PubMed:11588157
Annnotations
GlycoBiology-FMA
{"project":"GlycoBiology-FMA","denotations":[{"id":"_T1","span":{"begin":28,"end":44},"obj":"FMAID:196731"},{"id":"_T2","span":{"begin":28,"end":44},"obj":"FMAID:82742"},{"id":"_T3","span":{"begin":125,"end":127},"obj":"FMAID:178405"},{"id":"_T4","span":{"begin":130,"end":135},"obj":"FMAID:68646"},{"id":"_T5","span":{"begin":130,"end":135},"obj":"FMAID:169002"},{"id":"_T6","span":{"begin":165,"end":167},"obj":"FMAID:178405"},{"id":"_T7","span":{"begin":170,"end":175},"obj":"FMAID:68646"},{"id":"_T8","span":{"begin":170,"end":175},"obj":"FMAID:169002"},{"id":"_T9","span":{"begin":219,"end":235},"obj":"FMAID:82742"},{"id":"_T10","span":{"begin":219,"end":235},"obj":"FMAID:196731"},{"id":"_T11","span":{"begin":280,"end":284},"obj":"FMAID:265385"},{"id":"_T12","span":{"begin":330,"end":334},"obj":"FMAID:265385"},{"id":"_T13","span":{"begin":403,"end":405},"obj":"FMAID:178405"},{"id":"_T14","span":{"begin":408,"end":413},"obj":"FMAID:169002"},{"id":"_T15","span":{"begin":408,"end":413},"obj":"FMAID:68646"},{"id":"_T16","span":{"begin":462,"end":475},"obj":"FMAID:167256"},{"id":"_T17","span":{"begin":462,"end":475},"obj":"FMAID:62925"},{"id":"_T18","span":{"begin":594,"end":610},"obj":"FMAID:196731"},{"id":"_T19","span":{"begin":594,"end":610},"obj":"FMAID:82742"},{"id":"_T20","span":{"begin":705,"end":709},"obj":"FMAID:198663"},{"id":"_T21","span":{"begin":722,"end":727},"obj":"FMAID:68646"},{"id":"_T22","span":{"begin":722,"end":727},"obj":"FMAID:169002"},{"id":"_T23","span":{"begin":781,"end":794},"obj":"FMAID:196789"},{"id":"_T24","span":{"begin":781,"end":794},"obj":"FMAID:82794"},{"id":"_T25","span":{"begin":882,"end":886},"obj":"FMAID:265385"},{"id":"_T26","span":{"begin":956,"end":961},"obj":"FMAID:169002"},{"id":"_T27","span":{"begin":956,"end":961},"obj":"FMAID:68646"},{"id":"_T28","span":{"begin":981,"end":985},"obj":"FMAID:265385"},{"id":"_T29","span":{"begin":999,"end":1004},"obj":"FMAID:198663"},{"id":"_T30","span":{"begin":1080,"end":1096},"obj":"FMAID:196731"},{"id":"_T31","span":{"begin":1080,"end":1096},"obj":"FMAID:82742"},{"id":"_T32","span":{"begin":1113,"end":1126},"obj":"FMAID:167256"},{"id":"_T33","span":{"begin":1113,"end":1126},"obj":"FMAID:62925"},{"id":"_T34","span":{"begin":1251,"end":1267},"obj":"FMAID:82742"},{"id":"_T35","span":{"begin":1251,"end":1267},"obj":"FMAID:196731"},{"id":"_T36","span":{"begin":1313,"end":1319},"obj":"FMAID:226027"},{"id":"_T37","span":{"begin":1313,"end":1319},"obj":"FMAID:226028"},{"id":"_T38","span":{"begin":1369,"end":1375},"obj":"FMAID:226028"},{"id":"_T39","span":{"begin":1369,"end":1375},"obj":"FMAID:226027"},{"id":"_T40","span":{"begin":1414,"end":1419},"obj":"FMAID:265385"},{"id":"_T41","span":{"begin":1472,"end":1487},"obj":"FMAID:82742"},{"id":"_T42","span":{"begin":1472,"end":1487},"obj":"FMAID:196731"},{"id":"_T43","span":{"begin":1559,"end":1563},"obj":"FMAID:265385"},{"id":"_T44","span":{"begin":1573,"end":1578},"obj":"FMAID:68646"},{"id":"_T45","span":{"begin":1573,"end":1578},"obj":"FMAID:169002"}],"namespaces":[{"prefix":"FMAID","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"Galactosylation of N-linked oligosaccharides by human beta-1,4-galactosyltransferases I, II, III, IV, V, and VI expressed in Sf-9 cells.\nSeveral studies showed that Sf-9 cells can synthesize the galactosylated N-linked oligosaccharides if beta-1,4-galactosyltransferase (beta-1,4-GalT) is supplied. The full-length human beta-1,4-GalT I, II, III, IV, V, and VI cDNAs were independently transfected into Sf-9 cells, and the galactosylation of endogenous membrane glycoproteins was examined by lectin blot analysis using Ricinus communis agglutinin-I (RCA-I), which preferentially interacts with oligosaccharides terminated with Galbeta1--\u003e4GlcNAc group. Several RCA-I-reactive bands appeared in all of the gene-transfected cells, and disappeared on treatment of blots with beta-1,4-galactosidase or N-glycanase prior to incubation with lectin. Introduction of the antisense beta-1,4-GalT II and V cDNAs separately into human colorectal adenocarcinoma SW480 cells, in which beta-1,4-GalT I, II, and V genes were expressed, resulted in the reduction of RCA-I binding toward N-linked oligosaccharides of the membrane glycoproteins. Differences were found in their K(m) values toward UDP-Gal and GlcNAcbeta-S-pNP and in their acceptor specificities toward oligosaccharides with the GlcNAcbeta1--\u003e4(GlcNAcbeta1--\u003e2)Man branch and with the GlcNAcbeta1--\u003e6(GlcNAcbeta1--\u003e2)Man branch. These results indicate that beta-1,4-GalTs II, III, IV, V, and VI are involved in the N-linked oligosaccharide biosynthesis cooperatively but not in a redundant manner with beta-1,4-GalT I within cells."}
uniprot-human
{"project":"uniprot-human","denotations":[{"id":"T1","span":{"begin":54,"end":85},"obj":"http://www.uniprot.org/uniprot/O60513"},{"id":"T2","span":{"begin":239,"end":269},"obj":"http://www.uniprot.org/uniprot/O60513"},{"id":"T3","span":{"begin":54,"end":85},"obj":"http://www.uniprot.org/uniprot/Q9UBX8"},{"id":"T4","span":{"begin":239,"end":269},"obj":"http://www.uniprot.org/uniprot/Q9UBX8"},{"id":"T5","span":{"begin":54,"end":85},"obj":"http://www.uniprot.org/uniprot/Q5T4Y5"},{"id":"T6","span":{"begin":239,"end":269},"obj":"http://www.uniprot.org/uniprot/Q5T4Y5"},{"id":"T7","span":{"begin":54,"end":85},"obj":"http://www.uniprot.org/uniprot/Q14523"},{"id":"T8","span":{"begin":239,"end":269},"obj":"http://www.uniprot.org/uniprot/Q14523"},{"id":"T9","span":{"begin":54,"end":85},"obj":"http://www.uniprot.org/uniprot/O60512"},{"id":"T10","span":{"begin":239,"end":269},"obj":"http://www.uniprot.org/uniprot/O60512"},{"id":"T11","span":{"begin":54,"end":85},"obj":"http://www.uniprot.org/uniprot/O43286"},{"id":"T12","span":{"begin":239,"end":269},"obj":"http://www.uniprot.org/uniprot/O43286"},{"id":"T13","span":{"begin":271,"end":284},"obj":"http://www.uniprot.org/uniprot/O43286"},{"id":"T14","span":{"begin":321,"end":334},"obj":"http://www.uniprot.org/uniprot/O43286"},{"id":"T15","span":{"begin":873,"end":886},"obj":"http://www.uniprot.org/uniprot/O43286"},{"id":"T16","span":{"begin":873,"end":889},"obj":"http://www.uniprot.org/uniprot/O43286"},{"id":"T17","span":{"begin":54,"end":85},"obj":"http://www.uniprot.org/uniprot/Q9UBV7"},{"id":"T18","span":{"begin":239,"end":269},"obj":"http://www.uniprot.org/uniprot/Q9UBV7"}],"text":"Galactosylation of N-linked oligosaccharides by human beta-1,4-galactosyltransferases I, II, III, IV, V, and VI expressed in Sf-9 cells.\nSeveral studies showed that Sf-9 cells can synthesize the galactosylated N-linked oligosaccharides if beta-1,4-galactosyltransferase (beta-1,4-GalT) is supplied. The full-length human beta-1,4-GalT I, II, III, IV, V, and VI cDNAs were independently transfected into Sf-9 cells, and the galactosylation of endogenous membrane glycoproteins was examined by lectin blot analysis using Ricinus communis agglutinin-I (RCA-I), which preferentially interacts with oligosaccharides terminated with Galbeta1--\u003e4GlcNAc group. Several RCA-I-reactive bands appeared in all of the gene-transfected cells, and disappeared on treatment of blots with beta-1,4-galactosidase or N-glycanase prior to incubation with lectin. Introduction of the antisense beta-1,4-GalT II and V cDNAs separately into human colorectal adenocarcinoma SW480 cells, in which beta-1,4-GalT I, II, and V genes were expressed, resulted in the reduction of RCA-I binding toward N-linked oligosaccharides of the membrane glycoproteins. Differences were found in their K(m) values toward UDP-Gal and GlcNAcbeta-S-pNP and in their acceptor specificities toward oligosaccharides with the GlcNAcbeta1--\u003e4(GlcNAcbeta1--\u003e2)Man branch and with the GlcNAcbeta1--\u003e6(GlcNAcbeta1--\u003e2)Man branch. These results indicate that beta-1,4-GalTs II, III, IV, V, and VI are involved in the N-linked oligosaccharide biosynthesis cooperatively but not in a redundant manner with beta-1,4-GalT I within cells."}
