| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-116 |
Sentence |
denotes |
Glycopeptide export from mammalian microsomes is independent of calcium and is distinct from oligosaccharide export. |
| T1 |
0-116 |
Sentence |
denotes |
Glycopeptide export from mammalian microsomes is independent of calcium and is distinct from oligosaccharide export. |
| T1 |
0-116 |
Sentence |
denotes |
Glycopeptide export from mammalian microsomes is independent of calcium and is distinct from oligosaccharide export. |
| TextSentencer_T2 |
117-284 |
Sentence |
denotes |
Glycopeptides are exported from the endoplasmic reticulum to the cytosol of eukaryotic membranes in an ATP- and cytosol-requiring process (Romisch and Ali, 1997, Proc. |
| T2 |
117-284 |
Sentence |
denotes |
Glycopeptides are exported from the endoplasmic reticulum to the cytosol of eukaryotic membranes in an ATP- and cytosol-requiring process (Romisch and Ali, 1997, Proc. |
| T2 |
117-321 |
Sentence |
denotes |
Glycopeptides are exported from the endoplasmic reticulum to the cytosol of eukaryotic membranes in an ATP- and cytosol-requiring process (Romisch and Ali, 1997, Proc. Natl. Acad. Sci. USA,94, 6730-6734). |
| TextSentencer_T3 |
285-290 |
Sentence |
denotes |
Natl. |
| T3 |
285-290 |
Sentence |
denotes |
Natl. |
| TextSentencer_T4 |
291-296 |
Sentence |
denotes |
Acad. |
| T4 |
291-296 |
Sentence |
denotes |
Acad. |
| TextSentencer_T5 |
297-301 |
Sentence |
denotes |
Sci. |
| T5 |
297-301 |
Sentence |
denotes |
Sci. |
| TextSentencer_T6 |
302-321 |
Sentence |
denotes |
USA,94, 6730-6734). |
| T6 |
302-321 |
Sentence |
denotes |
USA,94, 6730-6734). |
| TextSentencer_T7 |
322-474 |
Sentence |
denotes |
Oligosaccharides of the polymannose-type are also exported from the endoplasmic reticulum of mammalian cells to the cytosol in an ATP-dependent fashion. |
| T3 |
322-474 |
Sentence |
denotes |
Oligosaccharides of the polymannose-type are also exported from the endoplasmic reticulum of mammalian cells to the cytosol in an ATP-dependent fashion. |
| T7 |
322-474 |
Sentence |
denotes |
Oligosaccharides of the polymannose-type are also exported from the endoplasmic reticulum of mammalian cells to the cytosol in an ATP-dependent fashion. |
| TextSentencer_T8 |
475-697 |
Sentence |
denotes |
These findings raise the strong possibility that the two substrate classes are transported by the same mechanism but the precise identity of the trans-location machinery for each substrate class has not been fully defined. |
| T4 |
475-697 |
Sentence |
denotes |
These findings raise the strong possibility that the two substrate classes are transported by the same mechanism but the precise identity of the trans-location machinery for each substrate class has not been fully defined. |
| T8 |
475-697 |
Sentence |
denotes |
These findings raise the strong possibility that the two substrate classes are transported by the same mechanism but the precise identity of the trans-location machinery for each substrate class has not been fully defined. |
| TextSentencer_T9 |
698-869 |
Sentence |
denotes |
Here we have investigated the mechanism by which a glycopeptide is exported from rat liver microsomes, and compare this to the export of free polymannose oligosaccharides. |
| T5 |
698-869 |
Sentence |
denotes |
Here we have investigated the mechanism by which a glycopeptide is exported from rat liver microsomes, and compare this to the export of free polymannose oligosaccharides. |
| T9 |
698-869 |
Sentence |
denotes |
Here we have investigated the mechanism by which a glycopeptide is exported from rat liver microsomes, and compare this to the export of free polymannose oligosaccharides. |
| TextSentencer_T10 |
870-1106 |
Sentence |
denotes |
Using EGTA and the endoplasmic reticulum calcium mobilizing agents thapsigargicin and calcium ionophores A23187 and ionomycin, we show that glycopeptides, in contrast to oligosaccharides, are exported by a calcium-independent mechanism. |
| T6 |
870-1106 |
Sentence |
denotes |
