PubMed:7524825 JSONTXT

{"project":"Glycan-Motif","denotations":[{"id":"T1","span":{"begin":19,"end":22},"obj":"https://glytoucan.org/Structures/Glycans/G01187XC"},{"id":"T2","span":{"begin":148,"end":152},"obj":"https://glytoucan.org/Structures/Glycans/G00054MO"},{"id":"T3","span":{"begin":154,"end":160},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T4","span":{"begin":212,"end":218},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T5","span":{"begin":319,"end":323},"obj":"https://glytoucan.org/Structures/Glycans/G00054MO"},{"id":"T6","span":{"begin":440,"end":444},"obj":"https://glytoucan.org/Structures/Glycans/G00054MO"},{"id":"T7","span":{"begin":460,"end":464},"obj":"https://glytoucan.org/Structures/Glycans/G00054MO"},{"id":"T8","span":{"begin":619,"end":623},"obj":"https://glytoucan.org/Structures/Glycans/G00054MO"},{"id":"T9","span":{"begin":836,"end":840},"obj":"https://glytoucan.org/Structures/Glycans/G00054MO"},{"id":"T10","span":{"begin":916,"end":920},"obj":"https://glytoucan.org/Structures/Glycans/G00054MO"},{"id":"T11","span":{"begin":1193,"end":1197},"obj":"https://glytoucan.org/Structures/Glycans/G00054MO"},{"id":"T12","span":{"begin":1276,"end":1280},"obj":"https://glytoucan.org/Structures/Glycans/G00054MO"},{"id":"T13","span":{"begin":1389,"end":1393},"obj":"https://glytoucan.org/Structures/Glycans/G00054MO"},{"id":"T14","span":{"begin":1636,"end":1640},"obj":"https://glytoucan.org/Structures/Glycans/G00054MO"}],"text":"Multivalent sialyl-LeX: potent inhibitors of E-selectin-mediated cell adhesion; reagent for staining activated endothelial cells.\nFree, monovalent, SLeX (Neu5Ac alpha 2-3Gal beta 1-4(Fuc alpha 1-3)-GlcNAc), SLn (Neu5Ac alpha 2-3Gal beta 1-4GlcNAc) and corresponding BSA-conjugated forms--displaying different ratios of SLeX and SLn to protein--were tested for their ability to inhibit binding of HL-60 cells to immobilized E-selectin. Free SLeX and conjugated SLeX-BSA inhibited cell binding in a dose-dependent manner. SLn and SLn-BSA did not inhibit binding. SLeX16BSA (16 mol tetrasaccharide/mol BSA) and monovalent SLeX inhibited cell binding with measured inhibitory concentrations (IC50S) of 1 microM and 1 mM, respectively, demonstrating a three-order-of-magnitude enhancement of inhibitory activity with the multivalent form of SLeX. A SLex7BSA conjugate was 10-fold less potent than those with 11 or 16 mol SLeX/mol BSA. An assay which measured neutrophil rolling on interleukin (IL)-1 beta-activated human umbilical vein endothelial cells (HUVECs) showed 50% reduction in the number of rolling neutrophils in the presence of 1 microM SLeX16BSA, whereas the level of free, monovalent SLeX oligosaccharide required to produce the same effect was approximately 0.3 mM. SLeX-BSA was found to be an excellent reagent for staining endothelial cells expressing E-selectin. Biotinylated SLeX-BSA in conjunction with Texas red avidin-stained lipopolysaccharide (LPS)-activated HUVECs, and co-incubation of activated cells with anti-E-selectin, specifically blocked staining. The distribution of E-selectin, as determined by binding of SLeX-BSA, was virtually identical with that obtained by binding of anti-E-selectin antibody.(ABSTRACT TRUNCATED AT 250 WORDS)"}

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{"project":"Glycosmos6-MAT","denotations":[{"id":"T1","span":{"begin":1026,"end":1030},"obj":"http://purl.obolibrary.org/obo/MAT_0000037"}],"text":"Multivalent sialyl-LeX: potent inhibitors of E-selectin-mediated cell adhesion; reagent for staining activated endothelial cells.\nFree, monovalent, SLeX (Neu5Ac alpha 2-3Gal beta 1-4(Fuc alpha 1-3)-GlcNAc), SLn (Neu5Ac alpha 2-3Gal beta 1-4GlcNAc) and corresponding BSA-conjugated forms--displaying different ratios of SLeX and SLn to protein--were tested for their ability to inhibit binding of HL-60 cells to immobilized E-selectin. Free SLeX and conjugated SLeX-BSA inhibited cell binding in a dose-dependent manner. SLn and SLn-BSA did not inhibit binding. SLeX16BSA (16 mol tetrasaccharide/mol BSA) and monovalent SLeX inhibited cell binding with measured inhibitory concentrations (IC50S) of 1 microM and 1 mM, respectively, demonstrating a three-order-of-magnitude enhancement of inhibitory activity with the multivalent form of SLeX. A SLex7BSA conjugate was 10-fold less potent than those with 11 or 16 mol SLeX/mol BSA. An assay which measured neutrophil rolling on interleukin (IL)-1 beta-activated human umbilical vein endothelial cells (HUVECs) showed 50% reduction in the number of rolling neutrophils in the presence of 1 microM SLeX16BSA, whereas the level of free, monovalent SLeX oligosaccharide required to produce the same effect was approximately 0.3 mM. SLeX-BSA was found to be an excellent reagent for staining endothelial cells expressing E-selectin. Biotinylated SLeX-BSA in conjunction with Texas red avidin-stained lipopolysaccharide (LPS)-activated HUVECs, and co-incubation of activated cells with anti-E-selectin, specifically blocked staining. The distribution of E-selectin, as determined by binding of SLeX-BSA, was virtually identical with that obtained by binding of anti-E-selectin antibody.(ABSTRACT TRUNCATED AT 250 WORDS)"}

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sialyl-LeX: potent inhibitors of E-selectin-mediated cell adhesion; reagent for staining activated endothelial cells.\nFree, monovalent, SLeX (Neu5Ac alpha 2-3Gal beta 1-4(Fuc alpha 1-3)-GlcNAc), SLn (Neu5Ac alpha 2-3Gal beta 1-4GlcNAc) and corresponding BSA-conjugated forms--displaying different ratios of SLeX and SLn to protein--were tested for their ability to inhibit binding of HL-60 cells to immobilized E-selectin. Free SLeX and conjugated SLeX-BSA inhibited cell binding in a dose-dependent manner. SLn and SLn-BSA did not inhibit binding. SLeX16BSA (16 mol tetrasaccharide/mol BSA) and monovalent SLeX inhibited cell binding with measured inhibitory concentrations (IC50S) of 1 microM and 1 mM, respectively, demonstrating a three-order-of-magnitude enhancement of inhibitory activity with the multivalent form of SLeX. A SLex7BSA conjugate was 10-fold less potent than those with 11 or 16 mol SLeX/mol BSA. An assay which measured neutrophil rolling on interleukin (IL)-1 beta-activated human umbilical vein endothelial cells (HUVECs) showed 50% reduction in the number of rolling neutrophils in the presence of 1 microM SLeX16BSA, whereas the level of free, monovalent SLeX oligosaccharide required to produce the same effect was approximately 0.3 mM. SLeX-BSA was found to be an excellent reagent for staining endothelial cells expressing E-selectin. Biotinylated SLeX-BSA in conjunction with Texas red avidin-stained lipopolysaccharide (LPS)-activated HUVECs, and co-incubation of activated cells with anti-E-selectin, specifically blocked staining. The distribution of E-selectin, as determined by binding of SLeX-BSA, was virtually identical with that obtained by binding of anti-E-selectin antibody.(ABSTRACT TRUNCATED AT 250 WORDS)"}