uniprot-mouse
{"project":"uniprot-mouse","denotations":[{"id":"T1","span":{"begin":63,"end":85},"obj":"http://www.uniprot.org/uniprot/P23336"},{"id":"T2","span":{"begin":248,"end":269},"obj":"http://www.uniprot.org/uniprot/P23336"},{"id":"T3","span":{"begin":873,"end":889},"obj":"http://www.uniprot.org/uniprot/Q9JMK0"}],"text":"Galactosylation of N-linked oligosaccharides by human beta-1,4-galactosyltransferases I, II, III, IV, V, and VI expressed in Sf-9 cells.\nSeveral studies showed that Sf-9 cells can synthesize the galactosylated N-linked oligosaccharides if beta-1,4-galactosyltransferase (beta-1,4-GalT) is supplied. The full-length human beta-1,4-GalT I, II, III, IV, V, and VI cDNAs were independently transfected into Sf-9 cells, and the galactosylation of endogenous membrane glycoproteins was examined by lectin blot analysis using Ricinus communis agglutinin-I (RCA-I), which preferentially interacts with oligosaccharides terminated with Galbeta1--\u003e4GlcNAc group. Several RCA-I-reactive bands appeared in all of the gene-transfected cells, and disappeared on treatment of blots with beta-1,4-galactosidase or N-glycanase prior to incubation with lectin. Introduction of the antisense beta-1,4-GalT II and V cDNAs separately into human colorectal adenocarcinoma SW480 cells, in which beta-1,4-GalT I, II, and V genes were expressed, resulted in the reduction of RCA-I binding toward N-linked oligosaccharides of the membrane glycoproteins. Differences were found in their K(m) values toward UDP-Gal and GlcNAcbeta-S-pNP and in their acceptor specificities toward oligosaccharides with the GlcNAcbeta1--\u003e4(GlcNAcbeta1--\u003e2)Man branch and with the GlcNAcbeta1--\u003e6(GlcNAcbeta1--\u003e2)Man branch. These results indicate that beta-1,4-GalTs II, III, IV, V, and VI are involved in the N-linked oligosaccharide biosynthesis cooperatively but not in a redundant manner with beta-1,4-GalT I within cells."}
GlycoBiology-NCBITAXON
{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":54,"end":58},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"},{"id":"T2","span":{"begin":54,"end":58},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T3","span":{"begin":130,"end":135},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T4","span":{"begin":170,"end":175},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T5","span":{"begin":239,"end":243},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T6","span":{"begin":239,"end":243},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"},{"id":"T7","span":{"begin":271,"end":275},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"},{"id":"T8","span":{"begin":271,"end":275},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T9","span":{"begin":321,"end":325},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"},{"id":"T10","span":{"begin":321,"end":325},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T11","span":{"begin":408,"end":413},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T12","span":{"begin":519,"end":526},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3987"},{"id":"T13","span":{"begin":519,"end":526},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/160061"},{"id":"T14","span":{"begin":519,"end":535},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3988"},{"id":"T15","span":{"begin":646,"end":651},"obj":"http://purl.bioontology.org/ontology/STY/T096"},{"id":"T16","span":{"begin":722,"end":727},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T17","span":{"begin":772,"end":776},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T18","span":{"begin":772,"end":776},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"},{"id":"T19","span":{"begin":873,"end":877},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T20","span":{"begin":873,"end":877},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"},{"id":"T21","span":{"begin":956,"end":961},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T22","span":{"begin":972,"end":976},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T23","span":{"begin":972,"end":976},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"},{"id":"T24","span":{"begin":1405,"end":1409},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T25","span":{"begin":1405,"end":1409},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"},{"id":"T26","span":{"begin":1550,"end":1554},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T27","span":{"begin":1550,"end":1554},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"},{"id":"T28","span":{"begin":1573,"end":1578},"obj":"http://purl.bioontology.org/ontology/STY/T025"}],"text":"Galactosylation of N-linked oligosaccharides by human beta-1,4-galactosyltransferases I, II, III, IV, V, and VI expressed in Sf-9 cells.\nSeveral studies showed that Sf-9 cells can synthesize the galactosylated N-linked oligosaccharides if beta-1,4-galactosyltransferase (beta-1,4-GalT) is supplied. The full-length human beta-1,4-GalT I, II, III, IV, V, and VI cDNAs were independently transfected into Sf-9 cells, and the galactosylation of endogenous membrane glycoproteins was examined by lectin blot analysis using Ricinus communis agglutinin-I (RCA-I), which preferentially interacts with oligosaccharides terminated with Galbeta1--\u003e4GlcNAc group. Several RCA-I-reactive bands appeared in all of the gene-transfected cells, and disappeared on treatment of blots with beta-1,4-galactosidase or N-glycanase prior to incubation with lectin. Introduction of the antisense beta-1,4-GalT II and V cDNAs separately into human colorectal adenocarcinoma SW480 cells, in which beta-1,4-GalT I, II, and V genes were expressed, resulted in the reduction of RCA-I binding toward N-linked oligosaccharides of the membrane glycoproteins. Differences were found in their K(m) values toward UDP-Gal and GlcNAcbeta-S-pNP and in their acceptor specificities toward oligosaccharides with the GlcNAcbeta1--\u003e4(GlcNAcbeta1--\u003e2)Man branch and with the GlcNAcbeta1--\u003e6(GlcNAcbeta1--\u003e2)Man branch. These results indicate that beta-1,4-GalTs II, III, IV, V, and VI are involved in the N-linked oligosaccharide biosynthesis cooperatively but not in a redundant manner with beta-1,4-GalT I within cells."}
sentences
