| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-165 |
Sentence |
denotes |
Molecular analysis of a UDP-GlcNAc:polypeptide alpha-N-acetylglucosaminyltransferase implicated in the initiation of mucin-type O-glycosylation in Trypanosoma cruzi. |
| T1 |
0-165 |
Sentence |
denotes |
Molecular analysis of a UDP-GlcNAc:polypeptide alpha-N-acetylglucosaminyltransferase implicated in the initiation of mucin-type O-glycosylation in Trypanosoma cruzi. |
| T1 |
0-165 |
Sentence |
denotes |
Molecular analysis of a UDP-GlcNAc:polypeptide alpha-N-acetylglucosaminyltransferase implicated in the initiation of mucin-type O-glycosylation in Trypanosoma cruzi. |
| TextSentencer_T2 |
166-396 |
Sentence |
denotes |
Trypanosoma cruzi, the causative agent of Chagas disease, is surrounded by a mucin coat that plays important functions in parasite survival/invasion and is extensively O-glycosylated by Golgi and cell surface glycosyltransferases. |
| T2 |
166-396 |
Sentence |
denotes |
Trypanosoma cruzi, the causative agent of Chagas disease, is surrounded by a mucin coat that plays important functions in parasite survival/invasion and is extensively O-glycosylated by Golgi and cell surface glycosyltransferases. |
| T2 |
166-396 |
Sentence |
denotes |
Trypanosoma cruzi, the causative agent of Chagas disease, is surrounded by a mucin coat that plays important functions in parasite survival/invasion and is extensively O-glycosylated by Golgi and cell surface glycosyltransferases. |
| TextSentencer_T3 |
397-599 |
Sentence |
denotes |
The addition of the first sugar, alpha-N-acetylglucosamine (GlcNAc) linked to Threonine (Thr), is catalyzed by a polypeptide alpha-GlcNAc-transferase (pp-alphaGlcNAcT) which is unstable to purification. |
| T3 |
397-599 |
Sentence |
denotes |
The addition of the first sugar, alpha-N-acetylglucosamine (GlcNAc) linked to Threonine (Thr), is catalyzed by a polypeptide alpha-GlcNAc-transferase (pp-alphaGlcNAcT) which is unstable to purification. |
| T3 |
397-599 |
Sentence |
denotes |
The addition of the first sugar, alpha-N-acetylglucosamine (GlcNAc) linked to Threonine (Thr), is catalyzed by a polypeptide alpha-GlcNAc-transferase (pp-alphaGlcNAcT) which is unstable to purification. |
| TextSentencer_T4 |
600-805 |
Sentence |
denotes |
Here, a comparison of the genomes of T. cruzi and Dictyostelium discoideum, an amoebazoan which also forms this linkage, identified two T. cruzi genes (TcOGNT1 and TcOGNT2) that might encode this activity. |
| T4 |
600-805 |
Sentence |
denotes |
Here, a comparison of the genomes of T. cruzi and Dictyostelium discoideum, an amoebazoan which also forms this linkage, identified two T. cruzi genes (TcOGNT1 and TcOGNT2) that might encode this activity. |
| T4 |
600-805 |
Sentence |
denotes |
Here, a comparison of the genomes of T. cruzi and Dictyostelium discoideum, an amoebazoan which also forms this linkage, identified two T. cruzi genes (TcOGNT1 and TcOGNT2) that might encode this activity. |
| TextSentencer_T5 |
806-1051 |
Sentence |
denotes |
Though neither was able to complement the Dictyostelium gene, expression in the trypanosomatid Leishmania tarentolae resulted in elevated levels of UDP-[(3)H]GlcNAc:Thr-peptide GlcNAc-transferase activity and UDP-[(3)H]GlcNAc breakdown activity. |
| T5 |
806-1051 |
Sentence |
denotes |
Though neither was able to complement the Dictyostelium gene, expression in the trypanosomatid Leishmania tarentolae resulted in elevated levels of UDP-[(3)H]GlcNAc:Thr-peptide GlcNAc-transferase activity and UDP-[(3)H]GlcNAc breakdown activity. |
| T5 |
806-1051 |
Sentence |
denotes |