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{"project":"uniprot-mouse","denotations":[{"id":"T1","span":{"begin":45,"end":55},"obj":"http://www.uniprot.org/uniprot/Q00690"},{"id":"T2","span":{"begin":423,"end":433},"obj":"http://www.uniprot.org/uniprot/Q00690"},{"id":"T3","span":{"begin":1364,"end":1374},"obj":"http://www.uniprot.org/uniprot/Q00690"},{"id":"T4","span":{"begin":1533,"end":1543},"obj":"http://www.uniprot.org/uniprot/Q00690"},{"id":"T5","span":{"begin":1596,"end":1606},"obj":"http://www.uniprot.org/uniprot/Q00690"},{"id":"T6","span":{"begin":1708,"end":1718},"obj":"http://www.uniprot.org/uniprot/Q00690"},{"id":"T7","span":{"begin":396,"end":398},"obj":"http://www.uniprot.org/uniprot/P27656"},{"id":"T8","span":{"begin":396,"end":398},"obj":"http://www.uniprot.org/uniprot/P38060"},{"id":"T9","span":{"begin":989,"end":999},"obj":"http://www.uniprot.org/uniprot/P10749"},{"id":"T10","span":{"begin":1748,"end":1750},"obj":"http://www.uniprot.org/uniprot/Q8VHK8"}],"text":"Multivalent sialyl-LeX: potent inhibitors of E-selectin-mediated cell adhesion; reagent for staining activated endothelial cells.\nFree, monovalent, SLeX (Neu5Ac alpha 2-3Gal beta 1-4(Fuc alpha 1-3)-GlcNAc), SLn (Neu5Ac alpha 2-3Gal beta 1-4GlcNAc) and corresponding BSA-conjugated forms--displaying different ratios of SLeX and SLn to protein--were tested for their ability to inhibit binding of HL-60 cells to immobilized E-selectin. Free SLeX and conjugated SLeX-BSA inhibited cell binding in a dose-dependent manner. SLn and SLn-BSA did not inhibit binding. SLeX16BSA (16 mol tetrasaccharide/mol BSA) and monovalent SLeX inhibited cell binding with measured inhibitory concentrations (IC50S) of 1 microM and 1 mM, respectively, demonstrating a three-order-of-magnitude enhancement of inhibitory activity with the multivalent form of SLeX. A SLex7BSA conjugate was 10-fold less potent than those with 11 or 16 mol SLeX/mol BSA. An assay which measured neutrophil rolling on interleukin (IL)-1 beta-activated human umbilical vein endothelial cells (HUVECs) showed 50% reduction in the number of rolling neutrophils in the presence of 1 microM SLeX16BSA, whereas the level of free, monovalent SLeX oligosaccharide required to produce the same effect was approximately 0.3 mM. SLeX-BSA was found to be an excellent reagent for staining endothelial cells expressing E-selectin. Biotinylated SLeX-BSA in conjunction with Texas red avidin-stained lipopolysaccharide (LPS)-activated HUVECs, and co-incubation of activated cells with anti-E-selectin, specifically blocked staining. The distribution of E-selectin, as determined by binding of SLeX-BSA, was virtually identical with that obtained by binding of anti-E-selectin antibody.(ABSTRACT TRUNCATED AT 250 WORDS)"}

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":123,"end":128},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T2","span":{"begin":174,"end":178},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"},{"id":"T3","span":{"begin":174,"end":178},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T4","span":{"begin":232,"end":236},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"},{"id":"T5","span":{"begin":232,"end":236},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T6","span":{"begin":402,"end":407},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T7","span":{"begin":619,"end":633},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/1206048"},{"id":"T8","span":{"begin":995,"end":999},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T9","span":{"begin":995,"end":999},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"},{"id":"T10","span":{"begin":1043,"end":1048},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T11","span":{"begin":1347,"end":1352},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T12","span":{"begin":1490,"end":1492},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/13893"},{"id":"T13","span":{"begin":1517,"end":1522},"obj":"http://purl.bioontology.org/ontology/STY/T025"}],"text":"Multivalent sialyl-LeX: potent inhibitors of E-selectin-mediated cell adhesion; reagent for staining activated endothelial cells.\nFree, monovalent, SLeX (Neu5Ac alpha 2-3Gal beta 1-4(Fuc alpha 1-3)-GlcNAc), SLn (Neu5Ac alpha 2-3Gal beta 1-4GlcNAc) and corresponding BSA-conjugated forms--displaying different ratios of SLeX and SLn to protein--were tested for their ability to inhibit binding of HL-60 cells to immobilized E-selectin. Free SLeX and conjugated SLeX-BSA inhibited cell binding in a dose-dependent manner. SLn and SLn-BSA did not inhibit binding. SLeX16BSA (16 mol tetrasaccharide/mol BSA) and monovalent SLeX inhibited cell binding with measured inhibitory concentrations (IC50S) of 1 microM and 1 mM, respectively, demonstrating a three-order-of-magnitude enhancement of inhibitory activity with the multivalent form of SLeX. A SLex7BSA conjugate was 10-fold less potent than those with 11 or 16 mol SLeX/mol BSA. An assay which measured neutrophil rolling on interleukin (IL)-1 beta-activated human umbilical vein endothelial cells (HUVECs) showed 50% reduction in the number of rolling neutrophils in the presence of 1 microM SLeX16BSA, whereas the level of free, monovalent SLeX oligosaccharide required to produce the same effect was approximately 0.3 mM. SLeX-BSA was found to be an excellent reagent for staining endothelial cells expressing E-selectin. Biotinylated SLeX-BSA in conjunction with Texas red avidin-stained lipopolysaccharide (LPS)-activated HUVECs, and co-incubation of activated cells with anti-E-selectin, specifically blocked staining. The distribution of E-selectin, as determined by binding of SLeX-BSA, was virtually identical with that obtained by binding of anti-E-selectin antibody.(ABSTRACT TRUNCATED AT 250 WORDS)"}

{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":12,"end":18},"obj":"http://purl.obolibrary.org/obo/GO_0097503"},{"id":"T2","span":{"begin":56,"end":78},"obj":"http://purl.obolibrary.org/obo/GO_0033627"},{"id":"T3","span":{"begin":65,"end":78},"obj":"http://purl.obolibrary.org/obo/GO_0007155"},{"id":"T4","span":{"begin":101,"end":128},"obj":"http://purl.obolibrary.org/obo/GO_0042118"},{"id":"T5","span":{"begin":101,"end":128},"obj":"http://purl.obolibrary.org/obo/GO_0045603"},{"id":"T6","span":{"begin":101,"end":128},"obj":"http://purl.obolibrary.org/obo/GO_1901552"},{"id":"T7","span":{"begin":101,"end":128},"obj":"http://purl.obolibrary.org/obo/GO_0001938"},{"id":"T8","span":{"begin":270,"end":280},"obj":"http://purl.obolibrary.org/obo/GO_0000746"},{"id":"T9","span":{"begin":449,"end":459},"obj":"http://purl.obolibrary.org/obo/GO_0000746"},{"id":"T10","span":{"begin":853,"end":862},"obj":"http://purl.obolibrary.org/obo/GO_0000746"},{"id":"T11","span":{"begin":377,"end":392},"obj":"http://purl.obolibrary.org/obo/GO_0051100"},{"id":"T12","span":{"begin":544,"end":559},"obj":"http://purl.obolibrary.org/obo/GO_0051100"},{"id":"T13","span":{"begin":989,"end":999},"obj":"http://purl.obolibrary.org/obo/GO_0032611"},{"id":"T14","span":{"begin":993,"end":1009},"obj":"http://purl.obolibrary.org/obo/GO_0036364"},{"id":"T15","span":{"begin":993,"end":1009},"obj":"http://purl.obolibrary.org/obo/GO_0046509"},{"id":"T16","span":{"begin":1507,"end":1522},"obj":"http://purl.obolibrary.org/obo/GO_0001775"}],"text":"Multivalent sialyl-LeX: potent inhibitors of E-selectin-mediated cell adhesion; reagent for staining activated endothelial cells.\nFree, monovalent, SLeX (Neu5Ac alpha 2-3Gal beta 1-4(Fuc alpha 1-3)-GlcNAc), SLn (Neu5Ac alpha 2-3Gal beta 1-4GlcNAc) and corresponding BSA-conjugated forms--displaying different ratios of SLeX and SLn to protein--were tested for their ability to inhibit binding of HL-60 cells to immobilized E-selectin. Free SLeX and conjugated SLeX-BSA inhibited cell binding in a dose-dependent manner. SLn and SLn-BSA did not inhibit binding. SLeX16BSA (16 mol tetrasaccharide/mol BSA) and monovalent SLeX inhibited cell binding with measured inhibitory concentrations (IC50S) of 1 microM and 1 mM, respectively, demonstrating a three-order-of-magnitude enhancement of inhibitory activity with the multivalent form of SLeX. A SLex7BSA conjugate was 10-fold less potent than those with 11 or 16 mol SLeX/mol BSA. An assay which measured neutrophil rolling on interleukin (IL)-1 beta-activated human umbilical vein endothelial cells (HUVECs) showed 50% reduction in the number of rolling neutrophils in the presence of 1 microM SLeX16BSA, whereas the level of free, monovalent SLeX oligosaccharide required to produce the same effect was approximately 0.3 mM. SLeX-BSA was found to be an excellent reagent for staining endothelial cells expressing E-selectin. Biotinylated SLeX-BSA in conjunction with Texas red avidin-stained lipopolysaccharide (LPS)-activated HUVECs, and co-incubation of activated cells with anti-E-selectin, specifically blocked staining. The distribution of E-selectin, as determined by binding of SLeX-BSA, was virtually identical with that obtained by binding of anti-E-selectin antibody.(ABSTRACT TRUNCATED AT 250 WORDS)"}

