| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-170 |
Sentence |
denotes |
Granulocyte-macrophage colony-stimulating factor stimulates JAK2 signaling pathway and rapidly activates p93fes, STAT1 p91, and STAT3 p92 in polymorphonuclear leukocytes. |
| T1 |
0-170 |
Sentence |
denotes |
Granulocyte-macrophage colony-stimulating factor stimulates JAK2 signaling pathway and rapidly activates p93fes, STAT1 p91, and STAT3 p92 in polymorphonuclear leukocytes. |
| T2 |
171-367 |
Sentence |
denotes |
Granulocyte-macrophage colony-stimulating factor (GM-CSF), supports proliferation, differentiation, and functional activation of hemopoietic cells by its interaction with a heterodimeric receptor. |
| T2 |
171-367 |
Sentence |
denotes |
Granulocyte-macrophage colony-stimulating factor (GM-CSF), supports proliferation, differentiation, and functional activation of hemopoietic cells by its interaction with a heterodimeric receptor. |
| T3 |
368-621 |
Sentence |
denotes |
Although GM-CSF receptor is devoid of tyrosine kinase enzymatic activity, GM-CSF-induced peripheral blood polymorphonuclear leukocytes (PMN) functional activation is mediated by the phosphorylation of a large number of intracellular signaling molecules. |
| T3 |
368-621 |
Sentence |
denotes |
Although GM-CSF receptor is devoid of tyrosine kinase enzymatic activity, GM-CSF-induced peripheral blood polymorphonuclear leukocytes (PMN) functional activation is mediated by the phosphorylation of a large number of intracellular signaling molecules. |
| T4 |
622-718 |
Sentence |
denotes |
We have previously shown that JAK2 becomes tyrosine-phosphorylated in response to GM-CSF in PMN. |
| T4 |
622-718 |
Sentence |
denotes |
We have previously shown that JAK2 becomes tyrosine-phosphorylated in response to GM-CSF in PMN. |
| T5 |
719-1049 |
Sentence |
denotes |
In the present study we demonstrate that also the signal transducers and activators of transcription (STAT) family members STAT1 p91 and STAT3 p92 and the product of the c-fps/fes protooncogene become tyrosine-phosphorylated upon GM-CSF stimulation and physically associated with both GM-CSF receptor beta common subunit and JAK2. |
| T5 |
719-1049 |
Sentence |
denotes |
In the present study we demonstrate that also the signal transducers and activators of transcription (STAT) family members STAT1 p91 and STAT3 p92 and the product of the c-fps/fes protooncogene become tyrosine-phosphorylated upon GM-CSF stimulation and physically associated with both GM-CSF receptor beta common subunit and JAK2. |
| T6 |
1050-1120 |
Sentence |
denotes |
Moreover GM-CSF was able to induce JAK2 and p93fes catalytic activity. |
| T6 |
1050-1120 |
Sentence |
denotes |
Moreover GM-CSF was able to induce JAK2 and p93fes catalytic activity. |
| T7 |
1121-1235 |
Sentence |
denotes |
We also demonstrate that the association of the GM-CSF receptor beta common subunit with JAK2 is ligand-dependent. |
| T7 |
1121-1235 |
Sentence |
denotes |
We also demonstrate that the association of the GM-CSF receptor beta common subunit with JAK2 is ligand-dependent. |
| T8 |
1236-1332 |
Sentence |
denotes |
Finally we demonstrate that GM-CSF induces a DNA-binding complex that contains both p91 and p92. |
| T8 |
1236-1332 |
Sentence |
denotes |
Finally we demonstrate that GM-CSF induces a DNA-binding complex that contains both p91 and p92. |
| T9 |
1333-1499 |
Sentence |
denotes |
These results identify a new signal transduction pathway activated by GM-CSF and provide a mechanism for rapid activation of gene expression in GM-CSF-stimulated PMN. |
| T9 |
1333-1499 |
Sentence |
denotes |
These results identify a new signal transduction pathway activated by GM-CSF and provide a mechanism for rapid activation of gene expression in GM-CSF-stimulated PMN. |