| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-119 |
Sentence |
denotes |
Post-translational modifications distinguish cell surface from Golgi-retained beta 1,4 galactosyltransferase molecules. |
| T1 |
0-119 |
Sentence |
denotes |
Post-translational modifications distinguish cell surface from Golgi-retained beta 1,4 galactosyltransferase molecules. |
| T1 |
0-119 |
Sentence |
denotes |
Post-translational modifications distinguish cell surface from Golgi-retained beta 1,4 galactosyltransferase molecules. |
| TextSentencer_T2 |
120-165 |
Sentence |
denotes |
Golgi localization involves active retention. |
| T2 |
120-165 |
Sentence |
denotes |
Golgi localization involves active retention. |
| T2 |
120-165 |
Sentence |
denotes |
Golgi localization involves active retention. |
| TextSentencer_T3 |
166-284 |
Sentence |
denotes |
beta 1,4 Galactosyltransferase (GalT) is a membrane-bound enzyme localized predominantly to the trans-Golgi cisternae. |
| T3 |
166-284 |
Sentence |
denotes |
beta 1,4 Galactosyltransferase (GalT) is a membrane-bound enzyme localized predominantly to the trans-Golgi cisternae. |
| T3 |
166-284 |
Sentence |
denotes |
beta 1,4 Galactosyltransferase (GalT) is a membrane-bound enzyme localized predominantly to the trans-Golgi cisternae. |
| TextSentencer_T4 |
285-459 |
Sentence |
denotes |
Our previous studies have shown that the transmembrane domain of bovine GalT plays a critical role in Golgi localization (Teasdale, R.D., D'Agostaro, G. and Gleeson, P.A., J. |
| T4 |
285-459 |
Sentence |
denotes |
Our previous studies have shown that the transmembrane domain of bovine GalT plays a critical role in Golgi localization (Teasdale, R.D., D'Agostaro, G. and Gleeson, P.A., J. |
| T4 |
285-495 |
Sentence |
denotes |
Our previous studies have shown that the transmembrane domain of bovine GalT plays a critical role in Golgi localization (Teasdale, R.D., D'Agostaro, G. and Gleeson, P.A., J. Biol. Chem., 267, 4084-4096, 1992). |
| TextSentencer_T5 |
460-465 |
Sentence |
denotes |
Biol. |
| T5 |
460-465 |
Sentence |
denotes |
Biol. |
| TextSentencer_T6 |
466-495 |
Sentence |
denotes |
Chem., 267, 4084-4096, 1992). |
| T6 |
466-495 |
Sentence |
denotes |
Chem., 267, 4084-4096, 1992). |
| TextSentencer_T7 |
496-717 |
Sentence |
denotes |
Here we have compared the localization and post-translational modifications of full-length bovine GalT with a GalT/hybrid molecule where the transmembrane domain of GalT was replaced with that of the transferrin receptor. |
| T5 |
496-717 |
Sentence |
denotes |
Here we have compared the localization and post-translational modifications of full-length bovine GalT with a GalT/hybrid molecule where the transmembrane domain of GalT was replaced with that of the transferrin receptor. |
| T7 |
496-717 |
Sentence |
denotes |
Here we have compared the localization and post-translational modifications of full-length bovine GalT with a GalT/hybrid molecule where the transmembrane domain of GalT was replaced with that of the transferrin receptor. |
| TextSentencer_T8 |
718-914 |
Sentence |
denotes |
GalT/hybrid molecules were expressed on the surface of transfected cells; however, differences were observed in the distribution of the hybrid molecules between transfected COS and murine L cells. |
| T6 |
718-914 |
Sentence |
denotes |
GalT/hybrid molecules were expressed on the surface of transfected cells; however, differences were observed in the distribution of the hybrid molecules between transfected COS and murine L cells. |
| T8 |
718-914 |
Sentence |
denotes |
GalT/hybrid molecules were expressed on the surface of transfected cells; however, differences were observed in the distribution of the hybrid molecules between transfected COS and murine L cells. |
| TextSentencer_T9 |
915-1218 |
Sentence |
denotes |
In transfected COS cells, the GalT/hybrid protein was expressed efficiently at the cell surface, with little Golgi-localized material, whereas in stable murine L cells, which expressed lower levels of the construct, hybrid molecules were detected both at the cell surface and within the Golgi apparatus. |
| T7 |
915-1218 |
Sentence |
denotes |
In transfected COS cells, the GalT/hybrid protein was expressed efficiently at the cell surface, with little Golgi-localized material, whereas in stable murine L cells, which expressed lower levels of the construct, hybrid molecules were detected both at the cell surface and within the Golgi apparatus. |
| T9 |
915-1218 |
Sentence |
denotes |
In transfected COS cells, the GalT/hybrid protein was expressed efficiently at the cell surface, with little Golgi-localized material, whereas in stable murine L cells, which expressed lower levels of the construct, hybrid molecules were detected both at the cell surface and within the Golgi apparatus. |
| TextSentencer_T10 |
1219-1355 |
Sentence |
denotes |
Expression of the GalT constructs in either COS or L cells produced two glycoprotein products which differed in molecular mass by 7 kDa. |
| T8 |
