PubMed:10358011 JSON TXT

Annnotations TAB JSON ListView MergeView

GGDB-2020

{"project":"GGDB-2020","denotations":[{"id":"T1","span":{"begin":132,"end":163},"obj":"https://acgg.asia/db/ggdb/info/gg077"},{"id":"T2","span":{"begin":282,"end":289},"obj":"https://acgg.asia/db/ggdb/info/gg004"},{"id":"T3","span":{"begin":282,"end":289},"obj":"https://acgg.asia/db/ggdb/info/gg005"},{"id":"T4","span":{"begin":282,"end":289},"obj":"https://acgg.asia/db/ggdb/info/gg006"},{"id":"T5","span":{"begin":282,"end":289},"obj":"https://acgg.asia/db/ggdb/info/gg007"},{"id":"T6","span":{"begin":282,"end":289},"obj":"https://acgg.asia/db/ggdb/info/gg008"},{"id":"T7","span":{"begin":282,"end":289},"obj":"https://acgg.asia/db/ggdb/info/gg003"},{"id":"T8","span":{"begin":647,"end":651},"obj":"https://acgg.asia/db/ggdb/info/gg115"},{"id":"T9","span":{"begin":647,"end":651},"obj":"https://acgg.asia/db/ggdb/info/gg111"},{"id":"T10","span":{"begin":1085,"end":1089},"obj":"https://acgg.asia/db/ggdb/info/gg115"},{"id":"T11","span":{"begin":1085,"end":1089},"obj":"https://acgg.asia/db/ggdb/info/gg111"},{"id":"T12","span":{"begin":1628,"end":1632},"obj":"https://acgg.asia/db/ggdb/info/gg115"},{"id":"T13","span":{"begin":1628,"end":1632},"obj":"https://acgg.asia/db/ggdb/info/gg111"},{"id":"T14","span":{"begin":2062,"end":2066},"obj":"https://acgg.asia/db/ggdb/info/gg115"},{"id":"T15","span":{"begin":2062,"end":2066},"obj":"https://acgg.asia/db/ggdb/info/gg111"}],"text":"Poly-N-acetyllactosamine synthesis in branched N-glycans is controlled by complemental branch specificity of I-extension enzyme and beta1,4-galactosyltransferase I.\nPoly-N-acetyllactosamine is a unique carbohydrate that can carry various functional oligosaccharides, such as sialyl Lewis X. It has been shown that the amount of poly-N-acetyllactosamine is increased in N-glycans, when they contain Galbeta1--\u003e4GlcNAcbeta1--\u003e6(Galbeta1--\u003e4GlcNAcbeta1 --\u003e2)Manalpha1--\u003e6 branched structure. To determine how this increased synthesis of poly-N-acetyllactosamines takes place, the branched acceptor was incubated with a mixture of i-extension enzyme (iGnT) and beta1, 4galactosyltransferase I (beta4Gal-TI). First, N-acetyllactosamine repeats were more readily added to the branched acceptor than the summation of poly-N-acetyllactosamines formed individually on each unbranched acceptor. Surprisingly, poly-N-acetyllactosamine was more efficiently formed on Galbeta1--\u003e4GlcNAcbeta1--\u003e2Manalpha--\u003eR side chain than in Galbeta1--\u003e4GlcNAcbeta1--\u003e6Manalpha--\u003eR, due to preferential action of iGnT on Galbeta1--\u003e4GlcNAcbeta1--\u003e2Manalpha--\u003eR side chain. On the other hand, galactosylation was much more efficient on beta1,6-linked GlcNAc than beta1,2-linked GlcNAc, preferentially forming Galbeta1--\u003e4GlcNAcbeta1--\u003e6(GlcNAcbeta1--\u003e2)Manalph a1--\u003e6Manbeta --\u003eR. Starting with this preformed acceptor, N-acetyllactosamine repeats were added almost equally to Galbeta1--\u003e4GlcNAcbeta1--\u003e6Manalpha--\u003eR and Galbeta1--\u003e4GlcNAcbeta1--\u003e2Manalpha--\u003eR side chains. Taken together, these results indicate that the complemental branch specificity of iGnT and beta4Gal-TI leads to efficient and equal addition of N-acetyllactosamine repeats on both side chains of GlcNAcbeta1--\u003e6(GlcNAcbeta1--\u003e2)Manalpha1--\u003e6Manbet a--\u003eR structure, which is consistent with the structures found in nature. The results also suggest that the addition of Galbeta1--\u003e4GlcNAcbeta1--\u003e6 side chain on Galbeta1--\u003e4GlcNAcbeta1--\u003e2Man--\u003eR side chain converts the acceptor to one that is much more favorable for iGnT and beta4Gal-TI."}

ggdb-test

{"project":"ggdb-test","denotations":[{"id":"T1","span":{"begin":132,"end":163},"obj":"https://acgg.asia/db/ggdb/info/gg077"},{"id":"T2","span":{"begin":282,"end":289},"obj":"https://acgg.asia/db/ggdb/info/gg003"},{"id":"T3","span":{"begin":282,"end":289},"obj":"https://acgg.asia/db/ggdb/info/gg004"},{"id":"T4","span":{"begin":282,"end":289},"obj":"https://acgg.asia/db/ggdb/info/gg005"},{"id":"T5","span":{"begin":282,"end":289},"obj":"https://acgg.asia/db/ggdb/info/gg006"},{"id":"T6","span":{"begin":282,"end":289},"obj":"https://acgg.asia/db/ggdb/info/gg007"},{"id":"T7","span":{"begin":282,"end":289},"obj":"https://acgg.asia/db/ggdb/info/gg008"},{"id":"T8","span":{"begin":647,"end":651},"obj":"https://acgg.asia/db/ggdb/info/gg111"},{"id":"T9","span":{"begin":647,"end":651},"obj":"https://acgg.asia/db/ggdb/info/gg115"},{"id":"T10","span":{"begin":1085,"end":1089},"obj":"https://acgg.asia/db/ggdb/info/gg111"},{"id":"T11","span":{"begin":1085,"end":1089},"obj":"https://acgg.asia/db/ggdb/info/gg115"},{"id":"T12","span":{"begin":1628,"end":1632},"obj":"https://acgg.asia/db/ggdb/info/gg111"},{"id":"T13","span":{"begin":1628,"end":1632},"obj":"https://acgg.asia/db/ggdb/info/gg115"},{"id":"T14","span":{"begin":2062,"end":2066},"obj":"https://acgg.asia/db/ggdb/info/gg111"},{"id":"T15","span":{"begin":2062,"end":2066},"obj":"https://acgg.asia/db/ggdb/info/gg115"}],"text":"Poly-N-acetyllactosamine synthesis in branched N-glycans is controlled by complemental branch specificity of I-extension enzyme and beta1,4-galactosyltransferase I.\nPoly-N-acetyllactosamine is a unique carbohydrate that can carry various functional oligosaccharides, such as sialyl Lewis X. It has been shown that the amount of poly-N-acetyllactosamine is increased in N-glycans, when they contain Galbeta1--\u003e4GlcNAcbeta1--\u003e6(Galbeta1--\u003e4GlcNAcbeta1 --\u003e2)Manalpha1--\u003e6 branched structure. To determine how this increased synthesis of poly-N-acetyllactosamines takes place, the branched acceptor was incubated with a mixture of i-extension enzyme (iGnT) and beta1, 4galactosyltransferase I (beta4Gal-TI). First, N-acetyllactosamine repeats were more readily added to the branched acceptor than the summation of poly-N-acetyllactosamines formed individually on each unbranched acceptor. Surprisingly, poly-N-acetyllactosamine was more efficiently formed on Galbeta1--\u003e4GlcNAcbeta1--\u003e2Manalpha--\u003eR side chain than in Galbeta1--\u003e4GlcNAcbeta1--\u003e6Manalpha--\u003eR, due to preferential action of iGnT on Galbeta1--\u003e4GlcNAcbeta1--\u003e2Manalpha--\u003eR side chain. On the other hand, galactosylation was much more efficient on beta1,6-linked GlcNAc than beta1,2-linked GlcNAc, preferentially forming Galbeta1--\u003e4GlcNAcbeta1--\u003e6(GlcNAcbeta1--\u003e2)Manalph a1--\u003e6Manbeta --\u003eR. Starting with this preformed acceptor, N-acetyllactosamine repeats were added almost equally to Galbeta1--\u003e4GlcNAcbeta1--\u003e6Manalpha--\u003eR and Galbeta1--\u003e4GlcNAcbeta1--\u003e2Manalpha--\u003eR side chains. Taken together, these results indicate that the complemental branch specificity of iGnT and beta4Gal-TI leads to efficient and equal addition of N-acetyllactosamine repeats on both side chains of GlcNAcbeta1--\u003e6(GlcNAcbeta1--\u003e2)Manalpha1--\u003e6Manbet a--\u003eR structure, which is consistent with the structures found in nature. The results also suggest that the addition of Galbeta1--\u003e4GlcNAcbeta1--\u003e6 side chain on Galbeta1--\u003e4GlcNAcbeta1--\u003e2Man--\u003eR side chain converts the acceptor to one that is much more favorable for iGnT and beta4Gal-TI."}

