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PubMed:9363441 JSONTXT

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Glycan-Motif

Id Subject Object Predicate Lexical cue
T1 44-47 https://glytoucan.org/Structures/Glycans/G61168WC denotes GM2
T2 44-47 https://glytoucan.org/Structures/Glycans/G79389NT denotes GM2
T3 48-51 https://glytoucan.org/Structures/Glycans/G02657AK denotes GD2
T4 48-51 https://glytoucan.org/Structures/Glycans/G41759HA denotes GD2
T5 609-612 https://glytoucan.org/Structures/Glycans/G61168WC denotes GM2
T6 609-612 https://glytoucan.org/Structures/Glycans/G79389NT denotes GM2
T7 614-617 https://glytoucan.org/Structures/Glycans/G02657AK denotes GD2
T8 614-617 https://glytoucan.org/Structures/Glycans/G41759HA denotes GD2

GlyCosmos6-Glycan-Motif-Image

Id Subject Object Predicate Lexical cue image
T1 44-47 Glycan_Motif denotes GM2 https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G79389NT|https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G61168WC
T3 48-51 Glycan_Motif denotes GD2 https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G41759HA|https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G02657AK
T5 609-612 Glycan_Motif denotes GM2 https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G79389NT|https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G61168WC
T7 614-617 Glycan_Motif denotes GD2 https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G41759HA|https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G02657AK

