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sentences

Id Subject Object Predicate Lexical cue
TextSentencer_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.
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.
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.
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.
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.
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.
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.
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.
T1 0-88 Sentence denotes Minimal structural and glycosylation requirements for ST6Gal I activity and trafficking.
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.
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.
T4 477-601 Sentence denotes In addition, N-linked glycosylation may stabilize the protein but is not absolutely required for catalytic activity in vivo.
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.
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.
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.
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.
T1 0-88 Sentence denotes Minimal structural and glycosylation requirements for ST6Gal I activity and trafficking.
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.
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.
T4 477-601 Sentence denotes In addition, N-linked glycosylation may stabilize the protein but is not absolutely required for catalytic activity in vivo.
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.
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.
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.
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.
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.

GlycoBiology-FMA

Id Subject Object Predicate Lexical cue
_T1 382-393 FMAID:165003 denotes endoplasmic
_T2 382-393 FMAID:66856 denotes endoplasmic
_T3 382-403 FMAID:188464 denotes endoplasmic reticulum
_T4 382-403 FMAID:67438 denotes endoplasmic reticulum
_T5 382-403 FMAID:165142 denotes endoplasmic reticulum
_T6 382-403 FMAID:165144 denotes endoplasmic reticulum
_T7 382-403 FMAID:63842 denotes endoplasmic reticulum
_T8 382-403 FMAID:162308 denotes endoplasmic reticulum
_T9 382-403 FMAID:80351 denotes endoplasmic reticulum
_T10 382-403 FMAID:210679 denotes endoplasmic reticulum
_T11 382-403 FMAID:212510 denotes endoplasmic reticulum
_T12 382-403 FMAID:165026 denotes endoplasmic reticulum
_T13 382-403 FMAID:165250 denotes endoplasmic reticulum
_T14 382-403 FMAID:67429 denotes endoplasmic reticulum
_T15 382-403 FMAID:66897 denotes endoplasmic reticulum
_T16 382-403 FMAID:66898 denotes endoplasmic reticulum
_T17 382-403 FMAID:210694 denotes endoplasmic reticulum
_T18 382-403 FMAID:165027 denotes endoplasmic reticulum
_T19 382-403 FMAID:211269 denotes endoplasmic reticulum
_T20 382-403 FMAID:199093 denotes endoplasmic reticulum
_T21 382-406 FMAID:165141 denotes endoplasmic reticulum to
_T22 382-406 FMAID:210706 denotes endoplasmic reticulum to
_T23 382-406 FMAID:67434 denotes endoplasmic reticulum to
_T24 394-403 FMAID:7646 denotes reticulum
_T25 394-403 FMAID:94520 denotes reticulum
_T26 531-538 FMAID:165447 denotes protein
_T27 531-538 FMAID:67257 denotes protein
_T28 636-643 FMAID:67257 denotes protein
_T29 636-643 FMAID:165447 denotes protein
_T30 658-669 FMAID:82739 denotes amino acids
_T31 658-669 FMAID:196728 denotes amino acids
_T32 788-799 FMAID:165003 denotes endoplasmic
_T33 788-799 FMAID:66856 denotes endoplasmic
_T34 788-809 FMAID:199093 denotes endoplasmic reticulum
_T35 788-809 FMAID:210679 denotes endoplasmic reticulum
_T36 788-809 FMAID:188464 denotes endoplasmic reticulum
_T37 788-809 FMAID:63842 denotes endoplasmic reticulum
_T38 788-809 FMAID:162308 denotes endoplasmic reticulum
_T39 788-809 FMAID:165026 denotes endoplasmic reticulum
_T40 788-809 FMAID:66897 denotes endoplasmic reticulum
_T41 788-809 FMAID:212510 denotes endoplasmic reticulum
_T42 788-809 FMAID:165250 denotes endoplasmic reticulum
_T43 788-809 FMAID:165027 denotes endoplasmic reticulum
_T44 788-809 FMAID:165142 denotes endoplasmic reticulum
_T45 788-809 FMAID:67434 denotes endoplasmic reticulum
_T46 788-809 FMAID:165141 denotes endoplasmic reticulum
_T47 788-809 FMAID:165144 denotes endoplasmic reticulum
_T48 788-809 FMAID:66898 denotes endoplasmic reticulum
_T49 788-809 FMAID:67429 denotes endoplasmic reticulum
_T50 788-809 FMAID:67438 denotes endoplasmic reticulum
_T51 788-809 FMAID:211269 denotes endoplasmic reticulum
_T52 788-809 FMAID:210694 denotes endoplasmic reticulum
_T53 788-809 FMAID:80351 denotes endoplasmic reticulum
_T54 800-809 FMAID:94520 denotes reticulum
_T55 800-809 FMAID:7646 denotes reticulum
_T56 932-939 FMAID:67257 denotes protein
_T57 932-939 FMAID:165447 denotes protein
_T58 1015-1030 FMAID:82742 denotes oligosaccharide
_T59 1015-1030 FMAID:196731 denotes oligosaccharide
_T60 1126-1134 FMAID:165447 denotes proteins
_T61 1126-1134 FMAID:67257 denotes proteins
_T62 1451-1467 FMAID:196731 denotes oligosaccharides
_T63 1451-1467 FMAID:82742 denotes oligosaccharides
_T64 1511-1518 FMAID:67257 denotes protein
_T65 1511-1518 FMAID:165447 denotes protein
_T66 1659-1668 FMAID:30322 denotes membranes
_T67 1659-1668 FMAID:93573 denotes membranes
_T68 1659-1668 FMAID:167608 denotes membranes
_T69 1659-1668 FMAID:7145 denotes membranes

