Id |
Subject |
Object |
Predicate |
Lexical cue |
TextSentencer_T1 |
0-86 |
Sentence |
denotes |
Phosphorylation and externalization of galectin-4 is controlled by Src family kinases. |
T1 |
0-86 |
Sentence |
denotes |
Phosphorylation and externalization of galectin-4 is controlled by Src family kinases. |
TextSentencer_T2 |
87-228 |
Sentence |
denotes |
Galectin-4 is a cytosolic protein that lacks a signal sequence but is externalized and binds to 3-O-sulfated glycoconjugates extracellularly. |
T2 |
87-228 |
Sentence |
denotes |
Galectin-4 is a cytosolic protein that lacks a signal sequence but is externalized and binds to 3-O-sulfated glycoconjugates extracellularly. |
TextSentencer_T3 |
229-333 |
Sentence |
denotes |
The mechanism of subcellular localization and externalization of galectin-4 has not yet been determined. |
T3 |
229-333 |
Sentence |
denotes |
The mechanism of subcellular localization and externalization of galectin-4 has not yet been determined. |
TextSentencer_T4 |
334-485 |
Sentence |
denotes |
A preliminary experiment using pervanadate (PV) showed that galectin-4 is tyrosine-phosphorylated in cells and suggested that Src kinases are involved. |
T4 |
334-485 |
Sentence |
denotes |
A preliminary experiment using pervanadate (PV) showed that galectin-4 is tyrosine-phosphorylated in cells and suggested that Src kinases are involved. |
TextSentencer_T5 |
486-634 |
Sentence |
denotes |
Cell transfection with galectin-4 and active Src plasmids showed that galectin-4 can be tyrosine phosphorylated by members of the Src kinase family. |
T5 |
486-634 |
Sentence |
denotes |
Cell transfection with galectin-4 and active Src plasmids showed that galectin-4 can be tyrosine phosphorylated by members of the Src kinase family. |
TextSentencer_T6 |
635-817 |
Sentence |
denotes |
The C-terminal peptide YVQI of galectin-4 was found to play an important role in its tyrosine phosphorylation, and the SH2 domains of Src and SHP2 were found to bind to this peptide. |
T6 |
635-817 |
Sentence |
denotes |
The C-terminal peptide YVQI of galectin-4 was found to play an important role in its tyrosine phosphorylation, and the SH2 domains of Src and SHP2 were found to bind to this peptide. |
TextSentencer_T7 |
818-993 |
Sentence |
denotes |
Immunofluorescence analysis showed that galectin-4 and phosphorylated proteins were intensely stained in the area of membrane protrusions of PV-treated or Src-activated cells. |
T7 |
818-993 |
Sentence |
denotes |
Immunofluorescence analysis showed that galectin-4 and phosphorylated proteins were intensely stained in the area of membrane protrusions of PV-treated or Src-activated cells. |
TextSentencer_T8 |
994-1192 |
Sentence |
denotes |
Furthermore, MUC1 derived from NUGC-4 cells was observed to bind to galectin-4, and externalization of the bound molecules from the cell to the medium increased in the hyperphosphorylated condition. |
T8 |
994-1192 |
Sentence |
denotes |
Furthermore, MUC1 derived from NUGC-4 cells was observed to bind to galectin-4, and externalization of the bound molecules from the cell to the medium increased in the hyperphosphorylated condition. |
TextSentencer_T9 |
1193-1367 |
Sentence |
denotes |
Study of the transfection of the mutant galectin-4 which lacks the C-terminal peptide revealed that the phosphorylation status is important for externalization of galectin-4. |
T9 |
1193-1367 |
Sentence |
denotes |
Study of the transfection of the mutant galectin-4 which lacks the C-terminal peptide revealed that the phosphorylation status is important for externalization of galectin-4. |
TextSentencer_T10 |
1368-1581 |
Sentence |
denotes |
These results suggest that externalization of galectin-4 can be regulated by signaling molecules and that it may function intracellularly as an adaptor protein serving to modulate the trafficking of glycoproteins. |
T10 |
1368-1581 |
Sentence |
denotes |
These results suggest that externalization of galectin-4 can be regulated by signaling molecules and that it may function intracellularly as an adaptor protein serving to modulate the trafficking of glycoproteins. |