sentences

Id Subject Object Predicate Lexical cue
TextSentencer_T1 0-176 Sentence denotes Beta 1,4 N-acetylgalactosaminyltransferase (GM2/GD2/GA2 synthase) forms homodimers in the endoplasmic reticulum: a strategy to test for dimerization of Golgi membrane proteins.
TextSentencer_T2 177-328 Sentence denotes Many Golgi membrane-bound glycosyltransferases exist as intermolecular disulfide bonded species, some of which have been demonstrated to be homodimers.
TextSentencer_T3 329-421 Sentence denotes Evidence for homodimer formation has come primarily from radiation inactivation experiments.
TextSentencer_T4 422-627 Sentence denotes We utilized an alternative strategy to test for homodimer formation of the cloned beta 1,4 N-acetylgalactosaminyltransferase (GalNAcT) responsible for synthesis of the glycosphingolipids GM2, GD2, and GA2.
TextSentencer_T5 628-877 Sentence denotes We stably transfected CHO cells with myc epitopetagged GalNAcT, which localizes primarily to the Golgi, and a hemagglutinin (HA) epitope-tagged GalNAcT fusion protein in which the cytoplasmic domain of GalNAcT was replaced by an ER retention signal.
TextSentencer_T6 878-955 Sentence denotes We then sought evidence for dimer formation between the two forms of GalNAcT.
TextSentencer_T7 956-1156 Sentence denotes Immunoprecipitation with anti-myc or anti-HA co-immunoprecipitated the HA-tagged form or the myc-tagged form, respectively, providing evidence for the physical association of the two forms of GalNAcT.
TextSentencer_T8 1157-1278 Sentence denotes As a result of this association, GalNAcT/myc increased in the ER as demonstrated by Western blots and immunofluorescence.
TextSentencer_T9 1279-1375 Sentence denotes The rapid formation of dimers provided further evidence for dimer formation occurring in the ER.
TextSentencer_T10 1376-1509 Sentence denotes In summary, these results demonstrate that GalNAcT forms homodimers as a result of intermolecular disulfide bond formation in the ER.
TextSentencer_T11 1510-1629 Sentence denotes Furthermore, this ER motif strategy is potentially useful for demonstrating homodimer formation of other Golgi enzymes.
T1 0-176 Sentence denotes Beta 1,4 N-acetylgalactosaminyltransferase (GM2/GD2/GA2 synthase) forms homodimers in the endoplasmic reticulum: a strategy to test for dimerization of Golgi membrane proteins.
T2 177-328 Sentence denotes Many Golgi membrane-bound glycosyltransferases exist as intermolecular disulfide bonded species, some of which have been demonstrated to be homodimers.
T3 329-421 Sentence denotes Evidence for homodimer formation has come primarily from radiation inactivation experiments.
T4 422-627 Sentence denotes We utilized an alternative strategy to test for homodimer formation of the cloned beta 1,4 N-acetylgalactosaminyltransferase (GalNAcT) responsible for synthesis of the glycosphingolipids GM2, GD2, and GA2.
T5 628-877 Sentence denotes We stably transfected CHO cells with myc epitopetagged GalNAcT, which localizes primarily to the Golgi, and a hemagglutinin (HA) epitope-tagged GalNAcT fusion protein in which the cytoplasmic domain of GalNAcT was replaced by an ER retention signal.
T6 878-955 Sentence denotes We then sought evidence for dimer formation between the two forms of GalNAcT.
T7 956-1156 Sentence denotes Immunoprecipitation with anti-myc or anti-HA co-immunoprecipitated the HA-tagged form or the myc-tagged form, respectively, providing evidence for the physical association of the two forms of GalNAcT.
T8 1157-1278 Sentence denotes As a result of this association, GalNAcT/myc increased in the ER as demonstrated by Western blots and immunofluorescence.
T9 1279-1375 Sentence denotes The rapid formation of dimers provided further evidence for dimer formation occurring in the ER.
T10 1376-1509 Sentence denotes In summary, these results demonstrate that GalNAcT forms homodimers as a result of intermolecular disulfide bond formation in the ER.
T11 1510-1629 Sentence denotes Furthermore, this ER motif strategy is potentially useful for demonstrating homodimer formation of other Golgi enzymes.
T1 0-176 Sentence denotes Beta 1,4 N-acetylgalactosaminyltransferase (GM2/GD2/GA2 synthase) forms homodimers in the endoplasmic reticulum: a strategy to test for dimerization of Golgi membrane proteins.
T2 177-328 Sentence denotes Many Golgi membrane-bound glycosyltransferases exist as intermolecular disulfide bonded species, some of which have been demonstrated to be homodimers.
T3 329-421 Sentence denotes Evidence for homodimer formation has come primarily from radiation inactivation experiments.
T4 422-627 Sentence denotes We utilized an alternative strategy to test for homodimer formation of the cloned beta 1,4 N-acetylgalactosaminyltransferase (GalNAcT) responsible for synthesis of the glycosphingolipids GM2, GD2, and GA2.
T5 628-877 Sentence denotes We stably transfected CHO cells with myc epitopetagged GalNAcT, which localizes primarily to the Golgi, and a hemagglutinin (HA) epitope-tagged GalNAcT fusion protein in which the cytoplasmic domain of GalNAcT was replaced by an ER retention signal.
T6 878-955 Sentence denotes We then sought evidence for dimer formation between the two forms of GalNAcT.
T7 956-1156 Sentence denotes Immunoprecipitation with anti-myc or anti-HA co-immunoprecipitated the HA-tagged form or the myc-tagged form, respectively, providing evidence for the physical association of the two forms of GalNAcT.
T8 1157-1278 Sentence denotes As a result of this association, GalNAcT/myc increased in the ER as demonstrated by Western blots and immunofluorescence.
T9 1279-1375 Sentence denotes The rapid formation of dimers provided further evidence for dimer formation occurring in the ER.
T10 1376-1509 Sentence denotes In summary, these results demonstrate that GalNAcT forms homodimers as a result of intermolecular disulfide bond formation in the ER.
T11 1510-1629 Sentence denotes Furthermore, this ER motif strategy is potentially useful for demonstrating homodimer formation of other Golgi enzymes.

GlyCosmos6-Glycan-Motif-Structure

Id Subject Object Predicate Lexical cue
T1 44-47 https://glytoucan.org/Structures/Glycans/G61168WC denotes GM2
T2 44-47 https://glytoucan.org/Structures/Glycans/G79389NT denotes GM2
T3 48-51 https://glytoucan.org/Structures/Glycans/G02657AK denotes GD2
T4 48-51 https://glytoucan.org/Structures/Glycans/G41759HA denotes GD2
T5 609-612 https://glytoucan.org/Structures/Glycans/G61168WC denotes GM2
T6 609-612 https://glytoucan.org/Structures/Glycans/G79389NT denotes GM2
T7 614-617 https://glytoucan.org/Structures/Glycans/G02657AK denotes GD2
T8 614-617 https://glytoucan.org/Structures/Glycans/G41759HA denotes GD2