GlyCosmos6-Glycan-Motif-Image

sentences

{"project":"sentences","denotations":[{"id":"T1","span":{"begin":0,"end":164},"obj":"Sentence"},{"id":"T2","span":{"begin":165,"end":290},"obj":"Sentence"},{"id":"T3","span":{"begin":291,"end":488},"obj":"Sentence"},{"id":"T4","span":{"begin":489,"end":703},"obj":"Sentence"},{"id":"T5","span":{"begin":704,"end":884},"obj":"Sentence"},{"id":"T6","span":{"begin":885,"end":1144},"obj":"Sentence"},{"id":"T7","span":{"begin":1145,"end":1351},"obj":"Sentence"},{"id":"T8","span":{"begin":1352,"end":1544},"obj":"Sentence"},{"id":"T9","span":{"begin":1545,"end":1866},"obj":"Sentence"},{"id":"T10","span":{"begin":1867,"end":2083},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Poly-N-acetyllactosamine synthesis in branched N-glycans is controlled by complemental branch specificity of I-extension enzyme and beta1,4-galactosyltransferase I.\nPoly-N-acetyllactosamine is a unique carbohydrate that can carry various functional oligosaccharides, such as sialyl Lewis X. It has been shown that the amount of poly-N-acetyllactosamine is increased in N-glycans, when they contain Galbeta1--\u003e4GlcNAcbeta1--\u003e6(Galbeta1--\u003e4GlcNAcbeta1 --\u003e2)Manalpha1--\u003e6 branched structure. To determine how this increased synthesis of poly-N-acetyllactosamines takes place, the branched acceptor was incubated with a mixture of i-extension enzyme (iGnT) and beta1, 4galactosyltransferase I (beta4Gal-TI). First, N-acetyllactosamine repeats were more readily added to the branched acceptor than the summation of poly-N-acetyllactosamines formed individually on each unbranched acceptor. Surprisingly, poly-N-acetyllactosamine was more efficiently formed on Galbeta1--\u003e4GlcNAcbeta1--\u003e2Manalpha--\u003eR side chain than in Galbeta1--\u003e4GlcNAcbeta1--\u003e6Manalpha--\u003eR, due to preferential action of iGnT on Galbeta1--\u003e4GlcNAcbeta1--\u003e2Manalpha--\u003eR side chain. On the other hand, galactosylation was much more efficient on beta1,6-linked GlcNAc than beta1,2-linked GlcNAc, preferentially forming Galbeta1--\u003e4GlcNAcbeta1--\u003e6(GlcNAcbeta1--\u003e2)Manalph a1--\u003e6Manbeta --\u003eR. Starting with this preformed acceptor, N-acetyllactosamine repeats were added almost equally to Galbeta1--\u003e4GlcNAcbeta1--\u003e6Manalpha--\u003eR and Galbeta1--\u003e4GlcNAcbeta1--\u003e2Manalpha--\u003eR side chains. Taken together, these results indicate that the complemental branch specificity of iGnT and beta4Gal-TI leads to efficient and equal addition of N-acetyllactosamine repeats on both side chains of GlcNAcbeta1--\u003e6(GlcNAcbeta1--\u003e2)Manalpha1--\u003e6Manbet a--\u003eR structure, which is consistent with the structures found in nature. The results also suggest that the addition of Galbeta1--\u003e4GlcNAcbeta1--\u003e6 side chain on Galbeta1--\u003e4GlcNAcbeta1--\u003e2Man--\u003eR side chain converts the acceptor to one that is much more favorable for iGnT and beta4Gal-TI."}

GlyCosmos6-Glycan-Motif-Structure

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":5,"end":24},"obj":"https://glytoucan.org/Structures/Glycans/G00055MO"},{"id":"T2","span":{"begin":170,"end":189},"obj":"https://glytoucan.org/Structures/Glycans/G00055MO"},{"id":"T3","span":{"begin":275,"end":289},"obj":"https://glytoucan.org/Structures/Glycans/G00054MO"},{"id":"T4","span":{"begin":282,"end":289},"obj":"https://glytoucan.org/Structures/Glycans/G00051MO"},{"id":"T5","span":{"begin":333,"end":352},"obj":"https://glytoucan.org/Structures/Glycans/G00055MO"},{"id":"T6","span":{"begin":539,"end":559},"obj":"https://glytoucan.org/Structures/Glycans/G00055MO"},{"id":"T7","span":{"begin":711,"end":730},"obj":"https://glytoucan.org/Structures/Glycans/G00055MO"},{"id":"T8","span":{"begin":815,"end":835},"obj":"https://glytoucan.org/Structures/Glycans/G00055MO"},{"id":"T9","span":{"begin":904,"end":923},"obj":"https://glytoucan.org/Structures/Glycans/G00055MO"},{"id":"T10","span":{"begin":1391,"end":1410},"obj":"https://glytoucan.org/Structures/Glycans/G00055MO"},{"id":"T11","span":{"begin":1690,"end":1709},"obj":"https://glytoucan.org/Structures/Glycans/G00055MO"}],"text":"Poly-N-acetyllactosamine synthesis in branched N-glycans is controlled by complemental branch specificity of I-extension enzyme and beta1,4-galactosyltransferase I.\nPoly-N-acetyllactosamine is a unique carbohydrate that can carry various functional oligosaccharides, such as sialyl Lewis X. It has been shown that the amount of poly-N-acetyllactosamine is increased in N-glycans, when they contain Galbeta1--\u003e4GlcNAcbeta1--\u003e6(Galbeta1--\u003e4GlcNAcbeta1 --\u003e2)Manalpha1--\u003e6 branched structure. To determine how this increased synthesis of poly-N-acetyllactosamines takes place, the branched acceptor was incubated with a mixture of i-extension enzyme (iGnT) and beta1, 4galactosyltransferase I (beta4Gal-TI). First, N-acetyllactosamine repeats were more readily added to the branched acceptor than the summation of poly-N-acetyllactosamines formed individually on each unbranched acceptor. Surprisingly, poly-N-acetyllactosamine was more efficiently formed on Galbeta1--\u003e4GlcNAcbeta1--\u003e2Manalpha--\u003eR side chain than in Galbeta1--\u003e4GlcNAcbeta1--\u003e6Manalpha--\u003eR, due to preferential action of iGnT on Galbeta1--\u003e4GlcNAcbeta1--\u003e2Manalpha--\u003eR side chain. On the other hand, galactosylation was much more efficient on beta1,6-linked GlcNAc than beta1,2-linked GlcNAc, preferentially forming Galbeta1--\u003e4GlcNAcbeta1--\u003e6(GlcNAcbeta1--\u003e2)Manalph a1--\u003e6Manbeta --\u003eR. Starting with this preformed acceptor, N-acetyllactosamine repeats were added almost equally to Galbeta1--\u003e4GlcNAcbeta1--\u003e6Manalpha--\u003eR and Galbeta1--\u003e4GlcNAcbeta1--\u003e2Manalpha--\u003eR side chains. Taken together, these results indicate that the complemental branch specificity of iGnT and beta4Gal-TI leads to efficient and equal addition of N-acetyllactosamine repeats on both side chains of GlcNAcbeta1--\u003e6(GlcNAcbeta1--\u003e2)Manalpha1--\u003e6Manbet a--\u003eR structure, which is consistent with the structures found in nature. The results also suggest that the addition of Galbeta1--\u003e4GlcNAcbeta1--\u003e6 side chain on Galbeta1--\u003e4GlcNAcbeta1--\u003e2Man--\u003eR side chain converts the acceptor to one that is much more favorable for iGnT and beta4Gal-TI."}

