Id |
Subject |
Object |
Predicate |
Lexical cue |
TextSentencer_T1 |
0-122 |
Sentence |
denotes |
Involvement of sialic acid in the regulation of γ--aminobutyric acid uptake activity of γ-aminobutyric acid transporter 1. |
T1 |
0-122 |
Sentence |
denotes |
Involvement of sialic acid in the regulation of γ--aminobutyric acid uptake activity of γ-aminobutyric acid transporter 1. |
T1 |
0-122 |
Sentence |
denotes |
Involvement of sialic acid in the regulation of γ--aminobutyric acid uptake activity of γ-aminobutyric acid transporter 1. |
TextSentencer_T2 |
123-254 |
Sentence |
denotes |
The γ-aminobutyric acid (GABA) transporters (GATs) have long been recognized for their key role in the uptake of neurotransmitters. |
T2 |
123-254 |
Sentence |
denotes |
The γ-aminobutyric acid (GABA) transporters (GATs) have long been recognized for their key role in the uptake of neurotransmitters. |
T2 |
123-254 |
Sentence |
denotes |
The γ-aminobutyric acid (GABA) transporters (GATs) have long been recognized for their key role in the uptake of neurotransmitters. |
TextSentencer_T3 |
255-472 |
Sentence |
denotes |
The GAT1 belongs to the family of Na(+)- and Cl(-)-coupled transport proteins, which possess 12 putative transmembrane (TM) domains and three N-glycosylation sites on the extracellular loop between TM domains 3 and 4. |
T3 |
255-472 |
Sentence |
denotes |
The GAT1 belongs to the family of Na(+)- and Cl(-)-coupled transport proteins, which possess 12 putative transmembrane (TM) domains and three N-glycosylation sites on the extracellular loop between TM domains 3 and 4. |
T3 |
255-472 |
Sentence |
denotes |
The GAT1 belongs to the family of Na(+)- and Cl(-)-coupled transport proteins, which possess 12 putative transmembrane (TM) domains and three N-glycosylation sites on the extracellular loop between TM domains 3 and 4. |
TextSentencer_T4 |
473-587 |
Sentence |
denotes |
Previously, we demonstrated that terminal trimming of N-glycans is important for the GABA uptake activity of GAT1. |
T4 |
473-587 |
Sentence |
denotes |
Previously, we demonstrated that terminal trimming of N-glycans is important for the GABA uptake activity of GAT1. |
T4 |
473-587 |
Sentence |
denotes |
Previously, we demonstrated that terminal trimming of N-glycans is important for the GABA uptake activity of GAT1. |
TextSentencer_T5 |
588-770 |
Sentence |
denotes |
In this work, we examined the effect of deficiency, removal or oxidation of surface sialic acid residues on GABA uptake activity to investigate their role in the GABA uptake of GAT1. |
T5 |
588-770 |
Sentence |
denotes |
In this work, we examined the effect of deficiency, removal or oxidation of surface sialic acid residues on GABA uptake activity to investigate their role in the GABA uptake of GAT1. |
T5 |
588-770 |
Sentence |
denotes |
In this work, we examined the effect of deficiency, removal or oxidation of surface sialic acid residues on GABA uptake activity to investigate their role in the GABA uptake of GAT1. |
TextSentencer_T6 |
771-1014 |
Sentence |
denotes |
We found that the reduced concentration of sialic acid on N-glycans was paralleled by a decreased GABA uptake activity of GAT1 in Chinese hamster ovary (CHO) Lec3 cells (mutant defective in sialic acid biosynthesis) in comparison to CHO cells. |
T6 |
771-1014 |
Sentence |
denotes |
We found that the reduced concentration of sialic acid on N-glycans was paralleled by a decreased GABA uptake activity of GAT1 in Chinese hamster ovary (CHO) Lec3 cells (mutant defective in sialic acid biosynthesis) in comparison to CHO cells. |
T6 |
771-1014 |
Sentence |
denotes |
We found that the reduced concentration of sialic acid on N-glycans was paralleled by a decreased GABA uptake activity of GAT1 in Chinese hamster ovary (CHO) Lec3 cells (mutant defective in sialic acid biosynthesis) in comparison to CHO cells. |
TextSentencer_T7 |
1015-1196 |
Sentence |
denotes |
Likewise, either enzymatic removal or chemical oxidation of terminal sialic acids using sialidase or sodium periodate, respectively, resulted in a strong reduction in GAT1 activity. |
T7 |
1015-1196 |
Sentence |
denotes |
Likewise, either enzymatic removal or chemical oxidation of terminal sialic acids using sialidase or sodium periodate, respectively, resulted in a strong reduction in GAT1 activity. |
T7 |
1015-1196 |
Sentence |
denotes |
Likewise, either enzymatic removal or chemical oxidation of terminal sialic acids using sialidase or sodium periodate, respectively, resulted in a strong reduction in GAT1 activity. |
TextSentencer_T8 |
1197-1322 |
Sentence |
denotes |
Kinetic analysis revealed that deficiency, removal or oxidation of terminal sialic acids did not affect the K(m) GABA values. |
T8 |
1197-1322 |
Sentence |
denotes |
Kinetic analysis revealed that deficiency, removal or oxidation of terminal sialic acids did not affect the K(m) GABA values. |
T8 |
1197-1322 |
Sentence |
denotes |
Kinetic analysis revealed that deficiency, removal or oxidation of terminal sialic acids did not affect the K(m) GABA values. |
TextSentencer_T9 |
1323-1476 |
Sentence |
denotes |
However, deficiency and removal of terminal sialic acids of GAT1 reduced the V(max) GABA values with a reduced apparent affinity for extracellular Na(+). |
T9 |
1323-1476 |
Sentence |
denotes |
However, deficiency and removal of terminal sialic acids of GAT1 reduced the V(max) GABA values with a reduced apparent affinity for extracellular Na(+). |
T9 |
1323-1476 |
Sentence |
denotes |
However, deficiency and removal of terminal sialic acids of GAT1 reduced the V(max) GABA values with a reduced apparent affinity for extracellular Na(+). |
TextSentencer_T10 |
1477-1620 |
Sentence |
denotes |
Oxidation of cell surface sialic acids also strongly reduced V(max) without affecting both affinities of GAT1 for GABA and Na(+), respectively. |
T10 |
1477-1620 |
Sentence |
denotes |
Oxidation of cell surface sialic acids also strongly reduced V(max) without affecting both affinities of GAT1 for GABA and Na(+), respectively. |
T10 |
1477-1620 |
Sentence |
denotes |
Oxidation of cell surface sialic acids also strongly reduced V(max) without affecting both affinities of GAT1 for GABA and Na(+), respectively. |
TextSentencer_T11 |
1621-1785 |
Sentence |
denotes |
These results demonstrated for the first time that the terminal sialic acid of N-linked oligosaccharides of GAT1 plays a crucial role in the GABA transport process. |
T11 |
1621-1785 |
Sentence |
denotes |
These results demonstrated for the first time that the terminal sialic acid of N-linked oligosaccharides of GAT1 plays a crucial role in the GABA transport process. |
T11 |
1621-1785 |
Sentence |
denotes |
These results demonstrated for the first time that the terminal sialic acid of N-linked oligosaccharides of GAT1 plays a crucial role in the GABA transport process. |