PubMed:7537558 JSONTXT

{"project":"Glycan-Motif","denotations":[{"id":"T1","span":{"begin":1196,"end":1205},"obj":"https://glytoucan.org/Structures/Glycans/G65889KE"},{"id":"T2","span":{"begin":1196,"end":1205},"obj":"https://glytoucan.org/Structures/Glycans/G68158BT"},{"id":"T3","span":{"begin":1284,"end":1292},"obj":"https://glytoucan.org/Structures/Glycans/G49108TO"},{"id":"T4","span":{"begin":1284,"end":1292},"obj":"https://glytoucan.org/Structures/Glycans/G89565QL"}],"text":"Enzymatic synthesis of a 6'-sulphated sialyl-Lewisx which is an inhibitor of L-selectin binding to peripheral addressin.\nA sulphated form of sialyl-Lewisx, NeuAc alpha 2-3Gal beta 1-4(Fuc alpha 1-3)GlcNAc6OSO3 beta 1-3Gal, was synthesized enzymatically from a precursor disaccharide, GlcNAc6OSO3 beta 1-3Gal, using sequential steps involving beta 1,4-galactosyltransferase, alpha 2,3-trans-sialidase and recombinant alpha 1,3-fucosyltransferase, respectively. Successful enzymatic fucosylation at the 3 position of the GlcNAc6OSO3 residue demonstrated that fucosyltransferase are capable of generating, in situ, sulphated sialyl Lewisx structures containing sulphate at the 6 position of GlcNAc. The sulphated sialyl-Lewisx pentasaccharide produced by this procedure inhibited binding of a soluble form of L-selectin to 35SO4-labelled peripheral addressin with an IC50 of 0.8 mM, whereas sialyl-Lewisx tetrasaccharide was a weaker inhibitor, displaying an IC50 of 3.2 mM. Hemmerich and Rosen (Biochemistry, 33, 4820-4829, 1994) recently reported the presence of Gal beta 1-4GlcNAcO6SO3 structures on murine peripheral addressin Sgp50, in addition to sialyl Lewisx structures sulphated at the 6-O-galactose position. Based on our data, we suggest that sialyl Lewisx sulphated at the 6-O-GlcNAc position may also exist on receptors and function as a ligand for L-selectin."}

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":1196,"end":1205},"obj":"Glycan_Motif"},{"id":"T3","span":{"begin":1284,"end":1292},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G68158BT"},{"id":"A2","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G65889KE"},{"id":"A3","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G89565QL"},{"id":"A4","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G49108TO"}],"text":"Enzymatic synthesis of a 6'-sulphated sialyl-Lewisx which is an inhibitor of L-selectin binding to peripheral addressin.\nA sulphated form of sialyl-Lewisx, NeuAc alpha 2-3Gal beta 1-4(Fuc alpha 1-3)GlcNAc6OSO3 beta 1-3Gal, was synthesized enzymatically from a precursor disaccharide, GlcNAc6OSO3 beta 1-3Gal, using sequential steps involving beta 1,4-galactosyltransferase, alpha 2,3-trans-sialidase and recombinant alpha 1,3-fucosyltransferase, respectively. Successful enzymatic fucosylation at the 3 position of the GlcNAc6OSO3 residue demonstrated that fucosyltransferase are capable of generating, in situ, sulphated sialyl Lewisx structures containing sulphate at the 6 position of GlcNAc. The sulphated sialyl-Lewisx pentasaccharide produced by this procedure inhibited binding of a soluble form of L-selectin to 35SO4-labelled peripheral addressin with an IC50 of 0.8 mM, whereas sialyl-Lewisx tetrasaccharide was a weaker inhibitor, displaying an IC50 of 3.2 mM. Hemmerich and Rosen (Biochemistry, 33, 4820-4829, 1994) recently reported the presence of Gal beta 1-4GlcNAcO6SO3 structures on murine peripheral addressin Sgp50, in addition to sialyl Lewisx structures sulphated at the 6-O-galactose position. Based on our data, we suggest that sialyl Lewisx sulphated at the 6-O-GlcNAc position may also exist on receptors and function as a ligand for L-selectin."}

{"project":"Glycosmos6-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":1284,"end":1292},"obj":"http://www.glycoepitope.jp/epitopes/EP0004"}],"text":"Enzymatic synthesis of a 6'-sulphated sialyl-Lewisx which is an inhibitor of L-selectin binding to peripheral addressin.\nA sulphated form of sialyl-Lewisx, NeuAc alpha 2-3Gal beta 1-4(Fuc alpha 1-3)GlcNAc6OSO3 beta 1-3Gal, was synthesized enzymatically from a precursor disaccharide, GlcNAc6OSO3 beta 1-3Gal, using sequential steps involving beta 1,4-galactosyltransferase, alpha 2,3-trans-sialidase and recombinant alpha 1,3-fucosyltransferase, respectively. Successful enzymatic fucosylation at the 3 position of the GlcNAc6OSO3 residue demonstrated that fucosyltransferase are capable of generating, in situ, sulphated sialyl Lewisx structures containing sulphate at the 6 position of GlcNAc. The sulphated sialyl-Lewisx pentasaccharide produced by this procedure inhibited binding of a soluble form of L-selectin to 35SO4-labelled peripheral addressin with an IC50 of 0.8 mM, whereas sialyl-Lewisx tetrasaccharide was a weaker inhibitor, displaying an IC50 of 3.2 mM. Hemmerich and Rosen (Biochemistry, 33, 4820-4829, 1994) recently reported the presence of Gal beta 1-4GlcNAcO6SO3 structures on murine peripheral addressin Sgp50, in addition to sialyl Lewisx structures sulphated at the 6-O-galactose position. Based on our data, we suggest that sialyl Lewisx sulphated at the 6-O-GlcNAc position may also exist on receptors and function as a ligand for L-selectin."}

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":1196,"end":1205},"obj":"https://glytoucan.org/Structures/Glycans/G65889KE"},{"id":"T2","span":{"begin":1196,"end":1205},"obj":"https://glytoucan.org/Structures/Glycans/G68158BT"},{"id":"T3","span":{"begin":1284,"end":1292},"obj":"https://glytoucan.org/Structures/Glycans/G49108TO"},{"id":"T4","span":{"begin":1284,"end":1292},"obj":"https://glytoucan.org/Structures/Glycans/G89565QL"}],"text":"Enzymatic synthesis of a 6'-sulphated sialyl-Lewisx which is an inhibitor of L-selectin binding to peripheral addressin.\nA sulphated form of sialyl-Lewisx, NeuAc alpha 2-3Gal beta 1-4(Fuc alpha 1-3)GlcNAc6OSO3 beta 1-3Gal, was synthesized enzymatically from a precursor disaccharide, GlcNAc6OSO3 beta 1-3Gal, using sequential steps involving beta 1,4-galactosyltransferase, alpha 2,3-trans-sialidase and recombinant alpha 1,3-fucosyltransferase, respectively. Successful enzymatic fucosylation at the 3 position of the GlcNAc6OSO3 residue demonstrated that fucosyltransferase are capable of generating, in situ, sulphated sialyl Lewisx structures containing sulphate at the 6 position of GlcNAc. The sulphated sialyl-Lewisx pentasaccharide produced by this procedure inhibited binding of a soluble form of L-selectin to 35SO4-labelled peripheral addressin with an IC50 of 0.8 mM, whereas sialyl-Lewisx tetrasaccharide was a weaker inhibitor, displaying an IC50 of 3.2 mM. Hemmerich and Rosen (Biochemistry, 33, 4820-4829, 1994) recently reported the presence of Gal beta 1-4GlcNAcO6SO3 structures on murine peripheral addressin Sgp50, in addition to sialyl Lewisx structures sulphated at the 6-O-galactose position. Based on our data, we suggest that sialyl Lewisx sulphated at the 6-O-GlcNAc position may also exist on receptors and function as a ligand for L-selectin."}