{"project":"GO-MF","denotations":[{"id":"T1","span":{"begin":47,"end":55},"obj":"http://purl.obolibrary.org/obo/GO_0030246"},{"id":"T2","span":{"begin":425,"end":433},"obj":"http://purl.obolibrary.org/obo/GO_0030246"},{"id":"T3","span":{"begin":1366,"end":1374},"obj":"http://purl.obolibrary.org/obo/GO_0030246"},{"id":"T4","span":{"begin":1535,"end":1543},"obj":"http://purl.obolibrary.org/obo/GO_0030246"},{"id":"T5","span":{"begin":1598,"end":1606},"obj":"http://purl.obolibrary.org/obo/GO_0030246"},{"id":"T6","span":{"begin":1710,"end":1718},"obj":"http://purl.obolibrary.org/obo/GO_0030246"},{"id":"T7","span":{"begin":385,"end":392},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T8","span":{"begin":484,"end":491},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T9","span":{"begin":552,"end":559},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T10","span":{"begin":639,"end":646},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T11","span":{"begin":1625,"end":1632},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T12","span":{"begin":1692,"end":1699},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T13","span":{"begin":385,"end":392},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T14","span":{"begin":484,"end":491},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T15","span":{"begin":552,"end":559},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T16","span":{"begin":639,"end":646},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T17","span":{"begin":1625,"end":1632},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T18","span":{"begin":1692,"end":1699},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T19","span":{"begin":385,"end":392},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T20","span":{"begin":484,"end":491},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T21","span":{"begin":552,"end":559},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T22","span":{"begin":639,"end":646},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T23","span":{"begin":1625,"end":1632},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T24","span":{"begin":1692,"end":1699},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T25","span":{"begin":385,"end":392},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T26","span":{"begin":484,"end":491},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T27","span":{"begin":552,"end":559},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T28","span":{"begin":639,"end":646},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T29","span":{"begin":1625,"end":1632},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T30","span":{"begin":1692,"end":1699},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T31","span":{"begin":989,"end":994},"obj":"http://purl.obolibrary.org/obo/GO_0005149"},{"id":"T32","span":{"begin":1719,"end":1727},"obj":"http://purl.obolibrary.org/obo/GO_0003823"}],"text":"Multivalent sialyl-LeX: potent inhibitors of E-selectin-mediated cell adhesion; reagent for staining activated endothelial cells.\nFree, monovalent, SLeX (Neu5Ac alpha 2-3Gal beta 1-4(Fuc alpha 1-3)-GlcNAc), SLn (Neu5Ac alpha 2-3Gal beta 1-4GlcNAc) and corresponding BSA-conjugated forms--displaying different ratios of SLeX and SLn to protein--were tested for their ability to inhibit binding of HL-60 cells to immobilized E-selectin. Free SLeX and conjugated SLeX-BSA inhibited cell binding in a dose-dependent manner. SLn and SLn-BSA did not inhibit binding. SLeX16BSA (16 mol tetrasaccharide/mol BSA) and monovalent SLeX inhibited cell binding with measured inhibitory concentrations (IC50S) of 1 microM and 1 mM, respectively, demonstrating a three-order-of-magnitude enhancement of inhibitory activity with the multivalent form of SLeX. A SLex7BSA conjugate was 10-fold less potent than those with 11 or 16 mol SLeX/mol BSA. An assay which measured neutrophil rolling on interleukin (IL)-1 beta-activated human umbilical vein endothelial cells (HUVECs) showed 50% reduction in the number of rolling neutrophils in the presence of 1 microM SLeX16BSA, whereas the level of free, monovalent SLeX oligosaccharide required to produce the same effect was approximately 0.3 mM. SLeX-BSA was found to be an excellent reagent for staining endothelial cells expressing E-selectin. Biotinylated SLeX-BSA in conjunction with Texas red avidin-stained lipopolysaccharide (LPS)-activated HUVECs, and co-incubation of activated cells with anti-E-selectin, specifically blocked staining. The distribution of E-selectin, as determined by binding of SLeX-BSA, was virtually identical with that obtained by binding of anti-E-selectin antibody.(ABSTRACT TRUNCATED AT 250 WORDS)"}

{"project":"GO-CC","denotations":[{"id":"T1","span":{"begin":65,"end":69},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T2","span":{"begin":479,"end":483},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T3","span":{"begin":123,"end":128},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T4","span":{"begin":402,"end":407},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T5","span":{"begin":1043,"end":1048},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T6","span":{"begin":1347,"end":1352},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T7","span":{"begin":1517,"end":1522},"obj":"http://purl.obolibrary.org/obo/GO_0005623"}],"text":"Multivalent sialyl-LeX: potent inhibitors of E-selectin-mediated cell adhesion; reagent for staining activated endothelial cells.\nFree, monovalent, SLeX (Neu5Ac alpha 2-3Gal beta 1-4(Fuc alpha 1-3)-GlcNAc), SLn (Neu5Ac alpha 2-3Gal beta 1-4GlcNAc) and corresponding BSA-conjugated forms--displaying different ratios of SLeX and SLn to protein--were tested for their ability to inhibit binding of HL-60 cells to immobilized E-selectin. Free SLeX and conjugated SLeX-BSA inhibited cell binding in a dose-dependent manner. SLn and SLn-BSA did not inhibit binding. SLeX16BSA (16 mol tetrasaccharide/mol BSA) and monovalent SLeX inhibited cell binding with measured inhibitory concentrations (IC50S) of 1 microM and 1 mM, respectively, demonstrating a three-order-of-magnitude enhancement of inhibitory activity with the multivalent form of SLeX. A SLex7BSA conjugate was 10-fold less potent than those with 11 or 16 mol SLeX/mol BSA. An assay which measured neutrophil rolling on interleukin (IL)-1 beta-activated human umbilical vein endothelial cells (HUVECs) showed 50% reduction in the number of rolling neutrophils in the presence of 1 microM SLeX16BSA, whereas the level of free, monovalent SLeX oligosaccharide required to produce the same effect was approximately 0.3 mM. SLeX-BSA was found to be an excellent reagent for staining endothelial cells expressing E-selectin. Biotinylated SLeX-BSA in conjunction with Texas red avidin-stained lipopolysaccharide (LPS)-activated HUVECs, and co-incubation of activated cells with anti-E-selectin, specifically blocked staining. The distribution of E-selectin, as determined by binding of SLeX-BSA, was virtually identical with that obtained by binding of anti-E-selectin antibody.(ABSTRACT TRUNCATED AT 250 WORDS)"}