{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":136},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":137,"end":298},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":299,"end":652},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":653,"end":842},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":843,"end":1127},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":1128,"end":1376},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":1377,"end":1579},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":136},"obj":"Sentence"},{"id":"T2","span":{"begin":137,"end":298},"obj":"Sentence"},{"id":"T3","span":{"begin":299,"end":652},"obj":"Sentence"},{"id":"T4","span":{"begin":653,"end":842},"obj":"Sentence"},{"id":"T5","span":{"begin":843,"end":1127},"obj":"Sentence"},{"id":"T6","span":{"begin":1128,"end":1376},"obj":"Sentence"},{"id":"T7","span":{"begin":1377,"end":1579},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":136},"obj":"Sentence"},{"id":"T2","span":{"begin":137,"end":298},"obj":"Sentence"},{"id":"T3","span":{"begin":299,"end":652},"obj":"Sentence"},{"id":"T4","span":{"begin":653,"end":842},"obj":"Sentence"},{"id":"T5","span":{"begin":843,"end":1127},"obj":"Sentence"},{"id":"T6","span":{"begin":1128,"end":1376},"obj":"Sentence"},{"id":"T7","span":{"begin":1377,"end":1579},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Galactosylation of N-linked oligosaccharides by human beta-1,4-galactosyltransferases I, II, III, IV, V, and VI expressed in Sf-9 cells.\nSeveral studies showed that Sf-9 cells can synthesize the galactosylated N-linked oligosaccharides if beta-1,4-galactosyltransferase (beta-1,4-GalT) is supplied. The full-length human beta-1,4-GalT I, II, III, IV, V, and VI cDNAs were independently transfected into Sf-9 cells, and the galactosylation of endogenous membrane glycoproteins was examined by lectin blot analysis using Ricinus communis agglutinin-I (RCA-I), which preferentially interacts with oligosaccharides terminated with Galbeta1--\u003e4GlcNAc group. Several RCA-I-reactive bands appeared in all of the gene-transfected cells, and disappeared on treatment of blots with beta-1,4-galactosidase or N-glycanase prior to incubation with lectin. Introduction of the antisense beta-1,4-GalT II and V cDNAs separately into human colorectal adenocarcinoma SW480 cells, in which beta-1,4-GalT I, II, and V genes were expressed, resulted in the reduction of RCA-I binding toward N-linked oligosaccharides of the membrane glycoproteins. Differences were found in their K(m) values toward UDP-Gal and GlcNAcbeta-S-pNP and in their acceptor specificities toward oligosaccharides with the GlcNAcbeta1--\u003e4(GlcNAcbeta1--\u003e2)Man branch and with the GlcNAcbeta1--\u003e6(GlcNAcbeta1--\u003e2)Man branch. These results indicate that beta-1,4-GalTs II, III, IV, V, and VI are involved in the N-linked oligosaccharide biosynthesis cooperatively but not in a redundant manner with beta-1,4-GalT I within cells."}
GO-BP
{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":54,"end":85},"obj":"http://purl.obolibrary.org/obo/GO_0003945"},{"id":"T2","span":{"begin":239,"end":269},"obj":"http://purl.obolibrary.org/obo/GO_0003945"},{"id":"T3","span":{"begin":271,"end":284},"obj":"http://purl.obolibrary.org/obo/GO_0003945"},{"id":"T4","span":{"begin":321,"end":334},"obj":"http://purl.obolibrary.org/obo/GO_0003945"},{"id":"T5","span":{"begin":873,"end":886},"obj":"http://purl.obolibrary.org/obo/GO_0003945"},{"id":"T6","span":{"begin":972,"end":985},"obj":"http://purl.obolibrary.org/obo/GO_0003945"},{"id":"T7","span":{"begin":1405,"end":1419},"obj":"http://purl.obolibrary.org/obo/GO_0003945"},{"id":"T8","span":{"begin":1472,"end":1500},"obj":"http://purl.obolibrary.org/obo/GO_0009312"},{"id":"T9","span":{"begin":1488,"end":1500},"obj":"http://purl.obolibrary.org/obo/GO_0009058"}],"text":"Galactosylation of N-linked oligosaccharides by human beta-1,4-galactosyltransferases I, II, III, IV, V, and VI expressed in Sf-9 cells.\nSeveral studies showed that Sf-9 cells can synthesize the galactosylated N-linked oligosaccharides if beta-1,4-galactosyltransferase (beta-1,4-GalT) is supplied. The full-length human beta-1,4-GalT I, II, III, IV, V, and VI cDNAs were independently transfected into Sf-9 cells, and the galactosylation of endogenous membrane glycoproteins was examined by lectin blot analysis using Ricinus communis agglutinin-I (RCA-I), which preferentially interacts with oligosaccharides terminated with Galbeta1--\u003e4GlcNAc group. Several RCA-I-reactive bands appeared in all of the gene-transfected cells, and disappeared on treatment of blots with beta-1,4-galactosidase or N-glycanase prior to incubation with lectin. Introduction of the antisense beta-1,4-GalT II and V cDNAs separately into human colorectal adenocarcinoma SW480 cells, in which beta-1,4-GalT I, II, and V genes were expressed, resulted in the reduction of RCA-I binding toward N-linked oligosaccharides of the membrane glycoproteins. Differences were found in their K(m) values toward UDP-Gal and GlcNAcbeta-S-pNP and in their acceptor specificities toward oligosaccharides with the GlcNAcbeta1--\u003e4(GlcNAcbeta1--\u003e2)Man branch and with the GlcNAcbeta1--\u003e6(GlcNAcbeta1--\u003e2)Man branch. These results indicate that beta-1,4-GalTs II, III, IV, V, and VI are involved in the N-linked oligosaccharide biosynthesis cooperatively but not in a redundant manner with beta-1,4-GalT I within cells."}
GO-MF
{"project":"GO-MF","denotations":[{"id":"T1","span":{"begin":1056,"end":1063},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T2","span":{"begin":1056,"end":1063},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T3","span":{"begin":1056,"end":1063},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T4","span":{"begin":1056,"end":1063},"obj":"http://purl.obolibrary.org/obo/GO_0005488"}],"text":"Galactosylation of N-linked oligosaccharides by human beta-1,4-galactosyltransferases I, II, III, IV, V, and VI expressed in Sf-9 cells.\nSeveral studies showed that Sf-9 cells can synthesize the galactosylated N-linked oligosaccharides if beta-1,4-galactosyltransferase (beta-1,4-GalT) is supplied. The full-length human beta-1,4-GalT I, II, III, IV, V, and VI cDNAs were independently transfected into Sf-9 cells, and the galactosylation of endogenous membrane glycoproteins was examined by lectin blot analysis using Ricinus communis agglutinin-I (RCA-I), which preferentially interacts with oligosaccharides terminated with Galbeta1--\u003e4GlcNAc group. Several RCA-I-reactive bands appeared in all of the gene-transfected cells, and disappeared on treatment of blots with beta-1,4-galactosidase or N-glycanase prior to incubation with lectin. Introduction of the antisense beta-1,4-GalT II and V cDNAs separately into human colorectal adenocarcinoma SW480 cells, in which beta-1,4-GalT I, II, and V genes were expressed, resulted in the reduction of RCA-I binding toward N-linked oligosaccharides of the membrane glycoproteins. Differences were found in their K(m) values toward UDP-Gal and GlcNAcbeta-S-pNP and in their acceptor specificities toward oligosaccharides with the GlcNAcbeta1--\u003e4(GlcNAcbeta1--\u003e2)Man branch and with the GlcNAcbeta1--\u003e6(GlcNAcbeta1--\u003e2)Man branch. These results indicate that beta-1,4-GalTs II, III, IV, V, and VI are involved in the N-linked oligosaccharide biosynthesis cooperatively but not in a redundant manner with beta-1,4-GalT I within cells."}
GO-CC