{"project":"GlycoBiology-FMA","denotations":[{"id":"_T1","span":{"begin":77,"end":87},"obj":"FMAID:167268"},{"id":"_T2","span":{"begin":77,"end":87},"obj":"FMAID:62933"},{"id":"_T3","span":{"begin":77,"end":87},"obj":"FMAID:167267"},{"id":"_T4","span":{"begin":77,"end":87},"obj":"FMAID:62932"},{"id":"_T5","span":{"begin":77,"end":87},"obj":"FMAID:167265"},{"id":"_T6","span":{"begin":77,"end":87},"obj":"FMAID:62931"},{"id":"_T7","span":{"begin":79,"end":87},"obj":"FMAID:165243"},{"id":"_T8","span":{"begin":79,"end":87},"obj":"FMAID:61795"},{"id":"_T9","span":{"begin":99,"end":109},"obj":"FMAID:222825"},{"id":"_T10","span":{"begin":99,"end":109},"obj":"FMAID:74552"},{"id":"_T11","span":{"begin":99,"end":109},"obj":"FMAID:179289"},{"id":"_T12","span":{"begin":270,"end":282},"obj":"FMAID:82744"},{"id":"_T13","span":{"begin":270,"end":282},"obj":"FMAID:196733"},{"id":"_T14","span":{"begin":806,"end":816},"obj":"FMAID:167267"},{"id":"_T15","span":{"begin":806,"end":816},"obj":"FMAID:62931"},{"id":"_T16","span":{"begin":806,"end":816},"obj":"FMAID:62933"},{"id":"_T17","span":{"begin":806,"end":816},"obj":"FMAID:167265"},{"id":"_T18","span":{"begin":806,"end":816},"obj":"FMAID:62932"},{"id":"_T19","span":{"begin":806,"end":816},"obj":"FMAID:167268"},{"id":"_T20","span":{"begin":808,"end":816},"obj":"FMAID:61795"},{"id":"_T21","span":{"begin":808,"end":816},"obj":"FMAID:165243"},{"id":"_T22","span":{"begin":835,"end":845},"obj":"FMAID:222825"},{"id":"_T23","span":{"begin":835,"end":845},"obj":"FMAID:179289"},{"id":"_T24","span":{"begin":835,"end":845},"obj":"FMAID:74552"},{"id":"_T25","span":{"begin":1107,"end":1117},"obj":"FMAID:74552"},{"id":"_T26","span":{"begin":1107,"end":1117},"obj":"FMAID:222825"},{"id":"_T27","span":{"begin":1107,"end":1117},"obj":"FMAID:179289"},{"id":"_T28","span":{"begin":1196,"end":1205},"obj":"FMAID:82794"},{"id":"_T29","span":{"begin":1196,"end":1205},"obj":"FMAID:196789"},{"id":"_T30","span":{"begin":1359,"end":1369},"obj":"FMAID:62931"},{"id":"_T31","span":{"begin":1359,"end":1369},"obj":"FMAID:167265"},{"id":"_T32","span":{"begin":1359,"end":1369},"obj":"FMAID:62932"},{"id":"_T33","span":{"begin":1359,"end":1369},"obj":"FMAID:167267"},{"id":"_T34","span":{"begin":1359,"end":1369},"obj":"FMAID:167268"},{"id":"_T35","span":{"begin":1359,"end":1369},"obj":"FMAID:62933"},{"id":"_T36","span":{"begin":1361,"end":1369},"obj":"FMAID:61795"},{"id":"_T37","span":{"begin":1361,"end":1369},"obj":"FMAID:165243"}],"namespaces":[{"prefix":"FMAID","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"Enzymatic synthesis of a 6'-sulphated sialyl-Lewisx which is an inhibitor of L-selectin binding to peripheral addressin.\nA sulphated form of sialyl-Lewisx, NeuAc alpha 2-3Gal beta 1-4(Fuc alpha 1-3)GlcNAc6OSO3 beta 1-3Gal, was synthesized enzymatically from a precursor disaccharide, GlcNAc6OSO3 beta 1-3Gal, using sequential steps involving beta 1,4-galactosyltransferase, alpha 2,3-trans-sialidase and recombinant alpha 1,3-fucosyltransferase, respectively. Successful enzymatic fucosylation at the 3 position of the GlcNAc6OSO3 residue demonstrated that fucosyltransferase are capable of generating, in situ, sulphated sialyl Lewisx structures containing sulphate at the 6 position of GlcNAc. The sulphated sialyl-Lewisx pentasaccharide produced by this procedure inhibited binding of a soluble form of L-selectin to 35SO4-labelled peripheral addressin with an IC50 of 0.8 mM, whereas sialyl-Lewisx tetrasaccharide was a weaker inhibitor, displaying an IC50 of 3.2 mM. Hemmerich and Rosen (Biochemistry, 33, 4820-4829, 1994) recently reported the presence of Gal beta 1-4GlcNAcO6SO3 structures on murine peripheral addressin Sgp50, in addition to sialyl Lewisx structures sulphated at the 6-O-galactose position. Based on our data, we suggest that sialyl Lewisx sulphated at the 6-O-GlcNAc position may also exist on receptors and function as a ligand for L-selectin."}