GlycoBiology-FMA

Id Subject Object Predicate Lexical cue
_T1 90-101 FMAID:66856 denotes endoplasmic
_T2 90-101 FMAID:165003 denotes endoplasmic
_T3 90-111 FMAID:162308 denotes endoplasmic reticulum
_T4 90-111 FMAID:165027 denotes endoplasmic reticulum
_T5 90-111 FMAID:66898 denotes endoplasmic reticulum
_T6 90-111 FMAID:165026 denotes endoplasmic reticulum
_T7 90-111 FMAID:210679 denotes endoplasmic reticulum
_T8 90-111 FMAID:66897 denotes endoplasmic reticulum
_T9 90-111 FMAID:210694 denotes endoplasmic reticulum
_T10 90-111 FMAID:80351 denotes endoplasmic reticulum
_T11 90-111 FMAID:63842 denotes endoplasmic reticulum
_T12 90-111 FMAID:188464 denotes endoplasmic reticulum
_T13 90-111 FMAID:212510 denotes endoplasmic reticulum
_T14 90-111 FMAID:67429 denotes endoplasmic reticulum
_T15 90-111 FMAID:165250 denotes endoplasmic reticulum
_T16 90-111 FMAID:199093 denotes endoplasmic reticulum
_T17 90-111 FMAID:211269 denotes endoplasmic reticulum
_T18 90-111 FMAID:165142 denotes endoplasmic reticulum
_T19 90-111 FMAID:165144 denotes endoplasmic reticulum
_T20 90-111 FMAID:67434 denotes endoplasmic reticulum
_T21 90-111 FMAID:165141 denotes endoplasmic reticulum
_T22 90-111 FMAID:67438 denotes endoplasmic reticulum
_T23 102-111 FMAID:7646 denotes reticulum
_T24 102-111 FMAID:94520 denotes reticulum
_T25 127-131 FMAID:178661 denotes test
_T26 158-175 FMAID:198528 denotes membrane proteins
_T27 158-175 FMAID:89997 denotes membrane proteins
_T28 167-175 FMAID:165447 denotes proteins
_T29 167-175 FMAID:67257 denotes proteins
_T30 182-196 FMAID:199154 denotes Golgi membrane
_T31 233-264 FMAID:85706 denotes intermolecular disulfide bonded
_T32 233-264 FMAID:202234 denotes intermolecular disulfide bonded
_T33 461-465 FMAID:178661 denotes test
_T34 590-608 FMAID:196810 denotes glycosphingolipids
_T35 590-608 FMAID:82813 denotes glycosphingolipids
_T36 590-608 FMAID:196807 denotes glycosphingolipids
_T37 590-608 FMAID:82812 denotes glycosphingolipids
_T38 590-608 FMAID:82819 denotes glycosphingolipids
_T39 590-608 FMAID:196814 denotes glycosphingolipids
_T40 590-608 FMAID:82817 denotes glycosphingolipids
_T41 590-608 FMAID:196812 denotes glycosphingolipids
_T42 590-608 FMAID:196808 denotes glycosphingolipids
_T43 590-608 FMAID:82815 denotes glycosphingolipids
_T44 590-608 FMAID:82814 denotes glycosphingolipids
_T45 590-608 FMAID:196813 denotes glycosphingolipids
_T46 590-608 FMAID:196809 denotes glycosphingolipids
_T47 590-608 FMAID:196815 denotes glycosphingolipids
_T48 590-608 FMAID:82811 denotes glycosphingolipids
_T49 590-608 FMAID:82818 denotes glycosphingolipids
_T50 590-608 FMAID:196806 denotes glycosphingolipids
_T51 654-659 FMAID:169002 denotes cells
_T52 654-659 FMAID:68646 denotes cells
_T53 787-794 FMAID:165447 denotes protein
_T54 787-794 FMAID:67257 denotes protein
_T55 808-819 FMAID:165187 denotes cytoplasmic
_T56 808-819 FMAID:164989 denotes cytoplasmic
_T57 808-819 FMAID:66835 denotes cytoplasmic
_T58 1459-1488 FMAID:85706 denotes intermolecular disulfide bond
_T59 1459-1488 FMAID:202234 denotes intermolecular disulfide bond

