| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-72 |
Sentence |
denotes |
The glut 1 glucose transporter interacts with calnexin and calreticulin. |
| T2 |
73-196 |
Sentence |
denotes |
Calnexin is an integral membrane protein that acts as a chaperone during glycoprotein folding in the endoplasmic reticulum. |
| T3 |
197-323 |
Sentence |
denotes |
Cross-linking studies were carried out with the aim of investigating the interactions of calnexin with glycoproteins in vitro. |
| T4 |
324-505 |
Sentence |
denotes |
A truncated version of the integral membrane glycoprotein Glut 1 (GT155) was synthesized in a rabbit reticulocyte translation system in the presence of canine pancreatic microsomes. |
| T5 |
506-647 |
Sentence |
denotes |
Following immunoprecipitation with an anticalnexin antiserum, a cross-linker-independent association was observed between GT155 and calnexin. |
| T6 |
648-861 |
Sentence |
denotes |
In addition, the anti-calnexin antiserum immunoprecipitated a UV-dependent cross-linking product consisting of GT155 and a protein of approximately 60 kDa designated CAP-60 (calnexin-associated protein of 60 kDa). |
| T7 |
862-1054 |
Sentence |
denotes |
Both the GT155-calnexin and the GT155-CAP-60 interactions were dependent on the presence of a correctly modified oligosaccharide group on GT155, a characteristic of many calnexin interactions. |
| T8 |
1055-1148 |
Sentence |
denotes |
A GT155 mutant that was not glycosylated (AGGT155) did not associate with calnexin or CAP-60. |
| T9 |
1149-1306 |
Sentence |
denotes |
Calreticulin, the soluble homologue of calnexin, was also shown to interact with GT155 only when the protein bore a correctly modified oligosaccharide group. |
| T10 |
1307-1411 |
Sentence |
denotes |
Thus, our data show that both calnexin and calreticulin with Glut 1 in a glycosylation-dependent manner. |
| T1 |
0-72 |
Sentence |
denotes |
The glut 1 glucose transporter interacts with calnexin and calreticulin. |
| T2 |
73-196 |
Sentence |
denotes |
Calnexin is an integral membrane protein that acts as a chaperone during glycoprotein folding in the endoplasmic reticulum. |
| T3 |
197-323 |
Sentence |
denotes |
Cross-linking studies were carried out with the aim of investigating the interactions of calnexin with glycoproteins in vitro. |
| T4 |
324-505 |
Sentence |
denotes |
A truncated version of the integral membrane glycoprotein Glut 1 (GT155) was synthesized in a rabbit reticulocyte translation system in the presence of canine pancreatic microsomes. |
| T5 |
506-647 |
Sentence |
denotes |
Following immunoprecipitation with an anticalnexin antiserum, a cross-linker-independent association was observed between GT155 and calnexin. |
| T6 |
648-861 |
Sentence |
denotes |
In addition, the anti-calnexin antiserum immunoprecipitated a UV-dependent cross-linking product consisting of GT155 and a protein of approximately 60 kDa designated CAP-60 (calnexin-associated protein of 60 kDa). |
| T7 |
862-1054 |
Sentence |
denotes |
Both the GT155-calnexin and the GT155-CAP-60 interactions were dependent on the presence of a correctly modified oligosaccharide group on GT155, a characteristic of many calnexin interactions. |
| T8 |
1055-1148 |
Sentence |
denotes |
A GT155 mutant that was not glycosylated (AGGT155) did not associate with calnexin or CAP-60. |
| T9 |
1149-1306 |
Sentence |
denotes |
Calreticulin, the soluble homologue of calnexin, was also shown to interact with GT155 only when the protein bore a correctly modified oligosaccharide group. |
| T10 |
1307-1411 |
Sentence |
denotes |
Thus, our data show that both calnexin and calreticulin with Glut 1 in a glycosylation-dependent manner. |