{"project":"uniprot-human","denotations":[{"id":"T1","span":{"begin":77,"end":87},"obj":"http://www.uniprot.org/uniprot/P14151"},{"id":"T2","span":{"begin":806,"end":816},"obj":"http://www.uniprot.org/uniprot/P14151"},{"id":"T3","span":{"begin":1359,"end":1369},"obj":"http://www.uniprot.org/uniprot/P14151"},{"id":"T4","span":{"begin":175,"end":181},"obj":"http://www.uniprot.org/uniprot/Q92988"},{"id":"T5","span":{"begin":210,"end":216},"obj":"http://www.uniprot.org/uniprot/Q92988"},{"id":"T6","span":{"begin":296,"end":302},"obj":"http://www.uniprot.org/uniprot/Q92988"},{"id":"T7","span":{"begin":1066,"end":1072},"obj":"http://www.uniprot.org/uniprot/Q92988"},{"id":"T8","span":{"begin":342,"end":372},"obj":"http://www.uniprot.org/uniprot/O60513"},{"id":"T9","span":{"begin":342,"end":372},"obj":"http://www.uniprot.org/uniprot/Q9UBX8"},{"id":"T10","span":{"begin":342,"end":372},"obj":"http://www.uniprot.org/uniprot/Q5T4Y5"},{"id":"T11","span":{"begin":342,"end":372},"obj":"http://www.uniprot.org/uniprot/Q14523"},{"id":"T12","span":{"begin":342,"end":372},"obj":"http://www.uniprot.org/uniprot/O60512"},{"id":"T13","span":{"begin":342,"end":372},"obj":"http://www.uniprot.org/uniprot/O43286"},{"id":"T14","span":{"begin":342,"end":372},"obj":"http://www.uniprot.org/uniprot/Q9UBV7"},{"id":"T15","span":{"begin":347,"end":379},"obj":"http://www.uniprot.org/uniprot/Q9NPC4"},{"id":"T16","span":{"begin":416,"end":444},"obj":"http://www.uniprot.org/uniprot/Q6P4F1"},{"id":"T17","span":{"begin":416,"end":444},"obj":"http://www.uniprot.org/uniprot/Q11128"},{"id":"T18","span":{"begin":416,"end":444},"obj":"http://www.uniprot.org/uniprot/Q11130"},{"id":"T19","span":{"begin":416,"end":444},"obj":"http://www.uniprot.org/uniprot/P51993"},{"id":"T20","span":{"begin":416,"end":444},"obj":"http://www.uniprot.org/uniprot/Q495W5"},{"id":"T21","span":{"begin":416,"end":444},"obj":"http://www.uniprot.org/uniprot/P22083"},{"id":"T22","span":{"begin":416,"end":444},"obj":"http://www.uniprot.org/uniprot/Q9Y231"}],"text":"Enzymatic synthesis of a 6'-sulphated sialyl-Lewisx which is an inhibitor of L-selectin binding to peripheral addressin.\nA sulphated form of sialyl-Lewisx, NeuAc alpha 2-3Gal beta 1-4(Fuc alpha 1-3)GlcNAc6OSO3 beta 1-3Gal, was synthesized enzymatically from a precursor disaccharide, GlcNAc6OSO3 beta 1-3Gal, using sequential steps involving beta 1,4-galactosyltransferase, alpha 2,3-trans-sialidase and recombinant alpha 1,3-fucosyltransferase, respectively. Successful enzymatic fucosylation at the 3 position of the GlcNAc6OSO3 residue demonstrated that fucosyltransferase are capable of generating, in situ, sulphated sialyl Lewisx structures containing sulphate at the 6 position of GlcNAc. The sulphated sialyl-Lewisx pentasaccharide produced by this procedure inhibited binding of a soluble form of L-selectin to 35SO4-labelled peripheral addressin with an IC50 of 0.8 mM, whereas sialyl-Lewisx tetrasaccharide was a weaker inhibitor, displaying an IC50 of 3.2 mM. Hemmerich and Rosen (Biochemistry, 33, 4820-4829, 1994) recently reported the presence of Gal beta 1-4GlcNAcO6SO3 structures on murine peripheral addressin Sgp50, in addition to sialyl Lewisx structures sulphated at the 6-O-galactose position. Based on our data, we suggest that sialyl Lewisx sulphated at the 6-O-GlcNAc position may also exist on receptors and function as a ligand for L-selectin."}

{"project":"uniprot-mouse","denotations":[{"id":"T1","span":{"begin":77,"end":87},"obj":"http://www.uniprot.org/uniprot/P18337"},{"id":"T2","span":{"begin":806,"end":816},"obj":"http://www.uniprot.org/uniprot/P18337"},{"id":"T3","span":{"begin":1359,"end":1369},"obj":"http://www.uniprot.org/uniprot/P18337"},{"id":"T4","span":{"begin":347,"end":379},"obj":"http://www.uniprot.org/uniprot/Q67BJ4"},{"id":"T5","span":{"begin":351,"end":372},"obj":"http://www.uniprot.org/uniprot/P23336"}],"text":"Enzymatic synthesis of a 6'-sulphated sialyl-Lewisx which is an inhibitor of L-selectin binding to peripheral addressin.\nA sulphated form of sialyl-Lewisx, NeuAc alpha 2-3Gal beta 1-4(Fuc alpha 1-3)GlcNAc6OSO3 beta 1-3Gal, was synthesized enzymatically from a precursor disaccharide, GlcNAc6OSO3 beta 1-3Gal, using sequential steps involving beta 1,4-galactosyltransferase, alpha 2,3-trans-sialidase and recombinant alpha 1,3-fucosyltransferase, respectively. Successful enzymatic fucosylation at the 3 position of the GlcNAc6OSO3 residue demonstrated that fucosyltransferase are capable of generating, in situ, sulphated sialyl Lewisx structures containing sulphate at the 6 position of GlcNAc. The sulphated sialyl-Lewisx pentasaccharide produced by this procedure inhibited binding of a soluble form of L-selectin to 35SO4-labelled peripheral addressin with an IC50 of 0.8 mM, whereas sialyl-Lewisx tetrasaccharide was a weaker inhibitor, displaying an IC50 of 3.2 mM. Hemmerich and Rosen (Biochemistry, 33, 4820-4829, 1994) recently reported the presence of Gal beta 1-4GlcNAcO6SO3 structures on murine peripheral addressin Sgp50, in addition to sialyl Lewisx structures sulphated at the 6-O-galactose position. Based on our data, we suggest that sialyl Lewisx sulphated at the 6-O-GlcNAc position may also exist on receptors and function as a ligand for L-selectin."}

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":175,"end":179},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"},{"id":"T2","span":{"begin":175,"end":179},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T3","span":{"begin":210,"end":214},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T4","span":{"begin":210,"end":214},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"},{"id":"T5","span":{"begin":296,"end":300},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"},{"id":"T6","span":{"begin":296,"end":300},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T7","span":{"begin":342,"end":346},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"},{"id":"T8","span":{"begin":342,"end":346},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T9","span":{"begin":1066,"end":1070},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"},{"id":"T10","span":{"begin":1066,"end":1070},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T11","span":{"begin":1320,"end":1329},"obj":"http://purl.bioontology.org/ontology/STY/T192"}],"text":"Enzymatic synthesis of a 6'-sulphated sialyl-Lewisx which is an inhibitor of L-selectin binding to peripheral addressin.\nA sulphated form of sialyl-Lewisx, NeuAc alpha 2-3Gal beta 1-4(Fuc alpha 1-3)GlcNAc6OSO3 beta 1-3Gal, was synthesized enzymatically from a precursor disaccharide, GlcNAc6OSO3 beta 1-3Gal, using sequential steps involving beta 1,4-galactosyltransferase, alpha 2,3-trans-sialidase and recombinant alpha 1,3-fucosyltransferase, respectively. Successful enzymatic fucosylation at the 3 position of the GlcNAc6OSO3 residue demonstrated that fucosyltransferase are capable of generating, in situ, sulphated sialyl Lewisx structures containing sulphate at the 6 position of GlcNAc. The sulphated sialyl-Lewisx pentasaccharide produced by this procedure inhibited binding of a soluble form of L-selectin to 35SO4-labelled peripheral addressin with an IC50 of 0.8 mM, whereas sialyl-Lewisx tetrasaccharide was a weaker inhibitor, displaying an IC50 of 3.2 mM. Hemmerich and Rosen (Biochemistry, 33, 4820-4829, 1994) recently reported the presence of Gal beta 1-4GlcNAcO6SO3 structures on murine peripheral addressin Sgp50, in addition to sialyl Lewisx structures sulphated at the 6-O-galactose position. Based on our data, we suggest that sialyl Lewisx sulphated at the 6-O-GlcNAc position may also exist on receptors and function as a ligand for L-selectin."}