1219-1355 |
Sentence |
denotes |
Expression of the GalT constructs in either COS or L cells produced two glycoprotein products which differed in molecular mass by 7 kDa. |
| T10 |
1219-1355 |
Sentence |
denotes |
Expression of the GalT constructs in either COS or L cells produced two glycoprotein products which differed in molecular mass by 7 kDa. |
| TextSentencer_T11 |
1356-1549 |
Sentence |
denotes |
The difference in size between the two products is due to post-translational modifications which are inhibited by brefeldin A and are therefore likely to occur in the trans-Golgi network (TGN). |
| T9 |
1356-1549 |
Sentence |
denotes |
The difference in size between the two products is due to post-translational modifications which are inhibited by brefeldin A and are therefore likely to occur in the trans-Golgi network (TGN). |
| T11 |
1356-1549 |
Sentence |
denotes |
The difference in size between the two products is due to post-translational modifications which are inhibited by brefeldin A and are therefore likely to occur in the trans-Golgi network (TGN). |
| TextSentencer_T12 |
1550-1693 |
Sentence |
denotes |
Very little of the high-molecular-weight species was detected for full-length GalT, whereas it was a major product for the GalT/hybrid protein. |
| T10 |
1550-1693 |
Sentence |
denotes |
Very little of the high-molecular-weight species was detected for full-length GalT, whereas it was a major product for the GalT/hybrid protein. |
| T12 |
1550-1693 |
Sentence |
denotes |
Very little of the high-molecular-weight species was detected for full-length GalT, whereas it was a major product for the GalT/hybrid protein. |
| TextSentencer_T13 |
1694-1769 |
Sentence |
denotes |
Only the higher molecular weight species was expressed at the cell surface. |
| T11 |
1694-1769 |
Sentence |
denotes |
Only the higher molecular weight species was expressed at the cell surface. |
| T13 |
1694-1769 |
Sentence |
denotes |
Only the higher molecular weight species was expressed at the cell surface. |
| TextSentencer_T14 |
1770-1970 |
Sentence |
denotes |
Thus, this additional 7 kDa post-translational modification distinguishes molecules retained within the Golgi apparatus (lower M(r) species) from those transported through the TGN to the cell surface. |
| T12 |
1770-1970 |
Sentence |
denotes |
Thus, this additional 7 kDa post-translational modification distinguishes molecules retained within the Golgi apparatus (lower M(r) species) from those transported through the TGN to the cell surface. |
| T14 |
1770-1970 |
Sentence |
denotes |
Thus, this additional 7 kDa post-translational modification distinguishes molecules retained within the Golgi apparatus (lower M(r) species) from those transported through the TGN to the cell surface. |
| TextSentencer_T15 |
1971-2232 |
Sentence |
denotes |
These studies indicate that (i) the level of expression influences the intracellular distribution of GalT/hybrid molecules and (ii) the localization of full-length GalT involves active retention within the Golgi stack, and not retrieval from later compartments. |
| T13 |
1971-2232 |
Sentence |
denotes |
These studies indicate that (i) the level of expression influences the intracellular distribution of GalT/hybrid molecules and (ii) the localization of full-length GalT involves active retention within the Golgi stack, and not retrieval from later compartments. |
| T15 |
1971-2232 |
Sentence |
denotes |
These studies indicate that (i) the level of expression influences the intracellular distribution of GalT/hybrid molecules and (ii) the localization of full-length GalT involves active retention within the Golgi stack, and not retrieval from later compartments. |
| TextSentencer_T16 |
2233-2504 |
Sentence |
denotes |
After treatment of membrane preparations from stable L cell clones with a heterobifunctional cross-linking agent, full-length bovine GalT molecules were found almost exclusively as high-molecular-weight aggregates, suggesting that GalT exists as an oligomer or aggregate. |
| T14 |
2233-2504 |
Sentence |
denotes |
After treatment of membrane preparations from stable L cell clones with a heterobifunctional cross-linking agent, full-length bovine GalT molecules were found almost exclusively as high-molecular-weight aggregates, suggesting that GalT exists as an oligomer or aggregate. |
| T16 |
2233-2504 |
Sentence |
denotes |
After treatment of membrane preparations from stable L cell clones with a heterobifunctional cross-linking agent, full-length bovine GalT molecules were found almost exclusively as high-molecular-weight aggregates, suggesting that GalT exists as an oligomer or aggregate. |
| TextSentencer_T17 |
2505-2574 |
Sentence |
denotes |
This ability to oligomerize may be a requirement for Golgi retention. |
| T15 |
2505-2574 |
Sentence |
denotes |
This ability to oligomerize may be a requirement for Golgi retention. |
| T17 |
2505-2574 |
Sentence |
denotes |
This ability to oligomerize may be a requirement for Golgi retention. |