Glycosmos6-GlycoEpitope

{"project":"Glycosmos6-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":275,"end":289},"obj":"http://www.glycoepitope.jp/epitopes/EP0012"}],"text":"Poly-N-acetyllactosamine synthesis in branched N-glycans is controlled by complemental branch specificity of I-extension enzyme and beta1,4-galactosyltransferase I.\nPoly-N-acetyllactosamine is a unique carbohydrate that can carry various functional oligosaccharides, such as sialyl Lewis X. It has been shown that the amount of poly-N-acetyllactosamine is increased in N-glycans, when they contain Galbeta1--\u003e4GlcNAcbeta1--\u003e6(Galbeta1--\u003e4GlcNAcbeta1 --\u003e2)Manalpha1--\u003e6 branched structure. To determine how this increased synthesis of poly-N-acetyllactosamines takes place, the branched acceptor was incubated with a mixture of i-extension enzyme (iGnT) and beta1, 4galactosyltransferase I (beta4Gal-TI). First, N-acetyllactosamine repeats were more readily added to the branched acceptor than the summation of poly-N-acetyllactosamines formed individually on each unbranched acceptor. Surprisingly, poly-N-acetyllactosamine was more efficiently formed on Galbeta1--\u003e4GlcNAcbeta1--\u003e2Manalpha--\u003eR side chain than in Galbeta1--\u003e4GlcNAcbeta1--\u003e6Manalpha--\u003eR, due to preferential action of iGnT on Galbeta1--\u003e4GlcNAcbeta1--\u003e2Manalpha--\u003eR side chain. On the other hand, galactosylation was much more efficient on beta1,6-linked GlcNAc than beta1,2-linked GlcNAc, preferentially forming Galbeta1--\u003e4GlcNAcbeta1--\u003e6(GlcNAcbeta1--\u003e2)Manalph a1--\u003e6Manbeta --\u003eR. Starting with this preformed acceptor, N-acetyllactosamine repeats were added almost equally to Galbeta1--\u003e4GlcNAcbeta1--\u003e6Manalpha--\u003eR and Galbeta1--\u003e4GlcNAcbeta1--\u003e2Manalpha--\u003eR side chains. Taken together, these results indicate that the complemental branch specificity of iGnT and beta4Gal-TI leads to efficient and equal addition of N-acetyllactosamine repeats on both side chains of GlcNAcbeta1--\u003e6(GlcNAcbeta1--\u003e2)Manalpha1--\u003e6Manbet a--\u003eR structure, which is consistent with the structures found in nature. The results also suggest that the addition of Galbeta1--\u003e4GlcNAcbeta1--\u003e6 side chain on Galbeta1--\u003e4GlcNAcbeta1--\u003e2Man--\u003eR side chain converts the acceptor to one that is much more favorable for iGnT and beta4Gal-TI."}

Glycosmos6-MAT

{"project":"Glycosmos6-MAT","denotations":[{"id":"T1","span":{"begin":1158,"end":1162},"obj":"http://purl.obolibrary.org/obo/MAT_0000091"}],"text":"Poly-N-acetyllactosamine synthesis in branched N-glycans is controlled by complemental branch specificity of I-extension enzyme and beta1,4-galactosyltransferase I.\nPoly-N-acetyllactosamine is a unique carbohydrate that can carry various functional oligosaccharides, such as sialyl Lewis X. It has been shown that the amount of poly-N-acetyllactosamine is increased in N-glycans, when they contain Galbeta1--\u003e4GlcNAcbeta1--\u003e6(Galbeta1--\u003e4GlcNAcbeta1 --\u003e2)Manalpha1--\u003e6 branched structure. To determine how this increased synthesis of poly-N-acetyllactosamines takes place, the branched acceptor was incubated with a mixture of i-extension enzyme (iGnT) and beta1, 4galactosyltransferase I (beta4Gal-TI). First, N-acetyllactosamine repeats were more readily added to the branched acceptor than the summation of poly-N-acetyllactosamines formed individually on each unbranched acceptor. Surprisingly, poly-N-acetyllactosamine was more efficiently formed on Galbeta1--\u003e4GlcNAcbeta1--\u003e2Manalpha--\u003eR side chain than in Galbeta1--\u003e4GlcNAcbeta1--\u003e6Manalpha--\u003eR, due to preferential action of iGnT on Galbeta1--\u003e4GlcNAcbeta1--\u003e2Manalpha--\u003eR side chain. On the other hand, galactosylation was much more efficient on beta1,6-linked GlcNAc than beta1,2-linked GlcNAc, preferentially forming Galbeta1--\u003e4GlcNAcbeta1--\u003e6(GlcNAcbeta1--\u003e2)Manalph a1--\u003e6Manbeta --\u003eR. Starting with this preformed acceptor, N-acetyllactosamine repeats were added almost equally to Galbeta1--\u003e4GlcNAcbeta1--\u003e6Manalpha--\u003eR and Galbeta1--\u003e4GlcNAcbeta1--\u003e2Manalpha--\u003eR side chains. Taken together, these results indicate that the complemental branch specificity of iGnT and beta4Gal-TI leads to efficient and equal addition of N-acetyllactosamine repeats on both side chains of GlcNAcbeta1--\u003e6(GlcNAcbeta1--\u003e2)Manalpha1--\u003e6Manbet a--\u003eR structure, which is consistent with the structures found in nature. The results also suggest that the addition of Galbeta1--\u003e4GlcNAcbeta1--\u003e6 side chain on Galbeta1--\u003e4GlcNAcbeta1--\u003e2Man--\u003eR side chain converts the acceptor to one that is much more favorable for iGnT and beta4Gal-TI."}