{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":10,"end":19},"obj":"http://purl.obolibrary.org/obo/GO_0009058"},{"id":"T2","span":{"begin":28,"end":37},"obj":"http://purl.obolibrary.org/obo/GO_0051923"},{"id":"T3","span":{"begin":123,"end":132},"obj":"http://purl.obolibrary.org/obo/GO_0051923"},{"id":"T4","span":{"begin":612,"end":621},"obj":"http://purl.obolibrary.org/obo/GO_0051923"},{"id":"T5","span":{"begin":700,"end":709},"obj":"http://purl.obolibrary.org/obo/GO_0051923"},{"id":"T6","span":{"begin":1175,"end":1184},"obj":"http://purl.obolibrary.org/obo/GO_0051923"},{"id":"T7","span":{"begin":658,"end":666},"obj":"http://purl.obolibrary.org/obo/GO_0051923"},{"id":"T8","span":{"begin":38,"end":44},"obj":"http://purl.obolibrary.org/obo/GO_0097503"},{"id":"T9","span":{"begin":141,"end":147},"obj":"http://purl.obolibrary.org/obo/GO_0097503"},{"id":"T10","span":{"begin":622,"end":628},"obj":"http://purl.obolibrary.org/obo/GO_0097503"},{"id":"T11","span":{"begin":710,"end":716},"obj":"http://purl.obolibrary.org/obo/GO_0097503"},{"id":"T12","span":{"begin":888,"end":894},"obj":"http://purl.obolibrary.org/obo/GO_0097503"},{"id":"T13","span":{"begin":1150,"end":1156},"obj":"http://purl.obolibrary.org/obo/GO_0097503"},{"id":"T14","span":{"begin":1251,"end":1257},"obj":"http://purl.obolibrary.org/obo/GO_0097503"},{"id":"T15","span":{"begin":342,"end":372},"obj":"http://purl.obolibrary.org/obo/GO_0003945"},{"id":"T16","span":{"begin":416,"end":444},"obj":"http://purl.obolibrary.org/obo/GO_0046920"},{"id":"T17","span":{"begin":481,"end":493},"obj":"http://purl.obolibrary.org/obo/GO_0036065"},{"id":"T18","span":{"begin":767,"end":784},"obj":"http://purl.obolibrary.org/obo/GO_0051100"}],"text":"Enzymatic synthesis of a 6'-sulphated sialyl-Lewisx which is an inhibitor of L-selectin binding to peripheral addressin.\nA sulphated form of sialyl-Lewisx, NeuAc alpha 2-3Gal beta 1-4(Fuc alpha 1-3)GlcNAc6OSO3 beta 1-3Gal, was synthesized enzymatically from a precursor disaccharide, GlcNAc6OSO3 beta 1-3Gal, using sequential steps involving beta 1,4-galactosyltransferase, alpha 2,3-trans-sialidase and recombinant alpha 1,3-fucosyltransferase, respectively. Successful enzymatic fucosylation at the 3 position of the GlcNAc6OSO3 residue demonstrated that fucosyltransferase are capable of generating, in situ, sulphated sialyl Lewisx structures containing sulphate at the 6 position of GlcNAc. The sulphated sialyl-Lewisx pentasaccharide produced by this procedure inhibited binding of a soluble form of L-selectin to 35SO4-labelled peripheral addressin with an IC50 of 0.8 mM, whereas sialyl-Lewisx tetrasaccharide was a weaker inhibitor, displaying an IC50 of 3.2 mM. Hemmerich and Rosen (Biochemistry, 33, 4820-4829, 1994) recently reported the presence of Gal beta 1-4GlcNAcO6SO3 structures on murine peripheral addressin Sgp50, in addition to sialyl Lewisx structures sulphated at the 6-O-galactose position. Based on our data, we suggest that sialyl Lewisx sulphated at the 6-O-GlcNAc position may also exist on receptors and function as a ligand for L-selectin."}

{"project":"GO-MF","denotations":[{"id":"T1","span":{"begin":79,"end":87},"obj":"http://purl.obolibrary.org/obo/GO_0030246"},{"id":"T2","span":{"begin":808,"end":816},"obj":"http://purl.obolibrary.org/obo/GO_0030246"},{"id":"T3","span":{"begin":1361,"end":1369},"obj":"http://purl.obolibrary.org/obo/GO_0030246"},{"id":"T4","span":{"begin":88,"end":95},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T5","span":{"begin":777,"end":784},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T6","span":{"begin":88,"end":95},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T7","span":{"begin":777,"end":784},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T8","span":{"begin":88,"end":95},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T9","span":{"begin":777,"end":784},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T10","span":{"begin":88,"end":95},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T11","span":{"begin":777,"end":784},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T12","span":{"begin":1348,"end":1354},"obj":"http://purl.obolibrary.org/obo/GO_0005488"}],"text":"Enzymatic synthesis of a 6'-sulphated sialyl-Lewisx which is an inhibitor of L-selectin binding to peripheral addressin.\nA sulphated form of sialyl-Lewisx, NeuAc alpha 2-3Gal beta 1-4(Fuc alpha 1-3)GlcNAc6OSO3 beta 1-3Gal, was synthesized enzymatically from a precursor disaccharide, GlcNAc6OSO3 beta 1-3Gal, using sequential steps involving beta 1,4-galactosyltransferase, alpha 2,3-trans-sialidase and recombinant alpha 1,3-fucosyltransferase, respectively. Successful enzymatic fucosylation at the 3 position of the GlcNAc6OSO3 residue demonstrated that fucosyltransferase are capable of generating, in situ, sulphated sialyl Lewisx structures containing sulphate at the 6 position of GlcNAc. The sulphated sialyl-Lewisx pentasaccharide produced by this procedure inhibited binding of a soluble form of L-selectin to 35SO4-labelled peripheral addressin with an IC50 of 0.8 mM, whereas sialyl-Lewisx tetrasaccharide was a weaker inhibitor, displaying an IC50 of 3.2 mM. Hemmerich and Rosen (Biochemistry, 33, 4820-4829, 1994) recently reported the presence of Gal beta 1-4GlcNAcO6SO3 structures on murine peripheral addressin Sgp50, in addition to sialyl Lewisx structures sulphated at the 6-O-galactose position. Based on our data, we suggest that sialyl Lewisx sulphated at the 6-O-GlcNAc position may also exist on receptors and function as a ligand for L-selectin."}

{"project":"NGLY1-deficiency","denotations":[{"id":"PD-NGLY1-deficiency-B_T1","span":{"begin":688,"end":694},"obj":"chem:24139"},{"id":"PD-NGLY1-deficiency-B_T2","span":{"begin":1286,"end":1292},"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":"Enzymatic synthesis of a 6'-sulphated sialyl-Lewisx which is an inhibitor of L-selectin binding to peripheral addressin.\nA sulphated form of sialyl-Lewisx, NeuAc alpha 2-3Gal beta 1-4(Fuc alpha 1-3)GlcNAc6OSO3 beta 1-3Gal, was synthesized enzymatically from a precursor disaccharide, GlcNAc6OSO3 beta 1-3Gal, using sequential steps involving beta 1,4-galactosyltransferase, alpha 2,3-trans-sialidase and recombinant alpha 1,3-fucosyltransferase, respectively. Successful enzymatic fucosylation at the 3 position of the GlcNAc6OSO3 residue demonstrated that fucosyltransferase are capable of generating, in situ, sulphated sialyl Lewisx structures containing sulphate at the 6 position of GlcNAc. The sulphated sialyl-Lewisx pentasaccharide produced by this procedure inhibited binding of a soluble form of L-selectin to 35SO4-labelled peripheral addressin with an IC50 of 0.8 mM, whereas sialyl-Lewisx tetrasaccharide was a weaker inhibitor, displaying an IC50 of 3.2 mM. Hemmerich and Rosen (Biochemistry, 33, 4820-4829, 1994) recently reported the presence of Gal beta 1-4GlcNAcO6SO3 structures on murine peripheral addressin Sgp50, in addition to sialyl Lewisx structures sulphated at the 6-O-galactose position. Based on our data, we suggest that sialyl Lewisx sulphated at the 6-O-GlcNAc position may also exist on receptors and function as a ligand for L-selectin."}

