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PubMed:10988254 JSONTXT 53 Projects

Annnotations TAB TSV DIC JSON TextAE Lectin_function IAV-Glycan

Id Subject Object Predicate Lexical cue
TextSentencer_T1 0-178 Sentence denotes The C-terminal N-glycosylation sites of the human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, adn -VI) are necessary for the expression of full enzyme activity.
T1 0-178 Sentence denotes The C-terminal N-glycosylation sites of the human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, adn -VI) are necessary for the expression of full enzyme activity.
T1 0-178 Sentence denotes The C-terminal N-glycosylation sites of the human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, adn -VI) are necessary for the expression of full enzyme activity.
TextSentencer_T2 179-288 Sentence denotes The alpha1,3/4-fucosyltransferases are involved in the synthesis of fucosylated cell surface glycoconjugates.
T2 179-288 Sentence denotes The alpha1,3/4-fucosyltransferases are involved in the synthesis of fucosylated cell surface glycoconjugates.
T2 179-288 Sentence denotes The alpha1,3/4-fucosyltransferases are involved in the synthesis of fucosylated cell surface glycoconjugates.
TextSentencer_T3 289-431 Sentence denotes Human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) contain two conserved C-terminal N-glycosylation sites (hFucTIII:
T3 289-431 Sentence denotes Human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) contain two conserved C-terminal N-glycosylation sites (hFucTIII:
T3 289-431 Sentence denotes Human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) contain two conserved C-terminal N-glycosylation sites (hFucTIII:
TextSentencer_T4 432-458 Sentence denotes Asn154 and Asn185; hFucTV:
T4 432-458 Sentence denotes Asn154 and Asn185; hFucTV:
T4 432-458 Sentence denotes Asn154 and Asn185; hFucTV:
TextSentencer_T5 459-490 Sentence denotes Asn167 and Asn198; and hFucTVI:
T5 459-490 Sentence denotes Asn167 and Asn198; and hFucTVI:
T5 459-490 Sentence denotes Asn167 and Asn198; and hFucTVI:
TextSentencer_T6 491-510 Sentence denotes Asn153 and Asn184).
T6 491-510 Sentence denotes Asn153 and Asn184).
T6 491-510 Sentence denotes Asn153 and Asn184).
TextSentencer_T7 511-662 Sentence denotes In the present study, we have analyzed the functional role of these potential N-glycosylation sites, laying the main emphasis on the sites in hFucTIII.
T7 511-662 Sentence denotes In the present study, we have analyzed the functional role of these potential N-glycosylation sites, laying the main emphasis on the sites in hFucTIII.
T7 511-662 Sentence denotes In the present study, we have analyzed the functional role of these potential N-glycosylation sites, laying the main emphasis on the sites in hFucTIII.
TextSentencer_T8 663-857 Sentence denotes Tunicamycin treatment completely abolished hFucTIII enzyme activity while castanospermine treatment diminished hFucTIII enzyme activity to approximately 40% of the activity of the native enzyme.
T8 663-857 Sentence denotes Tunicamycin treatment completely abolished hFucTIII enzyme activity while castanospermine treatment diminished hFucTIII enzyme activity to approximately 40% of the activity of the native enzyme.
T8 663-857 Sentence denotes Tunicamycin treatment completely abolished hFucTIII enzyme activity while castanospermine treatment diminished hFucTIII enzyme activity to approximately 40% of the activity of the native enzyme.
TextSentencer_T9 858-1101 Sentence denotes To further analyze the role of the conserved N-glycosylation sites in hFucTIII, -V, and -VI, we made a series of mutant genomic DNAs in which the asparagine residues in the potential C-terminal N-glycosylation sites were replaced by glutamine.
T9 858-1101 Sentence denotes To further analyze the role of the conserved N-glycosylation sites in hFucTIII, -V, and -VI, we made a series of mutant genomic DNAs in which the asparagine residues in the potential C-terminal N-glycosylation sites were replaced by glutamine.
T9 858-1101 Sentence denotes To further analyze the role of the conserved N-glycosylation sites in hFucTIII, -V, and -VI, we made a series of mutant genomic DNAs in which the asparagine residues in the potential C-terminal N-glycosylation sites were replaced by glutamine.
TextSentencer_T10 1102-1198 Sentence denotes Subsequently, the hFucTIII, -V, and -VI wild type and the mutants were expressed in COS-7 cells.
T10 1102-1198 Sentence denotes Subsequently, the hFucTIII, -V, and -VI wild type and the mutants were expressed in COS-7 cells.
T10 1102-1198 Sentence denotes Subsequently, the hFucTIII, -V, and -VI wild type and the mutants were expressed in COS-7 cells.
TextSentencer_T11 1199-1340 Sentence denotes All the mutants exhibited lower enzyme activity than the wild type and elimination of individual sites had different effects on the activity.
T11 1199-1340 Sentence denotes All the mutants exhibited lower enzyme activity than the wild type and elimination of individual sites had different effects on the activity.
T11 1199-1340 Sentence denotes All the mutants exhibited lower enzyme activity than the wild type and elimination of individual sites had different effects on the activity.
TextSentencer_T12 1341-1461 Sentence denotes The mutations did not affect the protein level of the mutants in the cells, but reduced the molecular mass as predicted.
T12 1341-1461 Sentence denotes The mutations did not affect the protein level of the mutants in the cells, but reduced the molecular mass as predicted.
T12 1341-1461 Sentence denotes The mutations did not affect the protein level of the mutants in the cells, but reduced the molecular mass as predicted.
TextSentencer_T13 1462-1630 Sentence denotes Kinetic analysis of hFucTIII revealed that lack of glycosylation at Asn185 did not change the Km values for the oligosaccharide acceptor and the nucleotide sugar donor.
T13 1462-1630 Sentence denotes Kinetic analysis of hFucTIII revealed that lack of glycosylation at Asn185 did not change the Km values for the oligosaccharide acceptor and the nucleotide sugar donor.
T13 1462-1630 Sentence denotes Kinetic analysis of hFucTIII revealed that lack of glycosylation at Asn185 did not change the Km values for the oligosaccharide acceptor and the nucleotide sugar donor.
TextSentencer_T14 1631-1806 Sentence denotes The present study demonstrates that hFucTIII, -V, and -VI require N-glycosylation at the two conserved C-terminal N-glycosylation sites for expression of full enzyme activity.
T14 1631-1806 Sentence denotes The present study demonstrates that hFucTIII, -V, and -VI require N-glycosylation at the two conserved C-terminal N-glycosylation sites for expression of full enzyme activity.
T14 1631-1806 Sentence denotes The present study demonstrates that hFucTIII, -V, and -VI require N-glycosylation at the two conserved C-terminal N-glycosylation sites for expression of full enzyme activity.