{"project":"UBERON-AE","denotations":[{"id":"T1","span":{"begin":1016,"end":1030},"obj":"http://purl.obolibrary.org/obo/UBERON_0002066"},{"id":"T2","span":{"begin":1016,"end":1042},"obj":"http://purl.obolibrary.org/obo/UBERON_0007777"},{"id":"T3","span":{"begin":1026,"end":1030},"obj":"http://purl.obolibrary.org/obo/UBERON_0001638"}],"text":"Multivalent sialyl-LeX: potent inhibitors of E-selectin-mediated cell adhesion; reagent for staining activated endothelial cells.\nFree, monovalent, SLeX (Neu5Ac alpha 2-3Gal beta 1-4(Fuc alpha 1-3)-GlcNAc), SLn (Neu5Ac alpha 2-3Gal beta 1-4GlcNAc) and corresponding BSA-conjugated forms--displaying different ratios of SLeX and SLn to protein--were tested for their ability to inhibit binding of HL-60 cells to immobilized E-selectin. Free SLeX and conjugated SLeX-BSA inhibited cell binding in a dose-dependent manner. SLn and SLn-BSA did not inhibit binding. SLeX16BSA (16 mol tetrasaccharide/mol BSA) and monovalent SLeX inhibited cell binding with measured inhibitory concentrations (IC50S) of 1 microM and 1 mM, respectively, demonstrating a three-order-of-magnitude enhancement of inhibitory activity with the multivalent form of SLeX. A SLex7BSA conjugate was 10-fold less potent than those with 11 or 16 mol SLeX/mol BSA. An assay which measured neutrophil rolling on interleukin (IL)-1 beta-activated human umbilical vein endothelial cells (HUVECs) showed 50% reduction in the number of rolling neutrophils in the presence of 1 microM SLeX16BSA, whereas the level of free, monovalent SLeX oligosaccharide required to produce the same effect was approximately 0.3 mM. SLeX-BSA was found to be an excellent reagent for staining endothelial cells expressing E-selectin. Biotinylated SLeX-BSA in conjunction with Texas red avidin-stained lipopolysaccharide (LPS)-activated HUVECs, and co-incubation of activated cells with anti-E-selectin, specifically blocked staining. The distribution of E-selectin, as determined by binding of SLeX-BSA, was virtually identical with that obtained by binding of anti-E-selectin antibody.(ABSTRACT TRUNCATED AT 250 WORDS)"}

{"project":"NGLY1-deficiency","denotations":[{"id":"PD-NGLY1-deficiency-B_T1","span":{"begin":198,"end":204},"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":"Multivalent sialyl-LeX: potent inhibitors of E-selectin-mediated cell adhesion; reagent for staining activated endothelial cells.\nFree, monovalent, SLeX (Neu5Ac alpha 2-3Gal beta 1-4(Fuc alpha 1-3)-GlcNAc), SLn (Neu5Ac alpha 2-3Gal beta 1-4GlcNAc) and corresponding BSA-conjugated forms--displaying different ratios of SLeX and SLn to protein--were tested for their ability to inhibit binding of HL-60 cells to immobilized E-selectin. Free SLeX and conjugated SLeX-BSA inhibited cell binding in a dose-dependent manner. SLn and SLn-BSA did not inhibit binding. SLeX16BSA (16 mol tetrasaccharide/mol BSA) and monovalent SLeX inhibited cell binding with measured inhibitory concentrations (IC50S) of 1 microM and 1 mM, respectively, demonstrating a three-order-of-magnitude enhancement of inhibitory activity with the multivalent form of SLeX. A SLex7BSA conjugate was 10-fold less potent than those with 11 or 16 mol SLeX/mol BSA. An assay which measured neutrophil rolling on interleukin (IL)-1 beta-activated human umbilical vein endothelial cells (HUVECs) showed 50% reduction in the number of rolling neutrophils in the presence of 1 microM SLeX16BSA, whereas the level of free, monovalent SLeX oligosaccharide required to produce the same effect was approximately 0.3 mM. SLeX-BSA was found to be an excellent reagent for staining endothelial cells expressing E-selectin. Biotinylated SLeX-BSA in conjunction with Texas red avidin-stained lipopolysaccharide (LPS)-activated HUVECs, and co-incubation of activated cells with anti-E-selectin, specifically blocked staining. The distribution of E-selectin, as determined by binding of SLeX-BSA, was virtually identical with that obtained by binding of anti-E-selectin antibody.(ABSTRACT TRUNCATED AT 250 WORDS)"}

{"project":"GlycoBiology-MAT","denotations":[{"id":"T1","span":{"begin":1026,"end":1030},"obj":"http://purl.obolibrary.org/obo/MAT_0000037"}],"text":"Multivalent sialyl-LeX: potent inhibitors of E-selectin-mediated cell adhesion; reagent for staining activated endothelial cells.\nFree, monovalent, SLeX (Neu5Ac alpha 2-3Gal beta 1-4(Fuc alpha 1-3)-GlcNAc), SLn (Neu5Ac alpha 2-3Gal beta 1-4GlcNAc) and corresponding BSA-conjugated forms--displaying different ratios of SLeX and SLn to protein--were tested for their ability to inhibit binding of HL-60 cells to immobilized E-selectin. Free SLeX and conjugated SLeX-BSA inhibited cell binding in a dose-dependent manner. SLn and SLn-BSA did not inhibit binding. SLeX16BSA (16 mol tetrasaccharide/mol BSA) and monovalent SLeX inhibited cell binding with measured inhibitory concentrations (IC50S) of 1 microM and 1 mM, respectively, demonstrating a three-order-of-magnitude enhancement of inhibitory activity with the multivalent form of SLeX. A SLex7BSA conjugate was 10-fold less potent than those with 11 or 16 mol SLeX/mol BSA. An assay which measured neutrophil rolling on interleukin (IL)-1 beta-activated human umbilical vein endothelial cells (HUVECs) showed 50% reduction in the number of rolling neutrophils in the presence of 1 microM SLeX16BSA, whereas the level of free, monovalent SLeX oligosaccharide required to produce the same effect was approximately 0.3 mM. SLeX-BSA was found to be an excellent reagent for staining endothelial cells expressing E-selectin. Biotinylated SLeX-BSA in conjunction with Texas red avidin-stained lipopolysaccharide (LPS)-activated HUVECs, and co-incubation of activated cells with anti-E-selectin, specifically blocked staining. The distribution of E-selectin, as determined by binding of SLeX-BSA, was virtually identical with that obtained by binding of anti-E-selectin antibody.(ABSTRACT TRUNCATED AT 250 WORDS)"}

