| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-73 |
Sentence |
denotes |
Identification of core 1 O-glycan T-synthase from Caenorhabditis elegans. |
| T1 |
0-73 |
Sentence |
denotes |
Identification of core 1 O-glycan T-synthase from Caenorhabditis elegans. |
| T1 |
0-73 |
Sentence |
denotes |
Identification of core 1 O-glycan T-synthase from Caenorhabditis elegans. |
| TextSentencer_T2 |
74-397 |
Sentence |
denotes |
The common O-glycan core structure in animal glycoproteins is the core 1 disaccharide Galbeta1-3GalNAcalpha1-Ser/Thr, which is generated by the addition of Gal to GalNAcalpha1-Ser/Thr by core 1 UDP-alpha-galactose (UDP-Gal):GalNAcalpha1-Ser/Thr beta1,3-galactosyltransferase (core 1 beta3-Gal-T or T-synthase, EC2.4.1.122). |
| T2 |
74-397 |
Sentence |
denotes |
The common O-glycan core structure in animal glycoproteins is the core 1 disaccharide Galbeta1-3GalNAcalpha1-Ser/Thr, which is generated by the addition of Gal to GalNAcalpha1-Ser/Thr by core 1 UDP-alpha-galactose (UDP-Gal):GalNAcalpha1-Ser/Thr beta1,3-galactosyltransferase (core 1 beta3-Gal-T or T-synthase, EC2.4.1.122). |
| T2 |
74-397 |
Sentence |
denotes |
The common O-glycan core structure in animal glycoproteins is the core 1 disaccharide Galbeta1-3GalNAcalpha1-Ser/Thr, which is generated by the addition of Gal to GalNAcalpha1-Ser/Thr by core 1 UDP-alpha-galactose (UDP-Gal):GalNAcalpha1-Ser/Thr beta1,3-galactosyltransferase (core 1 beta3-Gal-T or T-synthase, EC2.4.1.122). |
| TextSentencer_T3 |
398-628 |
Sentence |
denotes |
Although O-glycans play important roles in vertebrates, much remains to be learned from model organisms such as the free-living nematode Caenorhabditis elegans, which offer many advantages in exploring O-glycan structure/function. |
| T3 |
398-628 |
Sentence |
denotes |
Although O-glycans play important roles in vertebrates, much remains to be learned from model organisms such as the free-living nematode Caenorhabditis elegans, which offer many advantages in exploring O-glycan structure/function. |
| T3 |
398-628 |
Sentence |
denotes |
Although O-glycans play important roles in vertebrates, much remains to be learned from model organisms such as the free-living nematode Caenorhabditis elegans, which offer many advantages in exploring O-glycan structure/function. |
| TextSentencer_T4 |
629-734 |
Sentence |
denotes |
Here, we report the cloning and enzymatic characterization of T-synthase from C. elegans (Ce-T-synthase). |
| T4 |
629-734 |
Sentence |
denotes |
Here, we report the cloning and enzymatic characterization of T-synthase from C. elegans (Ce-T-synthase). |
| T4 |
629-734 |
Sentence |
denotes |
Here, we report the cloning and enzymatic characterization of T-synthase from C. elegans (Ce-T-synthase). |
| TextSentencer_T5 |
735-876 |
Sentence |
denotes |
A putative C. elegans gene for T-synthase, C38H2.2, was identified in GenBank by a BlastP search using the human T-synthase protein sequence. |
| T5 |
735-876 |
Sentence |
denotes |
A putative C. elegans gene for T-synthase, C38H2.2, was identified in GenBank by a BlastP search using the human T-synthase protein sequence. |
| T5 |
735-876 |
Sentence |
denotes |
A putative C. elegans gene for T-synthase, C38H2.2, was identified in GenBank by a BlastP search using the human T-synthase protein sequence. |
| TextSentencer_T6 |
877-1055 |
Sentence |
denotes |
The full-length cDNA for Ce-T-synthase, which was generated by polymerase chain reaction using a C. elegans cDNA library as the template, contains 1170 bp including the stop TAA. |
| T6 |
877-1055 |
Sentence |
denotes |
The full-length cDNA for Ce-T-synthase, which was generated by polymerase chain reaction using a C. elegans cDNA library as the template, contains 1170 bp including the stop TAA. |
| T6 |
877-1055 |
Sentence |
denotes |
The full-length cDNA for Ce-T-synthase, which was generated by polymerase chain reaction using a C. elegans cDNA library as the template, contains 1170 bp including the stop TAA. |
| TextSentencer_T7 |
1056-1197 |
Sentence |
denotes |
The cDNA encodes a protein of 389 amino acids with typical type II membrane topology and a remarkable 42.7% identity to the human T-synthase. |
| T7 |
1056-1197 |
Sentence |
denotes |
The cDNA encodes a protein of 389 amino acids with typical type II membrane topology and a remarkable 42.7% identity to the human T-synthase. |
| T7 |
1056-1197 |
Sentence |
denotes |
The cDNA encodes a protein of 389 amino acids with typical type II membrane topology and a remarkable 42.7% identity to the human T-synthase. |
