| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-116 |
Sentence |
denotes |
Effect of mannose chain length on targeting of glucocerebrosidase for enzyme replacement therapy of Gaucher disease. |
| T1 |
0-116 |
Sentence |
denotes |
Effect of mannose chain length on targeting of glucocerebrosidase for enzyme replacement therapy of Gaucher disease. |
| T1 |
0-116 |
Sentence |
denotes |
Effect of mannose chain length on targeting of glucocerebrosidase for enzyme replacement therapy of Gaucher disease. |
| TextSentencer_T2 |
117-237 |
Sentence |
denotes |
Recombinant human glucocerebrosidase (imiglucerase, Cerezyme) is used in enzyme replacement therapy for Gaucher disease. |
| T2 |
117-237 |
Sentence |
denotes |
Recombinant human glucocerebrosidase (imiglucerase, Cerezyme) is used in enzyme replacement therapy for Gaucher disease. |
| T2 |
117-237 |
Sentence |
denotes |
Recombinant human glucocerebrosidase (imiglucerase, Cerezyme) is used in enzyme replacement therapy for Gaucher disease. |
| TextSentencer_T3 |
238-450 |
Sentence |
denotes |
Complex oligosaccharides present on Chinese hamster ovary cell-expressed glucocerebrosidase (GCase) are enzymatically remodeled into a mannose core, facilitating mannose receptor-mediated uptake into macrophages. |
| T3 |
238-450 |
Sentence |
denotes |
Complex oligosaccharides present on Chinese hamster ovary cell-expressed glucocerebrosidase (GCase) are enzymatically remodeled into a mannose core, facilitating mannose receptor-mediated uptake into macrophages. |
| T3 |
238-450 |
Sentence |
denotes |
Complex oligosaccharides present on Chinese hamster ovary cell-expressed glucocerebrosidase (GCase) are enzymatically remodeled into a mannose core, facilitating mannose receptor-mediated uptake into macrophages. |
| TextSentencer_T4 |
451-627 |
Sentence |
denotes |
Alternative expression systems could be used to produce GCase containing larger oligomannose structures, offering the possibility of an improvement in targeting to macrophages. |
| T4 |
451-627 |
Sentence |
denotes |
Alternative expression systems could be used to produce GCase containing larger oligomannose structures, offering the possibility of an improvement in targeting to macrophages. |
| T4 |
451-627 |
Sentence |
denotes |
Alternative expression systems could be used to produce GCase containing larger oligomannose structures, offering the possibility of an improvement in targeting to macrophages. |
| TextSentencer_T5 |
628-737 |
Sentence |
denotes |
A secondary advantage of these expression systems would be to eliminate the need for carbohydrate remodeling. |
| T5 |
628-737 |
Sentence |
denotes |
A secondary advantage of these expression systems would be to eliminate the need for carbohydrate remodeling. |
| T5 |
628-737 |
Sentence |
denotes |
A secondary advantage of these expression systems would be to eliminate the need for carbohydrate remodeling. |
| TextSentencer_T6 |
738-861 |
Sentence |
denotes |
Here, multiple expression systems were used to produce GCase containing primarily terminal oligomannose, from Man2 to Man9. |
| T6 |
738-861 |
Sentence |
denotes |
Here, multiple expression systems were used to produce GCase containing primarily terminal oligomannose, from Man2 to Man9. |
| T6 |
738-861 |
Sentence |
denotes |
Here, multiple expression systems were used to produce GCase containing primarily terminal oligomannose, from Man2 to Man9. |
| TextSentencer_T7 |
862-1065 |
Sentence |
denotes |
GCase from these multiple expression systems was compared to Cerezyme with respect to affinity for mannose receptor and serum mannose-binding lectin (MBL), macrophage uptake, and intracellular half-life. |
| T7 |
862-1065 |
Sentence |
denotes |
GCase from these multiple expression systems was compared to Cerezyme with respect to affinity for mannose receptor and serum mannose-binding lectin (MBL), macrophage uptake, and intracellular half-life. |
| T7 |
862-1065 |
Sentence |
denotes |
GCase from these multiple expression systems was compared to Cerezyme with respect to affinity for mannose receptor and serum mannose-binding lectin (MBL), macrophage uptake, and intracellular half-life. |
| TextSentencer_T8 |
1066-1210 |
Sentence |
denotes |
In vivo studies comparing clearance and targeting of Cerezyme and the Man9 form of GCase were carried out in a Gaucher mouse model (D409V/null). |
| T8 |
1066-1210 |
Sentence |
denotes |
In vivo studies comparing clearance and targeting of Cerezyme and the Man9 form of GCase were carried out in a Gaucher mouse model (D409V/null). |
| T8 |
1066-1210 |
Sentence |
denotes |
In vivo studies comparing clearance and targeting of Cerezyme and the Man9 form of GCase were carried out in a Gaucher mouse model (D409V/null). |
| TextSentencer_T9 |
1211-1314 |
Sentence |
denotes |
Mannose receptor binding, macrophage uptake, and in vivo targeting were similar for all forms of GCase. |
| T9 |
1211-1314 |
Sentence |
denotes |
Mannose receptor binding, macrophage uptake, and in vivo targeting were similar for all forms of GCase. |
| T9 |
1211-1314 |
Sentence |
denotes |
Mannose receptor binding, macrophage uptake, and in vivo targeting were similar for all forms of GCase. |
| TextSentencer_T10 |
1315-1477 |
Sentence |
denotes |
Increased MBL binding was observed for all forms of GCase having larger mannose structures than those of Cerezyme, which could influence pharmacokinetic behavior. |
| T10 |
1315-1477 |
Sentence |
denotes |
Increased MBL binding was observed for all forms of GCase having larger mannose structures than those of Cerezyme, which could influence pharmacokinetic behavior. |
| T10 |
1315-1477 |
Sentence |
denotes |
Increased MBL binding was observed for all forms of GCase having larger mannose structures than those of Cerezyme, which could influence pharmacokinetic behavior. |
| TextSentencer_T11 |
1478-1743 |
Sentence |
denotes |
These studies demonstrate that although alternative cell expression systems are effective for producing oligomannose-terminated glucocerebrosidase, there is no biochemical or pharmacological advantage in producing GCase with an increased number of mannose residues. |
| T11 |
1478-1743 |
Sentence |
denotes |
These studies demonstrate that although alternative cell expression systems are effective for producing oligomannose-terminated glucocerebrosidase, there is no biochemical or pharmacological advantage in producing GCase with an increased number of mannose residues. |
| T11 |
1478-1743 |
Sentence |
denotes |
These studies demonstrate that although alternative cell expression systems are effective for producing oligomannose-terminated glucocerebrosidase, there is no biochemical or pharmacological advantage in producing GCase with an increased number of mannose residues. |
| TextSentencer_T12 |
1744-2004 |
Sentence |
denotes |
The display of alternative carbohydrate structures on GCase expressed in these systems also runs the risk of undesirable consequences, such as an increase in MBL binding or a possible increase in immunogenicity due to the presentation of non-mammalian glycans. |
| T12 |
1744-2004 |
Sentence |
denotes |
The display of alternative carbohydrate structures on GCase expressed in these systems also runs the risk of undesirable consequences, such as an increase in MBL binding or a possible increase in immunogenicity due to the presentation of non-mammalian glycans. |
| T12 |
1744-2004 |
Sentence |
denotes |
The display of alternative carbohydrate structures on GCase expressed in these systems also runs the risk of undesirable consequences, such as an increase in MBL binding or a possible increase in immunogenicity due to the presentation of non-mammalian glycans. |