{"project":"GlyTouCan-IUPAC","denotations":[{"id":"GlycanIUPAC_T1","span":{"begin":154,"end":160},"obj":"\"http://rdf.glycoinfo.org/glycan/G76685HR\""},{"id":"GlycanIUPAC_T2","span":{"begin":212,"end":218},"obj":"\"http://rdf.glycoinfo.org/glycan/G76685HR\""},{"id":"GlycanIUPAC_T3","span":{"begin":154,"end":160},"obj":"\"http://rdf.glycoinfo.org/glycan/G65881BF\""},{"id":"GlycanIUPAC_T4","span":{"begin":212,"end":218},"obj":"\"http://rdf.glycoinfo.org/glycan/G65881BF\""},{"id":"GlycanIUPAC_T5","span":{"begin":154,"end":160},"obj":"\"http://rdf.glycoinfo.org/glycan/G82702MH\""},{"id":"GlycanIUPAC_T6","span":{"begin":212,"end":218},"obj":"\"http://rdf.glycoinfo.org/glycan/G82702MH\""},{"id":"GlycanIUPAC_T7","span":{"begin":154,"end":160},"obj":"\"http://rdf.glycoinfo.org/glycan/G51494MY\""},{"id":"GlycanIUPAC_T8","span":{"begin":212,"end":218},"obj":"\"http://rdf.glycoinfo.org/glycan/G51494MY\""},{"id":"GlycanIUPAC_T9","span":{"begin":154,"end":160},"obj":"\"http://rdf.glycoinfo.org/glycan/G37109XL\""},{"id":"GlycanIUPAC_T10","span":{"begin":212,"end":218},"obj":"\"http://rdf.glycoinfo.org/glycan/G37109XL\""},{"id":"GlycanIUPAC_T11","span":{"begin":154,"end":160},"obj":"\"http://rdf.glycoinfo.org/glycan/G47427MX\""},{"id":"GlycanIUPAC_T12","span":{"begin":212,"end":218},"obj":"\"http://rdf.glycoinfo.org/glycan/G47427MX\""},{"id":"GlycanIUPAC_T13","span":{"begin":154,"end":160},"obj":"\"http://rdf.glycoinfo.org/glycan/G89927NS\""},{"id":"GlycanIUPAC_T14","span":{"begin":212,"end":218},"obj":"\"http://rdf.glycoinfo.org/glycan/G89927NS\""},{"id":"GlycanIUPAC_T15","span":{"begin":183,"end":186},"obj":"\"http://rdf.glycoinfo.org/glycan/G49112ZN\""},{"id":"GlycanIUPAC_T16","span":{"begin":183,"end":186},"obj":"\"http://rdf.glycoinfo.org/glycan/G50059AJ\""},{"id":"GlycanIUPAC_T17","span":{"begin":183,"end":186},"obj":"\"http://rdf.glycoinfo.org/glycan/G76218YK\""},{"id":"GlycanIUPAC_T18","span":{"begin":183,"end":186},"obj":"\"http://rdf.glycoinfo.org/glycan/G50102KR\""},{"id":"GlycanIUPAC_T19","span":{"begin":183,"end":186},"obj":"\"http://rdf.glycoinfo.org/glycan/G10717VS\""},{"id":"GlycanIUPAC_T20","span":{"begin":183,"end":186},"obj":"\"http://rdf.glycoinfo.org/glycan/G60524RK\""},{"id":"GlycanIUPAC_T21","span":{"begin":183,"end":186},"obj":"\"http://rdf.glycoinfo.org/glycan/G84407TT\""},{"id":"GlycanIUPAC_T22","span":{"begin":183,"end":186},"obj":"\"http://rdf.glycoinfo.org/glycan/G64717JT\""},{"id":"GlycanIUPAC_T23","span":{"begin":183,"end":186},"obj":"\"http://rdf.glycoinfo.org/glycan/G45003TT\""},{"id":"GlycanIUPAC_T24","span":{"begin":183,"end":186},"obj":"\"http://rdf.glycoinfo.org/glycan/G73923FP\""},{"id":"GlycanIUPAC_T25","span":{"begin":183,"end":186},"obj":"\"http://rdf.glycoinfo.org/glycan/G78231MB\""},{"id":"GlycanIUPAC_T26","span":{"begin":183,"end":186},"obj":"\"http://rdf.glycoinfo.org/glycan/G80487UG\""},{"id":"GlycanIUPAC_T27","span":{"begin":183,"end":186},"obj":"\"http://rdf.glycoinfo.org/glycan/G29758MI\""},{"id":"GlycanIUPAC_T28","span":{"begin":183,"end":186},"obj":"\"http://rdf.glycoinfo.org/glycan/G02671KD\""},{"id":"GlycanIUPAC_T29","span":{"begin":183,"end":186},"obj":"\"http://rdf.glycoinfo.org/glycan/G57926TZ\""},{"id":"GlycanIUPAC_T30","span":{"begin":183,"end":186},"obj":"\"http://rdf.glycoinfo.org/glycan/G41718FD\""},{"id":"GlycanIUPAC_T31","span":{"begin":183,"end":186},"obj":"\"http://rdf.glycoinfo.org/glycan/G99840FL\""},{"id":"GlycanIUPAC_T32","span":{"begin":183,"end":186},"obj":"\"http://rdf.glycoinfo.org/glycan/G64321UX\""},{"id":"GlycanIUPAC_T33","span":{"begin":183,"end":186},"obj":"\"http://rdf.glycoinfo.org/glycan/G11231EG\""},{"id":"GlycanIUPAC_T34","span":{"begin":183,"end":186},"obj":"\"http://rdf.glycoinfo.org/glycan/G62741TN\""},{"id":"GlycanIUPAC_T35","span":{"begin":183,"end":186},"obj":"\"http://rdf.glycoinfo.org/glycan/G51576ZQ\""},{"id":"GlycanIUPAC_T36","span":{"begin":183,"end":186},"obj":"\"http://rdf.glycoinfo.org/glycan/G66056LD\""},{"id":"GlycanIUPAC_T37","span":{"begin":183,"end":186},"obj":"\"http://rdf.glycoinfo.org/glycan/G02768BF\""},{"id":"GlycanIUPAC_T38","span":{"begin":183,"end":186},"obj":"\"http://rdf.glycoinfo.org/glycan/G26168RO\""},{"id":"GlycanIUPAC_T39","span":{"begin":183,"end":186},"obj":"\"http://rdf.glycoinfo.org/glycan/G42890HL\""},{"id":"GlycanIUPAC_T40","span":{"begin":183,"end":186},"obj":"\"http://rdf.glycoinfo.org/glycan/G17533VU\""},{"id":"GlycanIUPAC_T41","span":{"begin":183,"end":186},"obj":"\"http://rdf.glycoinfo.org/glycan/G34306RG\""},{"id":"GlycanIUPAC_T42","span":{"begin":183,"end":186},"obj":"\"http://rdf.glycoinfo.org/glycan/G88735KU\""},{"id":"GlycanIUPAC_T43","span":{"begin":183,"end":186},"obj":"\"http://rdf.glycoinfo.org/glycan/G82605UA\""},{"id":"GlycanIUPAC_T44","span":{"begin":198,"end":204},"obj":"\"http://rdf.glycoinfo.org/glycan/G26693XF\""},{"id":"GlycanIUPAC_T45","span":{"begin":198,"end":204},"obj":"\"http://rdf.glycoinfo.org/glycan/G01864SU\""},{"id":"GlycanIUPAC_T46","span":{"begin":198,"end":204},"obj":"\"http://rdf.glycoinfo.org/glycan/G17605FD\""},{"id":"GlycanIUPAC_T47","span":{"begin":198,"end":204},"obj":"\"http://rdf.glycoinfo.org/glycan/G41950LU\""},{"id":"GlycanIUPAC_T48","span":{"begin":198,"end":204},"obj":"\"http://rdf.glycoinfo.org/glycan/G57195RJ\""},{"id":"GlycanIUPAC_T49","span":{"begin":198,"end":204},"obj":"\"http://rdf.glycoinfo.org/glycan/G85391SA\""},{"id":"GlycanIUPAC_T50","span":{"begin":198,"end":204},"obj":"\"http://rdf.glycoinfo.org/glycan/G89565QL\""},{"id":"GlycanIUPAC_T51","span":{"begin":198,"end":204},"obj":"\"http://rdf.glycoinfo.org/glycan/G80869MR\""},{"id":"GlycanIUPAC_T52","span":{"begin":198,"end":204},"obj":"\"http://rdf.glycoinfo.org/glycan/G55978NL\""},{"id":"GlycanIUPAC_T53","span":{"begin":198,"end":204},"obj":"\"http://rdf.glycoinfo.org/glycan/G54644LT\""},{"id":"GlycanIUPAC_T54","span":{"begin":198,"end":204},"obj":"\"http://rdf.glycoinfo.org/glycan/G25694UG\""},{"id":"GlycanIUPAC_T55","span":{"begin":198,"end":204},"obj":"\"http://rdf.glycoinfo.org/glycan/G25126RB\""},{"id":"GlycanIUPAC_T56","span":{"begin":198,"end":204},"obj":"\"http://rdf.glycoinfo.org/glycan/G51848AD\""},{"id":"GlycanIUPAC_T57","span":{"begin":198,"end":204},"obj":"\"http://rdf.glycoinfo.org/glycan/G94667GM\""},{"id":"GlycanIUPAC_T58","span":{"begin":198,"end":204},"obj":"\"http://rdf.glycoinfo.org/glycan/G30124BO\""},{"id":"GlycanIUPAC_T59","span":{"begin":198,"end":204},"obj":"\"http://rdf.glycoinfo.org/glycan/G82777EZ\""},{"id":"GlycanIUPAC_T60","span":{"begin":198,"end":204},"obj":"\"http://rdf.glycoinfo.org/glycan/G10151YZ\""},{"id":"GlycanIUPAC_T61","span":{"begin":198,"end":204},"obj":"\"http://rdf.glycoinfo.org/glycan/G17585ZM\""},{"id":"GlycanIUPAC_T62","span":{"begin":198,"end":204},"obj":"\"http://rdf.glycoinfo.org/glycan/G04411CJ\""},{"id":"GlycanIUPAC_T63","span":{"begin":198,"end":204},"obj":"\"http://rdf.glycoinfo.org/glycan/G38254HJ\""},{"id":"GlycanIUPAC_T64","span":{"begin":198,"end":204},"obj":"\"http://rdf.glycoinfo.org/glycan/G75188FS\""},{"id":"GlycanIUPAC_T65","span":{"begin":198,"end":204},"obj":"\"http://rdf.glycoinfo.org/glycan/G70374VG\""},{"id":"GlycanIUPAC_T66","span":{"begin":198,"end":204},"obj":"\"http://rdf.glycoinfo.org/glycan/G45176LJ\""},{"id":"GlycanIUPAC_T67","span":{"begin":198,"end":204},"obj":"\"http://rdf.glycoinfo.org/glycan/G30874VW\""},{"id":"GlycanIUPAC_T68","span":{"begin":198,"end":204},"obj":"\"http://rdf.glycoinfo.org/glycan/G69333MI\""},{"id":"GlycanIUPAC_T69","span":{"begin":198,"end":204},"obj":"\"http://rdf.glycoinfo.org/glycan/G10676XO\""},{"id":"GlycanIUPAC_T70","span":{"begin":198,"end":204},"obj":"\"http://rdf.glycoinfo.org/glycan/G14843DJ\""},{"id":"GlycanIUPAC_T71","span":{"begin":198,"end":204},"obj":"\"http://rdf.glycoinfo.org/glycan/G47546FR\""},{"id":"GlycanIUPAC_T72","span":{"begin":198,"end":204},"obj":"\"http://rdf.glycoinfo.org/glycan/G73695ZM\""},{"id":"GlycanIUPAC_T73","span":{"begin":198,"end":204},"obj":"\"http://rdf.glycoinfo.org/glycan/G31923TJ\""},{"id":"GlycanIUPAC_T74","span":{"begin":198,"end":204},"obj":"\"http://rdf.glycoinfo.org/glycan/G60519EP\""},{"id":"GlycanIUPAC_T75","span":{"begin":198,"end":204},"obj":"\"http://rdf.glycoinfo.org/glycan/G07933IA\""},{"id":"GlycanIUPAC_T76","span":{"begin":198,"end":204},"obj":"\"http://rdf.glycoinfo.org/glycan/G40745NH\""},{"id":"GlycanIUPAC_T77","span":{"begin":198,"end":204},"obj":"\"http://rdf.glycoinfo.org/glycan/G54496YV\""},{"id":"GlycanIUPAC_T78","span":{"begin":198,"end":204},"obj":"\"http://rdf.glycoinfo.org/glycan/G62953SQ\""},{"id":"GlycanIUPAC_T79","span":{"begin":198,"end":204},"obj":"\"http://rdf.glycoinfo.org/glycan/G70070AY\""},{"id":"GlycanIUPAC_T80","span":{"begin":198,"end":204},"obj":"\"http://rdf.glycoinfo.org/glycan/G78792WC\""},{"id":"GlycanIUPAC_T81","span":{"begin":198,"end":204},"obj":"\"http://rdf.glycoinfo.org/glycan/G25238AV\""},{"id":"GlycanIUPAC_T82","span":{"begin":198,"end":204},"obj":"\"http://rdf.glycoinfo.org/glycan/G40510DP\""},{"id":"GlycanIUPAC_T83","span":{"begin":198,"end":204},"obj":"\"http://rdf.glycoinfo.org/glycan/G61120TK\""},{"id":"GlycanIUPAC_T84","span":{"begin":198,"end":204},"obj":"\"http://rdf.glycoinfo.org/glycan/G41342KV\""},{"id":"GlycanIUPAC_T85","span":{"begin":198,"end":204},"obj":"\"http://rdf.glycoinfo.org/glycan/G90703NA\""},{"id":"GlycanIUPAC_T86","span":{"begin":198,"end":204},"obj":"\"http://rdf.glycoinfo.org/glycan/G01591HR\""},{"id":"GlycanIUPAC_T87","span":{"begin":198,"end":204},"obj":"\"http://rdf.glycoinfo.org/glycan/G56520XN\""},{"id":"GlycanIUPAC_T88","span":{"begin":198,"end":204},"obj":"\"http://rdf.glycoinfo.org/glycan/G81830JX\""}],"text":"Multivalent sialyl-LeX: potent inhibitors of E-selectin-mediated cell adhesion; reagent for staining activated endothelial cells.\nFree, monovalent, SLeX (Neu5Ac alpha 2-3Gal beta 1-4(Fuc alpha 1-3)-GlcNAc), SLn (Neu5Ac alpha 2-3Gal beta 1-4GlcNAc) and corresponding BSA-conjugated forms--displaying different ratios of SLeX and SLn to protein--were tested for their ability to inhibit binding of HL-60 cells to immobilized E-selectin. Free SLeX and conjugated SLeX-BSA inhibited cell binding in a dose-dependent manner. SLn and SLn-BSA did not inhibit binding. SLeX16BSA (16 mol tetrasaccharide/mol BSA) and monovalent SLeX inhibited cell binding with measured inhibitory concentrations (IC50S) of 1 microM and 1 mM, respectively, demonstrating a three-order-of-magnitude enhancement of inhibitory activity with the multivalent form of SLeX. A SLex7BSA conjugate was 10-fold less potent than those with 11 or 16 mol SLeX/mol BSA. An assay which measured neutrophil rolling on interleukin (IL)-1 beta-activated human umbilical vein endothelial cells (HUVECs) showed 50% reduction in the number of rolling neutrophils in the presence of 1 microM SLeX16BSA, whereas the level of free, monovalent SLeX oligosaccharide required to produce the same effect was approximately 0.3 mM. SLeX-BSA was found to be an excellent reagent for staining endothelial cells expressing E-selectin. Biotinylated SLeX-BSA in conjunction with Texas red avidin-stained lipopolysaccharide (LPS)-activated HUVECs, and co-incubation of activated cells with anti-E-selectin, specifically blocked staining. The distribution of E-selectin, as determined by binding of SLeX-BSA, was virtually identical with that obtained by binding of anti-E-selectin antibody.(ABSTRACT TRUNCATED AT 250 WORDS)"}

