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Id Subject Object Predicate Lexical cue
TextSentencer_T1 0-156 Sentence denotes In yeast the export of small glycopeptides from the endoplasmic reticulum into the cytosol is not affected by the structure of their oligosaccharide chains.
T1 0-156 Sentence denotes In yeast the export of small glycopeptides from the endoplasmic reticulum into the cytosol is not affected by the structure of their oligosaccharide chains.
T1 0-156 Sentence denotes In yeast the export of small glycopeptides from the endoplasmic reticulum into the cytosol is not affected by the structure of their oligosaccharide chains.
TextSentencer_T2 157-368 Sentence denotes A "quality control" system associated with the endoplasmic reticulum (ER) that discriminates between misfolded proteins and correctly folded proteins is present in a variety of eukaryotic cells, including yeast.
T2 157-368 Sentence denotes A "quality control" system associated with the endoplasmic reticulum (ER) that discriminates between misfolded proteins and correctly folded proteins is present in a variety of eukaryotic cells, including yeast.
T2 157-368 Sentence denotes A "quality control" system associated with the endoplasmic reticulum (ER) that discriminates between misfolded proteins and correctly folded proteins is present in a variety of eukaryotic cells, including yeast.
TextSentencer_T3 369-539 Sentence denotes Recently, it has been shown that misfolded proteins that are N -glycosylated in the lumen of the ER are transported out of the ER, de-N-glycosylated by a soluble peptide:
T3 369-539 Sentence denotes Recently, it has been shown that misfolded proteins that are N -glycosylated in the lumen of the ER are transported out of the ER, de-N-glycosylated by a soluble peptide:
T3 369-603 Sentence denotes Recently, it has been shown that misfolded proteins that are N -glycosylated in the lumen of the ER are transported out of the ER, de-N-glycosylated by a soluble peptide: N -glycanase (PNGase) and degraded by action of the proteasome.
TextSentencer_T4 540-603 Sentence denotes N -glycanase (PNGase) and degraded by action of the proteasome.
T4 540-603 Sentence denotes N -glycanase (PNGase) and degraded by action of the proteasome.
TextSentencer_T5 604-827 Sentence denotes It also has been shown that small N -glycosylatable peptides follow a fate similar to that of misfolded proteins, i.e., glycosylation in the lumen of the ER, transport out of the ER, and de- N -glycosylation in the cytosol.
T4 604-827 Sentence denotes It also has been shown that small N -glycosylatable peptides follow a fate similar to that of misfolded proteins, i.e., glycosylation in the lumen of the ER, transport out of the ER, and de- N -glycosylation in the cytosol.
T5 604-827 Sentence denotes It also has been shown that small N -glycosylatable peptides follow a fate similar to that of misfolded proteins, i.e., glycosylation in the lumen of the ER, transport out of the ER, and de- N -glycosylation in the cytosol.
TextSentencer_T6 828-971 Sentence denotes These processes of retrograde glycopeptide transport and de- N -glycosylation have been observed in mammalian cells, as well as in yeast cells.
T5 828-971 Sentence denotes These processes of retrograde glycopeptide transport and de- N -glycosylation have been observed in mammalian cells, as well as in yeast cells.
T6 828-971 Sentence denotes These processes of retrograde glycopeptide transport and de- N -glycosylation have been observed in mammalian cells, as well as in yeast cells.
TextSentencer_T7 972-1086 Sentence denotes However, little is known about the mechanism involved in the movement of glycopeptides from the ER to the cytosol.
T6 972-1086 Sentence denotes However, little is known about the mechanism involved in the movement of glycopeptides from the ER to the cytosol.
T7 972-1086 Sentence denotes However, little is known about the mechanism involved in the movement of glycopeptides from the ER to the cytosol.
TextSentencer_T8 1087-1297 Sentence denotes Here we report a simple method for assaying N -glycosylation/de- N -glycosylation by simple paper chromatographic and electrophoretic techniques using an N -glycosylatable(3)H-labeled tripeptide as a substrate.
T7 1087-1297 Sentence denotes Here we report a simple method for assaying N -glycosylation/de- N -glycosylation by simple paper chromatographic and electrophoretic techniques using an N -glycosylatable(3)H-labeled tripeptide as a substrate.
T8 1087-1297 Sentence denotes Here we report a simple method for assaying N -glycosylation/de- N -glycosylation by simple paper chromatographic and electrophoretic techniques using an N -glycosylatable(3)H-labeled tripeptide as a substrate.
TextSentencer_T9 1298-1526 Sentence denotes With this method, we confirmed the cytosolic localization of the de- N -glycosylated peptide, which supports the idea that de- N -glycosylation occurs after the export of the glycopeptide from the lumen of the ER to the cytosol.
T8 1298-1526 Sentence denotes With this method, we confirmed the cytosolic localization of the de- N -glycosylated peptide, which supports the idea that de- N -glycosylation occurs after the export of the glycopeptide from the lumen of the ER to the cytosol.
T9 1298-1526 Sentence denotes With this method, we confirmed the cytosolic localization of the de- N -glycosylated peptide, which supports the idea that de- N -glycosylation occurs after the export of the glycopeptide from the lumen of the ER to the cytosol.
TextSentencer_T10 1527-1691 Sentence denotes Further, we found that the variations in the structure of the oligosaccharide chain on the glycopeptide did not cause differences in the export of the glycopeptide.
T9 1527-1691 Sentence denotes Further, we found that the variations in the structure of the oligosaccharide chain on the glycopeptide did not cause differences in the export of the glycopeptide.
T10 1527-1691 Sentence denotes Further, we found that the variations in the structure of the oligosaccharide chain on the glycopeptide did not cause differences in the export of the glycopeptide.
TextSentencer_T11 1692-1821 Sentence denotes This finding suggests that the mechanism for the export of small glycopeptides may differ from that of misfolded (glyco)proteins.
T10 1692-1821 Sentence denotes This finding suggests that the mechanism for the export of small glycopeptides may differ from that of misfolded (glyco)proteins.
T11 1692-1821 Sentence denotes This finding suggests that the mechanism for the export of small glycopeptides may differ from that of misfolded (glyco)proteins.