PubMed:21658684 JSONTXT

{"project":"GlyCosmos600-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":177,"end":182},"obj":"https://glytoucan.org/Structures/Glycans/G91237TK"},{"id":"T2","span":{"begin":177,"end":182},"obj":"https://glytoucan.org/Structures/Glycans/G56516VH"}],"text":"CST-II's recognition domain for acceptor substrates in α-(2→8)-sialylations.\nCST-II is a bacterial sialyltransferase known for its ability to perform α-(2→8)-sialylations using GM(3) related trisaccharide substrates. Previously, we probed the enzyme's substrate specificity and developed an efficient synthesis for α-(2→8)-oligosialosides, and we suggested that CST-II could have a very small substrate recognition domain. Here we report our full studies on CST-II's recognition feature for acceptor substrates. The current study further demonstrates the versatility of CST-II in preparing complex oligosaccharides that contain α-(2→8)-oligosialyl moieties."}

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":177,"end":182},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G91237TK"},{"id":"A2","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G56516VH"}],"text":"CST-II's recognition domain for acceptor substrates in α-(2→8)-sialylations.\nCST-II is a bacterial sialyltransferase known for its ability to perform α-(2→8)-sialylations using GM(3) related trisaccharide substrates. Previously, we probed the enzyme's substrate specificity and developed an efficient synthesis for α-(2→8)-oligosialosides, and we suggested that CST-II could have a very small substrate recognition domain. Here we report our full studies on CST-II's recognition feature for acceptor substrates. The current study further demonstrates the versatility of CST-II in preparing complex oligosaccharides that contain α-(2→8)-oligosialyl moieties."}

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":76},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":77,"end":216},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":217,"end":422},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":423,"end":511},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":512,"end":657},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":76},"obj":"Sentence"},{"id":"T2","span":{"begin":77,"end":216},"obj":"Sentence"},{"id":"T3","span":{"begin":217,"end":422},"obj":"Sentence"},{"id":"T4","span":{"begin":423,"end":511},"obj":"Sentence"},{"id":"T5","span":{"begin":512,"end":657},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"CST-II's recognition domain for acceptor substrates in α-(2→8)-sialylations.\nCST-II is a bacterial sialyltransferase known for its ability to perform α-(2→8)-sialylations using GM(3) related trisaccharide substrates. Previously, we probed the enzyme's substrate specificity and developed an efficient synthesis for α-(2→8)-oligosialosides, and we suggested that CST-II could have a very small substrate recognition domain. Here we report our full studies on CST-II's recognition feature for acceptor substrates. The current study further demonstrates the versatility of CST-II in preparing complex oligosaccharides that contain α-(2→8)-oligosialyl moieties."}

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":177,"end":182},"obj":"https://glytoucan.org/Structures/Glycans/G56516VH"},{"id":"T2","span":{"begin":177,"end":182},"obj":"https://glytoucan.org/Structures/Glycans/G91237TK"}],"text":"CST-II's recognition domain for acceptor substrates in α-(2→8)-sialylations.\nCST-II is a bacterial sialyltransferase known for its ability to perform α-(2→8)-sialylations using GM(3) related trisaccharide substrates. Previously, we probed the enzyme's substrate specificity and developed an efficient synthesis for α-(2→8)-oligosialosides, and we suggested that CST-II could have a very small substrate recognition domain. Here we report our full studies on CST-II's recognition feature for acceptor substrates. The current study further demonstrates the versatility of CST-II in preparing complex oligosaccharides that contain α-(2→8)-oligosialyl moieties."}