| TextSentencer_T8 |
1198-1311 |
Sentence |
denotes |
Ce-T-synthase has seven Cys residues in the lumenal domain including six conserved Cys residues in all orthologs. |
| T8 |
1198-1311 |
Sentence |
denotes |
Ce-T-synthase has seven Cys residues in the lumenal domain including six conserved Cys residues in all orthologs. |
| T8 |
1198-1311 |
Sentence |
denotes |
Ce-T-synthase has seven Cys residues in the lumenal domain including six conserved Cys residues in all orthologs. |
| TextSentencer_T9 |
1312-1435 |
Sentence |
denotes |
The Ce-T-synthase has four potential N-glycosylation sequons, whereas the mammalian orthologs lack N-glycosylation sequons. |
| T9 |
1312-1435 |
Sentence |
denotes |
The Ce-T-synthase has four potential N-glycosylation sequons, whereas the mammalian orthologs lack N-glycosylation sequons. |
| T9 |
1312-1435 |
Sentence |
denotes |
The Ce-T-synthase has four potential N-glycosylation sequons, whereas the mammalian orthologs lack N-glycosylation sequons. |
| TextSentencer_T10 |
1436-1538 |
Sentence |
denotes |
Only one gene for Ce-T-synthase was identified in the genome-wide search, and it contains eight exons. |
| T10 |
1436-1538 |
Sentence |
denotes |
Only one gene for Ce-T-synthase was identified in the genome-wide search, and it contains eight exons. |
| T10 |
1436-1538 |
Sentence |
denotes |
Only one gene for Ce-T-synthase was identified in the genome-wide search, and it contains eight exons. |
| TextSentencer_T11 |
1539-1719 |
Sentence |
denotes |
Promoter analysis of the Ce-T-synthase using green fluorescent protein (GFP) constructs shows that the gene is expressed at all developmental stages and appears to be in all cells. |
| T11 |
1539-1719 |
Sentence |
denotes |
Promoter analysis of the Ce-T-synthase using green fluorescent protein (GFP) constructs shows that the gene is expressed at all developmental stages and appears to be in all cells. |
| T11 |
1539-1719 |
Sentence |
denotes |
Promoter analysis of the Ce-T-synthase using green fluorescent protein (GFP) constructs shows that the gene is expressed at all developmental stages and appears to be in all cells. |
| TextSentencer_T12 |
1720-1971 |
Sentence |
denotes |
Unexpectedly, only minimal activity was recovered in the recombinant, soluble Ce-T-synthase secreted from a wide variety of mammalian cell lines, whereas robust enzyme activity was recovered in the soluble Ce-T-synthase expressed in Hi-5 insect cells. |
| T12 |
1720-1971 |
Sentence |
denotes |
Unexpectedly, only minimal activity was recovered in the recombinant, soluble Ce-T-synthase secreted from a wide variety of mammalian cell lines, whereas robust enzyme activity was recovered in the soluble Ce-T-synthase expressed in Hi-5 insect cells. |
| T12 |
1720-1971 |
Sentence |
denotes |
Unexpectedly, only minimal activity was recovered in the recombinant, soluble Ce-T-synthase secreted from a wide variety of mammalian cell lines, whereas robust enzyme activity was recovered in the soluble Ce-T-synthase expressed in Hi-5 insect cells. |
| TextSentencer_T13 |
1972-2194 |
Sentence |
denotes |
Vertebrate T-synthase requires the molecular chaperone Cosmc, but our results show that Ce-T-synthase does not require Cosmc and might require invertebrate-specific factors for the formation of the optimally active enzyme. |
| T13 |
1972-2194 |
Sentence |
denotes |
Vertebrate T-synthase requires the molecular chaperone Cosmc, but our results show that Ce-T-synthase does not require Cosmc and might require invertebrate-specific factors for the formation of the optimally active enzyme. |
| T13 |
1972-2194 |
Sentence |
denotes |
Vertebrate T-synthase requires the molecular chaperone Cosmc, but our results show that Ce-T-synthase does not require Cosmc and might require invertebrate-specific factors for the formation of the optimally active enzyme. |
| TextSentencer_T14 |
2195-2390 |
Sentence |
denotes |
These results show that the Ce-T-synthase is a functional ortholog to the human T-synthase in generating core 1 O-glycans and open new avenues to explore O-glycan function in this model organism. |
| T14 |
2195-2390 |
Sentence |
denotes |
These results show that the Ce-T-synthase is a functional ortholog to the human T-synthase in generating core 1 O-glycans and open new avenues to explore O-glycan function in this model organism. |
| T14 |
2195-2390 |
Sentence |
denotes |
These results show that the Ce-T-synthase is a functional ortholog to the human T-synthase in generating core 1 O-glycans and open new avenues to explore O-glycan function in this model organism. |