uniprot-mouse

Id Subject Object Predicate Lexical cue
T1 315-318 http://www.uniprot.org/uniprot/Q61024 denotes Asn
T2 327-330 http://www.uniprot.org/uniprot/Q61024 denotes Asn
T3 1043-1046 http://www.uniprot.org/uniprot/Q61024 denotes Asn

GlycoBiology-NCBITAXON

Id Subject Object Predicate Lexical cue
T1 1540-1551 http://purl.bioontology.org/ontology/NCBITAXON/265229 denotes oligomerize
T2 1540-1551 http://purl.bioontology.org/ontology/NCBITAXON/441291 denotes oligomerize

GO-BP

Id Subject Object Predicate Lexical cue
T1 23-36 http://purl.obolibrary.org/obo/GO_0070085 denotes glycosylation
T2 115-128 http://purl.obolibrary.org/obo/GO_0070085 denotes glycosylation
T3 344-357 http://purl.obolibrary.org/obo/GO_0070085 denotes glycosylation
T4 499-512 http://purl.obolibrary.org/obo/GO_0070085 denotes glycosylation
T5 981-994 http://purl.obolibrary.org/obo/GO_0070085 denotes glycosylation
T6 299-311 http://purl.obolibrary.org/obo/GO_0070085 denotes glycosylated
T7 748-760 http://purl.obolibrary.org/obo/GO_0070085 denotes glycosylated
T8 382-422 http://purl.obolibrary.org/obo/GO_0006888 denotes endoplasmic reticulum to Golgi transport
T9 382-422 http://purl.obolibrary.org/obo/GO_0006890 denotes endoplasmic reticulum to Golgi transport
T10 382-422 http://purl.obolibrary.org/obo/GO_0035621 denotes endoplasmic reticulum to Golgi transport
T11 382-422 http://purl.obolibrary.org/obo/GO_1902953 denotes endoplasmic reticulum to Golgi transport
T12 407-438 http://purl.obolibrary.org/obo/GO_0006893 denotes Golgi transport of the membrane
T13 413-422 http://purl.obolibrary.org/obo/GO_0006810 denotes transport
T14 413-438 http://purl.obolibrary.org/obo/GO_0055085 denotes transport of the membrane
T15 517-538 http://purl.obolibrary.org/obo/GO_0050821 denotes stabilize the protein
T16 574-592 http://purl.obolibrary.org/obo/GO_0003824 denotes catalytic activity
T17 713-721 http://purl.obolibrary.org/obo/GO_0046903 denotes secreted
T18 1160-1168 http://purl.obolibrary.org/obo/GO_0046903 denotes secreted
T19 713-732 http://purl.obolibrary.org/obo/GO_0051047 denotes secreted and active
T20 1180-1189 http://purl.obolibrary.org/obo/GO_0051179 denotes localized
T21 1262-1274 http://purl.obolibrary.org/obo/GO_0051179 denotes localization
T22 1180-1202 http://purl.obolibrary.org/obo/GO_0051645 denotes localized in the Golgi
T23 1256-1274 http://purl.obolibrary.org/obo/GO_0051645 denotes Golgi localization
T24 1590-1599 http://purl.obolibrary.org/obo/GO_0051235 denotes retention

GO-MF

Id Subject Object Predicate Lexical cue
T1 1511-1536 http://purl.obolibrary.org/obo/GO_0043621 denotes protein to self-associate