glycogenes

{"project":"glycogenes","denotations":[{"id":"PD-GlycoGenes20190927-B_T1","span":{"begin":294,"end":297},"obj":"https://acgg.asia/db/ggdb/info/gg135"},{"id":"PD-GlycoGenes20190927-B_T2","span":{"begin":647,"end":651},"obj":"https://acgg.asia/db/ggdb/info/gg115"},{"id":"PD-GlycoGenes20190927-B_T3","span":{"begin":1085,"end":1089},"obj":"https://acgg.asia/db/ggdb/info/gg115"},{"id":"PD-GlycoGenes20190927-B_T4","span":{"begin":1628,"end":1632},"obj":"https://acgg.asia/db/ggdb/info/gg115"},{"id":"PD-GlycoGenes20190927-B_T5","span":{"begin":2062,"end":2066},"obj":"https://acgg.asia/db/ggdb/info/gg115"}],"text":"Poly-N-acetyllactosamine synthesis in branched N-glycans is controlled by complemental branch specificity of I-extension enzyme and beta1,4-galactosyltransferase I.\nPoly-N-acetyllactosamine is a unique carbohydrate that can carry various functional oligosaccharides, such as sialyl Lewis X. It has been shown that the amount of poly-N-acetyllactosamine is increased in N-glycans, when they contain Galbeta1--\u003e4GlcNAcbeta1--\u003e6(Galbeta1--\u003e4GlcNAcbeta1 --\u003e2)Manalpha1--\u003e6 branched structure. To determine how this increased synthesis of poly-N-acetyllactosamines takes place, the branched acceptor was incubated with a mixture of i-extension enzyme (iGnT) and beta1, 4galactosyltransferase I (beta4Gal-TI). First, N-acetyllactosamine repeats were more readily added to the branched acceptor than the summation of poly-N-acetyllactosamines formed individually on each unbranched acceptor. Surprisingly, poly-N-acetyllactosamine was more efficiently formed on Galbeta1--\u003e4GlcNAcbeta1--\u003e2Manalpha--\u003eR side chain than in Galbeta1--\u003e4GlcNAcbeta1--\u003e6Manalpha--\u003eR, due to preferential action of iGnT on Galbeta1--\u003e4GlcNAcbeta1--\u003e2Manalpha--\u003eR side chain. On the other hand, galactosylation was much more efficient on beta1,6-linked GlcNAc than beta1,2-linked GlcNAc, preferentially forming Galbeta1--\u003e4GlcNAcbeta1--\u003e6(GlcNAcbeta1--\u003e2)Manalph a1--\u003e6Manbeta --\u003eR. Starting with this preformed acceptor, N-acetyllactosamine repeats were added almost equally to Galbeta1--\u003e4GlcNAcbeta1--\u003e6Manalpha--\u003eR and Galbeta1--\u003e4GlcNAcbeta1--\u003e2Manalpha--\u003eR side chains. Taken together, these results indicate that the complemental branch specificity of iGnT and beta4Gal-TI leads to efficient and equal addition of N-acetyllactosamine repeats on both side chains of GlcNAcbeta1--\u003e6(GlcNAcbeta1--\u003e2)Manalpha1--\u003e6Manbet a--\u003eR structure, which is consistent with the structures found in nature. The results also suggest that the addition of Galbeta1--\u003e4GlcNAcbeta1--\u003e6 side chain on Galbeta1--\u003e4GlcNAcbeta1--\u003e2Man--\u003eR side chain converts the acceptor to one that is much more favorable for iGnT and beta4Gal-TI."}

NGLY1-deficiency

{"project":"NGLY1-deficiency","denotations":[{"id":"PD-NGLY1-deficiency-B_T1","span":{"begin":1222,"end":1228},"obj":"chem:24139"},{"id":"PD-NGLY1-deficiency-B_T2","span":{"begin":1249,"end":1255},"obj":"chem:24139"}],"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":"Poly-N-acetyllactosamine synthesis in branched N-glycans is controlled by complemental branch specificity of I-extension enzyme and beta1,4-galactosyltransferase I.\nPoly-N-acetyllactosamine is a unique carbohydrate that can carry various functional oligosaccharides, such as sialyl Lewis X. It has been shown that the amount of poly-N-acetyllactosamine is increased in N-glycans, when they contain Galbeta1--\u003e4GlcNAcbeta1--\u003e6(Galbeta1--\u003e4GlcNAcbeta1 --\u003e2)Manalpha1--\u003e6 branched structure. To determine how this increased synthesis of poly-N-acetyllactosamines takes place, the branched acceptor was incubated with a mixture of i-extension enzyme (iGnT) and beta1, 4galactosyltransferase I (beta4Gal-TI). First, N-acetyllactosamine repeats were more readily added to the branched acceptor than the summation of poly-N-acetyllactosamines formed individually on each unbranched acceptor. Surprisingly, poly-N-acetyllactosamine was more efficiently formed on Galbeta1--\u003e4GlcNAcbeta1--\u003e2Manalpha--\u003eR side chain than in Galbeta1--\u003e4GlcNAcbeta1--\u003e6Manalpha--\u003eR, due to preferential action of iGnT on Galbeta1--\u003e4GlcNAcbeta1--\u003e2Manalpha--\u003eR side chain. On the other hand, galactosylation was much more efficient on beta1,6-linked GlcNAc than beta1,2-linked GlcNAc, preferentially forming Galbeta1--\u003e4GlcNAcbeta1--\u003e6(GlcNAcbeta1--\u003e2)Manalph a1--\u003e6Manbeta --\u003eR. Starting with this preformed acceptor, N-acetyllactosamine repeats were added almost equally to Galbeta1--\u003e4GlcNAcbeta1--\u003e6Manalpha--\u003eR and Galbeta1--\u003e4GlcNAcbeta1--\u003e2Manalpha--\u003eR side chains. Taken together, these results indicate that the complemental branch specificity of iGnT and beta4Gal-TI leads to efficient and equal addition of N-acetyllactosamine repeats on both side chains of GlcNAcbeta1--\u003e6(GlcNAcbeta1--\u003e2)Manalpha1--\u003e6Manbet a--\u003eR structure, which is consistent with the structures found in nature. The results also suggest that the addition of Galbeta1--\u003e4GlcNAcbeta1--\u003e6 side chain on Galbeta1--\u003e4GlcNAcbeta1--\u003e2Man--\u003eR side chain converts the acceptor to one that is much more favorable for iGnT and beta4Gal-TI."}

Glycan-GlyCosmos

{"project":"Glycan-GlyCosmos","denotations":[{"id":"T1","span":{"begin":275,"end":289},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G00054MO"},{"id":"A2","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00054MO"}],"text":"Poly-N-acetyllactosamine synthesis in branched N-glycans is controlled by complemental branch specificity of I-extension enzyme and beta1,4-galactosyltransferase I.\nPoly-N-acetyllactosamine is a unique carbohydrate that can carry various functional oligosaccharides, such as sialyl Lewis X. It has been shown that the amount of poly-N-acetyllactosamine is increased in N-glycans, when they contain Galbeta1--\u003e4GlcNAcbeta1--\u003e6(Galbeta1--\u003e4GlcNAcbeta1 --\u003e2)Manalpha1--\u003e6 branched structure. To determine how this increased synthesis of poly-N-acetyllactosamines takes place, the branched acceptor was incubated with a mixture of i-extension enzyme (iGnT) and beta1, 4galactosyltransferase I (beta4Gal-TI). First, N-acetyllactosamine repeats were more readily added to the branched acceptor than the summation of poly-N-acetyllactosamines formed individually on each unbranched acceptor. Surprisingly, poly-N-acetyllactosamine was more efficiently formed on Galbeta1--\u003e4GlcNAcbeta1--\u003e2Manalpha--\u003eR side chain than in Galbeta1--\u003e4GlcNAcbeta1--\u003e6Manalpha--\u003eR, due to preferential action of iGnT on Galbeta1--\u003e4GlcNAcbeta1--\u003e2Manalpha--\u003eR side chain. On the other hand, galactosylation was much more efficient on beta1,6-linked GlcNAc than beta1,2-linked GlcNAc, preferentially forming Galbeta1--\u003e4GlcNAcbeta1--\u003e6(GlcNAcbeta1--\u003e2)Manalph a1--\u003e6Manbeta --\u003eR. Starting with this preformed acceptor, N-acetyllactosamine repeats were added almost equally to Galbeta1--\u003e4GlcNAcbeta1--\u003e6Manalpha--\u003eR and Galbeta1--\u003e4GlcNAcbeta1--\u003e2Manalpha--\u003eR side chains. Taken together, these results indicate that the complemental branch specificity of iGnT and beta4Gal-TI leads to efficient and equal addition of N-acetyllactosamine repeats on both side chains of GlcNAcbeta1--\u003e6(GlcNAcbeta1--\u003e2)Manalpha1--\u003e6Manbet a--\u003eR structure, which is consistent with the structures found in nature. The results also suggest that the addition of Galbeta1--\u003e4GlcNAcbeta1--\u003e6 side chain on Galbeta1--\u003e4GlcNAcbeta1--\u003e2Man--\u003eR side chain converts the acceptor to one that is much more favorable for iGnT and beta4Gal-TI."}

