Id |
Subject |
Object |
Predicate |
Lexical cue |
TextSentencer_T1 |
0-128 |
Sentence |
denotes |
N-glycosylation at one rabies virus glycoprotein sequon influences N-glycan processing at a distant sequon on the same molecule. |
TextSentencer_T2 |
129-277 |
Sentence |
denotes |
Rabies glycoprotein (RGP(WT)) contains N-glycosylation sequons at Asn(37), Asn(247), and Asn(319), although Asn(37) is not efficiently glycosylated. |
TextSentencer_T3 |
278-445 |
Sentence |
denotes |
To examine N-glycan processing at Asn(247) and Asn(319), full-length glycosylation mutants, RGP(-2-) and RGP(--3), were expressed, and Endo H sensitivity was compared. |
TextSentencer_T4 |
446-620 |
Sentence |
denotes |
When the Asn(247) sequon is present alone in RGP(-2-), 90% of its N-glycans are high-mannose type, whereas only 35% of the N-glycans at Asn(319) in RGP(--3) are high-mannose. |
TextSentencer_T5 |
621-705 |
Sentence |
denotes |
When both sequons are present in RGP(-23), 87% of the N-glycans are of complex type. |
TextSentencer_T6 |
706-886 |
Sentence |
denotes |
The differing patterns of Endo H sensitivity at sequons present individually or together suggests that glycosylation of one sequon affects glycosylation at another, distant sequon. |
TextSentencer_T7 |
887-984 |
Sentence |
denotes |
To explore this further, we constructed soluble forms of RGP: RGP(WT)T441His and RGP(--3)T441His. |
TextSentencer_T8 |
985-1127 |
Sentence |
denotes |
Tryptic glycopeptides from these purified secreted proteins were isolated by HPLC and characterized by a 3D oligosaccharide mapping technique. |
TextSentencer_T9 |
1128-1227 |
Sentence |
denotes |
RGP(WT)T441His had fucosylated, bi- and triantennary complex type glycans at Asn(247) and Asn(319). |
TextSentencer_T10 |
1228-1368 |
Sentence |
denotes |
However, Asn(247) had half as many neutral glycans, more monosialylated glycans, and fewer disialylated glycans when compared with Asn(319). |
TextSentencer_T11 |
1369-1552 |
Sentence |
denotes |
Moreover, when comparing the N-glycans at Asn(319) on RGP(--3)T441His and RGP(WT)T441His, the former had 30% more neutral, 28% more monosialylated, and 33% fewer disialylated glycans. |
TextSentencer_T12 |
1553-1717 |
Sentence |
denotes |
This suggests that the N-glycan at Asn(247) allows additional N-glycan processing to occur at Asn(319), yielding more heavily sialylated bi- and triantennary forms. |
TextSentencer_T13 |
1718-1873 |
Sentence |
denotes |
The mechanism(s) by which glycosylation at one sequon influences N-glycan processing at a distant sequon on the same glycoprotein remains to be determined. |
T1 |
0-128 |
Sentence |
denotes |
N-glycosylation at one rabies virus glycoprotein sequon influences N-glycan processing at a distant sequon on the same molecule. |
T2 |
129-277 |
Sentence |
denotes |
Rabies glycoprotein (RGP(WT)) contains N-glycosylation sequons at Asn(37), Asn(247), and Asn(319), although Asn(37) is not efficiently glycosylated. |
T3 |
278-445 |
Sentence |
denotes |
To examine N-glycan processing at Asn(247) and Asn(319), full-length glycosylation mutants, RGP(-2-) and RGP(--3), were expressed, and Endo H sensitivity was compared. |
T4 |
446-620 |
Sentence |
denotes |
When the Asn(247) sequon is present alone in RGP(-2-), 90% of its N-glycans are high-mannose type, whereas only 35% of the N-glycans at Asn(319) in RGP(--3) are high-mannose. |
T5 |
621-705 |
Sentence |
denotes |
When both sequons are present in RGP(-23), 87% of the N-glycans are of complex type. |
T6 |
706-886 |
Sentence |
denotes |
The differing patterns of Endo H sensitivity at sequons present individually or together suggests that glycosylation of one sequon affects glycosylation at another, distant sequon. |