Using EGTA and the endoplasmic reticulum calcium mobilizing agents thapsigargicin and calcium ionophores A23187 and ionomycin, we show that glycopeptides, in contrast to oligosaccharides, are exported by a calcium-independent mechanism. |
| T10 |
870-1106 |
Sentence |
denotes |
Using EGTA and the endoplasmic reticulum calcium mobilizing agents thapsigargicin and calcium ionophores A23187 and ionomycin, we show that glycopeptides, in contrast to oligosaccharides, are exported by a calcium-independent mechanism. |
| TextSentencer_T11 |
1107-1264 |
Sentence |
denotes |
On the other hand, Mg(2+)is required in the assay for the transport of glycopeptide from mammalian microsomes which is in common with oligosaccharide export. |
| T7 |
1107-1264 |
Sentence |
denotes |
On the other hand, Mg(2+)is required in the assay for the transport of glycopeptide from mammalian microsomes which is in common with oligosaccharide export. |
| T11 |
1107-1264 |
Sentence |
denotes |
On the other hand, Mg(2+)is required in the assay for the transport of glycopeptide from mammalian microsomes which is in common with oligosaccharide export. |
| TextSentencer_T12 |
1265-1650 |
Sentence |
denotes |
Deoxynojirimycin and castanospermine, inhibitors of ER glucosidases, when added to rat liver microsomes prior to loading with peptide that bears an N -glycosylation sequon, had no effect on the release of glucosylated glycopeptides from membranes, indicating that removal of the alpha-glucose units from the oligomannose glycan structure of the glycopeptide is not required for export. |
| T8 |
1265-1650 |
Sentence |
denotes |
Deoxynojirimycin and castanospermine, inhibitors of ER glucosidases, when added to rat liver microsomes prior to loading with peptide that bears an N -glycosylation sequon, had no effect on the release of glucosylated glycopeptides from membranes, indicating that removal of the alpha-glucose units from the oligomannose glycan structure of the glycopeptide is not required for export. |
| T12 |
1265-1650 |
Sentence |
denotes |
Deoxynojirimycin and castanospermine, inhibitors of ER glucosidases, when added to rat liver microsomes prior to loading with peptide that bears an N -glycosylation sequon, had no effect on the release of glucosylated glycopeptides from membranes, indicating that removal of the alpha-glucose units from the oligomannose glycan structure of the glycopeptide is not required for export. |
| TextSentencer_T13 |
1651-1804 |
Sentence |
denotes |
In contrast to oligosaccharides, where transport is efficiently inhibited, mannosides were without effect or only weak inhibitors of glycopeptide export. |
| T9 |
1651-1804 |
Sentence |
denotes |
In contrast to oligosaccharides, where transport is efficiently inhibited, mannosides were without effect or only weak inhibitors of glycopeptide export. |
| T13 |
1651-1804 |
Sentence |
denotes |
In contrast to oligosaccharides, where transport is efficiently inhibited, mannosides were without effect or only weak inhibitors of glycopeptide export. |
| TextSentencer_T14 |
1805-2118 |
Sentence |
denotes |
Taken together, these data suggest that glycopeptides are exported by a distinct mechanism from oligosaccharides of the polymannose-type and that the peptide moiety is an important structural determinant for glycopeptide export and capable of directing translocation of substrates to a specific transport pathway. |
| T10 |
1805-2118 |
Sentence |
denotes |
Taken together, these data suggest that glycopeptides are exported by a distinct mechanism from oligosaccharides of the polymannose-type and that the peptide moiety is an important structural determinant for glycopeptide export and capable of directing translocation of substrates to a specific transport pathway. |
| T14 |
1805-2118 |
Sentence |
denotes |
Taken together, these data suggest that glycopeptides are exported by a distinct mechanism from oligosaccharides of the polymannose-type and that the peptide moiety is an important structural determinant for glycopeptide export and capable of directing translocation of substrates to a specific transport pathway. |