GlyCosmos-GlycoEpitope

{"project":"GlyCosmos-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":275,"end":289},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A1","pred":"glycoepitope_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0012"}],"text":"Poly-N-acetyllactosamine synthesis in branched N-glycans is controlled by complemental branch specificity of I-extension enzyme and beta1,4-galactosyltransferase I.\nPoly-N-acetyllactosamine is a unique carbohydrate that can carry various functional oligosaccharides, such as sialyl Lewis X. It has been shown that the amount of poly-N-acetyllactosamine is increased in N-glycans, when they contain Galbeta1--\u003e4GlcNAcbeta1--\u003e6(Galbeta1--\u003e4GlcNAcbeta1 --\u003e2)Manalpha1--\u003e6 branched structure. To determine how this increased synthesis of poly-N-acetyllactosamines takes place, the branched acceptor was incubated with a mixture of i-extension enzyme (iGnT) and beta1, 4galactosyltransferase I (beta4Gal-TI). First, N-acetyllactosamine repeats were more readily added to the branched acceptor than the summation of poly-N-acetyllactosamines formed individually on each unbranched acceptor. Surprisingly, poly-N-acetyllactosamine was more efficiently formed on Galbeta1--\u003e4GlcNAcbeta1--\u003e2Manalpha--\u003eR side chain than in Galbeta1--\u003e4GlcNAcbeta1--\u003e6Manalpha--\u003eR, due to preferential action of iGnT on Galbeta1--\u003e4GlcNAcbeta1--\u003e2Manalpha--\u003eR side chain. On the other hand, galactosylation was much more efficient on beta1,6-linked GlcNAc than beta1,2-linked GlcNAc, preferentially forming Galbeta1--\u003e4GlcNAcbeta1--\u003e6(GlcNAcbeta1--\u003e2)Manalph a1--\u003e6Manbeta --\u003eR. Starting with this preformed acceptor, N-acetyllactosamine repeats were added almost equally to Galbeta1--\u003e4GlcNAcbeta1--\u003e6Manalpha--\u003eR and Galbeta1--\u003e4GlcNAcbeta1--\u003e2Manalpha--\u003eR side chains. Taken together, these results indicate that the complemental branch specificity of iGnT and beta4Gal-TI leads to efficient and equal addition of N-acetyllactosamine repeats on both side chains of GlcNAcbeta1--\u003e6(GlcNAcbeta1--\u003e2)Manalpha1--\u003e6Manbet a--\u003eR structure, which is consistent with the structures found in nature. The results also suggest that the addition of Galbeta1--\u003e4GlcNAcbeta1--\u003e6 side chain on Galbeta1--\u003e4GlcNAcbeta1--\u003e2Man--\u003eR side chain converts the acceptor to one that is much more favorable for iGnT and beta4Gal-TI."}

GlyCosmos15-CL

{"project":"GlyCosmos15-CL","denotations":[{"id":"T1","span":{"begin":0,"end":4},"obj":"Cell"},{"id":"T3","span":{"begin":165,"end":169},"obj":"Cell"},{"id":"T5","span":{"begin":328,"end":332},"obj":"Cell"},{"id":"T7","span":{"begin":534,"end":538},"obj":"Cell"},{"id":"T9","span":{"begin":810,"end":814},"obj":"Cell"},{"id":"T11","span":{"begin":899,"end":903},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000096"},{"id":"A2","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000775"},{"id":"A3","pred":"cl_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CL:0000096"},{"id":"A4","pred":"cl_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CL:0000775"},{"id":"A5","pred":"cl_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/CL:0000096"},{"id":"A6","pred":"cl_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/CL:0000775"},{"id":"A7","pred":"cl_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/CL:0000096"},{"id":"A8","pred":"cl_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/CL:0000775"},{"id":"A9","pred":"cl_id","subj":"T9","obj":"http://purl.obolibrary.org/obo/CL:0000096"},{"id":"A10","pred":"cl_id","subj":"T9","obj":"http://purl.obolibrary.org/obo/CL:0000775"},{"id":"A11","pred":"cl_id","subj":"T11","obj":"http://purl.obolibrary.org/obo/CL:0000096"},{"id":"A12","pred":"cl_id","subj":"T11","obj":"http://purl.obolibrary.org/obo/CL:0000775"}],"text":"Poly-N-acetyllactosamine synthesis in branched N-glycans is controlled by complemental branch specificity of I-extension enzyme and beta1,4-galactosyltransferase I.\nPoly-N-acetyllactosamine is a unique carbohydrate that can carry various functional oligosaccharides, such as sialyl Lewis X. It has been shown that the amount of poly-N-acetyllactosamine is increased in N-glycans, when they contain Galbeta1--\u003e4GlcNAcbeta1--\u003e6(Galbeta1--\u003e4GlcNAcbeta1 --\u003e2)Manalpha1--\u003e6 branched structure. To determine how this increased synthesis of poly-N-acetyllactosamines takes place, the branched acceptor was incubated with a mixture of i-extension enzyme (iGnT) and beta1, 4galactosyltransferase I (beta4Gal-TI). First, N-acetyllactosamine repeats were more readily added to the branched acceptor than the summation of poly-N-acetyllactosamines formed individually on each unbranched acceptor. Surprisingly, poly-N-acetyllactosamine was more efficiently formed on Galbeta1--\u003e4GlcNAcbeta1--\u003e2Manalpha--\u003eR side chain than in Galbeta1--\u003e4GlcNAcbeta1--\u003e6Manalpha--\u003eR, due to preferential action of iGnT on Galbeta1--\u003e4GlcNAcbeta1--\u003e2Manalpha--\u003eR side chain. On the other hand, galactosylation was much more efficient on beta1,6-linked GlcNAc than beta1,2-linked GlcNAc, preferentially forming Galbeta1--\u003e4GlcNAcbeta1--\u003e6(GlcNAcbeta1--\u003e2)Manalph a1--\u003e6Manbeta --\u003eR. Starting with this preformed acceptor, N-acetyllactosamine repeats were added almost equally to Galbeta1--\u003e4GlcNAcbeta1--\u003e6Manalpha--\u003eR and Galbeta1--\u003e4GlcNAcbeta1--\u003e2Manalpha--\u003eR side chains. Taken together, these results indicate that the complemental branch specificity of iGnT and beta4Gal-TI leads to efficient and equal addition of N-acetyllactosamine repeats on both side chains of GlcNAcbeta1--\u003e6(GlcNAcbeta1--\u003e2)Manalpha1--\u003e6Manbet a--\u003eR structure, which is consistent with the structures found in nature. The results also suggest that the addition of Galbeta1--\u003e4GlcNAcbeta1--\u003e6 side chain on Galbeta1--\u003e4GlcNAcbeta1--\u003e2Man--\u003eR side chain converts the acceptor to one that is much more favorable for iGnT and beta4Gal-TI."}