{"project":"GO-CC","denotations":[{"id":"T1","span":{"begin":130,"end":135},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T2","span":{"begin":170,"end":175},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T3","span":{"begin":408,"end":413},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T4","span":{"begin":722,"end":727},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T5","span":{"begin":956,"end":961},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T6","span":{"begin":1573,"end":1578},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T7","span":{"begin":453,"end":461},"obj":"http://purl.obolibrary.org/obo/GO_0016020"},{"id":"T8","span":{"begin":1104,"end":1112},"obj":"http://purl.obolibrary.org/obo/GO_0016020"}],"text":"Galactosylation of N-linked oligosaccharides by human beta-1,4-galactosyltransferases I, II, III, IV, V, and VI expressed in Sf-9 cells.\nSeveral studies showed that Sf-9 cells can synthesize the galactosylated N-linked oligosaccharides if beta-1,4-galactosyltransferase (beta-1,4-GalT) is supplied. The full-length human beta-1,4-GalT I, II, III, IV, V, and VI cDNAs were independently transfected into Sf-9 cells, and the galactosylation of endogenous membrane glycoproteins was examined by lectin blot analysis using Ricinus communis agglutinin-I (RCA-I), which preferentially interacts with oligosaccharides terminated with Galbeta1--\u003e4GlcNAc group. Several RCA-I-reactive bands appeared in all of the gene-transfected cells, and disappeared on treatment of blots with beta-1,4-galactosidase or N-glycanase prior to incubation with lectin. Introduction of the antisense beta-1,4-GalT II and V cDNAs separately into human colorectal adenocarcinoma SW480 cells, in which beta-1,4-GalT I, II, and V genes were expressed, resulted in the reduction of RCA-I binding toward N-linked oligosaccharides of the membrane glycoproteins. Differences were found in their K(m) values toward UDP-Gal and GlcNAcbeta-S-pNP and in their acceptor specificities toward oligosaccharides with the GlcNAcbeta1--\u003e4(GlcNAcbeta1--\u003e2)Man branch and with the GlcNAcbeta1--\u003e6(GlcNAcbeta1--\u003e2)Man branch. These results indicate that beta-1,4-GalTs II, III, IV, V, and VI are involved in the N-linked oligosaccharide biosynthesis cooperatively but not in a redundant manner with beta-1,4-GalT I within cells."}
EDAM-topics
{"project":"EDAM-topics","denotations":[{"id":"T1","span":{"begin":48,"end":53},"obj":"http://edamontology.org/topic_2815"},{"id":"T2","span":{"begin":145,"end":152},"obj":"http://edamontology.org/topic_3678"},{"id":"T3","span":{"begin":315,"end":320},"obj":"http://edamontology.org/topic_2815"},{"id":"T4","span":{"begin":361,"end":366},"obj":"http://edamontology.org/topic_3512"},{"id":"T5","span":{"begin":453,"end":475},"obj":"http://edamontology.org/topic_0820"},{"id":"T6","span":{"begin":579,"end":588},"obj":"http://edamontology.org/topic_0602"},{"id":"T7","span":{"begin":611,"end":621},"obj":"http://edamontology.org/topic_0749"},{"id":"T8","span":{"begin":896,"end":901},"obj":"http://edamontology.org/topic_3512"},{"id":"T9","span":{"begin":918,"end":923},"obj":"http://edamontology.org/topic_2815"},{"id":"T10","span":{"begin":999,"end":1019},"obj":"http://edamontology.org/topic_0203"},{"id":"T11","span":{"begin":1104,"end":1126},"obj":"http://edamontology.org/topic_0820"}],"text":"Galactosylation of N-linked oligosaccharides by human beta-1,4-galactosyltransferases I, II, III, IV, V, and VI expressed in Sf-9 cells.\nSeveral studies showed that Sf-9 cells can synthesize the galactosylated N-linked oligosaccharides if beta-1,4-galactosyltransferase (beta-1,4-GalT) is supplied. The full-length human beta-1,4-GalT I, II, III, IV, V, and VI cDNAs were independently transfected into Sf-9 cells, and the galactosylation of endogenous membrane glycoproteins was examined by lectin blot analysis using Ricinus communis agglutinin-I (RCA-I), which preferentially interacts with oligosaccharides terminated with Galbeta1--\u003e4GlcNAc group. Several RCA-I-reactive bands appeared in all of the gene-transfected cells, and disappeared on treatment of blots with beta-1,4-galactosidase or N-glycanase prior to incubation with lectin. Introduction of the antisense beta-1,4-GalT II and V cDNAs separately into human colorectal adenocarcinoma SW480 cells, in which beta-1,4-GalT I, II, and V genes were expressed, resulted in the reduction of RCA-I binding toward N-linked oligosaccharides of the membrane glycoproteins. Differences were found in their K(m) values toward UDP-Gal and GlcNAcbeta-S-pNP and in their acceptor specificities toward oligosaccharides with the GlcNAcbeta1--\u003e4(GlcNAcbeta1--\u003e2)Man branch and with the GlcNAcbeta1--\u003e6(GlcNAcbeta1--\u003e2)Man branch. These results indicate that beta-1,4-GalTs II, III, IV, V, and VI are involved in the N-linked oligosaccharide biosynthesis cooperatively but not in a redundant manner with beta-1,4-GalT I within cells."}
EDAM-DFO
{"project":"EDAM-DFO","denotations":[{"id":"T1","span":{"begin":504,"end":512},"obj":"http://edamontology.org/operation_2945"}],"text":"Galactosylation of N-linked oligosaccharides by human beta-1,4-galactosyltransferases I, II, III, IV, V, and VI expressed in Sf-9 cells.\nSeveral studies showed that Sf-9 cells can synthesize the galactosylated N-linked oligosaccharides if beta-1,4-galactosyltransferase (beta-1,4-GalT) is supplied. The full-length human beta-1,4-GalT I, II, III, IV, V, and VI cDNAs were independently transfected into Sf-9 cells, and the galactosylation of endogenous membrane glycoproteins was examined by lectin blot analysis using Ricinus communis agglutinin-I (RCA-I), which preferentially interacts with oligosaccharides terminated with Galbeta1--\u003e4GlcNAc group. Several RCA-I-reactive bands appeared in all of the gene-transfected cells, and disappeared on treatment of blots with beta-1,4-galactosidase or N-glycanase prior to incubation with lectin. Introduction of the antisense beta-1,4-GalT II and V cDNAs separately into human colorectal adenocarcinoma SW480 cells, in which beta-1,4-GalT I, II, and V genes were expressed, resulted in the reduction of RCA-I binding toward N-linked oligosaccharides of the membrane glycoproteins. Differences were found in their K(m) values toward UDP-Gal and GlcNAcbeta-S-pNP and in their acceptor specificities toward oligosaccharides with the GlcNAcbeta1--\u003e4(GlcNAcbeta1--\u003e2)Man branch and with the GlcNAcbeta1--\u003e6(GlcNAcbeta1--\u003e2)Man branch. These results indicate that beta-1,4-GalTs II, III, IV, V, and VI are involved in the N-linked oligosaccharide biosynthesis cooperatively but not in a redundant manner with beta-1,4-GalT I within cells."}
NGLY1-deficiency
{"project":"NGLY1-deficiency","denotations":[{"id":"PD-NGLY1-deficiency-B_T1","span":{"begin":798,"end":809},"obj":"hgnc:17646"}],"namespaces":[{"prefix":"hgnc","uri":"https://www.genenames.org/data/gene-symbol-report/#!/hgnc_id/HGNC:"},{"prefix":"omim","uri":"https://www.omim.org/entry/"},{"prefix":"chem","uri":"https://pubchem.ncbi.nlm.nih.gov/compound/"}],"text":"Galactosylation of N-linked oligosaccharides by human beta-1,4-galactosyltransferases I, II, III, IV, V, and VI expressed in Sf-9 cells.\nSeveral studies showed that Sf-9 cells can synthesize the galactosylated N-linked oligosaccharides if beta-1,4-galactosyltransferase (beta-1,4-GalT) is supplied. The full-length human beta-1,4-GalT I, II, III, IV, V, and VI cDNAs were independently transfected into Sf-9 cells, and the galactosylation of endogenous membrane glycoproteins was examined by lectin blot analysis using Ricinus communis agglutinin-I (RCA-I), which preferentially interacts with oligosaccharides terminated with Galbeta1--\u003e4GlcNAc group. Several RCA-I-reactive bands appeared in all of the gene-transfected cells, and disappeared on treatment of blots with beta-1,4-galactosidase or N-glycanase prior to incubation with lectin. Introduction of the antisense beta-1,4-GalT II and V cDNAs separately into human colorectal adenocarcinoma SW480 cells, in which beta-1,4-GalT I, II, and V genes were expressed, resulted in the reduction of RCA-I binding toward N-linked oligosaccharides of the membrane glycoproteins. Differences were found in their K(m) values toward UDP-Gal and GlcNAcbeta-S-pNP and in their acceptor specificities toward oligosaccharides with the GlcNAcbeta1--\u003e4(GlcNAcbeta1--\u003e2)Man branch and with the GlcNAcbeta1--\u003e6(GlcNAcbeta1--\u003e2)Man branch. These results indicate that beta-1,4-GalTs II, III, IV, V, and VI are involved in the N-linked oligosaccharide biosynthesis cooperatively but not in a redundant manner with beta-1,4-GalT I within cells."}
DisGeNET5_gene_disease
