinase, activating downstream substrates to generate the effects on NSCLC proliferation and morphology. |
T11 |
1836-2004 |
Sentence |
denotes |
In addition, protein kinase CK2 (CK2) is suggested as a dominant kinase, activating downstream substrates to generate the effects on NSCLC proliferation and morphology. |