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1065},"obj":"\"http://rdf.glycoinfo.org/glycan/G47955HA\""},{"id":"GlycanIUPAC_T182","span":{"begin":1062,"end":1065},"obj":"\"http://rdf.glycoinfo.org/glycan/G60982WS\""},{"id":"GlycanIUPAC_T183","span":{"begin":1062,"end":1065},"obj":"\"http://rdf.glycoinfo.org/glycan/G37035KG\""},{"id":"GlycanIUPAC_T184","span":{"begin":1062,"end":1065},"obj":"\"http://rdf.glycoinfo.org/glycan/G46297FI\""},{"id":"GlycanIUPAC_T185","span":{"begin":1062,"end":1065},"obj":"\"http://rdf.glycoinfo.org/glycan/G35475KI\""},{"id":"GlycanIUPAC_T186","span":{"begin":1062,"end":1065},"obj":"\"http://rdf.glycoinfo.org/glycan/G29771JN\""},{"id":"GlycanIUPAC_T187","span":{"begin":1062,"end":1065},"obj":"\"http://rdf.glycoinfo.org/glycan/G61285YR\""},{"id":"GlycanIUPAC_T188","span":{"begin":1062,"end":1065},"obj":"\"http://rdf.glycoinfo.org/glycan/G54785MW\""},{"id":"GlycanIUPAC_T189","span":{"begin":1062,"end":1065},"obj":"\"http://rdf.glycoinfo.org/glycan/G53039GT\""},{"id":"GlycanIUPAC_T190","span":{"begin":1062,"end":1065},"obj":"\"http://rdf.glycoinfo.org/glycan/G00601HK\""},{"id":"GlycanIUPAC_T191","span":{"begin":1062,"end":1065},"obj":"\"http://rdf.glycoinfo.org/glycan/G10485IJ\""},{"id":"GlycanIUPAC_T192","span":{"begin":1062,"end":1065},"obj":"\"http://rdf.glycoinfo.org/glycan/G16393IB\""},{"id":"GlycanIUPAC_T193","span":{"begin":1062,"end":1065},"obj":"\"http://rdf.glycoinfo.org/glycan/G98436FZ\""},{"id":"GlycanIUPAC_T194","span":{"begin":1062,"end":1065},"obj":"\"http://rdf.glycoinfo.org/glycan/G18825IA\""},{"id":"GlycanIUPAC_T195","span":{"begin":1062,"end":1065},"obj":"\"http://rdf.glycoinfo.org/glycan/G61281HQ\""},{"id":"GlycanIUPAC_T196","span":{"begin":1062,"end":1065},"obj":"\"http://rdf.glycoinfo.org/glycan/G07798TI\""},{"id":"GlycanIUPAC_T197","span":{"begin":1062,"end":1065},"obj":"\"http://rdf.glycoinfo.org/glycan/G55921QA\""},{"id":"GlycanIUPAC_T198","span":{"begin":1062,"end":1065},"obj":"\"http://rdf.glycoinfo.org/glycan/G99066DL\""},{"id":"GlycanIUPAC_T199","span":{"begin":1062,"end":1065},"obj":"\"http://rdf.glycoinfo.org/glycan/G33451PQ\""},{"id":"GlycanIUPAC_T200","span":{"begin":1062,"end":1065},"obj":"\"http://rdf.glycoinfo.org/glycan/G02111XU\""},{"id":"GlycanIUPAC_T201","span":{"begin":1062,"end":1065},"obj":"\"http://rdf.glycoinfo.org/glycan/G85193OM\""},{"id":"GlycanIUPAC_T202","span":{"begin":1062,"end":1065},"obj":"\"http://rdf.glycoinfo.org/glycan/G89174YQ\""},{"id":"GlycanIUPAC_T203","span":{"begin":1062,"end":1065},"obj":"\"http://rdf.glycoinfo.org/glycan/G28802LE\""},{"id":"GlycanIUPAC_T204","span":{"begin":1062,"end":1065},"obj":"\"http://rdf.glycoinfo.org/glycan/G56061JK\""},{"id":"GlycanIUPAC_T205","span":{"begin":1062,"end":1065},"obj":"\"http://rdf.glycoinfo.org/glycan/G68941BC\""},{"id":"GlycanIUPAC_T206","span":{"begin":1062,"end":1065},"obj":"\"http://rdf.glycoinfo.org/glycan/G55436FC\""},{"id":"GlycanIUPAC_T207","span":{"begin":1062,"end":1065},"obj":"\"http://rdf.glycoinfo.org/glycan/G24002PU\""},{"id":"GlycanIUPAC_T208","span":{"begin":1062,"end":1065},"obj":"\"http://rdf.glycoinfo.org/glycan/G61387SV\""},{"id":"GlycanIUPAC_T209","span":{"begin":1062,"end":1065},"obj":"\"http://rdf.glycoinfo.org/glycan/G31834HW\""},{"id":"GlycanIUPAC_T210","span":{"begin":1062,"end":1065},"obj":"\"http://rdf.glycoinfo.org/glycan/G35324RT\""},{"id":"GlycanIUPAC_T211","span":{"begin":1062,"end":1065},"obj":"\"http://rdf.glycoinfo.org/glycan/G34803QO\""},{"id":"GlycanIUPAC_T212","span":{"begin":1062,"end":1065},"obj":"\"http://rdf.glycoinfo.org/glycan/G92898FF\""},{"id":"GlycanIUPAC_T213","span":{"begin":1062,"end":1065},"obj":"\"http://rdf.glycoinfo.org/glycan/G01318VX\""},{"id":"GlycanIUPAC_T214","span":{"begin":1062,"end":1065},"obj":"\"http://rdf.glycoinfo.org/glycan/G83200MX\""},{"id":"GlycanIUPAC_T215","span":{"begin":1062,"end":1065},"obj":"\"http://rdf.glycoinfo.org/glycan/G56286UC\""},{"id":"GlycanIUPAC_T216","span":{"begin":1062,"end":1065},"obj":"\"http://rdf.glycoinfo.org/glycan/G07304QA\""},{"id":"GlycanIUPAC_T217","span":{"begin":1062,"end":1065},"obj":"\"http://rdf.glycoinfo.org/glycan/G06868OU\""},{"id":"GlycanIUPAC_T218","span":{"begin":1062,"end":1065},"obj":"\"http://rdf.glycoinfo.org/glycan/G12647BS\""},{"id":"GlycanIUPAC_T219","span":{"begin":1062,"end":1065},"obj":"\"http://rdf.glycoinfo.org/glycan/G51841DF\""},{"id":"GlycanIUPAC_T220","span":{"begin":1062,"end":1065},"obj":"\"http://rdf.glycoinfo.org/glycan/G32122AJ\""},{"id":"GlycanIUPAC_T221","span":{"begin":1062,"end":1065},"obj":"\"http://rdf.glycoinfo.org/glycan/G41125MN\""},{"id":"GlycanIUPAC_T222","span":{"begin":1062,"end":1065},"obj":"\"http://rdf.glycoinfo.org/glycan/G16093XS\""},{"id":"GlycanIUPAC_T223","span":{"begin":1062,"end":1065},"obj":"\"http://rdf.glycoinfo.org/glycan/G62425IX\""},{"id":"GlycanIUPAC_T224","span":{"begin":1062,"end":1065},"obj":"\"http://rdf.glycoinfo.org/glycan/G15673TO\""},{"id":"GlycanIUPAC_T225","span":{"begin":1062,"end":1065},"obj":"\"http://rdf.glycoinfo.org/glycan/G32857IK\""},{"id":"GlycanIUPAC_T226","span":{"begin":1062,"end":1065},"obj":"\"http://rdf.glycoinfo.org/glycan/G60047CJ\""},{"id":"GlycanIUPAC_T227","span":{"begin":1062,"end":1065},"obj":"\"http://rdf.glycoinfo.org/glycan/G55718ZB\""},{"id":"GlycanIUPAC_T228","span":{"begin":1062,"end":1065},"obj":"\"http://rdf.glycoinfo.org/glycan/G88355ZE\""},{"id":"GlycanIUPAC_T229","span":{"begin":1062,"end":1065},"obj":"\"http://rdf.glycoinfo.org/glycan/G11283PA\""},{"id":"GlycanIUPAC_T230","span":{"begin":1062,"end":1065},"obj":"\"http://rdf.glycoinfo.org/glycan/G71737IZ\""},{"id":"GlycanIUPAC_T231","span":{"begin":1062,"end":1065},"obj":"\"http://rdf.glycoinfo.org/glycan/G60912WZ\""},{"id":"GlycanIUPAC_T232","span":{"begin":1062,"end":1065},"obj":"\"http://rdf.glycoinfo.org/glycan/G99655SO\""},{"id":"GlycanIUPAC_T233","span":{"begin":1062,"end":1065},"obj":"\"http://rdf.glycoinfo.org/glycan/G10300TW\""},{"id":"GlycanIUPAC_T234","span":{"begin":1062,"end":1065},"obj":"\"http://rdf.glycoinfo.org/glycan/G89509FL\""},{"id":"GlycanIUPAC_T235","span":{"begin":1062,"end":1065},"obj":"\"http://rdf.glycoinfo.org/glycan/G31465TH\""},{"id":"GlycanIUPAC_T236","span":{"begin":1062,"end":1065},"obj":"\"http://rdf.glycoinfo.org/glycan/G94101LU\""},{"id":"GlycanIUPAC_T237","span":{"begin":1062,"end":1065},"obj":"\"http://rdf.glycoinfo.org/glycan/G38610BB\""},{"id":"GlycanIUPAC_T238","span":{"begin":1062,"end":1065},"obj":"\"http://rdf.glycoinfo.org/glycan/G85893UF\""}],"text":"Enzymatic synthesis of a 6'-sulphated sialyl-Lewisx which is an inhibitor of L-selectin binding to peripheral addressin.\nA sulphated form of sialyl-Lewisx, NeuAc alpha 2-3Gal beta 1-4(Fuc alpha 1-3)GlcNAc6OSO3 beta 1-3Gal, was synthesized enzymatically from a precursor disaccharide, GlcNAc6OSO3 beta 1-3Gal, using sequential steps involving beta 1,4-galactosyltransferase, alpha 2,3-trans-sialidase and recombinant alpha 1,3-fucosyltransferase, respectively. Successful enzymatic fucosylation at the 3 position of the GlcNAc6OSO3 residue demonstrated that fucosyltransferase are capable of generating, in situ, sulphated sialyl Lewisx structures containing sulphate at the 6 position of GlcNAc. The sulphated sialyl-Lewisx pentasaccharide produced by this procedure inhibited binding of a soluble form of L-selectin to 35SO4-labelled peripheral addressin with an IC50 of 0.8 mM, whereas sialyl-Lewisx tetrasaccharide was a weaker inhibitor, displaying an IC50 of 3.2 mM. Hemmerich and Rosen (Biochemistry, 33, 4820-4829, 1994) recently reported the presence of Gal beta 1-4GlcNAcO6SO3 structures on murine peripheral addressin Sgp50, in addition to sialyl Lewisx structures sulphated at the 6-O-galactose position. Based on our data, we suggest that sialyl Lewisx sulphated at the 6-O-GlcNAc position may also exist on receptors and function as a ligand for L-selectin."}

