Id |
Subject |
Object |
Predicate |
Lexical cue |
TextSentencer_T1 |
0-127 |
Sentence |
denotes |
A biochemical and pharmacological comparison of enzyme replacement therapies for the glycolipid storage disorder Fabry disease. |
T1 |
0-127 |
Sentence |
denotes |
A biochemical and pharmacological comparison of enzyme replacement therapies for the glycolipid storage disorder Fabry disease. |
T1 |
0-127 |
Sentence |
denotes |
A biochemical and pharmacological comparison of enzyme replacement therapies for the glycolipid storage disorder Fabry disease. |
TextSentencer_T2 |
128-233 |
Sentence |
denotes |
Fabry disease is a lysosomal storage disease arising from deficiency of the enzyme alpha-galactosidase A. |
T2 |
128-233 |
Sentence |
denotes |
Fabry disease is a lysosomal storage disease arising from deficiency of the enzyme alpha-galactosidase A. |
T2 |
128-411 |
Sentence |
denotes |
Fabry disease is a lysosomal storage disease arising from deficiency of the enzyme alpha-galactosidase A. Two recombinant protein therapeutics, Fabrazyme (agalsidase beta) and Replagal (agalsidase alfa), have been approved in Europe as enzyme replacement therapies for Fabry disease. |
TextSentencer_T3 |
234-411 |
Sentence |
denotes |
Two recombinant protein therapeutics, Fabrazyme (agalsidase beta) and Replagal (agalsidase alfa), have been approved in Europe as enzyme replacement therapies for Fabry disease. |
T3 |
234-411 |
Sentence |
denotes |
Two recombinant protein therapeutics, Fabrazyme (agalsidase beta) and Replagal (agalsidase alfa), have been approved in Europe as enzyme replacement therapies for Fabry disease. |
TextSentencer_T4 |
412-597 |
Sentence |
denotes |
Both contain the same human enzyme, alpha-galactosidase A, but they are produced using different protein expression systems and have been approved for administration at different doses. |
T3 |
412-597 |
Sentence |
denotes |
Both contain the same human enzyme, alpha-galactosidase A, but they are produced using different protein expression systems and have been approved for administration at different doses. |
T4 |
412-597 |
Sentence |
denotes |
Both contain the same human enzyme, alpha-galactosidase A, but they are produced using different protein expression systems and have been approved for administration at different doses. |
TextSentencer_T5 |
598-809 |
Sentence |
denotes |
To determine if there is recognizable biochemical basis for the different doses, we performed a comparison of the two drugs, focusing on factors that are likely to influence biological activity and availability. |
T4 |
598-809 |
Sentence |
denotes |
To determine if there is recognizable biochemical basis for the different doses, we performed a comparison of the two drugs, focusing on factors that are likely to influence biological activity and availability. |
T5 |
598-809 |
Sentence |
denotes |
To determine if there is recognizable biochemical basis for the different doses, we performed a comparison of the two drugs, focusing on factors that are likely to influence biological activity and availability. |
TextSentencer_T6 |
810-924 |
Sentence |
denotes |
The two drugs have similar glycosylation, both in the type and location of the oligosaccharide structures present. |
T5 |
810-924 |
Sentence |
denotes |
The two drugs have similar glycosylation, both in the type and location of the oligosaccharide structures present. |
T6 |
810-924 |
Sentence |
denotes |
The two drugs have similar glycosylation, both in the type and location of the oligosaccharide structures present. |
TextSentencer_T7 |
925-1153 |
Sentence |
denotes |
Differences in glycosylation were mainly limited to the levels of sialic acid and mannose-6-phosphate present, with Fabrazyme having a higher percentage of fully sialylated oligosaccharides and a higher level of phosphorylation. |
T6 |
925-1153 |
Sentence |
denotes |
Differences in glycosylation were mainly limited to the levels of sialic acid and mannose-6-phosphate present, with Fabrazyme having a higher percentage of fully sialylated oligosaccharides and a higher level of phosphorylation. |
T7 |
925-1153 |
Sentence |
denotes |
Differences in glycosylation were mainly limited to the levels of sialic acid and mannose-6-phosphate present, with Fabrazyme having a higher percentage of fully sialylated oligosaccharides and a higher level of phosphorylation. |
TextSentencer_T8 |
1154-1322 |
Sentence |
denotes |
The higher levels of phosphorylated oligomannose residues correlated with increased binding to mannose-6-phosphate receptors and uptake into Fabry fibroblasts in vitro. |
T7 |
1154-1322 |
Sentence |
denotes |
The higher levels of phosphorylated oligomannose residues correlated with increased binding to mannose-6-phosphate receptors and uptake into Fabry fibroblasts in vitro. |
T8 |
1154-1322 |
Sentence |
denotes |
The higher levels of phosphorylated oligomannose residues correlated with increased binding to mannose-6-phosphate receptors and uptake into Fabry fibroblasts in vitro. |
TextSentencer_T9 |
1323-1409 |
Sentence |
denotes |
Biodistribution studies in a mouse model of Fabry disease showed similar organ uptake. |
T8 |
1323-1409 |
Sentence |
denotes |
Biodistribution studies in a mouse model of Fabry disease showed similar organ uptake. |
T9 |
1323-1409 |
Sentence |
denotes |
Biodistribution studies in a mouse model of Fabry disease showed similar organ uptake. |
TextSentencer_T10 |
1410-1566 |
Sentence |
denotes |
Likewise, antigenicity studies using antisera from Fabry patients demonstrated that both drugs were indistinguishable in terms of antibody cross-reactivity. |
T9 |
1410-1566 |
Sentence |
denotes |
Likewise, antigenicity studies using antisera from Fabry patients demonstrated that both drugs were indistinguishable in terms of antibody cross-reactivity. |
T10 |
1410-1566 |
Sentence |
denotes |
Likewise, antigenicity studies using antisera from Fabry patients demonstrated that both drugs were indistinguishable in terms of antibody cross-reactivity. |
TextSentencer_T11 |
1567-1774 |
Sentence |
denotes |
Based on these studies and present knowledge regarding the influence of glycosylation on protein biodistribution and cellular uptake, the two protein preparations appear to be functionally indistinguishable. |
T10 |
1567-1774 |
Sentence |
denotes |
Based on these studies and present knowledge regarding the influence of glycosylation on protein biodistribution and cellular uptake, the two protein preparations appear to be functionally indistinguishable. |
T11 |
1567-1774 |
Sentence |
denotes |
Based on these studies and present knowledge regarding the influence of glycosylation on protein biodistribution and cellular uptake, the two protein preparations appear to be functionally indistinguishable. |
TextSentencer_T12 |
1775-1896 |
Sentence |
denotes |
Therefore, the data from these studies provide no rationale for the use of these proteins at different therapeutic doses. |
T11 |
1775-1896 |
Sentence |
denotes |
Therefore, the data from these studies provide no rationale for the use of these proteins at different therapeutic doses. |
T12 |
1775-1896 |
Sentence |
denotes |
Therefore, the data from these studies provide no rationale for the use of these proteins at different therapeutic doses. |