GlyCosmos15-UBERON

{"project":"GlyCosmos15-UBERON","denotations":[{"id":"T1","span":{"begin":111,"end":120},"obj":"Body_part"},{"id":"T2","span":{"begin":629,"end":638},"obj":"Body_part"},{"id":"T3","span":{"begin":1158,"end":1162},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_2000106"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_2000106"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/UBERON_0002398"}],"text":"Poly-N-acetyllactosamine synthesis in branched N-glycans is controlled by complemental branch specificity of I-extension enzyme and beta1,4-galactosyltransferase I.\nPoly-N-acetyllactosamine is a unique carbohydrate that can carry various functional oligosaccharides, such as sialyl Lewis X. It has been shown that the amount of poly-N-acetyllactosamine is increased in N-glycans, when they contain Galbeta1--\u003e4GlcNAcbeta1--\u003e6(Galbeta1--\u003e4GlcNAcbeta1 --\u003e2)Manalpha1--\u003e6 branched structure. To determine how this increased synthesis of poly-N-acetyllactosamines takes place, the branched acceptor was incubated with a mixture of i-extension enzyme (iGnT) and beta1, 4galactosyltransferase I (beta4Gal-TI). First, N-acetyllactosamine repeats were more readily added to the branched acceptor than the summation of poly-N-acetyllactosamines formed individually on each unbranched acceptor. Surprisingly, poly-N-acetyllactosamine was more efficiently formed on Galbeta1--\u003e4GlcNAcbeta1--\u003e2Manalpha--\u003eR side chain than in Galbeta1--\u003e4GlcNAcbeta1--\u003e6Manalpha--\u003eR, due to preferential action of iGnT on Galbeta1--\u003e4GlcNAcbeta1--\u003e2Manalpha--\u003eR side chain. On the other hand, galactosylation was much more efficient on beta1,6-linked GlcNAc than beta1,2-linked GlcNAc, preferentially forming Galbeta1--\u003e4GlcNAcbeta1--\u003e6(GlcNAcbeta1--\u003e2)Manalph a1--\u003e6Manbeta --\u003eR. Starting with this preformed acceptor, N-acetyllactosamine repeats were added almost equally to Galbeta1--\u003e4GlcNAcbeta1--\u003e6Manalpha--\u003eR and Galbeta1--\u003e4GlcNAcbeta1--\u003e2Manalpha--\u003eR side chains. Taken together, these results indicate that the complemental branch specificity of iGnT and beta4Gal-TI leads to efficient and equal addition of N-acetyllactosamine repeats on both side chains of GlcNAcbeta1--\u003e6(GlcNAcbeta1--\u003e2)Manalpha1--\u003e6Manbet a--\u003eR structure, which is consistent with the structures found in nature. The results also suggest that the addition of Galbeta1--\u003e4GlcNAcbeta1--\u003e6 side chain on Galbeta1--\u003e4GlcNAcbeta1--\u003e2Man--\u003eR side chain converts the acceptor to one that is much more favorable for iGnT and beta4Gal-TI."}

GlyCosmos15-MAT

{"project":"GlyCosmos15-MAT","denotations":[{"id":"T1","span":{"begin":1158,"end":1162},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000091"}],"text":"Poly-N-acetyllactosamine synthesis in branched N-glycans is controlled by complemental branch specificity of I-extension enzyme and beta1,4-galactosyltransferase I.\nPoly-N-acetyllactosamine is a unique carbohydrate that can carry various functional oligosaccharides, such as sialyl Lewis X. It has been shown that the amount of poly-N-acetyllactosamine is increased in N-glycans, when they contain Galbeta1--\u003e4GlcNAcbeta1--\u003e6(Galbeta1--\u003e4GlcNAcbeta1 --\u003e2)Manalpha1--\u003e6 branched structure. To determine how this increased synthesis of poly-N-acetyllactosamines takes place, the branched acceptor was incubated with a mixture of i-extension enzyme (iGnT) and beta1, 4galactosyltransferase I (beta4Gal-TI). First, N-acetyllactosamine repeats were more readily added to the branched acceptor than the summation of poly-N-acetyllactosamines formed individually on each unbranched acceptor. Surprisingly, poly-N-acetyllactosamine was more efficiently formed on Galbeta1--\u003e4GlcNAcbeta1--\u003e2Manalpha--\u003eR side chain than in Galbeta1--\u003e4GlcNAcbeta1--\u003e6Manalpha--\u003eR, due to preferential action of iGnT on Galbeta1--\u003e4GlcNAcbeta1--\u003e2Manalpha--\u003eR side chain. On the other hand, galactosylation was much more efficient on beta1,6-linked GlcNAc than beta1,2-linked GlcNAc, preferentially forming Galbeta1--\u003e4GlcNAcbeta1--\u003e6(GlcNAcbeta1--\u003e2)Manalph a1--\u003e6Manbeta --\u003eR. Starting with this preformed acceptor, N-acetyllactosamine repeats were added almost equally to Galbeta1--\u003e4GlcNAcbeta1--\u003e6Manalpha--\u003eR and Galbeta1--\u003e4GlcNAcbeta1--\u003e2Manalpha--\u003eR side chains. Taken together, these results indicate that the complemental branch specificity of iGnT and beta4Gal-TI leads to efficient and equal addition of N-acetyllactosamine repeats on both side chains of GlcNAcbeta1--\u003e6(GlcNAcbeta1--\u003e2)Manalpha1--\u003e6Manbet a--\u003eR structure, which is consistent with the structures found in nature. The results also suggest that the addition of Galbeta1--\u003e4GlcNAcbeta1--\u003e6 side chain on Galbeta1--\u003e4GlcNAcbeta1--\u003e2Man--\u003eR side chain converts the acceptor to one that is much more favorable for iGnT and beta4Gal-TI."}

sentences

GlyCosmos15-Sentences

{"project":"GlyCosmos15-Sentences","blocks":[{"id":"T1","span":{"begin":0,"end":164},"obj":"Sentence"},{"id":"T2","span":{"begin":165,"end":488},"obj":"Sentence"},{"id":"T3","span":{"begin":489,"end":703},"obj":"Sentence"},{"id":"T4","span":{"begin":704,"end":884},"obj":"Sentence"},{"id":"T5","span":{"begin":885,"end":1144},"obj":"Sentence"},{"id":"T6","span":{"begin":1145,"end":1544},"obj":"Sentence"},{"id":"T7","span":{"begin":1545,"end":1866},"obj":"Sentence"},{"id":"T8","span":{"begin":1867,"end":2083},"obj":"Sentence"}],"text":"Poly-N-acetyllactosamine synthesis in branched N-glycans is controlled by complemental branch specificity of I-extension enzyme and beta1,4-galactosyltransferase I.\nPoly-N-acetyllactosamine is a unique carbohydrate that can carry various functional oligosaccharides, such as sialyl Lewis X. It has been shown that the amount of poly-N-acetyllactosamine is increased in N-glycans, when they contain Galbeta1--\u003e4GlcNAcbeta1--\u003e6(Galbeta1--\u003e4GlcNAcbeta1 --\u003e2)Manalpha1--\u003e6 branched structure. To determine how this increased synthesis of poly-N-acetyllactosamines takes place, the branched acceptor was incubated with a mixture of i-extension enzyme (iGnT) and beta1, 4galactosyltransferase I (beta4Gal-TI). First, N-acetyllactosamine repeats were more readily added to the branched acceptor than the summation of poly-N-acetyllactosamines formed individually on each unbranched acceptor. Surprisingly, poly-N-acetyllactosamine was more efficiently formed on Galbeta1--\u003e4GlcNAcbeta1--\u003e2Manalpha--\u003eR side chain than in Galbeta1--\u003e4GlcNAcbeta1--\u003e6Manalpha--\u003eR, due to preferential action of iGnT on Galbeta1--\u003e4GlcNAcbeta1--\u003e2Manalpha--\u003eR side chain. On the other hand, galactosylation was much more efficient on beta1,6-linked GlcNAc than beta1,2-linked GlcNAc, preferentially forming Galbeta1--\u003e4GlcNAcbeta1--\u003e6(GlcNAcbeta1--\u003e2)Manalph a1--\u003e6Manbeta --\u003eR. Starting with this preformed acceptor, N-acetyllactosamine repeats were added almost equally to Galbeta1--\u003e4GlcNAcbeta1--\u003e6Manalpha--\u003eR and Galbeta1--\u003e4GlcNAcbeta1--\u003e2Manalpha--\u003eR side chains. Taken together, these results indicate that the complemental branch specificity of iGnT and beta4Gal-TI leads to efficient and equal addition of N-acetyllactosamine repeats on both side chains of GlcNAcbeta1--\u003e6(GlcNAcbeta1--\u003e2)Manalpha1--\u003e6Manbet a--\u003eR structure, which is consistent with the structures found in nature. The results also suggest that the addition of Galbeta1--\u003e4GlcNAcbeta1--\u003e6 side chain on Galbeta1--\u003e4GlcNAcbeta1--\u003e2Man--\u003eR side chain converts the acceptor to one that is much more favorable for iGnT and beta4Gal-TI."}