{"project":"DisGeNET5_gene_disease","denotations":[{"id":"11588157-4#30#46#gene9334","span":{"begin":873,"end":889},"obj":"gene9334"},{"id":"11588157-4#81#106#diseaseC1319315","span":{"begin":924,"end":949},"obj":"diseaseC1319315"}],"relations":[{"id":"30#46#gene933481#106#diseaseC1319315","pred":"associated_with","subj":"11588157-4#30#46#gene9334","obj":"11588157-4#81#106#diseaseC1319315"}],"text":"Galactosylation of N-linked oligosaccharides by human beta-1,4-galactosyltransferases I, II, III, IV, V, and VI expressed in Sf-9 cells.\nSeveral studies showed that Sf-9 cells can synthesize the galactosylated N-linked oligosaccharides if beta-1,4-galactosyltransferase (beta-1,4-GalT) is supplied. The full-length human beta-1,4-GalT I, II, III, IV, V, and VI cDNAs were independently transfected into Sf-9 cells, and the galactosylation of endogenous membrane glycoproteins was examined by lectin blot analysis using Ricinus communis agglutinin-I (RCA-I), which preferentially interacts with oligosaccharides terminated with Galbeta1--\u003e4GlcNAc group. Several RCA-I-reactive bands appeared in all of the gene-transfected cells, and disappeared on treatment of blots with beta-1,4-galactosidase or N-glycanase prior to incubation with lectin. Introduction of the antisense beta-1,4-GalT II and V cDNAs separately into human colorectal adenocarcinoma SW480 cells, in which beta-1,4-GalT I, II, and V genes were expressed, resulted in the reduction of RCA-I binding toward N-linked oligosaccharides of the membrane glycoproteins. Differences were found in their K(m) values toward UDP-Gal and GlcNAcbeta-S-pNP and in their acceptor specificities toward oligosaccharides with the GlcNAcbeta1--\u003e4(GlcNAcbeta1--\u003e2)Man branch and with the GlcNAcbeta1--\u003e6(GlcNAcbeta1--\u003e2)Man branch. These results indicate that beta-1,4-GalTs II, III, IV, V, and VI are involved in the N-linked oligosaccharide biosynthesis cooperatively but not in a redundant manner with beta-1,4-GalT I within cells."}
Lectin
{"project":"Lectin","denotations":[{"id":"Lectin_T1","span":{"begin":1309,"end":1312},"obj":"https://acgg.asia/db/lfdb/LfDB0217"},{"id":"Lectin_T2","span":{"begin":1365,"end":1368},"obj":"https://acgg.asia/db/lfdb/LfDB0217"},{"id":"Lectin_T3","span":{"begin":550,"end":555},"obj":"https://acgg.asia/db/lfdb/LfDB0231"},{"id":"Lectin_T4","span":{"begin":661,"end":666},"obj":"https://acgg.asia/db/lfdb/LfDB0231"},{"id":"Lectin_T5","span":{"begin":1050,"end":1055},"obj":"https://acgg.asia/db/lfdb/LfDB0231"}],"text":"Galactosylation of N-linked oligosaccharides by human beta-1,4-galactosyltransferases I, II, III, IV, V, and VI expressed in Sf-9 cells.\nSeveral studies showed that Sf-9 cells can synthesize the galactosylated N-linked oligosaccharides if beta-1,4-galactosyltransferase (beta-1,4-GalT) is supplied. The full-length human beta-1,4-GalT I, II, III, IV, V, and VI cDNAs were independently transfected into Sf-9 cells, and the galactosylation of endogenous membrane glycoproteins was examined by lectin blot analysis using Ricinus communis agglutinin-I (RCA-I), which preferentially interacts with oligosaccharides terminated with Galbeta1--\u003e4GlcNAc group. Several RCA-I-reactive bands appeared in all of the gene-transfected cells, and disappeared on treatment of blots with beta-1,4-galactosidase or N-glycanase prior to incubation with lectin. Introduction of the antisense beta-1,4-GalT II and V cDNAs separately into human colorectal adenocarcinoma SW480 cells, in which beta-1,4-GalT I, II, and V genes were expressed, resulted in the reduction of RCA-I binding toward N-linked oligosaccharides of the membrane glycoproteins. Differences were found in their K(m) values toward UDP-Gal and GlcNAcbeta-S-pNP and in their acceptor specificities toward oligosaccharides with the GlcNAcbeta1--\u003e4(GlcNAcbeta1--\u003e2)Man branch and with the GlcNAcbeta1--\u003e6(GlcNAcbeta1--\u003e2)Man branch. These results indicate that beta-1,4-GalTs II, III, IV, V, and VI are involved in the N-linked oligosaccharide biosynthesis cooperatively but not in a redundant manner with beta-1,4-GalT I within cells."}
GlyTouCan-IUPAC
{"project":"GlyTouCan-IUPAC","denotations":[{"id":"GlycanIUPAC_T1","span":{"begin":694,"end":697},"obj":"\"http://rdf.glycoinfo.org/glycan/G41652MJ\""},{"id":"GlycanIUPAC_T2","span":{"begin":694,"end":697},"obj":"\"http://rdf.glycoinfo.org/glycan/G20761YC\""},{"id":"GlycanIUPAC_T3","span":{"begin":694,"end":697},"obj":"\"http://rdf.glycoinfo.org/glycan/G19807HM\""},{"id":"GlycanIUPAC_T4","span":{"begin":694,"end":697},"obj":"\"http://rdf.glycoinfo.org/glycan/G20351TE\""},{"id":"GlycanIUPAC_T5","span":{"begin":694,"end":697},"obj":"\"http://rdf.glycoinfo.org/glycan/G71957MR\""},{"id":"GlycanIUPAC_T6","span":{"begin":694,"end":697},"obj":"\"http://rdf.glycoinfo.org/glycan/G59040AE\""},{"id":"GlycanIUPAC_T7","span":{"begin":694,"end":697},"obj":"\"http://rdf.glycoinfo.org/glycan/G14987PW\""},{"id":"GlycanIUPAC_T8","span":{"begin":694,"end":697},"obj":"\"http://rdf.glycoinfo.org/glycan/G95064PC\""},{"id":"GlycanIUPAC_T9","span":{"begin":694,"end":697},"obj":"\"http://rdf.glycoinfo.org/glycan/G39143AQ\""},{"id":"GlycanIUPAC_T10","span":{"begin":694,"end":697},"obj":"\"http://rdf.glycoinfo.org/glycan/G65149OO\""},{"id":"GlycanIUPAC_T11","span":{"begin":694,"end":697},"obj":"\"http://rdf.glycoinfo.org/glycan/G02766SY\""},{"id":"GlycanIUPAC_T12","span":{"begin":694,"end":697},"obj":"\"http://rdf.glycoinfo.org/glycan/G26019KJ\""},{"id":"GlycanIUPAC_T13","span":{"begin":694,"end":697},"obj":"\"http://rdf.glycoinfo.org/glycan/G36429CZ\""},{"id":"GlycanIUPAC_T14","span":{"begin":694,"end":697},"obj":"\"http://rdf.glycoinfo.org/glycan/G89633TP\""},{"id":"GlycanIUPAC_T15","span":{"begin":694,"end":697},"obj":"\"http://rdf.glycoinfo.org/glycan/G28494FO\""},{"id":"GlycanIUPAC_T16","span":{"begin":694,"end":697},"obj":"\"http://rdf.glycoinfo.org/glycan/G06219CP\""},{"id":"GlycanIUPAC_T17","span":{"begin":694,"end":697},"obj":"\"http://rdf.glycoinfo.org/glycan/G44237SM\""},{"id":"GlycanIUPAC_T18","span":{"begin":694,"end":697},"obj":"\"http://rdf.glycoinfo.org/glycan/G57948RL\""},{"id":"GlycanIUPAC_T19","span":{"begin":694,"end":697},"obj":"\"http://rdf.glycoinfo.org/glycan/G64016DN\""},{"id":"GlycanIUPAC_T20","span":{"begin":694,"end":697},"obj":"\"http://rdf.glycoinfo.org/glycan/G14536PC\""},{"id":"GlycanIUPAC_T21","span":{"begin":694,"end":697},"obj":"\"http://rdf.glycoinfo.org/glycan/G14356FW\""},{"id":"GlycanIUPAC_T22","span":{"begin":694,"end":697},"obj":"\"http://rdf.glycoinfo.org/glycan/G34565UO\""},{"id":"GlycanIUPAC_T23","span":{"begin":694,"end":697},"obj":"\"http://rdf.glycoinfo.org/glycan/G67124MW\""},{"id":"GlycanIUPAC_T24","span":{"begin":694,"end":697},"obj":"\"http://rdf.glycoinfo.org/glycan/G71457ZU\""},{"id":"GlycanIUPAC_T25","span":{"begin":694,"end":697},"obj":"\"http://rdf.glycoinfo.org/glycan/G55228VZ\""},{"id":"GlycanIUPAC_T26","span":{"begin":694,"end":697},"obj":"\"http://rdf.glycoinfo.org/glycan/G31034MJ\""},{"id":"GlycanIUPAC_T27","span":{"begin":694,"end":697},"obj":"\"http://rdf.glycoinfo.org/glycan/G25776IP\""},{"id":"GlycanIUPAC_T28","span":{"begin":694,"end":697},"obj":"\"http://rdf.glycoinfo.org/glycan/G64442BV\""},{"id":"GlycanIUPAC_T29","span":{"begin":694,"end":697},"obj":"\"http://rdf.glycoinfo.org/glycan/G57018LE\""},{"id":"GlycanIUPAC_T30","span":{"begin":694,"end":697},"obj":"\"http://rdf.glycoinfo.org/glycan/G61761GX\""},{"id":"GlycanIUPAC_T31","span":{"begin":694,"end":697},"obj":"\"http://rdf.glycoinfo.org/glycan/G76318UX\""},{"id":"GlycanIUPAC_T32","span":{"begin":694,"end":697},"obj":"