uniprot-human

Id Subject Object Predicate Lexical cue
T1 44-64 http://www.uniprot.org/uniprot/Q00973 denotes GM2/GD2/GA2 synthase
T2 753-755 http://www.uniprot.org/uniprot/P69208 denotes HA
T3 998-1000 http://www.uniprot.org/uniprot/P69208 denotes HA
T4 1027-1029 http://www.uniprot.org/uniprot/P69208 denotes HA
T5 857-859 http://www.uniprot.org/uniprot/P03372 denotes ER
T6 1219-1221 http://www.uniprot.org/uniprot/P03372 denotes ER
T7 1372-1374 http://www.uniprot.org/uniprot/P03372 denotes ER
T8 1506-1508 http://www.uniprot.org/uniprot/P03372 denotes ER
T9 1528-1530 http://www.uniprot.org/uniprot/P03372 denotes ER

uniprot-mouse

Id Subject Object Predicate Lexical cue
T1 665-668 http://www.uniprot.org/uniprot/Q9Z304 denotes myc
T2 986-989 http://www.uniprot.org/uniprot/Q9Z304 denotes myc
T3 1049-1052 http://www.uniprot.org/uniprot/Q9Z304 denotes myc
T4 1198-1201 http://www.uniprot.org/uniprot/Q9Z304 denotes myc
T5 665-668 http://www.uniprot.org/uniprot/P01108 denotes myc
T6 986-989 http://www.uniprot.org/uniprot/P01108 denotes myc
T7 1049-1052 http://www.uniprot.org/uniprot/P01108 denotes myc
T8 1198-1201 http://www.uniprot.org/uniprot/P01108 denotes myc
T9 857-859 http://www.uniprot.org/uniprot/P19785 denotes ER
T10 1219-1221 http://www.uniprot.org/uniprot/P19785 denotes ER
T11 1372-1374 http://www.uniprot.org/uniprot/P19785 denotes ER
T12 1506-1508 http://www.uniprot.org/uniprot/P19785 denotes ER
T13 1528-1530 http://www.uniprot.org/uniprot/P19785 denotes ER

GlycoBiology-NCBITAXON

Id Subject Object Predicate Lexical cue
T1 0-4 http://purl.bioontology.org/ontology/NCBITAXON/3554 denotes Beta
T2 0-4 http://purl.bioontology.org/ontology/NCBITAXON/158455 denotes Beta
T3 177-181 http://purl.bioontology.org/ontology/NCBITAXON/9973 denotes Many
T4 504-508 http://purl.bioontology.org/ontology/NCBITAXON/3554 denotes beta
T5 504-508 http://purl.bioontology.org/ontology/NCBITAXON/158455 denotes beta
T6 654-659 http://purl.bioontology.org/ontology/STY/T025 denotes cells
T7 1001-1003 http://purl.bioontology.org/ontology/NCBITAXON/13893 denotes co

GO-BP

Id Subject Object Predicate Lexical cue
T1 152-175 http://purl.obolibrary.org/obo/GO_1903292 denotes Golgi membrane proteins
T2 352-361 http://purl.obolibrary.org/obo/GO_0009058 denotes formation
T3 480-489 http://purl.obolibrary.org/obo/GO_0009058 denotes formation
T4 912-921 http://purl.obolibrary.org/obo/GO_0009058 denotes formation
T5 1289-1298 http://purl.obolibrary.org/obo/GO_0009058 denotes formation
T6 1345-1354 http://purl.obolibrary.org/obo/GO_0009058 denotes formation
T7 1489-1498 http://purl.obolibrary.org/obo/GO_0009058 denotes formation
T8 1596-1605 http://purl.obolibrary.org/obo/GO_0009058 denotes formation
T9 573-582 http://purl.obolibrary.org/obo/GO_0009058 denotes synthesis
T10 573-608 http://purl.obolibrary.org/obo/GO_0006688 denotes synthesis of the glycosphingolipids
T11 650-653 http://purl.obolibrary.org/obo/GO_0043848 denotes CHO
T12 698-707 http://purl.obolibrary.org/obo/GO_0051179 denotes localizes
T13 860-869 http://purl.obolibrary.org/obo/GO_0051235 denotes retention
T14 870-876 http://purl.obolibrary.org/obo/GO_0023052 denotes signal