{"project":"GlycoBiology-Motifs","denotations":[{"id":"T1","span":{"begin":19,"end":22},"obj":"http://rdf.glycoinfo.org/glycan/G00051MO"},{"id":"T2","span":{"begin":148,"end":152},"obj":"http://rdf.glycoinfo.org/glycan/G00054MO"},{"id":"T3","span":{"begin":319,"end":323},"obj":"http://rdf.glycoinfo.org/glycan/G00054MO"},{"id":"T4","span":{"begin":440,"end":444},"obj":"http://rdf.glycoinfo.org/glycan/G00054MO"},{"id":"T5","span":{"begin":460,"end":464},"obj":"http://rdf.glycoinfo.org/glycan/G00054MO"},{"id":"T6","span":{"begin":619,"end":623},"obj":"http://rdf.glycoinfo.org/glycan/G00054MO"},{"id":"T7","span":{"begin":836,"end":840},"obj":"http://rdf.glycoinfo.org/glycan/G00054MO"},{"id":"T8","span":{"begin":916,"end":920},"obj":"http://rdf.glycoinfo.org/glycan/G00054MO"},{"id":"T9","span":{"begin":1193,"end":1197},"obj":"http://rdf.glycoinfo.org/glycan/G00054MO"},{"id":"T10","span":{"begin":1276,"end":1280},"obj":"http://rdf.glycoinfo.org/glycan/G00054MO"},{"id":"T11","span":{"begin":1389,"end":1393},"obj":"http://rdf.glycoinfo.org/glycan/G00054MO"},{"id":"T12","span":{"begin":1636,"end":1640},"obj":"http://rdf.glycoinfo.org/glycan/G00054MO"},{"id":"T13","span":{"begin":1463,"end":1466},"obj":"http://rdf.glycoinfo.org/glycan/G00022MO"}],"text":"Multivalent sialyl-LeX: potent inhibitors of E-selectin-mediated cell adhesion; reagent for staining activated endothelial cells.\nFree, monovalent, SLeX (Neu5Ac alpha 2-3Gal beta 1-4(Fuc alpha 1-3)-GlcNAc), SLn (Neu5Ac alpha 2-3Gal beta 1-4GlcNAc) and corresponding BSA-conjugated forms--displaying different ratios of SLeX and SLn to protein--were tested for their ability to inhibit binding of HL-60 cells to immobilized E-selectin. Free SLeX and conjugated SLeX-BSA inhibited cell binding in a dose-dependent manner. SLn and SLn-BSA did not inhibit binding. SLeX16BSA (16 mol tetrasaccharide/mol BSA) and monovalent SLeX inhibited cell binding with measured inhibitory concentrations (IC50S) of 1 microM and 1 mM, respectively, demonstrating a three-order-of-magnitude enhancement of inhibitory activity with the multivalent form of SLeX. A SLex7BSA conjugate was 10-fold less potent than those with 11 or 16 mol SLeX/mol BSA. An assay which measured neutrophil rolling on interleukin (IL)-1 beta-activated human umbilical vein endothelial cells (HUVECs) showed 50% reduction in the number of rolling neutrophils in the presence of 1 microM SLeX16BSA, whereas the level of free, monovalent SLeX oligosaccharide required to produce the same effect was approximately 0.3 mM. SLeX-BSA was found to be an excellent reagent for staining endothelial cells expressing E-selectin. Biotinylated SLeX-BSA in conjunction with Texas red avidin-stained lipopolysaccharide (LPS)-activated HUVECs, and co-incubation of activated cells with anti-E-selectin, specifically blocked staining. The distribution of E-selectin, as determined by binding of SLeX-BSA, was virtually identical with that obtained by binding of anti-E-selectin antibody.(ABSTRACT TRUNCATED AT 250 WORDS)"}

