| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-147 |
Sentence |
denotes |
Glycopeptide export from the endoplasmic reticulum into cytosol is mediated by a mechanism distinct from that for export of misfolded glycoprotein. |
| T1 |
0-147 |
Sentence |
denotes |
Glycopeptide export from the endoplasmic reticulum into cytosol is mediated by a mechanism distinct from that for export of misfolded glycoprotein. |
| TextSentencer_T2 |
148-339 |
Sentence |
denotes |
When glycoproteins formed in the endoplasmic reticulum (ER) are misfolded, they are generally translocated into the cytosol for ubiquitination and are subsequently degraded by the proteasome. |
| T2 |
148-339 |
Sentence |
denotes |
When glycoproteins formed in the endoplasmic reticulum (ER) are misfolded, they are generally translocated into the cytosol for ubiquitination and are subsequently degraded by the proteasome. |
| TextSentencer_T3 |
340-496 |
Sentence |
denotes |
This system, the so-called ER-associated glycoprotein degradation, is important for eukaryotes to maintain the quality of glycoproteins generated in the ER. |
| T3 |
340-496 |
Sentence |
denotes |
This system, the so-called ER-associated glycoprotein degradation, is important for eukaryotes to maintain the quality of glycoproteins generated in the ER. |
| TextSentencer_T4 |
497-622 |
Sentence |
denotes |
It has been established in yeast that several distinct proteins are involved in this translocation and degradation processes. |
| T4 |
497-622 |
Sentence |
denotes |
It has been established in yeast that several distinct proteins are involved in this translocation and degradation processes. |
| TextSentencer_T5 |
623-708 |
Sentence |
denotes |
Small glycopeptides formed in the ER are exported to the cytosol in a similar manner. |
| T5 |
623-708 |
Sentence |
denotes |
Small glycopeptides formed in the ER are exported to the cytosol in a similar manner. |
| TextSentencer_T6 |
709-851 |
Sentence |
denotes |
This glycopeptide export system is conserved from yeast to mammalian cells, suggesting its basic biological significance for eukaryotic cells. |
| T6 |
709-851 |
Sentence |
denotes |
This glycopeptide export system is conserved from yeast to mammalian cells, suggesting its basic biological significance for eukaryotic cells. |
| TextSentencer_T7 |
852-1093 |
Sentence |
denotes |
These two export systems (for misfolded glycoproteins and glycopeptides) share some properties, such as a requirement for ATP and involvement of Sec61p, a central membrane protein presumably forming a dislocon channel for export of proteins. |
| T7 |
852-1093 |
Sentence |
denotes |
These two export systems (for misfolded glycoproteins and glycopeptides) share some properties, such as a requirement for ATP and involvement of Sec61p, a central membrane protein presumably forming a dislocon channel for export of proteins. |
| TextSentencer_T8 |
1094-1161 |
Sentence |
denotes |
However, the machinery of glycopeptide export is poorly understood. |
| T8 |
1094-1161 |
Sentence |
denotes |
However, the machinery of glycopeptide export is poorly understood. |
| TextSentencer_T9 |
1162-1351 |
Sentence |
denotes |
In this study, various mutants known to have an effect on export/degradation of misfolded glycoproteins were examined for glycopeptide export activity with a newly established assay method. |
| T9 |
1162-1351 |
Sentence |
denotes |
In this study, various mutants known to have an effect on export/degradation of misfolded glycoproteins were examined for glycopeptide export activity with a newly established assay method. |
| TextSentencer_T10 |
1352-1444 |
Sentence |
denotes |
Surprisingly, most of the mutants were found not to exhibit a defect in glycopeptide export. |
| T10 |
1352-1444 |
Sentence |
denotes |
Surprisingly, most of the mutants were found not to exhibit a defect in glycopeptide export. |
| TextSentencer_T11 |
1445-1605 |
Sentence |
denotes |
The only gene that was found to be required on efficient export of both types of substrates was PMR1, the gene encoding the medial-Golgi Ca(2+)/Mn(2+)-ion pump. |
| T11 |
1445-1605 |
Sentence |
denotes |
The only gene that was found to be required on efficient export of both types of substrates was PMR1, the gene encoding the medial-Golgi Ca(2+)/Mn(2+)-ion pump. |
| TextSentencer_T12 |
1606-1791 |
Sentence |
denotes |
These results provide evidence that although the systems involved in export of misfolded glycoproteins and glycopeptides share some properties, they have exhibited distinct differences. |
| T12 |
1606-1791 |
Sentence |
denotes |
These results provide evidence that although the systems involved in export of misfolded glycoproteins and glycopeptides share some properties, they have exhibited distinct differences. |