T7 |
887-984 |
Sentence |
denotes |
To explore this further, we constructed soluble forms of RGP: RGP(WT)T441His and RGP(--3)T441His. |
T8 |
985-1127 |
Sentence |
denotes |
Tryptic glycopeptides from these purified secreted proteins were isolated by HPLC and characterized by a 3D oligosaccharide mapping technique. |
T9 |
1128-1227 |
Sentence |
denotes |
RGP(WT)T441His had fucosylated, bi- and triantennary complex type glycans at Asn(247) and Asn(319). |
T10 |
1228-1368 |
Sentence |
denotes |
However, Asn(247) had half as many neutral glycans, more monosialylated glycans, and fewer disialylated glycans when compared with Asn(319). |
T11 |
1369-1552 |
Sentence |
denotes |
Moreover, when comparing the N-glycans at Asn(319) on RGP(--3)T441His and RGP(WT)T441His, the former had 30% more neutral, 28% more monosialylated, and 33% fewer disialylated glycans. |
T12 |
1553-1717 |
Sentence |
denotes |
This suggests that the N-glycan at Asn(247) allows additional N-glycan processing to occur at Asn(319), yielding more heavily sialylated bi- and triantennary forms. |
T13 |
1718-1873 |
Sentence |
denotes |
The mechanism(s) by which glycosylation at one sequon influences N-glycan processing at a distant sequon on the same glycoprotein remains to be determined. |
T1 |
0-128 |
Sentence |
denotes |
N-glycosylation at one rabies virus glycoprotein sequon influences N-glycan processing at a distant sequon on the same molecule. |
T2 |
129-277 |
Sentence |
denotes |
Rabies glycoprotein (RGP(WT)) contains N-glycosylation sequons at Asn(37), Asn(247), and Asn(319), although Asn(37) is not efficiently glycosylated. |
T3 |
278-445 |
Sentence |
denotes |
To examine N-glycan processing at Asn(247) and Asn(319), full-length glycosylation mutants, RGP(-2-) and RGP(--3), were expressed, and Endo H sensitivity was compared. |
T4 |
446-620 |
Sentence |
denotes |
When the Asn(247) sequon is present alone in RGP(-2-), 90% of its N-glycans are high-mannose type, whereas only 35% of the N-glycans at Asn(319) in RGP(--3) are high-mannose. |
T5 |
621-705 |
Sentence |
denotes |
When both sequons are present in RGP(-23), 87% of the N-glycans are of complex type. |
T6 |
706-886 |
Sentence |
denotes |
The differing patterns of Endo H sensitivity at sequons present individually or together suggests that glycosylation of one sequon affects glycosylation at another, distant sequon. |
T7 |
887-984 |
Sentence |
denotes |
To explore this further, we constructed soluble forms of RGP: RGP(WT)T441His and RGP(--3)T441His. |
T8 |
985-1127 |
Sentence |
denotes |
Tryptic glycopeptides from these purified secreted proteins were isolated by HPLC and characterized by a 3D oligosaccharide mapping technique. |
T9 |
1128-1227 |
Sentence |
denotes |
RGP(WT)T441His had fucosylated, bi- and triantennary complex type glycans at Asn(247) and Asn(319). |
T10 |
1228-1368 |
Sentence |
denotes |
However, Asn(247) had half as many neutral glycans, more monosialylated glycans, and fewer disialylated glycans when compared with Asn(319). |
T11 |
1369-1552 |
Sentence |
denotes |
Moreover, when comparing the N-glycans at Asn(319) on RGP(--3)T441His and RGP(WT)T441His, the former had 30% more neutral, 28% more monosialylated, and 33% fewer disialylated glycans. |
T12 |
1553-1717 |
Sentence |
denotes |
This suggests that the N-glycan at Asn(247) allows additional N-glycan processing to occur at Asn(319), yielding more heavily sialylated bi- and triantennary forms. |
T13 |
1718-1873 |
Sentence |
denotes |
The mechanism(s) by which glycosylation at one sequon influences N-glycan processing at a distant sequon on the same glycoprotein remains to be determined. |