{"project":"GlyCosmos600-GlycoGenes2","denotations":[{"id":"T1","span":{"begin":0,"end":3},"obj":"https://acgg.asia/db/ggdb/info/gg178"},{"id":"T2","span":{"begin":0,"end":3},"obj":"https://acgg.asia/db/ggdb/info/gg041"},{"id":"T3","span":{"begin":77,"end":80},"obj":"https://acgg.asia/db/ggdb/info/gg178"},{"id":"T4","span":{"begin":77,"end":80},"obj":"https://acgg.asia/db/ggdb/info/gg041"},{"id":"T5","span":{"begin":362,"end":365},"obj":"https://acgg.asia/db/ggdb/info/gg178"},{"id":"T6","span":{"begin":362,"end":365},"obj":"https://acgg.asia/db/ggdb/info/gg041"},{"id":"T7","span":{"begin":458,"end":461},"obj":"https://acgg.asia/db/ggdb/info/gg178"},{"id":"T8","span":{"begin":458,"end":461},"obj":"https://acgg.asia/db/ggdb/info/gg041"},{"id":"T9","span":{"begin":570,"end":573},"obj":"https://acgg.asia/db/ggdb/info/gg178"},{"id":"T10","span":{"begin":570,"end":573},"obj":"https://acgg.asia/db/ggdb/info/gg041"}],"text":"CST-II's recognition domain for acceptor substrates in α-(2→8)-sialylations.\nCST-II is a bacterial sialyltransferase known for its ability to perform α-(2→8)-sialylations using GM(3) related trisaccharide substrates. Previously, we probed the enzyme's substrate specificity and developed an efficient synthesis for α-(2→8)-oligosialosides, and we suggested that CST-II could have a very small substrate recognition domain. Here we report our full studies on CST-II's recognition feature for acceptor substrates. The current study further demonstrates the versatility of CST-II in preparing complex oligosaccharides that contain α-(2→8)-oligosialyl moieties."}

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_R91","pred":"arg1Of","subj":"EnjuParser_T91","obj":"EnjuParser_T94"},{"id":"EnjuParser_R92","pred":"arg2Of","subj":"EnjuParser_T95","obj":"EnjuParser_T94"},{"id":"EnjuParser_R93","pred":"arg2Of","subj":"EnjuParser_T97","obj":"EnjuParser_T95"},{"id":"EnjuParser_R94","pred":"arg1Of","subj":"EnjuParser_T97","obj":"EnjuParser_T96"},{"id":"EnjuParser_R95","pred":"arg1Of","subj":"EnjuParser_T97","obj":"EnjuParser_T98"},{"id":"EnjuParser_R96","pred":"arg1Of","subj":"EnjuParser_T97","obj":"EnjuParser_T99"},{"id":"EnjuParser_R97","pred":"arg2Of","subj":"EnjuParser_T105","obj":"EnjuParser_T99"},{"id":"EnjuParser_R98","pred":"arg1Of","subj":"EnjuParser_T105","obj":"EnjuParser_T100"},{"id":"EnjuParser_R99","pred":"arg1Of","subj":"EnjuParser_T100","obj":"EnjuParser_T101"},{"id":"EnjuParser_R100","pred":"arg2Of","subj":"EnjuParser_T102","obj":"EnjuParser_T101"},{"id":"EnjuParser_R101","pred":"arg3Of","subj":"EnjuParser_T103","obj":"EnjuParser_T101"},{"id":"EnjuParser_R102","pred":"arg1Of","subj":"EnjuParser_T105","obj":"EnjuParser_T104"}],"namespaces":[{"prefix":"_base","uri":"http://kmcs.nii.ac.jp/enju/"}],"text":"CST-II's recognition domain for acceptor substrates in α-(2→8)-sialylations.\nCST-II is a bacterial sialyltransferase known for its ability to perform α-(2→8)-sialylations using GM(3) related trisaccharide substrates. Previously, we probed the enzyme's substrate specificity and developed an efficient synthesis for α-(2→8)-oligosialosides, and we suggested that CST-II could have a very small substrate recognition domain. Here we report our full studies on CST-II's recognition feature for acceptor substrates. The current study further demonstrates the versatility of CST-II in preparing complex oligosaccharides that contain α-(2→8)-oligosialyl moieties."}

{"project":"GlyCosmos600-FMA","denotations":[{"id":"T1","span":{"begin":598,"end":614},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"fma_id","subj":"T1","obj":"http://purl.org/sig/ont/fma/fma82742"}],"text":"CST-II's recognition domain for acceptor substrates in α-(2→8)-sialylations.\nCST-II is a bacterial sialyltransferase known for its ability to perform α-(2→8)-sialylations using GM(3) related trisaccharide substrates. Previously, we probed the enzyme's substrate specificity and developed an efficient synthesis for α-(2→8)-oligosialosides, and we suggested that CST-II could have a very small substrate recognition domain. Here we report our full studies on CST-II's recognition feature for acceptor substrates. The current study further demonstrates the versatility of CST-II in preparing complex oligosaccharides that contain α-(2→8)-oligosialyl moieties."}