GlyCosmos15-Glycan

{"project":"GlyCosmos15-Glycan","denotations":[{"id":"T1","span":{"begin":275,"end":289},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G00054MO"},{"id":"A2","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00054MO"}],"text":"Poly-N-acetyllactosamine synthesis in branched N-glycans is controlled by complemental branch specificity of I-extension enzyme and beta1,4-galactosyltransferase I.\nPoly-N-acetyllactosamine is a unique carbohydrate that can carry various functional oligosaccharides, such as sialyl Lewis X. It has been shown that the amount of poly-N-acetyllactosamine is increased in N-glycans, when they contain Galbeta1--\u003e4GlcNAcbeta1--\u003e6(Galbeta1--\u003e4GlcNAcbeta1 --\u003e2)Manalpha1--\u003e6 branched structure. To determine how this increased synthesis of poly-N-acetyllactosamines takes place, the branched acceptor was incubated with a mixture of i-extension enzyme (iGnT) and beta1, 4galactosyltransferase I (beta4Gal-TI). First, N-acetyllactosamine repeats were more readily added to the branched acceptor than the summation of poly-N-acetyllactosamines formed individually on each unbranched acceptor. Surprisingly, poly-N-acetyllactosamine was more efficiently formed on Galbeta1--\u003e4GlcNAcbeta1--\u003e2Manalpha--\u003eR side chain than in Galbeta1--\u003e4GlcNAcbeta1--\u003e6Manalpha--\u003eR, due to preferential action of iGnT on Galbeta1--\u003e4GlcNAcbeta1--\u003e2Manalpha--\u003eR side chain. On the other hand, galactosylation was much more efficient on beta1,6-linked GlcNAc than beta1,2-linked GlcNAc, preferentially forming Galbeta1--\u003e4GlcNAcbeta1--\u003e6(GlcNAcbeta1--\u003e2)Manalph a1--\u003e6Manbeta --\u003eR. Starting with this preformed acceptor, N-acetyllactosamine repeats were added almost equally to Galbeta1--\u003e4GlcNAcbeta1--\u003e6Manalpha--\u003eR and Galbeta1--\u003e4GlcNAcbeta1--\u003e2Manalpha--\u003eR side chains. Taken together, these results indicate that the complemental branch specificity of iGnT and beta4Gal-TI leads to efficient and equal addition of N-acetyllactosamine repeats on both side chains of GlcNAcbeta1--\u003e6(GlcNAcbeta1--\u003e2)Manalpha1--\u003e6Manbet a--\u003eR structure, which is consistent with the structures found in nature. The results also suggest that the addition of Galbeta1--\u003e4GlcNAcbeta1--\u003e6 side chain on Galbeta1--\u003e4GlcNAcbeta1--\u003e2Man--\u003eR side chain converts the acceptor to one that is much more favorable for iGnT and beta4Gal-TI."}

GlyCosmos15-GlycoEpitope

{"project":"GlyCosmos15-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":275,"end":289},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A1","pred":"glycoepitope_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0012"}],"text":"Poly-N-acetyllactosamine synthesis in branched N-glycans is controlled by complemental branch specificity of I-extension enzyme and beta1,4-galactosyltransferase I.\nPoly-N-acetyllactosamine is a unique carbohydrate that can carry various functional oligosaccharides, such as sialyl Lewis X. It has been shown that the amount of poly-N-acetyllactosamine is increased in N-glycans, when they contain Galbeta1--\u003e4GlcNAcbeta1--\u003e6(Galbeta1--\u003e4GlcNAcbeta1 --\u003e2)Manalpha1--\u003e6 branched structure. To determine how this increased synthesis of poly-N-acetyllactosamines takes place, the branched acceptor was incubated with a mixture of i-extension enzyme (iGnT) and beta1, 4galactosyltransferase I (beta4Gal-TI). First, N-acetyllactosamine repeats were more readily added to the branched acceptor than the summation of poly-N-acetyllactosamines formed individually on each unbranched acceptor. Surprisingly, poly-N-acetyllactosamine was more efficiently formed on Galbeta1--\u003e4GlcNAcbeta1--\u003e2Manalpha--\u003eR side chain than in Galbeta1--\u003e4GlcNAcbeta1--\u003e6Manalpha--\u003eR, due to preferential action of iGnT on Galbeta1--\u003e4GlcNAcbeta1--\u003e2Manalpha--\u003eR side chain. On the other hand, galactosylation was much more efficient on beta1,6-linked GlcNAc than beta1,2-linked GlcNAc, preferentially forming Galbeta1--\u003e4GlcNAcbeta1--\u003e6(GlcNAcbeta1--\u003e2)Manalph a1--\u003e6Manbeta --\u003eR. Starting with this preformed acceptor, N-acetyllactosamine repeats were added almost equally to Galbeta1--\u003e4GlcNAcbeta1--\u003e6Manalpha--\u003eR and Galbeta1--\u003e4GlcNAcbeta1--\u003e2Manalpha--\u003eR side chains. Taken together, these results indicate that the complemental branch specificity of iGnT and beta4Gal-TI leads to efficient and equal addition of N-acetyllactosamine repeats on both side chains of GlcNAcbeta1--\u003e6(GlcNAcbeta1--\u003e2)Manalpha1--\u003e6Manbet a--\u003eR structure, which is consistent with the structures found in nature. The results also suggest that the addition of Galbeta1--\u003e4GlcNAcbeta1--\u003e6 side chain on Galbeta1--\u003e4GlcNAcbeta1--\u003e2Man--\u003eR side chain converts the acceptor to one that is much more favorable for iGnT and beta4Gal-TI."}

Anatomy-UBERON

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":111,"end":120},"obj":"Body_part"},{"id":"T2","span":{"begin":629,"end":638},"obj":"Body_part"},{"id":"T3","span":{"begin":1158,"end":1162},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_2000106"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_2000106"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/UBERON_0002398"}],"text":"Poly-N-acetyllactosamine synthesis in branched N-glycans is controlled by complemental branch specificity of I-extension enzyme and beta1,4-galactosyltransferase I.\nPoly-N-acetyllactosamine is a unique carbohydrate that can carry various functional oligosaccharides, such as sialyl Lewis X. It has been shown that the amount of poly-N-acetyllactosamine is increased in N-glycans, when they contain Galbeta1--\u003e4GlcNAcbeta1--\u003e6(Galbeta1--\u003e4GlcNAcbeta1 --\u003e2)Manalpha1--\u003e6 branched structure. To determine how this increased synthesis of poly-N-acetyllactosamines takes place, the branched acceptor was incubated with a mixture of i-extension enzyme (iGnT) and beta1, 4galactosyltransferase I (beta4Gal-TI). First, N-acetyllactosamine repeats were more readily added to the branched acceptor than the summation of poly-N-acetyllactosamines formed individually on each unbranched acceptor. Surprisingly, poly-N-acetyllactosamine was more efficiently formed on Galbeta1--\u003e4GlcNAcbeta1--\u003e2Manalpha--\u003eR side chain than in Galbeta1--\u003e4GlcNAcbeta1--\u003e6Manalpha--\u003eR, due to preferential action of iGnT on Galbeta1--\u003e4GlcNAcbeta1--\u003e2Manalpha--\u003eR side chain. On the other hand, galactosylation was much more efficient on beta1,6-linked GlcNAc than beta1,2-linked GlcNAc, preferentially forming Galbeta1--\u003e4GlcNAcbeta1--\u003e6(GlcNAcbeta1--\u003e2)Manalph a1--\u003e6Manbeta --\u003eR. Starting with this preformed acceptor, N-acetyllactosamine repeats were added almost equally to Galbeta1--\u003e4GlcNAcbeta1--\u003e6Manalpha--\u003eR and Galbeta1--\u003e4GlcNAcbeta1--\u003e2Manalpha--\u003eR side chains. Taken together, these results indicate that the complemental branch specificity of iGnT and beta4Gal-TI leads to efficient and equal addition of N-acetyllactosamine repeats on both side chains of GlcNAcbeta1--\u003e6(GlcNAcbeta1--\u003e2)Manalpha1--\u003e6Manbet a--\u003eR structure, which is consistent with the structures found in nature. The results also suggest that the addition of Galbeta1--\u003e4GlcNAcbeta1--\u003e6 side chain on Galbeta1--\u003e4GlcNAcbeta1--\u003e2Man--\u003eR side chain converts the acceptor to one that is much more favorable for iGnT and beta4Gal-TI."}

