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PubMed:16306051 JSONTXT 64 Projects

Annnotations TAB TSV DIC JSON TextAE Lectin_function IAV-Glycan

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.