\"http://rdf.glycoinfo.org/glycan/G61906ER\""},{"id":"GlycanIUPAC_T33","span":{"begin":694,"end":697},"obj":"\"http://rdf.glycoinfo.org/glycan/G68723GR\""},{"id":"GlycanIUPAC_T34","span":{"begin":694,"end":697},"obj":"\"http://rdf.glycoinfo.org/glycan/G19540LE\""},{"id":"GlycanIUPAC_T35","span":{"begin":694,"end":697},"obj":"\"http://rdf.glycoinfo.org/glycan/G74944PO\""},{"id":"GlycanIUPAC_T36","span":{"begin":694,"end":697},"obj":"\"http://rdf.glycoinfo.org/glycan/G89489ZJ\""},{"id":"GlycanIUPAC_T37","span":{"begin":694,"end":697},"obj":"\"http://rdf.glycoinfo.org/glycan/G04434YU\""},{"id":"GlycanIUPAC_T38","span":{"begin":694,"end":697},"obj":"\"http://rdf.glycoinfo.org/glycan/G21450PB\""},{"id":"GlycanIUPAC_T39","span":{"begin":694,"end":697},"obj":"\"http://rdf.glycoinfo.org/glycan/G93629QY\""},{"id":"GlycanIUPAC_T40","span":{"begin":694,"end":697},"obj":"\"http://rdf.glycoinfo.org/glycan/G02603TR\""},{"id":"GlycanIUPAC_T41","span":{"begin":694,"end":697},"obj":"\"http://rdf.glycoinfo.org/glycan/G40280JP\""},{"id":"GlycanIUPAC_T42","span":{"begin":694,"end":697},"obj":"\"http://rdf.glycoinfo.org/glycan/G95259IC\""},{"id":"GlycanIUPAC_T43","span":{"begin":694,"end":697},"obj":"\"http://rdf.glycoinfo.org/glycan/G26900FE\""},{"id":"GlycanIUPAC_T44","span":{"begin":694,"end":697},"obj":"\"http://rdf.glycoinfo.org/glycan/G21346KK\""},{"id":"GlycanIUPAC_T45","span":{"begin":694,"end":697},"obj":"\"http://rdf.glycoinfo.org/glycan/G62509FF\""},{"id":"GlycanIUPAC_T46","span":{"begin":694,"end":697},"obj"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271","span":{"begin":1365,"end":1368},"obj":"\"http://rdf.glycoinfo.org/glycan/G79061OT\""},{"id":"GlycanIUPAC_T272","span":{"begin":1309,"end":1312},"obj":"\"http://rdf.glycoinfo.org/glycan/G45970UX\""},{"id":"GlycanIUPAC_T273","span":{"begin":1365,"end":1368},"obj":"\"http://rdf.glycoinfo.org/glycan/G45970UX\""},{"id":"GlycanIUPAC_T274","span":{"begin":1309,"end":1312},"obj":"\"http://rdf.glycoinfo.org/glycan/G93661NW\""},{"id":"GlycanIUPAC_T275","span":{"begin":1365,"end":1368},"obj":"\"http://rdf.glycoinfo.org/glycan/G93661NW\""},{"id":"GlycanIUPAC_T276","span":{"begin":1309,"end":1312},"obj":"\"http://rdf.glycoinfo.org/glycan/G04988XL\""},{"id":"GlycanIUPAC_T277","span":{"begin":1365,"end":1368},"obj":"\"http://rdf.glycoinfo.org/glycan/G04988XL\""},{"id":"GlycanIUPAC_T278","span":{"begin":1309,"end":1312},"obj":"\"http://rdf.glycoinfo.org/glycan/G85800UH\""},{"id":"GlycanIUPAC_T279","span":{"begin":1365,"end":1368},"obj":"\"http://rdf.glycoinfo.org/glycan/G85800UH\""},{"id":"GlycanIUPAC_T280","span":{"begin":1309,"end":1312},"obj":"\"http://rdf.glycoinfo.org/glycan/G96338GZ\""},{"id":"GlycanIUPAC_T281","span":{"begin":1365,"end":1368},"obj":"\"http://rdf.glycoinfo.org/glycan/G96338GZ\""},{"id":"GlycanIUPAC_T282","span":{"begin":1309,"end":1312},"obj":"\"http://rdf.glycoinfo.org/glycan/G96296PU\""},{"id":"GlycanIUPAC_T283","span":{"begin":1365,"end":1368},"obj":"\"http://rdf.glycoinfo.org/glycan/G96296PU\""},{"id":"GlycanIUPAC_T284","span":{"begin":1309,"end":1312},"obj":"\"http://rdf.glycoinfo.org/glycan/G59124WZ\""},{"id":"GlycanIUPAC_T285","span":{"begin":1365,"end":1368},"obj":"\"http://rdf.glycoinfo.org/glycan/G59124WZ\""},{"id":"GlycanIUPAC_T286","span":{"begin":1309,"end":1312},"obj":"\"http://rdf.glycoinfo.org/glycan/G57275GR\""},{"id":"GlycanIUPAC_T287","span":{"begin":1365,"end":1368},"obj":"\"http://rdf.glycoinfo.org/glycan/G57275GR\""},{"id":"GlycanIUPAC_T288","span":{"begin":1309,"end":1312},"obj":"\"http://rdf.glycoinfo.org/glycan/G46105MZ\""},{"id":"GlycanIUPAC_T289","span":{"begin":1365,"end":1368},"obj":"\"http://rdf.glycoinfo.org/glycan/G46105MZ\""},{"id":"GlycanIUPAC_T290","span":{"begin":1309,"end":1312},"obj":"\"http://rdf.glycoinfo.org/glycan/G76001GO\""},{"id":"GlycanIUPAC_T291","span":{"begin":1365,"end":1368},"obj":"\"http://rdf.glycoinfo.org/glycan/G76001GO\""},{"id":"GlycanIUPAC_T292","span":{"begin":1309,"end":1312},"obj":"\"http://rdf.glycoinfo.org/glycan/G89599ML\""},{"id":"GlycanIUPAC_T293","span":{"begin":1365,"end":1368},"obj":"\"http://rdf.glycoinfo.org/glycan/G89599ML\""},{"id":"GlycanIUPAC_T294","span":{"begin":1309,"end":1312},"obj":"\"http://rdf.glycoinfo.org/glycan/G85872BD\""},{"id":"GlycanIUPAC_T295","span":{"begin":1365,"end":1368},"obj":"\"http://rdf.glycoinfo.org/glycan/G85872BD\""},{"id":"GlycanIUPAC_T296","span":{"begin":1309,"end":1312},"obj":"\"http://rdf.glycoinfo.org/glycan/G69460YK\""},{"id":"GlycanIUPAC_T297","span":{"begin":1365,"end":1368},"obj":"\"http://rdf.glycoinfo.org/glycan/G69460YK\""},{"id":"GlycanIUPAC_T298","span":{"begin":1309,"end":1312},"obj":"\"http://rdf.glycoinfo.org/glycan/G25240JV\""},{"id":"GlycanIUPAC_T299","span":{"begin":1365,"end":1368},"obj":"\"http://rdf.glycoinfo.org/glycan/G25240JV\""},{"id":"GlycanIUPAC_T300","span":{"begin":1309,"end":1312},"obj":"\"http://rdf.glycoinfo.org/glycan/G80489OS\""},{"id":"GlycanIUPAC_T301","span":{"begin":1365,"end":1368},"obj":"\"http://rdf.glycoinfo.org/glycan/G80489OS\""},{"id":"GlycanIUPAC_T302","span":{"begin":1309,"end":1312},"obj":"\"http://rdf.glycoinfo.org/glycan/G35726XK\""},{"id":"GlycanIUPAC_T303","span":{"begin":1365,"end":1368},"obj":"\"http://rdf.glycoinfo.org/glycan/G35726XK\""},{"id":"GlycanIUPAC_T304","span":{"begin":1309,"end":1312},"obj":"\"http://rdf.glycoinfo.org/glycan/G11002JA\""},{"id":"GlycanIUPAC_T305","span":{"begin":1365,"end":1368},"obj":"\"http://rdf.glycoinfo.org/glycan/G11002JA\""},{"id":"GlycanIUPAC_T306","span":{"begin":1309,"end":1312},"obj":"\"http://rdf.glycoinfo.org/glycan/G85388FO\""},{"id":"GlycanIUPAC_T307","span":{"begin":1365,"end":1368},"obj":"\"http://rdf.glycoinfo.org/glycan/G85388FO\""},{"id":"GlycanIUPAC_T308","span":{"begin":1309,"end":1312},"obj":"\"http://rdf.glycoinfo.org/glycan/G20221JL\""},{"id":"GlycanIUPAC_T309","span":{"begin":1365,"end":1368},"obj":"\"http://rdf.glycoinfo.org/glycan/G20221JL\""},{"id":"GlycanIUPAC_T310","span":{"begin":1309,"end":1312},"obj":"\"http://rdf.glycoinfo.org/glycan/G39026SP\""},{"id":"GlycanIUPAC_T311","span":{"begin":1365,"end":1368},"obj":"\"http://rdf.glycoinfo.org/glycan/G39026SP\""},{"id":"GlycanIUPAC_T312","span":{"begin":1309,"end":1312},"obj":"\"http://rdf.glycoinfo.org/glycan/G66979UZ\""},{"id":"GlycanIUPAC_T313","span":{"begin":1365,"end":1368},"obj":"\"http://rdf.glycoinfo.org/glycan/G66979UZ\""},{"id":"GlycanIUPAC_T314","span":{"begin":1309,"end":1312},"obj":"\"http://rdf.glycoinfo.org/glycan/G68566EA\""},{"id":"GlycanIUPAC_T315","span":{"begin":1365,"end":1368},"obj":"\"http://rdf.glycoinfo.org/glycan/G68566EA\""},{"id":"GlycanIUPAC_T316","span":{"begin":1309,"end":1312},"obj":"\"http://rdf.glycoinfo.org/glycan/G20255ZD\""},{"id":"GlycanIUPAC_T317","span":{"begin":1365,"end":1368},"obj":"\"http://rdf.glycoinfo.org/glycan/G20255ZD\""},{"id":"GlycanIUPAC_T318","span":{"begin":1309,"end":1312},"obj":"\"http://rdf.glycoinfo.org/glycan/G68860MF\""},{"id":"GlycanIUPAC_T319","span":{"begin":1365,"end":1368},"obj":"\"http://rdf.glycoinfo.org/glycan/G68860MF\""},{"id":"GlycanIUPAC_T320","span":{"begin":1309,"end":1312},"obj":"\"http://rdf.glycoinfo.org/glycan/G50413KD\""},{"id":"GlycanIUPAC_T321","span":{"begin":1365,"end":1368},"obj":"\"http://rdf.glycoinfo.org/glycan/G50413KD\""}],"text":"Galactosylation of N-linked oligosaccharides by human beta-1,4-galactosyltransferases I, II, III, IV, V, and VI expressed in Sf-9 cells.