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":120},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":121,"end":459},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":460,"end":695},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":696,"end":971},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":972,"end":1215},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":1216,"end":1370},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":120},"obj":"Sentence"},{"id":"T2","span":{"begin":121,"end":459},"obj":"Sentence"},{"id":"T3","span":{"begin":460,"end":695},"obj":"Sentence"},{"id":"T4","span":{"begin":696,"end":971},"obj":"Sentence"},{"id":"T5","span":{"begin":972,"end":1215},"obj":"Sentence"},{"id":"T6","span":{"begin":1216,"end":1370},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":120},"obj":"Sentence"},{"id":"T2","span":{"begin":121,"end":459},"obj":"Sentence"},{"id":"T3","span":{"begin":460,"end":695},"obj":"Sentence"},{"id":"T4","span":{"begin":696,"end":971},"obj":"Sentence"},{"id":"T5","span":{"begin":972,"end":1215},"obj":"Sentence"},{"id":"T6","span":{"begin":1216,"end":1370},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Enzymatic synthesis of a 6'-sulphated sialyl-Lewisx which is an inhibitor of L-selectin binding to peripheral addressin.\nA sulphated form of sialyl-Lewisx, NeuAc alpha 2-3Gal beta 1-4(Fuc alpha 1-3)GlcNAc6OSO3 beta 1-3Gal, was synthesized enzymatically from a precursor disaccharide, GlcNAc6OSO3 beta 1-3Gal, using sequential steps involving beta 1,4-galactosyltransferase, alpha 2,3-trans-sialidase and recombinant alpha 1,3-fucosyltransferase, respectively. Successful enzymatic fucosylation at the 3 position of the GlcNAc6OSO3 residue demonstrated that fucosyltransferase are capable of generating, in situ, sulphated sialyl Lewisx structures containing sulphate at the 6 position of GlcNAc. The sulphated sialyl-Lewisx pentasaccharide produced by this procedure inhibited binding of a soluble form of L-selectin to 35SO4-labelled peripheral addressin with an IC50 of 0.8 mM, whereas sialyl-Lewisx tetrasaccharide was a weaker inhibitor, displaying an IC50 of 3.2 mM. Hemmerich and Rosen (Biochemistry, 33, 4820-4829, 1994) recently reported the presence of Gal beta 1-4GlcNAcO6SO3 structures on murine peripheral addressin Sgp50, in addition to sialyl Lewisx structures sulphated at the 6-O-galactose position. Based on our data, we suggest that sialyl Lewisx sulphated at the 6-O-GlcNAc position may also exist on receptors and function as a ligand for L-selectin."}

{"project":"Lectin","denotations":[{"id":"Lectin_T1","span":{"begin":79,"end":87},"obj":"https://acgg.asia/db/lfdb/LfDB0013"},{"id":"Lectin_T2","span":{"begin":808,"end":816},"obj":"https://acgg.asia/db/lfdb/LfDB0013"},{"id":"Lectin_T3","span":{"begin":1361,"end":1369},"obj":"https://acgg.asia/db/lfdb/LfDB0013"},{"id":"Lectin_T4","span":{"begin":79,"end":87},"obj":"https://acgg.asia/db/lfdb/LfDB0043"},{"id":"Lectin_T5","span":{"begin":808,"end":816},"obj":"https://acgg.asia/db/lfdb/LfDB0043"},{"id":"Lectin_T6","span":{"begin":1361,"end":1369},"obj":"https://acgg.asia/db/lfdb/LfDB0043"},{"id":"Lectin_T7","span":{"begin":77,"end":87},"obj":"https://acgg.asia/db/lfdb/LfDB0142"},{"id":"Lectin_T8","span":{"begin":806,"end":816},"obj":"https://acgg.asia/db/lfdb/LfDB0142"},{"id":"Lectin_T9","span":{"begin":1359,"end":1369},"obj":"https://acgg.asia/db/lfdb/LfDB0142"}],"text":"Enzymatic synthesis of a 6'-sulphated sialyl-Lewisx which is an inhibitor of L-selectin binding to peripheral addressin.\nA sulphated form of sialyl-Lewisx, NeuAc alpha 2-3Gal beta 1-4(Fuc alpha 1-3)GlcNAc6OSO3 beta 1-3Gal, was synthesized enzymatically from a precursor disaccharide, GlcNAc6OSO3 beta 1-3Gal, using sequential steps involving beta 1,4-galactosyltransferase, alpha 2,3-trans-sialidase and recombinant alpha 1,3-fucosyltransferase, respectively. Successful enzymatic fucosylation at the 3 position of the GlcNAc6OSO3 residue demonstrated that fucosyltransferase are capable of generating, in situ, sulphated sialyl Lewisx structures containing sulphate at the 6 position of GlcNAc. The sulphated sialyl-Lewisx pentasaccharide produced by this procedure inhibited binding of a soluble form of L-selectin to 35SO4-labelled peripheral addressin with an IC50 of 0.8 mM, whereas sialyl-Lewisx tetrasaccharide was a weaker inhibitor, displaying an IC50 of 3.2 mM. Hemmerich and Rosen (Biochemistry, 33, 4820-4829, 1994) recently reported the presence of Gal beta 1-4GlcNAcO6SO3 structures on murine peripheral addressin Sgp50, in addition to sialyl Lewisx structures sulphated at the 6-O-galactose position. Based on our data, we suggest that sialyl Lewisx sulphated at the 6-O-GlcNAc position may also exist on receptors and function as a ligand for L-selectin."}