GO-CC

Id Subject Object Predicate Lexical cue
T1 90-111 http://purl.obolibrary.org/obo/GO_0005783 denotes endoplasmic reticulum
T2 152-157 http://purl.obolibrary.org/obo/GO_0005794 denotes Golgi
T3 182-187 http://purl.obolibrary.org/obo/GO_0005794 denotes Golgi
T4 725-730 http://purl.obolibrary.org/obo/GO_0005794 denotes Golgi
T5 1615-1620 http://purl.obolibrary.org/obo/GO_0005794 denotes Golgi
T6 152-166 http://purl.obolibrary.org/obo/GO_0000139 denotes Golgi membrane
T7 182-196 http://purl.obolibrary.org/obo/GO_0000139 denotes Golgi membrane
T8 152-175 http://purl.obolibrary.org/obo/GO_0030173 denotes Golgi membrane proteins
T9 158-166 http://purl.obolibrary.org/obo/GO_0016020 denotes membrane
T10 188-196 http://purl.obolibrary.org/obo/GO_0016020 denotes membrane
T11 654-659 http://purl.obolibrary.org/obo/GO_0005623 denotes cells
T12 808-819 http://purl.obolibrary.org/obo/GO_0005737 denotes cytoplasmic
T13 857-859 http://purl.obolibrary.org/obo/GO_0005783 denotes ER
T14 1219-1221 http://purl.obolibrary.org/obo/GO_0005783 denotes ER
T15 1372-1374 http://purl.obolibrary.org/obo/GO_0005783 denotes ER
T16 1506-1508 http://purl.obolibrary.org/obo/GO_0005783 denotes ER
T17 1528-1530 http://purl.obolibrary.org/obo/GO_0005783 denotes ER

GlycoBiology-Epitope

Id Subject Object Predicate Lexical cue
PD-GlycoEpitope-B_T1 48-51 http://www.glycoepitope.jp/epitopes/EP0061 denotes GD2
PD-GlycoEpitope-B_T2 614-617 http://www.glycoepitope.jp/epitopes/EP0061 denotes GD2

GlyCosmos15-Glycan

Id Subject Object Predicate Lexical cue image
T1 44-47 Glycan denotes GM2 https://api.glycosmos.org/wurcs2image/latest/png/binary/G79389NT
T2 48-51 Glycan denotes GD2 https://api.glycosmos.org/wurcs2image/latest/png/binary/G02657AK
T3 52-55 Glycan denotes GA2 https://api.glycosmos.org/wurcs2image/latest/png/binary/G90562PB
T4 609-612 Glycan denotes GM2 https://api.glycosmos.org/wurcs2image/latest/png/binary/G79389NT
T5 614-617 Glycan denotes GD2 https://api.glycosmos.org/wurcs2image/latest/png/binary/G02657AK
T6 623-626 Glycan denotes GA2 https://api.glycosmos.org/wurcs2image/latest/png/binary/G90562PB

Glycan-GlyCosmos

Id Subject Object Predicate Lexical cue image
T1 44-47 Glycan denotes GM2 https://api.glycosmos.org/wurcs2image/latest/png/binary/G79389NT
T2 48-51 Glycan denotes GD2 https://api.glycosmos.org/wurcs2image/latest/png/binary/G02657AK
T3 52-55 Glycan denotes GA2 https://api.glycosmos.org/wurcs2image/latest/png/binary/G90562PB
T4 609-612 Glycan denotes GM2 https://api.glycosmos.org/wurcs2image/latest/png/binary/G79389NT
T5 614-617 Glycan denotes GD2 https://api.glycosmos.org/wurcs2image/latest/png/binary/G02657AK
T6 623-626 Glycan denotes GA2 https://api.glycosmos.org/wurcs2image/latest/png/binary/G90562PB