\nSeveral studies showed that Sf-9 cells can synthesize the galactosylated N-linked oligosaccharides if beta-1,4-galactosyltransferase (beta-1,4-GalT) is supplied. The full-length human beta-1,4-GalT I, II, III, IV, V, and VI cDNAs were independently transfected into Sf-9 cells, and the galactosylation of endogenous membrane glycoproteins was examined by lectin blot analysis using Ricinus communis agglutinin-I (RCA-I), which preferentially interacts with oligosaccharides terminated with Galbeta1--\u003e4GlcNAc group. Several RCA-I-reactive bands appeared in all of the gene-transfected cells, and disappeared on treatment of blots with beta-1,4-galactosidase or N-glycanase prior to incubation with lectin. Introduction of the antisense beta-1,4-GalT II and V cDNAs separately into human colorectal adenocarcinoma SW480 cells, in which beta-1,4-GalT I, II, and V genes were expressed, resulted in the reduction of RCA-I binding toward N-linked oligosaccharides of the membrane glycoproteins. Differences were found in their K(m) values toward UDP-Gal and GlcNAcbeta-S-pNP and in their acceptor specificities toward oligosaccharides with the GlcNAcbeta1--\u003e4(GlcNAcbeta1--\u003e2)Man branch and with the GlcNAcbeta1--\u003e6(GlcNAcbeta1--\u003e2)Man branch. These results indicate that beta-1,4-GalTs II, III, IV, V, and VI are involved in the N-linked oligosaccharide biosynthesis cooperatively but not in a redundant manner with beta-1,4-GalT I within cells."}
DisGeNET
{"project":"DisGeNET","denotations":[{"id":"T0","span":{"begin":873,"end":889},"obj":"gene:9334"},{"id":"T1","span":{"begin":924,"end":949},"obj":"disease:C1319315"}],"relations":[{"id":"R1","pred":"associated_with","subj":"T0","obj":"T1"}],"namespaces":[{"prefix":"gene","uri":"http://www.ncbi.nlm.nih.gov/gene/"},{"prefix":"disease","uri":"http://purl.bioontology.org/ontology/MEDLINEPLUS/"}],"text":"Galactosylation of N-linked oligosaccharides by human beta-1,4-galactosyltransferases I, II, III, IV, V, and VI expressed in Sf-9 cells.\nSeveral studies showed that Sf-9 cells can synthesize the galactosylated N-linked oligosaccharides if beta-1,4-galactosyltransferase (beta-1,4-GalT) is supplied. The full-length human beta-1,4-GalT I, II, III, IV, V, and VI cDNAs were independently transfected into Sf-9 cells, and the galactosylation of endogenous membrane glycoproteins was examined by lectin blot analysis using Ricinus communis agglutinin-I (RCA-I), which preferentially interacts with oligosaccharides terminated with Galbeta1--\u003e4GlcNAc group. Several RCA-I-reactive bands appeared in all of the gene-transfected cells, and disappeared on treatment of blots with beta-1,4-galactosidase or N-glycanase prior to incubation with lectin. Introduction of the antisense beta-1,4-GalT II and V cDNAs separately into human colorectal adenocarcinoma SW480 cells, in which beta-1,4-GalT I, II, and V genes were expressed, resulted in the reduction of RCA-I binding toward N-linked oligosaccharides of the membrane glycoproteins. Differences were found in their K(m) values toward UDP-Gal and GlcNAcbeta-S-pNP and in their acceptor specificities toward oligosaccharides with the GlcNAcbeta1--\u003e4(GlcNAcbeta1--\u003e2)Man branch and with the GlcNAcbeta1--\u003e6(GlcNAcbeta1--\u003e2)Man branch. These results indicate that beta-1,4-GalTs II, III, IV, V, and VI are involved in the N-linked oligosaccharide biosynthesis cooperatively but not in a redundant manner with beta-1,4-GalT I within cells."}
mondo_disease
{"project":"mondo_disease","denotations":[{"id":"T1","span":{"begin":924,"end":949},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0005008"}],"text":"Galactosylation of N-linked oligosaccharides by human beta-1,4-galactosyltransferases I, II, III, IV, V, and VI expressed in Sf-9 cells.\nSeveral studies showed that Sf-9 cells can synthesize the galactosylated N-linked oligosaccharides if beta-1,4-galactosyltransferase (beta-1,4-GalT) is supplied. The full-length human beta-1,4-GalT I, II, III, IV, V, and VI cDNAs were independently transfected into Sf-9 cells, and the galactosylation of endogenous membrane glycoproteins was examined by lectin blot analysis using Ricinus communis agglutinin-I (RCA-I), which preferentially interacts with oligosaccharides terminated with Galbeta1--\u003e4GlcNAc group. Several RCA-I-reactive bands appeared in all of the gene-transfected cells, and disappeared on treatment of blots with beta-1,4-galactosidase or N-glycanase prior to incubation with lectin. Introduction of the antisense beta-1,4-GalT II and V cDNAs separately into human colorectal adenocarcinoma SW480 cells, in which beta-1,4-GalT I, II, and V genes were expressed, resulted in the reduction of RCA-I binding toward N-linked oligosaccharides of the membrane glycoproteins. Differences were found in their K(m) values toward UDP-Gal and GlcNAcbeta-S-pNP and in their acceptor specificities toward oligosaccharides with the GlcNAcbeta1--\u003e4(GlcNAcbeta1--\u003e2)Man branch and with the GlcNAcbeta1--\u003e6(GlcNAcbeta1--\u003e2)Man branch. These results indicate that beta-1,4-GalTs II, III, IV, V, and VI are involved in the N-linked oligosaccharide biosynthesis cooperatively but not in a redundant manner with beta-1,4-GalT I within cells."}
Lectin-carbogrove
{"project":"Lectin-carbogrove","denotations":[{"id":"T1","span":{"begin":519,"end":546},"obj":"GL_000028"},{"id":"T2","span":{"begin":550,"end":553},"obj":"GL_000028"},{"id":"T3","span":{"begin":661,"end":664},"obj":"GL_000028"},{"id":"T4","span":{"begin":1050,"end":1053},"obj":"GL_000028"}],"namespaces":[{"prefix":"_base","uri":"https://glycosmos.org/lectins/"}],"text":"Galactosylation of N-linked oligosaccharides by human beta-1,4-galactosyltransferases I, II, III, IV, V, and VI expressed in Sf-9 cells.\nSeveral studies showed that Sf-9 cells can synthesize the galactosylated N-linked oligosaccharides if beta-1,4-galactosyltransferase (beta-1,4-GalT) is supplied. The full-length human beta-1,4-GalT I, II, III, IV, V, and VI cDNAs were independently transfected into Sf-9 cells, and the galactosylation of endogenous membrane glycoproteins was examined by lectin blot analysis using Ricinus communis agglutinin-I (RCA-I), which preferentially interacts with oligosaccharides terminated with Galbeta1--\u003e4GlcNAc group. Several RCA-I-reactive bands appeared in all of the gene-transfected cells, and disappeared on treatment of blots with beta-1,4-galactosidase or N-glycanase prior to incubation with lectin. Introduction of the antisense beta-1,4-GalT II and V cDNAs separately into human colorectal adenocarcinoma SW480 cells, in which beta-1,4-GalT I, II, and V genes were expressed, resulted in the reduction of RCA-I binding toward N-linked oligosaccharides of the membrane glycoproteins. Differences were found in their K(m) values toward UDP-Gal and GlcNAcbeta-S-pNP and in their acceptor specificities toward oligosaccharides with the GlcNAcbeta1--\u003e4(GlcNAcbeta1--\u003e2)Man branch and with the GlcNAcbeta1--\u003e6(GlcNAcbeta1--\u003e2)Man branch. These results indicate that beta-1,4-GalTs II, III, IV, V, and VI are involved in the N-linked oligosaccharide biosynthesis cooperatively but not in a redundant manner with beta-1,4-GalT I within cells."}
Lectin-Jamboree
