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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.
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.
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.
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.
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.
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.
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.
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.
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.
T5 621-705 Sentence denotes When both sequons are present in RGP(-23), 87% of the N-glycans are of complex type.
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.
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.
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.
T7 887-984 Sentence denotes To explore this further, we constructed soluble forms of RGP: RGP(WT)T441His and RGP(--3)T441His.
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.
T8 985-1127 Sentence denotes Tryptic glycopeptides from these purified secreted proteins were isolated by HPLC and characterized by a 3D oligosaccharide mapping technique.
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).
T9 1128-1227 Sentence denotes RGP(WT)T441His had fucosylated, bi- and triantennary complex type glycans at Asn(247) and Asn(319).
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).
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).
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.
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.
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.
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.
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.
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.
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.