GO-CC

Id Subject Object Predicate Lexical cue
T1 164-172 http://purl.obolibrary.org/obo/GO_0016020 denotes membrane
T2 430-438 http://purl.obolibrary.org/obo/GO_0016020 denotes membrane
T3 881-889 http://purl.obolibrary.org/obo/GO_0016020 denotes membrane
T4 1397-1405 http://purl.obolibrary.org/obo/GO_0016020 denotes membrane
T5 1659-1668 http://purl.obolibrary.org/obo/GO_0016020 denotes membranes
T6 382-403 http://purl.obolibrary.org/obo/GO_0005783 denotes endoplasmic reticulum
T7 788-809 http://purl.obolibrary.org/obo/GO_0005783 denotes endoplasmic reticulum
T8 407-412 http://purl.obolibrary.org/obo/GO_0005794 denotes Golgi
T9 1197-1202 http://purl.obolibrary.org/obo/GO_0005794 denotes Golgi
T10 1256-1261 http://purl.obolibrary.org/obo/GO_0005794 denotes Golgi
T11 1607-1612 http://purl.obolibrary.org/obo/GO_0005794 denotes Golgi

EDAM-topics

Id Subject Object Predicate Lexical cue
T1 382-403 http://edamontology.org/topic_0616 denotes endoplasmic reticulum
T2 531-538 http://edamontology.org/topic_0078 denotes protein
T3 636-643 http://edamontology.org/topic_0078 denotes protein
T4 658-669 http://edamontology.org/topic_0154 denotes amino acids
T5 788-809 http://edamontology.org/topic_0616 denotes endoplasmic reticulum
T6 932-939 http://edamontology.org/topic_0078 denotes protein
T7 1126-1134 http://edamontology.org/topic_0078 denotes proteins
T8 1511-1518 http://edamontology.org/topic_0078 denotes protein

EDAM-DFO

Id Subject Object Predicate Lexical cue
T1 8-18 http://edamontology.org/data_0883 denotes structural
T2 267-279 http://edamontology.org/operation_2246 denotes demonstrated
T3 531-538 http://edamontology.org/format_1208 denotes protein
T4 531-538 http://edamontology.org/data_1467 denotes protein
T5 636-643 http://edamontology.org/format_1208 denotes protein
T6 636-643 http://edamontology.org/data_1467 denotes protein
T7 932-939 http://edamontology.org/format_1208 denotes protein
T8 932-939 http://edamontology.org/data_1467 denotes protein
T9 1116-1125 http://edamontology.org/operation_3429 denotes generates
T10 1126-1134 http://edamontology.org/data_1467 denotes proteins
T11 1126-1134 http://edamontology.org/format_1208 denotes proteins
T12 1278-1288 http://edamontology.org/operation_3465 denotes correlated
T13 1418-1425 http://edamontology.org/operation_2423 denotes predict
T14 1511-1518 http://edamontology.org/data_1467 denotes protein
T15 1511-1518 http://edamontology.org/format_1208 denotes protein

HP-phenotype

Id Subject Object Predicate Lexical cue hp_id
T1 1643-1653 Phenotype denotes inactivity HP:0001254

Anatomy-UBERON

Id Subject Object Predicate Lexical cue uberon_id
T1 164-172 Body_part denotes membrane http://purl.obolibrary.org/obo/GO_0016020|http://purl.obolibrary.org/obo/UBERON_0000094|http://purl.obolibrary.org/obo/UBERON_0000158
T4 394-403 Body_part denotes reticulum http://purl.obolibrary.org/obo/UBERON_0007361
T5 407-412 Body_part denotes Golgi http://purl.obolibrary.org/obo/GO_0005794
T6 430-438 Body_part denotes membrane http://purl.obolibrary.org/obo/GO_0016020|http://purl.obolibrary.org/obo/UBERON_0000094|http://purl.obolibrary.org/obo/UBERON_0000158
T9 800-809 Body_part denotes reticulum http://purl.obolibrary.org/obo/UBERON_0007361
T10 881-889 Body_part denotes membrane http://purl.obolibrary.org/obo/GO_0016020|http://purl.obolibrary.org/obo/UBERON_0000094|http://purl.obolibrary.org/obo/UBERON_0000158
T13 1197-1202 Body_part denotes Golgi http://purl.obolibrary.org/obo/GO_0005794
T14 1256-1261 Body_part denotes Golgi http://purl.obolibrary.org/obo/GO_0005794
T15 1397-1405 Body_part denotes membrane http://purl.obolibrary.org/obo/GO_0016020|http://purl.obolibrary.org/obo/UBERON_0000094|http://purl.obolibrary.org/obo/UBERON_0000158
T18 1607-1612 Body_part denotes Golgi http://purl.obolibrary.org/obo/GO_0005794
T19 1659-1668 Body_part denotes membranes http://purl.obolibrary.org/obo/GO_0016020|http://purl.obolibrary.org/obo/UBERON_0000094|http://purl.obolibrary.org/obo/UBERON_0000158