{"project":"GlycoBiology-Epitope","denotations":[{"id":"PD-GlycoEpitope-B_T1","span":{"begin":1284,"end":1292},"obj":"http://www.glycoepitope.jp/epitopes/EP0004"},{"id":"PD-GlycoEpitope-B_T2","span":{"begin":826,"end":834},"obj":"id"}],"text":"Enzymatic synthesis of a 6'-sulphated sialyl-Lewisx which is an inhibitor of L-selectin binding to peripheral addressin.\nA sulphated form of sialyl-Lewisx, NeuAc alpha 2-3Gal beta 1-4(Fuc alpha 1-3)GlcNAc6OSO3 beta 1-3Gal, was synthesized enzymatically from a precursor disaccharide, GlcNAc6OSO3 beta 1-3Gal, using sequential steps involving beta 1,4-galactosyltransferase, alpha 2,3-trans-sialidase and recombinant alpha 1,3-fucosyltransferase, respectively. Successful enzymatic fucosylation at the 3 position of the GlcNAc6OSO3 residue demonstrated that fucosyltransferase are capable of generating, in situ, sulphated sialyl Lewisx structures containing sulphate at the 6 position of GlcNAc. The sulphated sialyl-Lewisx pentasaccharide produced by this procedure inhibited binding of a soluble form of L-selectin to 35SO4-labelled peripheral addressin with an IC50 of 0.8 mM, whereas sialyl-Lewisx tetrasaccharide was a weaker inhibitor, displaying an IC50 of 3.2 mM. Hemmerich and Rosen (Biochemistry, 33, 4820-4829, 1994) recently reported the presence of Gal beta 1-4GlcNAcO6SO3 structures on murine peripheral addressin Sgp50, in addition to sialyl Lewisx structures sulphated at the 6-O-galactose position. Based on our data, we suggest that sialyl Lewisx sulphated at the 6-O-GlcNAc position may also exist on receptors and function as a ligand for L-selectin."}

{"project":"Glycan-GlyCosmos","denotations":[{"id":"T1","span":{"begin":156,"end":161},"obj":"Glycan"},{"id":"T2","span":{"begin":1284,"end":1292},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G76685HR"},{"id":"A3","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G49108TO"},{"id":"A4","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G49108TO"}],"text":"Enzymatic synthesis of a 6'-sulphated sialyl-Lewisx which is an inhibitor of L-selectin binding to peripheral addressin.\nA sulphated form of sialyl-Lewisx, NeuAc alpha 2-3Gal beta 1-4(Fuc alpha 1-3)GlcNAc6OSO3 beta 1-3Gal, was synthesized enzymatically from a precursor disaccharide, GlcNAc6OSO3 beta 1-3Gal, using sequential steps involving beta 1,4-galactosyltransferase, alpha 2,3-trans-sialidase and recombinant alpha 1,3-fucosyltransferase, respectively. Successful enzymatic fucosylation at the 3 position of the GlcNAc6OSO3 residue demonstrated that fucosyltransferase are capable of generating, in situ, sulphated sialyl Lewisx structures containing sulphate at the 6 position of GlcNAc. The sulphated sialyl-Lewisx pentasaccharide produced by this procedure inhibited binding of a soluble form of L-selectin to 35SO4-labelled peripheral addressin with an IC50 of 0.8 mM, whereas sialyl-Lewisx tetrasaccharide was a weaker inhibitor, displaying an IC50 of 3.2 mM. Hemmerich and Rosen (Biochemistry, 33, 4820-4829, 1994) recently reported the presence of Gal beta 1-4GlcNAcO6SO3 structures on murine peripheral addressin Sgp50, in addition to sialyl Lewisx structures sulphated at the 6-O-galactose position. Based on our data, we suggest that sialyl Lewisx sulphated at the 6-O-GlcNAc position may also exist on receptors and function as a ligand for L-selectin."}

{"project":"GlyCosmos-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":1284,"end":1292},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A1","pred":"glycoepitope_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0004"}],"text":"Enzymatic synthesis of a 6'-sulphated sialyl-Lewisx which is an inhibitor of L-selectin binding to peripheral addressin.\nA sulphated form of sialyl-Lewisx, NeuAc alpha 2-3Gal beta 1-4(Fuc alpha 1-3)GlcNAc6OSO3 beta 1-3Gal, was synthesized enzymatically from a precursor disaccharide, GlcNAc6OSO3 beta 1-3Gal, using sequential steps involving beta 1,4-galactosyltransferase, alpha 2,3-trans-sialidase and recombinant alpha 1,3-fucosyltransferase, respectively. Successful enzymatic fucosylation at the 3 position of the GlcNAc6OSO3 residue demonstrated that fucosyltransferase are capable of generating, in situ, sulphated sialyl Lewisx structures containing sulphate at the 6 position of GlcNAc. The sulphated sialyl-Lewisx pentasaccharide produced by this procedure inhibited binding of a soluble form of L-selectin to 35SO4-labelled peripheral addressin with an IC50 of 0.8 mM, whereas sialyl-Lewisx tetrasaccharide was a weaker inhibitor, displaying an IC50 of 3.2 mM. Hemmerich and Rosen (Biochemistry, 33, 4820-4829, 1994) recently reported the presence of Gal beta 1-4GlcNAcO6SO3 structures on murine peripheral addressin Sgp50, in addition to sialyl Lewisx structures sulphated at the 6-O-galactose position. Based on our data, we suggest that sialyl Lewisx sulphated at the 6-O-GlcNAc position may also exist on receptors and function as a ligand for L-selectin."}