Though neither was able to complement the Dictyostelium gene, expression in the trypanosomatid Leishmania tarentolae resulted in elevated levels of UDP-[(3)H]GlcNAc:Thr-peptide GlcNAc-transferase activity and UDP-[(3)H]GlcNAc breakdown activity. |
| TextSentencer_T6 |
1052-1235 |
Sentence |
denotes |
The ectodomain of TcOGNT2 was expressed and the secreted protein was found to retain both activities after extensive purification away from other proteins and the endogenous activity. |
| T6 |
1052-1235 |
Sentence |
denotes |
The ectodomain of TcOGNT2 was expressed and the secreted protein was found to retain both activities after extensive purification away from other proteins and the endogenous activity. |
| T6 |
1052-1235 |
Sentence |
denotes |
The ectodomain of TcOGNT2 was expressed and the secreted protein was found to retain both activities after extensive purification away from other proteins and the endogenous activity. |
| TextSentencer_T7 |
1236-1356 |
Sentence |
denotes |
Product analysis showed that (3)H was transferred as GlcNAc to a hydroxyamino acid, and breakdown was due to hydrolysis. |
| T7 |
1236-1356 |
Sentence |
denotes |
Product analysis showed that (3)H was transferred as GlcNAc to a hydroxyamino acid, and breakdown was due to hydrolysis. |
| T7 |
1236-1356 |
Sentence |
denotes |
Product analysis showed that (3)H was transferred as GlcNAc to a hydroxyamino acid, and breakdown was due to hydrolysis. |
| TextSentencer_T8 |
1357-1568 |
Sentence |
denotes |
Both activities were specific for UDP-GlcNAc relative to UDP-GalNAc and were abolished by active site point mutations that inactivate a related Dictyostelium enzyme and distantly related animal pp-alphaGalNAcTs. |
| T8 |
1357-1568 |
Sentence |
denotes |
Both activities were specific for UDP-GlcNAc relative to UDP-GalNAc and were abolished by active site point mutations that inactivate a related Dictyostelium enzyme and distantly related animal pp-alphaGalNAcTs. |
| T8 |
1357-1568 |
Sentence |
denotes |
Both activities were specific for UDP-GlcNAc relative to UDP-GalNAc and were abolished by active site point mutations that inactivate a related Dictyostelium enzyme and distantly related animal pp-alphaGalNAcTs. |
| TextSentencer_T9 |
1569-1700 |
Sentence |
denotes |
The peptide preference and the alkaline pH optimum were indistinguishable from those of the native activity in T. cruzi microsomes. |
| T9 |
1569-1700 |
Sentence |
denotes |
The peptide preference and the alkaline pH optimum were indistinguishable from those of the native activity in T. cruzi microsomes. |
| T9 |
1569-1700 |
Sentence |
denotes |
The peptide preference and the alkaline pH optimum were indistinguishable from those of the native activity in T. cruzi microsomes. |
| TextSentencer_T10 |
1701-1938 |
Sentence |
denotes |
The results suggest that mucin-type O-glycosylation in T. cruzi is initiated by conserved members of CAZy family GT60, which is homologous to the GT27 family of animal pp-alphaGalNAcTs that initiate mucin-type O-glycosylation in animals. |
| T10 |
1701-1938 |
Sentence |
denotes |
The results suggest that mucin-type O-glycosylation in T. cruzi is initiated by conserved members of CAZy family GT60, which is homologous to the GT27 family of animal pp-alphaGalNAcTs that initiate mucin-type O-glycosylation in animals. |
| T10 |
1701-1938 |
Sentence |
denotes |
The results suggest that mucin-type O-glycosylation in T. cruzi is initiated by conserved members of CAZy family GT60, which is homologous to the GT27 family of animal pp-alphaGalNAcTs that initiate mucin-type O-glycosylation in animals. |