{"project":"Lectin","denotations":[{"id":"Lectin_T1","span":{"begin":47,"end":55},"obj":"https://acgg.asia/db/lfdb/LfDB0013"},{"id":"Lectin_T2","span":{"begin":425,"end":433},"obj":"https://acgg.asia/db/lfdb/LfDB0013"},{"id":"Lectin_T3","span":{"begin":1366,"end":1374},"obj":"https://acgg.asia/db/lfdb/LfDB0013"},{"id":"Lectin_T4","span":{"begin":1535,"end":1543},"obj":"https://acgg.asia/db/lfdb/LfDB0013"},{"id":"Lectin_T5","span":{"begin":1598,"end":1606},"obj":"https://acgg.asia/db/lfdb/LfDB0013"},{"id":"Lectin_T6","span":{"begin":1710,"end":1718},"obj":"https://acgg.asia/db/lfdb/LfDB0013"},{"id":"Lectin_T7","span":{"begin":45,"end":55},"obj":"https://acgg.asia/db/lfdb/LfDB0043"},{"id":"Lectin_T8","span":{"begin":423,"end":433},"obj":"https://acgg.asia/db/lfdb/LfDB0043"},{"id":"Lectin_T9","span":{"begin":1364,"end":1374},"obj":"https://acgg.asia/db/lfdb/LfDB0043"},{"id":"Lectin_T10","span":{"begin":1533,"end":1543},"obj":"https://acgg.asia/db/lfdb/LfDB0043"},{"id":"Lectin_T11","span":{"begin":1596,"end":1606},"obj":"https://acgg.asia/db/lfdb/LfDB0043"},{"id":"Lectin_T12","span":{"begin":1708,"end":1718},"obj":"https://acgg.asia/db/lfdb/LfDB0043"},{"id":"Lectin_T13","span":{"begin":47,"end":55},"obj":"https://acgg.asia/db/lfdb/LfDB0142"},{"id":"Lectin_T14","span":{"begin":425,"end":433},"obj":"https://acgg.asia/db/lfdb/LfDB0142"},{"id":"Lectin_T15","span":{"begin":1366,"end":1374},"obj":"https://acgg.asia/db/lfdb/LfDB0142"},{"id":"Lectin_T16","span":{"begin":1535,"end":1543},"obj":"https://acgg.asia/db/lfdb/LfDB0142"},{"id":"Lectin_T17","span":{"begin":1598,"end":1606},"obj":"https://acgg.asia/db/lfdb/LfDB0142"},{"id":"Lectin_T18","span":{"begin":1710,"end":1718},"obj":"https://acgg.asia/db/lfdb/LfDB0142"}],"text":"Multivalent sialyl-LeX: potent inhibitors of E-selectin-mediated cell adhesion; reagent for staining activated endothelial cells.\nFree, monovalent, SLeX (Neu5Ac alpha 2-3Gal beta 1-4(Fuc alpha 1-3)-GlcNAc), SLn (Neu5Ac alpha 2-3Gal beta 1-4GlcNAc) and corresponding BSA-conjugated forms--displaying different ratios of SLeX and SLn to protein--were tested for their ability to inhibit binding of HL-60 cells to immobilized E-selectin. Free SLeX and conjugated SLeX-BSA inhibited cell binding in a dose-dependent manner. SLn and SLn-BSA did not inhibit binding. SLeX16BSA (16 mol tetrasaccharide/mol BSA) and monovalent SLeX inhibited cell binding with measured inhibitory concentrations (IC50S) of 1 microM and 1 mM, respectively, demonstrating a three-order-of-magnitude enhancement of inhibitory activity with the multivalent form of SLeX. A SLex7BSA conjugate was 10-fold less potent than those with 11 or 16 mol SLeX/mol BSA. An assay which measured neutrophil rolling on interleukin (IL)-1 beta-activated human umbilical vein endothelial cells (HUVECs) showed 50% reduction in the number of rolling neutrophils in the presence of 1 microM SLeX16BSA, whereas the level of free, monovalent SLeX oligosaccharide required to produce the same effect was approximately 0.3 mM. SLeX-BSA was found to be an excellent reagent for staining endothelial cells expressing E-selectin. Biotinylated SLeX-BSA in conjunction with Texas red avidin-stained lipopolysaccharide (LPS)-activated HUVECs, and co-incubation of activated cells with anti-E-selectin, specifically blocked staining. The distribution of E-selectin, as determined by binding of SLeX-BSA, was virtually identical with that obtained by binding of anti-E-selectin antibody.(ABSTRACT TRUNCATED AT 250 WORDS)"}

