| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-114 |
Sentence |
denotes |
Substitution of the N-glycan function in glycosyltransferases by specific amino acids: ST3Gal-V as a model enzyme. |
| T1 |
0-114 |
Sentence |
denotes |
Substitution of the N-glycan function in glycosyltransferases by specific amino acids: ST3Gal-V as a model enzyme. |
| T1 |
0-114 |
Sentence |
denotes |
Substitution of the N-glycan function in glycosyltransferases by specific amino acids: ST3Gal-V as a model enzyme. |
| TextSentencer_T2 |
115-189 |
Sentence |
denotes |
The sialyltranferase ST3Gal-V transfers a sialic acid to lactosylceramide. |
| T2 |
115-189 |
Sentence |
denotes |
The sialyltranferase ST3Gal-V transfers a sialic acid to lactosylceramide. |
| T2 |
115-189 |
Sentence |
denotes |
The sialyltranferase ST3Gal-V transfers a sialic acid to lactosylceramide. |
| TextSentencer_T3 |
190-402 |
Sentence |
denotes |
We investigated the role of each of the N-glycans modifying mouse ST3Gal-V (mST3Gal-V) by measuring the in vitro enzyme activity of Chinese hamster ovary (CHO) cells transfected with ST3Gal-V cDNA or its mutants. |
| T3 |
190-402 |
Sentence |
denotes |
We investigated the role of each of the N-glycans modifying mouse ST3Gal-V (mST3Gal-V) by measuring the in vitro enzyme activity of Chinese hamster ovary (CHO) cells transfected with ST3Gal-V cDNA or its mutants. |
| T3 |
190-402 |
Sentence |
denotes |
We investigated the role of each of the N-glycans modifying mouse ST3Gal-V (mST3Gal-V) by measuring the in vitro enzyme activity of Chinese hamster ovary (CHO) cells transfected with ST3Gal-V cDNA or its mutants. |
| TextSentencer_T4 |
403-623 |
Sentence |
denotes |
By examining mutants of mST3Gal-V, in which each asparagine was replaced with glutamine (N180Q, N224Q, N334Q), we determined that all three sites are N-glycosylated and that each N-glycan is required for enzyme activity. |
| T4 |
403-623 |
Sentence |
denotes |
By examining mutants of mST3Gal-V, in which each asparagine was replaced with glutamine (N180Q, N224Q, N334Q), we determined that all three sites are N-glycosylated and that each N-glycan is required for enzyme activity. |
| T4 |
403-623 |
Sentence |
denotes |
By examining mutants of mST3Gal-V, in which each asparagine was replaced with glutamine (N180Q, N224Q, N334Q), we determined that all three sites are N-glycosylated and that each N-glycan is required for enzyme activity. |
| TextSentencer_T5 |
624-716 |
Sentence |
denotes |
Despite their importance, N-glycosylation sites in ST3Gal-V are not conserved among species. |
| T5 |
624-716 |
Sentence |
denotes |
Despite their importance, N-glycosylation sites in ST3Gal-V are not conserved among species. |
| T5 |
624-716 |
Sentence |
denotes |
Despite their importance, N-glycosylation sites in ST3Gal-V are not conserved among species. |
| TextSentencer_T6 |
717-1036 |
Sentence |
denotes |
Therefore, we considered whether the function in the activity that is performed in mST3Gal-V by the N-glycan could be substituted for by specific amino acid residues selected from the ST3Gal-V of other species or from related sialyltransferases (ST3Gal-I, -II, -III, and -IV), placed at or near the glycosylation sites. |
| T6 |
717-1036 |
Sentence |
denotes |
Therefore, we considered whether the function in the activity that is performed in mST3Gal-V by the N-glycan could be substituted for by specific amino acid residues selected from the ST3Gal-V of other species or from related sialyltransferases (ST3Gal-I, -II, -III, and -IV), placed at or near the glycosylation sites. |
| T6 |
717-1036 |
