> top > projects > sentences > docs > PubMed:10764842 > annotations
sentences Home  

PubMed:10764842 JSONTXT 55 Projects

Annnotations TAB TSV DIC JSON TextAE Lectin_function IAV-Glycan

Id Subject Object Predicate Lexical cue
TextSentencer_T1 0-88 Sentence denotes Minimal structural and glycosylation requirements for ST6Gal I activity and trafficking.
T1 0-88 Sentence denotes Minimal structural and glycosylation requirements for ST6Gal I activity and trafficking.
T1 0-88 Sentence denotes Minimal structural and glycosylation requirements for ST6Gal I activity and trafficking.
TextSentencer_T2 89-258 Sentence denotes The influence of N-linked glycosylation on the activity and trafficking of membrane associated and soluble forms of the STtyr isoform of the ST6Gal I has been evaluated.
T2 89-258 Sentence denotes The influence of N-linked glycosylation on the activity and trafficking of membrane associated and soluble forms of the STtyr isoform of the ST6Gal I has been evaluated.
T2 89-258 Sentence denotes The influence of N-linked glycosylation on the activity and trafficking of membrane associated and soluble forms of the STtyr isoform of the ST6Gal I has been evaluated.
TextSentencer_T3 259-476 Sentence denotes We have demonstrated that the enzyme is glycosylated on Asn 146 and Asn 158 and that glycosylation is not required for the endoplasmic reticulum to Golgi transport of the membrane-associated form of the STtyr isoform.
T3 259-476 Sentence denotes We have demonstrated that the enzyme is glycosylated on Asn 146 and Asn 158 and that glycosylation is not required for the endoplasmic reticulum to Golgi transport of the membrane-associated form of the STtyr isoform.
T3 259-476 Sentence denotes We have demonstrated that the enzyme is glycosylated on Asn 146 and Asn 158 and that glycosylation is not required for the endoplasmic reticulum to Golgi transport of the membrane-associated form of the STtyr isoform.
TextSentencer_T4 477-601 Sentence denotes In addition, N-linked glycosylation may stabilize the protein but is not absolutely required for catalytic activity in vivo.
T4 477-601 Sentence denotes In addition, N-linked glycosylation may stabilize the protein but is not absolutely required for catalytic activity in vivo.
T4 477-601 Sentence denotes In addition, N-linked glycosylation may stabilize the protein but is not absolutely required for catalytic activity in vivo.
TextSentencer_T5 602-853 Sentence denotes In contrast, soluble forms of the protein consisting of amino acids 64-403, 89-403, and 97-403 are efficiently secreted and active in their fully glycosylated forms, but retained in the endoplasmic reticulum and inactive in their unglycosylated forms.
T5 602-853 Sentence denotes In contrast, soluble forms of the protein consisting of amino acids 64-403, 89-403, and 97-403 are efficiently secreted and active in their fully glycosylated forms, but retained in the endoplasmic reticulum and inactive in their unglycosylated forms.
T5 602-853 Sentence denotes In contrast, soluble forms of the protein consisting of amino acids 64-403, 89-403, and 97-403 are efficiently secreted and active in their fully glycosylated forms, but retained in the endoplasmic reticulum and inactive in their unglycosylated forms.
TextSentencer_T6 854-995 Sentence denotes These results suggest that membrane associated and soluble forms of the STtyr protein have different requirements for N-linked glycosylation.
T6 854-995 Sentence denotes These results suggest that membrane associated and soluble forms of the STtyr protein have different requirements for N-linked glycosylation.
T6 854-995 Sentence denotes These results suggest that membrane associated and soluble forms of the STtyr protein have different requirements for N-linked glycosylation.
TextSentencer_T7 996-1243 Sentence denotes Elimination of the oligosaccharide attached to Asn 158 in the full length STtyr single and double glycosylation mutants generates proteins that are not cleaved and secreted but stably localized in the Golgi, like the STcys isoform of the ST6Gal I.
T7 996-1243 Sentence denotes Elimination of the oligosaccharide attached to Asn 158 in the full length STtyr single and double glycosylation mutants generates proteins that are not cleaved and secreted but stably localized in the Golgi, like the STcys isoform of the ST6Gal I.
T7 996-1414 Sentence denotes Elimination of the oligosaccharide attached to Asn 158 in the full length STtyr single and double glycosylation mutants generates proteins that are not cleaved and secreted but stably localized in the Golgi, like the STcys isoform of the ST6Gal I. This stable Golgi localization is correlated with the observation that these two mutants are active in in vivo assays but inactive in in vitro assays of membrane lysates.
TextSentencer_T8 1244-1414 Sentence denotes This stable Golgi localization is correlated with the observation that these two mutants are active in in vivo assays but inactive in in vitro assays of membrane lysates.
T8 1244-1414 Sentence denotes This stable Golgi localization is correlated with the observation that these two mutants are active in in vivo assays but inactive in in vitro assays of membrane lysates.
TextSentencer_T9 1415-1711 Sentence denotes We predict that removal of N-linked oligosaccharides leads to an increased ability of the STtyr protein to self-associate or oligomerize which subsequently allows more stable retention in the Golgi and increased aggregation and inactivity when membranes are lysed in the in vitro activity assays.
T8 1415-1711 Sentence denotes We predict that removal of N-linked oligosaccharides leads to an increased ability of the STtyr protein to self-associate or oligomerize which subsequently allows more stable retention in the Golgi and increased aggregation and inactivity when membranes are lysed in the in vitro activity assays.
T9 1415-1711 Sentence denotes We predict that removal of N-linked oligosaccharides leads to an increased ability of the STtyr protein to self-associate or oligomerize which subsequently allows more stable retention in the Golgi and increased aggregation and inactivity when membranes are lysed in the in vitro activity assays.