Id |
Subject |
Object |
Predicate |
Lexical cue |
TextSentencer_T1 |
0-107 |
Sentence |
denotes |
A defect in exodegradative pathways provides insight into endodegradation of heparan and dermatan sulfates. |
T1 |
0-107 |
Sentence |
denotes |
A defect in exodegradative pathways provides insight into endodegradation of heparan and dermatan sulfates. |
T1 |
0-107 |
Sentence |
denotes |
A defect in exodegradative pathways provides insight into endodegradation of heparan and dermatan sulfates. |
TextSentencer_T2 |
108-195 |
Sentence |
denotes |
Within cells, dermatan sulfate (DS) and heparan sulfate (HS) are degraded in two steps. |
T2 |
108-195 |
Sentence |
denotes |
Within cells, dermatan sulfate (DS) and heparan sulfate (HS) are degraded in two steps. |
T2 |
108-195 |
Sentence |
denotes |
Within cells, dermatan sulfate (DS) and heparan sulfate (HS) are degraded in two steps. |
TextSentencer_T3 |
196-391 |
Sentence |
denotes |
The initial endohydrolysis of these polysaccharides is followed by the sequential action of lysosomal exoenzymes to reduce the resulting oligosaccharides to monosaccharides and inorganic sulfate. |
T3 |
196-391 |
Sentence |
denotes |
The initial endohydrolysis of these polysaccharides is followed by the sequential action of lysosomal exoenzymes to reduce the resulting oligosaccharides to monosaccharides and inorganic sulfate. |
T3 |
196-391 |
Sentence |
denotes |
The initial endohydrolysis of these polysaccharides is followed by the sequential action of lysosomal exoenzymes to reduce the resulting oligosaccharides to monosaccharides and inorganic sulfate. |
TextSentencer_T4 |
392-528 |
Sentence |
denotes |
Mucopolysaccharidosis (MPS) type II is a lysosomal storage disorder caused by a deficiency of the exoenzyme iduronate-2-sulfatase (I2S). |
T4 |
392-528 |
Sentence |
denotes |
Mucopolysaccharidosis (MPS) type II is a lysosomal storage disorder caused by a deficiency of the exoenzyme iduronate-2-sulfatase (I2S). |
T4 |
392-528 |
Sentence |
denotes |
Mucopolysaccharidosis (MPS) type II is a lysosomal storage disorder caused by a deficiency of the exoenzyme iduronate-2-sulfatase (I2S). |
TextSentencer_T5 |
529-680 |
Sentence |
denotes |
Consequently, partially degraded fragments of DS and HS have been shown to accumulate in the lysosomes of affected cells and are excreted in the urine. |
T5 |
529-680 |
Sentence |
denotes |
Consequently, partially degraded fragments of DS and HS have been shown to accumulate in the lysosomes of affected cells and are excreted in the urine. |
T5 |
529-680 |
Sentence |
denotes |
Consequently, partially degraded fragments of DS and HS have been shown to accumulate in the lysosomes of affected cells and are excreted in the urine. |
TextSentencer_T6 |
681-892 |
Sentence |
denotes |
Di- to hexadecasaccharides, isolated from the urine of a MPS II patient using anion exchange and gel filtration chromatography, were identified using electrospray ionization-tandem mass spectrometry (ESI-MS/MS). |
T6 |
681-892 |
Sentence |
denotes |
Di- to hexadecasaccharides, isolated from the urine of a MPS II patient using anion exchange and gel filtration chromatography, were identified using electrospray ionization-tandem mass spectrometry (ESI-MS/MS). |
T6 |
681-892 |
Sentence |
denotes |
Di- to hexadecasaccharides, isolated from the urine of a MPS II patient using anion exchange and gel filtration chromatography, were identified using electrospray ionization-tandem mass spectrometry (ESI-MS/MS). |
TextSentencer_T7 |
893-1020 |
Sentence |
denotes |
These oligosaccharides were shown to have non-reducing terminal iduronate-2-sulfate residues by digestion with recombinant I2S. |
T7 |
893-1020 |
Sentence |
denotes |
These oligosaccharides were shown to have non-reducing terminal iduronate-2-sulfate residues by digestion with recombinant I2S. |
T7 |
893-1020 |
Sentence |
denotes |
These oligosaccharides were shown to have non-reducing terminal iduronate-2-sulfate residues by digestion with recombinant I2S. |
TextSentencer_T8 |
1021-1183 |
Sentence |
denotes |
A pattern of growing oligosaccharide chains composed of alternating uronic acid and N-acetylhexosamine residues was identified and suggested to originate from DS. |
T8 |
1021-1183 |
Sentence |
denotes |
A pattern of growing oligosaccharide chains composed of alternating uronic acid and N-acetylhexosamine residues was identified and suggested to originate from DS. |
T8 |
1021-1183 |
Sentence |
denotes |
A pattern of growing oligosaccharide chains composed of alternating uronic acid and N-acetylhexosamine residues was identified and suggested to originate from DS. |
TextSentencer_T9 |
1184-1430 |
Sentence |
denotes |
A series of oligosaccharides consisting of hexosamine/N-acetylhexosamine alternating with uronic acid residues was also identified and on the basis of the presence of unacetylated hexosamine; these oligosaccharides are proposed to derive from HS. |
T9 |
1184-1430 |
Sentence |
denotes |
A series of oligosaccharides consisting of hexosamine/N-acetylhexosamine alternating with uronic acid residues was also identified and on the basis of the presence of unacetylated hexosamine; these oligosaccharides are proposed to derive from HS. |
T9 |
1184-1430 |
Sentence |
denotes |
A series of oligosaccharides consisting of hexosamine/N-acetylhexosamine alternating with uronic acid residues was also identified and on the basis of the presence of unacetylated hexosamine; these oligosaccharides are proposed to derive from HS. |
TextSentencer_T10 |
1431-1601 |
Sentence |
denotes |
The presence of both odd and even-length oligosaccharides suggests both endo-beta-glucuronidase and endo-N-acetylhexosaminidase activities toward both glycosaminoglycans. |
T10 |
1431-1601 |
Sentence |
denotes |
The presence of both odd and even-length oligosaccharides suggests both endo-beta-glucuronidase and endo-N-acetylhexosaminidase activities toward both glycosaminoglycans. |
T10 |
1431-1601 |
Sentence |
denotes |
The presence of both odd and even-length oligosaccharides suggests both endo-beta-glucuronidase and endo-N-acetylhexosaminidase activities toward both glycosaminoglycans. |
TextSentencer_T11 |
1602-1869 |
Sentence |
denotes |
Furthermore, the putative HS oligosaccharide structures identified indicate that heparanase activities are directed toward regions of both low and high sulfation, while the N-acetylhexosaminidase activity acted only in regions of low sulfation in this polysaccharide. |
T11 |
1602-1869 |
Sentence |
denotes |
Furthermore, the putative HS oligosaccharide structures identified indicate that heparanase activities are directed toward regions of both low and high sulfation, while the N-acetylhexosaminidase activity acted only in regions of low sulfation in this polysaccharide. |
T11 |
1602-1869 |
Sentence |
denotes |
Furthermore, the putative HS oligosaccharide structures identified indicate that heparanase activities are directed toward regions of both low and high sulfation, while the N-acetylhexosaminidase activity acted only in regions of low sulfation in this polysaccharide. |