Anatomy-MAT

{"project":"Anatomy-MAT","denotations":[{"id":"T1","span":{"begin":1158,"end":1162},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000091"}],"text":"Poly-N-acetyllactosamine synthesis in branched N-glycans is controlled by complemental branch specificity of I-extension enzyme and beta1,4-galactosyltransferase I.\nPoly-N-acetyllactosamine is a unique carbohydrate that can carry various functional oligosaccharides, such as sialyl Lewis X. It has been shown that the amount of poly-N-acetyllactosamine is increased in N-glycans, when they contain Galbeta1--\u003e4GlcNAcbeta1--\u003e6(Galbeta1--\u003e4GlcNAcbeta1 --\u003e2)Manalpha1--\u003e6 branched structure. To determine how this increased synthesis of poly-N-acetyllactosamines takes place, the branched acceptor was incubated with a mixture of i-extension enzyme (iGnT) and beta1, 4galactosyltransferase I (beta4Gal-TI). First, N-acetyllactosamine repeats were more readily added to the branched acceptor than the summation of poly-N-acetyllactosamines formed individually on each unbranched acceptor. Surprisingly, poly-N-acetyllactosamine was more efficiently formed on Galbeta1--\u003e4GlcNAcbeta1--\u003e2Manalpha--\u003eR side chain than in Galbeta1--\u003e4GlcNAcbeta1--\u003e6Manalpha--\u003eR, due to preferential action of iGnT on Galbeta1--\u003e4GlcNAcbeta1--\u003e2Manalpha--\u003eR side chain. On the other hand, galactosylation was much more efficient on beta1,6-linked GlcNAc than beta1,2-linked GlcNAc, preferentially forming Galbeta1--\u003e4GlcNAcbeta1--\u003e6(GlcNAcbeta1--\u003e2)Manalph a1--\u003e6Manbeta --\u003eR. Starting with this preformed acceptor, N-acetyllactosamine repeats were added almost equally to Galbeta1--\u003e4GlcNAcbeta1--\u003e6Manalpha--\u003eR and Galbeta1--\u003e4GlcNAcbeta1--\u003e2Manalpha--\u003eR side chains. Taken together, these results indicate that the complemental branch specificity of iGnT and beta4Gal-TI leads to efficient and equal addition of N-acetyllactosamine repeats on both side chains of GlcNAcbeta1--\u003e6(GlcNAcbeta1--\u003e2)Manalpha1--\u003e6Manbet a--\u003eR structure, which is consistent with the structures found in nature. The results also suggest that the addition of Galbeta1--\u003e4GlcNAcbeta1--\u003e6 side chain on Galbeta1--\u003e4GlcNAcbeta1--\u003e2Man--\u003eR side chain converts the acceptor to one that is much more favorable for iGnT and beta4Gal-TI."}

CL-cell

{"project":"CL-cell","denotations":[{"id":"T1","span":{"begin":0,"end":4},"obj":"Cell"},{"id":"T3","span":{"begin":165,"end":169},"obj":"Cell"},{"id":"T5","span":{"begin":328,"end":332},"obj":"Cell"},{"id":"T7","span":{"begin":534,"end":538},"obj":"Cell"},{"id":"T9","span":{"begin":810,"end":814},"obj":"Cell"},{"id":"T11","span":{"begin":899,"end":903},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000096"},{"id":"A2","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000775"},{"id":"A3","pred":"cl_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CL:0000096"},{"id":"A4","pred":"cl_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CL:0000775"},{"id":"A5","pred":"cl_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/CL:0000096"},{"id":"A6","pred":"cl_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/CL:0000775"},{"id":"A7","pred":"cl_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/CL:0000096"},{"id":"A8","pred":"cl_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/CL:0000775"},{"id":"A9","pred":"cl_id","subj":"T9","obj":"http://purl.obolibrary.org/obo/CL:0000096"},{"id":"A10","pred":"cl_id","subj":"T9","obj":"http://purl.obolibrary.org/obo/CL:0000775"},{"id":"A11","pred":"cl_id","subj":"T11","obj":"http://purl.obolibrary.org/obo/CL:0000096"},{"id":"A12","pred":"cl_id","subj":"T11","obj":"http://purl.obolibrary.org/obo/CL:0000775"}],"text":"Poly-N-acetyllactosamine synthesis in branched N-glycans is controlled by complemental branch specificity of I-extension enzyme and beta1,4-galactosyltransferase I.\nPoly-N-acetyllactosamine is a unique carbohydrate that can carry various functional oligosaccharides, such as sialyl Lewis X. It has been shown that the amount of poly-N-acetyllactosamine is increased in N-glycans, when they contain Galbeta1--\u003e4GlcNAcbeta1--\u003e6(Galbeta1--\u003e4GlcNAcbeta1 --\u003e2)Manalpha1--\u003e6 branched structure. To determine how this increased synthesis of poly-N-acetyllactosamines takes place, the branched acceptor was incubated with a mixture of i-extension enzyme (iGnT) and beta1, 4galactosyltransferase I (beta4Gal-TI). First, N-acetyllactosamine repeats were more readily added to the branched acceptor than the summation of poly-N-acetyllactosamines formed individually on each unbranched acceptor. Surprisingly, poly-N-acetyllactosamine was more efficiently formed on Galbeta1--\u003e4GlcNAcbeta1--\u003e2Manalpha--\u003eR side chain than in Galbeta1--\u003e4GlcNAcbeta1--\u003e6Manalpha--\u003eR, due to preferential action of iGnT on Galbeta1--\u003e4GlcNAcbeta1--\u003e2Manalpha--\u003eR side chain. On the other hand, galactosylation was much more efficient on beta1,6-linked GlcNAc than beta1,2-linked GlcNAc, preferentially forming Galbeta1--\u003e4GlcNAcbeta1--\u003e6(GlcNAcbeta1--\u003e2)Manalph a1--\u003e6Manbeta --\u003eR. Starting with this preformed acceptor, N-acetyllactosamine repeats were added almost equally to Galbeta1--\u003e4GlcNAcbeta1--\u003e6Manalpha--\u003eR and Galbeta1--\u003e4GlcNAcbeta1--\u003e2Manalpha--\u003eR side chains. Taken together, these results indicate that the complemental branch specificity of iGnT and beta4Gal-TI leads to efficient and equal addition of N-acetyllactosamine repeats on both side chains of GlcNAcbeta1--\u003e6(GlcNAcbeta1--\u003e2)Manalpha1--\u003e6Manbet a--\u003eR structure, which is consistent with the structures found in nature. The results also suggest that the addition of Galbeta1--\u003e4GlcNAcbeta1--\u003e6 side chain on Galbeta1--\u003e4GlcNAcbeta1--\u003e2Man--\u003eR side chain converts the acceptor to one that is much more favorable for iGnT and beta4Gal-TI."}