GlyCosmos15-UBERON

Id Subject Object Predicate Lexical cue uberon_id
T1 102-111 Body_part denotes reticulum http://purl.obolibrary.org/obo/UBERON_0007361
T2 152-166 Body_part denotes Golgi membrane http://purl.obolibrary.org/obo/GO_0000139
T3 182-196 Body_part denotes Golgi membrane http://purl.obolibrary.org/obo/GO_0000139
T4 725-730 Body_part denotes Golgi http://purl.obolibrary.org/obo/GO_0005794
T5 808-819 Body_part denotes cytoplasmic http://purl.obolibrary.org/obo/GO_0005737
T6 1615-1620 Body_part denotes Golgi http://purl.obolibrary.org/obo/GO_0005794

GlyCosmos15-Sentences

Id Subject Object Predicate Lexical cue
T1 0-176 Sentence denotes Beta 1,4 N-acetylgalactosaminyltransferase (GM2/GD2/GA2 synthase) forms homodimers in the endoplasmic reticulum: a strategy to test for dimerization of Golgi membrane proteins.
T2 177-328 Sentence denotes Many Golgi membrane-bound glycosyltransferases exist as intermolecular disulfide bonded species, some of which have been demonstrated to be homodimers.
T3 329-421 Sentence denotes Evidence for homodimer formation has come primarily from radiation inactivation experiments.
T4 422-627 Sentence denotes We utilized an alternative strategy to test for homodimer formation of the cloned beta 1,4 N-acetylgalactosaminyltransferase (GalNAcT) responsible for synthesis of the glycosphingolipids GM2, GD2, and GA2.
T5 628-877 Sentence denotes We stably transfected CHO cells with myc epitopetagged GalNAcT, which localizes primarily to the Golgi, and a hemagglutinin (HA) epitope-tagged GalNAcT fusion protein in which the cytoplasmic domain of GalNAcT was replaced by an ER retention signal.
T6 878-955 Sentence denotes We then sought evidence for dimer formation between the two forms of GalNAcT.
T7 956-1156 Sentence denotes Immunoprecipitation with anti-myc or anti-HA co-immunoprecipitated the HA-tagged form or the myc-tagged form, respectively, providing evidence for the physical association of the two forms of GalNAcT.
T8 1157-1278 Sentence denotes As a result of this association, GalNAcT/myc increased in the ER as demonstrated by Western blots and immunofluorescence.
T9 1279-1375 Sentence denotes The rapid formation of dimers provided further evidence for dimer formation occurring in the ER.
T10 1376-1509 Sentence denotes In summary, these results demonstrate that GalNAcT forms homodimers as a result of intermolecular disulfide bond formation in the ER.
T11 1510-1629 Sentence denotes Furthermore, this ER motif strategy is potentially useful for demonstrating homodimer formation of other Golgi enzymes.

GlyCosmos15-FMA

Id Subject Object Predicate Lexical cue db_id
T1 90-111 Body_part denotes endoplasmic reticulum FMA:63842
T2 152-166 Body_part denotes Golgi membrane FMA:0326754
T3 182-196 Body_part denotes Golgi membrane FMA:0326754
T4 808-819 Body_part denotes cytoplasmic FMA:66835

Anatomy-UBERON

Id Subject Object Predicate Lexical cue uberon_id
T1 102-111 Body_part denotes reticulum http://purl.obolibrary.org/obo/UBERON_0007361
T2 152-166 Body_part denotes Golgi membrane http://purl.obolibrary.org/obo/GO_0000139
T3 182-196 Body_part denotes Golgi membrane http://purl.obolibrary.org/obo/GO_0000139
T4 725-730 Body_part denotes Golgi http://purl.obolibrary.org/obo/GO_0005794
T5 808-819 Body_part denotes cytoplasmic http://purl.obolibrary.org/obo/GO_0005737
T6 1615-1620 Body_part denotes Golgi http://purl.obolibrary.org/obo/GO_0005794