{"project":"Lectin-Jamboree","denotations":[{"id":"T1","span":{"begin":492,"end":498},"obj":"lectin"},{"id":"T2","span":{"begin":835,"end":841},"obj":"lectin"}],"text":"Galactosylation of N-linked oligosaccharides by human beta-1,4-galactosyltransferases I, II, III, IV, V, and VI expressed in Sf-9 cells.\nSeveral studies showed that Sf-9 cells can synthesize the galactosylated N-linked oligosaccharides if beta-1,4-galactosyltransferase (beta-1,4-GalT) is supplied. The full-length human beta-1,4-GalT I, II, III, IV, V, and VI cDNAs were independently transfected into Sf-9 cells, and the galactosylation of endogenous membrane glycoproteins was examined by lectin blot analysis using Ricinus communis agglutinin-I (RCA-I), which preferentially interacts with oligosaccharides terminated with Galbeta1--\u003e4GlcNAc group. Several RCA-I-reactive bands appeared in all of the gene-transfected cells, and disappeared on treatment of blots with beta-1,4-galactosidase or N-glycanase prior to incubation with lectin. Introduction of the antisense beta-1,4-GalT II and V cDNAs separately into human colorectal adenocarcinoma SW480 cells, in which beta-1,4-GalT I, II, and V genes were expressed, resulted in the reduction of RCA-I binding toward N-linked oligosaccharides of the membrane glycoproteins. Differences were found in their K(m) values toward UDP-Gal and GlcNAcbeta-S-pNP and in their acceptor specificities toward oligosaccharides with the GlcNAcbeta1--\u003e4(GlcNAcbeta1--\u003e2)Man branch and with the GlcNAcbeta1--\u003e6(GlcNAcbeta1--\u003e2)Man branch. These results indicate that beta-1,4-GalTs II, III, IV, V, and VI are involved in the N-linked oligosaccharide biosynthesis cooperatively but not in a redundant manner with beta-1,4-GalT I within cells."}
Lectin-Jamboree-Sentence
{"project":"Lectin-Jamboree-Sentence","blocks":[{"id":"T1","span":{"begin":0,"end":136},"obj":"Sentence"},{"id":"T2","span":{"begin":137,"end":298},"obj":"Sentence"},{"id":"T3","span":{"begin":299,"end":652},"obj":"Sentence"},{"id":"T4","span":{"begin":653,"end":842},"obj":"Sentence"},{"id":"T5","span":{"begin":843,"end":1127},"obj":"Sentence"},{"id":"T6","span":{"begin":1128,"end":1376},"obj":"Sentence"},{"id":"T7","span":{"begin":1377,"end":1579},"obj":"Sentence"}],"text":"Galactosylation of N-linked oligosaccharides by human beta-1,4-galactosyltransferases I, II, III, IV, V, and VI expressed in Sf-9 cells.\nSeveral studies showed that Sf-9 cells can synthesize the galactosylated N-linked oligosaccharides if beta-1,4-galactosyltransferase (beta-1,4-GalT) is supplied. The full-length human beta-1,4-GalT I, II, III, IV, V, and VI cDNAs were independently transfected into Sf-9 cells, and the galactosylation of endogenous membrane glycoproteins was examined by lectin blot analysis using Ricinus communis agglutinin-I (RCA-I), which preferentially interacts with oligosaccharides terminated with Galbeta1--\u003e4GlcNAc group. Several RCA-I-reactive bands appeared in all of the gene-transfected cells, and disappeared on treatment of blots with beta-1,4-galactosidase or N-glycanase prior to incubation with lectin. Introduction of the antisense beta-1,4-GalT II and V cDNAs separately into human colorectal adenocarcinoma SW480 cells, in which beta-1,4-GalT I, II, and V genes were expressed, resulted in the reduction of RCA-I binding toward N-linked oligosaccharides of the membrane glycoproteins. Differences were found in their K(m) values toward UDP-Gal and GlcNAcbeta-S-pNP and in their acceptor specificities toward oligosaccharides with the GlcNAcbeta1--\u003e4(GlcNAcbeta1--\u003e2)Man branch and with the GlcNAcbeta1--\u003e6(GlcNAcbeta1--\u003e2)Man branch. These results indicate that beta-1,4-GalTs II, III, IV, V, and VI are involved in the N-linked oligosaccharide biosynthesis cooperatively but not in a redundant manner with beta-1,4-GalT I within cells."}
NCBITAXON
{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":48,"end":53},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":315,"end":320},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":519,"end":535},"obj":"OrganismTaxon"},{"id":"T4","span":{"begin":918,"end":923},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9606"},{"id":"A2","pred":"db_id","subj":"T2","obj":"9606"},{"id":"A3","pred":"db_id","subj":"T3","obj":"3988"},{"id":"A4","pred":"db_id","subj":"T4","obj":"9606"}],"text":"Galactosylation of N-linked oligosaccharides by human beta-1,4-galactosyltransferases I, II, III, IV, V, and VI expressed in Sf-9 cells.\nSeveral studies showed that Sf-9 cells can synthesize the galactosylated N-linked oligosaccharides if beta-1,4-galactosyltransferase (beta-1,4-GalT) is supplied. The full-length human beta-1,4-GalT I, II, III, IV, V, and VI cDNAs were independently transfected into Sf-9 cells, and the galactosylation of endogenous membrane glycoproteins was examined by lectin blot analysis using Ricinus communis agglutinin-I (RCA-I), which preferentially interacts with oligosaccharides terminated with Galbeta1--\u003e4GlcNAc group. Several RCA-I-reactive bands appeared in all of the gene-transfected cells, and disappeared on treatment of blots with beta-1,4-galactosidase or N-glycanase prior to incubation with lectin. Introduction of the antisense beta-1,4-GalT II and V cDNAs separately into human colorectal adenocarcinoma SW480 cells, in which beta-1,4-GalT I, II, and V genes were expressed, resulted in the reduction of RCA-I binding toward N-linked oligosaccharides of the membrane glycoproteins. Differences were found in their K(m) values toward UDP-Gal and GlcNAcbeta-S-pNP and in their acceptor specificities toward oligosaccharides with the GlcNAcbeta1--\u003e4(GlcNAcbeta1--\u003e2)Man branch and with the GlcNAcbeta1--\u003e6(GlcNAcbeta1--\u003e2)Man branch. These results indicate that beta-1,4-GalTs II, III, IV, V, and VI are involved in the N-linked oligosaccharide biosynthesis cooperatively but not in a redundant manner with beta-1,4-GalT I within cells."}
Anatomy-UBERON
{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":453,"end":461},"obj":"Body_part"},{"id":"T4","span":{"begin":1104,"end":1112},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/GO_0016020"},{"id":"A2","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0000094"},{"id":"A3","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0000158"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/GO_0016020"},{"id":"A5","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/UBERON_0000094"},{"id":"A6","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/UBERON_0000158"}],"text":"Galactosylation of N-linked oligosaccharides by human beta-1,4-galactosyltransferases I, II, III, IV, V, and VI expressed in Sf-9 cells.\nSeveral studies showed that Sf-9 cells can synthesize the galactosylated N-linked oligosaccharides if beta-1,4-galactosyltransferase (beta-1,4-GalT) is supplied. The full-length human beta-1,4-GalT I, II, III, IV, V, and VI cDNAs were independently transfected into Sf-9 cells, and the galactosylation of endogenous membrane glycoproteins was examined by lectin blot analysis using Ricinus communis agglutinin-I (RCA-I), which preferentially interacts with oligosaccharides terminated with Galbeta1--\u003e4GlcNAc group. Several RCA-I-reactive bands appeared in all of the gene-transfected cells, and disappeared on treatment of blots with beta-1,4-galactosidase or N-glycanase prior to incubation with lectin. Introduction of the antisense beta-1,4-GalT II and V cDNAs separately into human colorectal adenocarcinoma SW480 cells, in which beta-1,4-GalT I, II, and V genes were expressed, resulted in the reduction of RCA-I binding toward N-linked oligosaccharides of the membrane glycoproteins. Differences were found in their K(m) values toward UDP-Gal and GlcNAcbeta-S-pNP and in their acceptor specificities toward oligosaccharides with the GlcNAcbeta1--\u003e4(GlcNAcbeta1--\u003e2)Man branch and with the GlcNAcbeta1--\u003e6(GlcNAcbeta1--\u003e2)Man branch. These results indicate that beta-1,4-GalTs II, III, IV, V, and VI are involved in the N-linked oligosaccharide biosynthesis cooperatively but not in a redundant manner with beta-1,4-GalT I within cells."}