Sentence |
denotes |
Therefore, we considered whether the function in the activity that is performed in mST3Gal-V by the N-glycan could be substituted for by specific amino acid residues selected from the ST3Gal-V of other species or from related sialyltransferases (ST3Gal-I, -II, -III, and -IV), placed at or near the glycosylation sites. |
| TextSentencer_T7 |
1037-1244 |
Sentence |
denotes |
To this end, we constructed a series of interspecies mutants for mST3Gal-V, specifically, mST3Gal-V-H177D-N180S (medaka or tetraodon type), mST3Gal-V-N224K (human type), and mST3Gal-V-T336Q (zebrafish type). |
| T7 |
1037-1244 |
Sentence |
denotes |
To this end, we constructed a series of interspecies mutants for mST3Gal-V, specifically, mST3Gal-V-H177D-N180S (medaka or tetraodon type), mST3Gal-V-N224K (human type), and mST3Gal-V-T336Q (zebrafish type). |
| T7 |
1037-1244 |
Sentence |
denotes |
To this end, we constructed a series of interspecies mutants for mST3Gal-V, specifically, mST3Gal-V-H177D-N180S (medaka or tetraodon type), mST3Gal-V-N224K (human type), and mST3Gal-V-T336Q (zebrafish type). |
| TextSentencer_T8 |
1245-1334 |
Sentence |
denotes |
The ST3Gal-V activity of these mutants was quite similar to that of the wild-type enzyme. |
| T8 |
1245-1334 |
Sentence |
denotes |
The ST3Gal-V activity of these mutants was quite similar to that of the wild-type enzyme. |
| T8 |
1245-1334 |
Sentence |
denotes |
The ST3Gal-V activity of these mutants was quite similar to that of the wild-type enzyme. |
| TextSentencer_T9 |
1335-1523 |
Sentence |
denotes |
Thus, we have demonstrated here that the N-glycans on mST3Gal-V are required for activity but can be substituted for specific amino acid residues placed at or near the glycosylation sites. |
| T9 |
1335-1523 |
Sentence |
denotes |
Thus, we have demonstrated here that the N-glycans on mST3Gal-V are required for activity but can be substituted for specific amino acid residues placed at or near the glycosylation sites. |
| T9 |
1335-1523 |
Sentence |
denotes |
Thus, we have demonstrated here that the N-glycans on mST3Gal-V are required for activity but can be substituted for specific amino acid residues placed at or near the glycosylation sites. |
| TextSentencer_T10 |
1524-1636 |
Sentence |
denotes |
We named this method SUNGA (substitution of N-glycan functions in glycosyltransferases by specific amino acids). |
| T10 |
1524-1636 |
Sentence |
denotes |
We named this method SUNGA (substitution of N-glycan functions in glycosyltransferases by specific amino acids). |
| T10 |
1524-1636 |
Sentence |
denotes |
We named this method SUNGA (substitution of N-glycan functions in glycosyltransferases by specific amino acids). |
| TextSentencer_T11 |
1637-1884 |
Sentence |
denotes |
Furthermore, we verified that the ST3Gal-V mutant created using the SUNGA method maintains its high activity when expressed in Escherichia coli thereby establishing the usefulness of the SUNGA method in exploring the function of N-glycans in vivo. |
| T11 |
1637-1884 |
Sentence |
denotes |
Furthermore, we verified that the ST3Gal-V mutant created using the SUNGA method maintains its high activity when expressed in Escherichia coli thereby establishing the usefulness of the SUNGA method in exploring the function of N-glycans in vivo. |
| T11 |
1637-1884 |
Sentence |
denotes |
Furthermore, we verified that the ST3Gal-V mutant created using the SUNGA method maintains its high activity when expressed in Escherichia coli thereby establishing the usefulness of the SUNGA method in exploring the function of N-glycans in vivo. |