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":120},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":121,"end":459},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":460,"end":695},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":696,"end":971},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":972,"end":1215},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":1216,"end":1370},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":120},"obj":"Sentence"},{"id":"T2","span":{"begin":121,"end":459},"obj":"Sentence"},{"id":"T3","span":{"begin":460,"end":695},"obj":"Sentence"},{"id":"T4","span":{"begin":696,"end":971},"obj":"Sentence"},{"id":"T5","span":{"begin":972,"end":1215},"obj":"Sentence"},{"id":"T6","span":{"begin":1216,"end":1370},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":120},"obj":"Sentence"},{"id":"T2","span":{"begin":121,"end":459},"obj":"Sentence"},{"id":"T3","span":{"begin":460,"end":695},"obj":"Sentence"},{"id":"T4","span":{"begin":696,"end":971},"obj":"Sentence"},{"id":"T5","span":{"begin":972,"end":1215},"obj":"Sentence"},{"id":"T6","span":{"begin":1216,"end":1370},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Enzymatic synthesis of a 6'-sulphated sialyl-Lewisx which is an inhibitor of L-selectin binding to peripheral addressin.\nA sulphated form of sialyl-Lewisx, NeuAc alpha 2-3Gal beta 1-4(Fuc alpha 1-3)GlcNAc6OSO3 beta 1-3Gal, was synthesized enzymatically from a precursor disaccharide, GlcNAc6OSO3 beta 1-3Gal, using sequential steps involving beta 1,4-galactosyltransferase, alpha 2,3-trans-sialidase and recombinant alpha 1,3-fucosyltransferase, respectively. Successful enzymatic fucosylation at the 3 position of the GlcNAc6OSO3 residue demonstrated that fucosyltransferase are capable of generating, in situ, sulphated sialyl Lewisx structures containing sulphate at the 6 position of GlcNAc. The sulphated sialyl-Lewisx pentasaccharide produced by this procedure inhibited binding of a soluble form of L-selectin to 35SO4-labelled peripheral addressin with an IC50 of 0.8 mM, whereas sialyl-Lewisx tetrasaccharide was a weaker inhibitor, displaying an IC50 of 3.2 mM. Hemmerich and Rosen (Biochemistry, 33, 4820-4829, 1994) recently reported the presence of Gal beta 1-4GlcNAcO6SO3 structures on murine peripheral addressin Sgp50, in addition to sialyl Lewisx structures sulphated at the 6-O-galactose position. Based on our data, we suggest that sialyl Lewisx sulphated at the 6-O-GlcNAc position may also exist on receptors and function as a ligand for L-selectin."}

{"project":"GlyCosmos15-Sentences","blocks":[{"id":"T1","span":{"begin":0,"end":120},"obj":"Sentence"},{"id":"T2","span":{"begin":121,"end":459},"obj":"Sentence"},{"id":"T3","span":{"begin":460,"end":695},"obj":"Sentence"},{"id":"T4","span":{"begin":696,"end":971},"obj":"Sentence"},{"id":"T5","span":{"begin":972,"end":1215},"obj":"Sentence"},{"id":"T6","span":{"begin":1216,"end":1370},"obj":"Sentence"}],"text":"Enzymatic synthesis of a 6'-sulphated sialyl-Lewisx which is an inhibitor of L-selectin binding to peripheral addressin.\nA sulphated form of sialyl-Lewisx, NeuAc alpha 2-3Gal beta 1-4(Fuc alpha 1-3)GlcNAc6OSO3 beta 1-3Gal, was synthesized enzymatically from a precursor disaccharide, GlcNAc6OSO3 beta 1-3Gal, using sequential steps involving beta 1,4-galactosyltransferase, alpha 2,3-trans-sialidase and recombinant alpha 1,3-fucosyltransferase, respectively. Successful enzymatic fucosylation at the 3 position of the GlcNAc6OSO3 residue demonstrated that fucosyltransferase are capable of generating, in situ, sulphated sialyl Lewisx structures containing sulphate at the 6 position of GlcNAc. The sulphated sialyl-Lewisx pentasaccharide produced by this procedure inhibited binding of a soluble form of L-selectin to 35SO4-labelled peripheral addressin with an IC50 of 0.8 mM, whereas sialyl-Lewisx tetrasaccharide was a weaker inhibitor, displaying an IC50 of 3.2 mM. Hemmerich and Rosen (Biochemistry, 33, 4820-4829, 1994) recently reported the presence of Gal beta 1-4GlcNAcO6SO3 structures on murine peripheral addressin Sgp50, in addition to sialyl Lewisx structures sulphated at the 6-O-galactose position. Based on our data, we suggest that sialyl Lewisx sulphated at the 6-O-GlcNAc position may also exist on receptors and function as a ligand for L-selectin."}

{"project":"GlyCosmos15-Glycan","denotations":[{"id":"T1","span":{"begin":156,"end":161},"obj":"Glycan"},{"id":"T2","span":{"begin":1284,"end":1292},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G76685HR"},{"id":"A3","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G49108TO"},{"id":"A4","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G49108TO"}],"text":"Enzymatic synthesis of a 6'-sulphated sialyl-Lewisx which is an inhibitor of L-selectin binding to peripheral addressin.\nA sulphated form of sialyl-Lewisx, NeuAc alpha 2-3Gal beta 1-4(Fuc alpha 1-3)GlcNAc6OSO3 beta 1-3Gal, was synthesized enzymatically from a precursor disaccharide, GlcNAc6OSO3 beta 1-3Gal, using sequential steps involving beta 1,4-galactosyltransferase, alpha 2,3-trans-sialidase and recombinant alpha 1,3-fucosyltransferase, respectively. Successful enzymatic fucosylation at the 3 position of the GlcNAc6OSO3 residue demonstrated that fucosyltransferase are capable of generating, in situ, sulphated sialyl Lewisx structures containing sulphate at the 6 position of GlcNAc. The sulphated sialyl-Lewisx pentasaccharide produced by this procedure inhibited binding of a soluble form of L-selectin to 35SO4-labelled peripheral addressin with an IC50 of 0.8 mM, whereas sialyl-Lewisx tetrasaccharide was a weaker inhibitor, displaying an IC50 of 3.2 mM. Hemmerich and Rosen (Biochemistry, 33, 4820-4829, 1994) recently reported the presence of Gal beta 1-4GlcNAcO6SO3 structures on murine peripheral addressin Sgp50, in addition to sialyl Lewisx structures sulphated at the 6-O-galactose position. Based on our data, we suggest that sialyl Lewisx sulphated at the 6-O-GlcNAc position may also exist on receptors and function as a ligand for L-selectin."}

{"project":"GlyCosmos15-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":1284,"end":1292},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A1","pred":"glycoepitope_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0004"}],"text":"Enzymatic synthesis of a 6'-sulphated sialyl-Lewisx which is an inhibitor of L-selectin binding to peripheral addressin.\nA sulphated form of sialyl-Lewisx, NeuAc alpha 2-3Gal beta 1-4(Fuc alpha 1-3)GlcNAc6OSO3 beta 1-3Gal, was synthesized enzymatically from a precursor disaccharide, GlcNAc6OSO3 beta 1-3Gal, using sequential steps involving beta 1,4-galactosyltransferase, alpha 2,3-trans-sialidase and recombinant alpha 1,3-fucosyltransferase, respectively. Successful enzymatic fucosylation at the 3 position of the GlcNAc6OSO3 residue demonstrated that fucosyltransferase are capable of generating, in situ, sulphated sialyl Lewisx structures containing sulphate at the 6 position of GlcNAc. The sulphated sialyl-Lewisx pentasaccharide produced by this procedure inhibited binding of a soluble form of L-selectin to 35SO4-labelled peripheral addressin with an IC50 of 0.8 mM, whereas sialyl-Lewisx tetrasaccharide was a weaker inhibitor, displaying an IC50 of 3.2 mM. Hemmerich and Rosen (Biochemistry, 33, 4820-4829, 1994) recently reported the presence of Gal beta 1-4GlcNAcO6SO3 structures on murine peripheral addressin Sgp50, in addition to sialyl Lewisx structures sulphated at the 6-O-galactose position. Based on our data, we suggest that sialyl Lewisx sulphated at the 6-O-GlcNAc position may also exist on receptors and function as a ligand for L-selectin."}