{"project":"performance-test","denotations":[{"id":"PD-UBERON-AE-B_T1","span":{"begin":1026,"end":1030},"obj":"http://purl.obolibrary.org/obo/UBERON_0001638"},{"id":"PD-UBERON-AE-B_T2","span":{"begin":1016,"end":1030},"obj":"http://purl.obolibrary.org/obo/UBERON_0002066"},{"id":"PD-UBERON-AE-B_T3","span":{"begin":1016,"end":1042},"obj":"http://purl.obolibrary.org/obo/UBERON_0007777"}],"text":"Multivalent sialyl-LeX: potent inhibitors of E-selectin-mediated cell adhesion; reagent for staining activated endothelial cells.\nFree, monovalent, SLeX (Neu5Ac alpha 2-3Gal beta 1-4(Fuc alpha 1-3)-GlcNAc), SLn (Neu5Ac alpha 2-3Gal beta 1-4GlcNAc) and corresponding BSA-conjugated forms--displaying different ratios of SLeX and SLn to protein--were tested for their ability to inhibit binding of HL-60 cells to immobilized E-selectin. Free SLeX and conjugated SLeX-BSA inhibited cell binding in a dose-dependent manner. SLn and SLn-BSA did not inhibit binding. SLeX16BSA (16 mol tetrasaccharide/mol BSA) and monovalent SLeX inhibited cell binding with measured inhibitory concentrations (IC50S) of 1 microM and 1 mM, respectively, demonstrating a three-order-of-magnitude enhancement of inhibitory activity with the multivalent form of SLeX. A SLex7BSA conjugate was 10-fold less potent than those with 11 or 16 mol SLeX/mol BSA. An assay which measured neutrophil rolling on interleukin (IL)-1 beta-activated human umbilical vein endothelial cells (HUVECs) showed 50% reduction in the number of rolling neutrophils in the presence of 1 microM SLeX16BSA, whereas the level of free, monovalent SLeX oligosaccharide required to produce the same effect was approximately 0.3 mM. SLeX-BSA was found to be an excellent reagent for staining endothelial cells expressing E-selectin. Biotinylated SLeX-BSA in conjunction with Texas red avidin-stained lipopolysaccharide (LPS)-activated HUVECs, and co-incubation of activated cells with anti-E-selectin, specifically blocked staining. The distribution of E-selectin, as determined by binding of SLeX-BSA, was virtually identical with that obtained by binding of anti-E-selectin antibody.(ABSTRACT TRUNCATED AT 250 WORDS)"}

{"project":"Anatomy-MAT","denotations":[{"id":"T1","span":{"begin":1026,"end":1030},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000037"}],"text":"Multivalent sialyl-LeX: potent inhibitors of E-selectin-mediated cell adhesion; reagent for staining activated endothelial cells.\nFree, monovalent, SLeX (Neu5Ac alpha 2-3Gal beta 1-4(Fuc alpha 1-3)-GlcNAc), SLn (Neu5Ac alpha 2-3Gal beta 1-4GlcNAc) and corresponding BSA-conjugated forms--displaying different ratios of SLeX and SLn to protein--were tested for their ability to inhibit binding of HL-60 cells to immobilized E-selectin. Free SLeX and conjugated SLeX-BSA inhibited cell binding in a dose-dependent manner. SLn and SLn-BSA did not inhibit binding. SLeX16BSA (16 mol tetrasaccharide/mol BSA) and monovalent SLeX inhibited cell binding with measured inhibitory concentrations (IC50S) of 1 microM and 1 mM, respectively, demonstrating a three-order-of-magnitude enhancement of inhibitory activity with the multivalent form of SLeX. A SLex7BSA conjugate was 10-fold less potent than those with 11 or 16 mol SLeX/mol BSA. An assay which measured neutrophil rolling on interleukin (IL)-1 beta-activated human umbilical vein endothelial cells (HUVECs) showed 50% reduction in the number of rolling neutrophils in the presence of 1 microM SLeX16BSA, whereas the level of free, monovalent SLeX oligosaccharide required to produce the same effect was approximately 0.3 mM. SLeX-BSA was found to be an excellent reagent for staining endothelial cells expressing E-selectin. Biotinylated SLeX-BSA in conjunction with Texas red avidin-stained lipopolysaccharide (LPS)-activated HUVECs, and co-incubation of activated cells with anti-E-selectin, specifically blocked staining. The distribution of E-selectin, as determined by binding of SLeX-BSA, was virtually identical with that obtained by binding of anti-E-selectin antibody.(ABSTRACT TRUNCATED AT 250 WORDS)"}

{"project":"Glycan-GlyCosmos","denotations":[{"id":"T1","span":{"begin":154,"end":160},"obj":"Glycan"},{"id":"T2","span":{"begin":212,"end":218},"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/G76685HR"},{"id":"A4","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR"}],"text":"Multivalent sialyl-LeX: potent inhibitors of E-selectin-mediated cell adhesion; reagent for staining activated endothelial cells.\nFree, monovalent, SLeX (Neu5Ac alpha 2-3Gal beta 1-4(Fuc alpha 1-3)-GlcNAc), SLn (Neu5Ac alpha 2-3Gal beta 1-4GlcNAc) and corresponding BSA-conjugated forms--displaying different ratios of SLeX and SLn to protein--were tested for their ability to inhibit binding of HL-60 cells to immobilized E-selectin. Free SLeX and conjugated SLeX-BSA inhibited cell binding in a dose-dependent manner. SLn and SLn-BSA did not inhibit binding. SLeX16BSA (16 mol tetrasaccharide/mol BSA) and monovalent SLeX inhibited cell binding with measured inhibitory concentrations (IC50S) of 1 microM and 1 mM, respectively, demonstrating a three-order-of-magnitude enhancement of inhibitory activity with the multivalent form of SLeX. A SLex7BSA conjugate was 10-fold less potent than those with 11 or 16 mol SLeX/mol BSA. An assay which measured neutrophil rolling on interleukin (IL)-1 beta-activated human umbilical vein endothelial cells (HUVECs) showed 50% reduction in the number of rolling neutrophils in the presence of 1 microM SLeX16BSA, whereas the level of free, monovalent SLeX oligosaccharide required to produce the same effect was approximately 0.3 mM. SLeX-BSA was found to be an excellent reagent for staining endothelial cells expressing E-selectin. Biotinylated SLeX-BSA in conjunction with Texas red avidin-stained lipopolysaccharide (LPS)-activated HUVECs, and co-incubation of activated cells with anti-E-selectin, specifically blocked staining. The distribution of E-selectin, as determined by binding of SLeX-BSA, was virtually identical with that obtained by binding of anti-E-selectin antibody.(ABSTRACT TRUNCATED AT 250 WORDS)"}

{"project":"GlyCosmos15-NCBITAXON","denotations":[{"id":"T1","span":{"begin":1010,"end":1015},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9606"}],"text":"Multivalent sialyl-LeX: potent inhibitors of E-selectin-mediated cell adhesion; reagent for staining activated endothelial cells.\nFree, monovalent, SLeX (Neu5Ac alpha 2-3Gal beta 1-4(Fuc alpha 1-3)-GlcNAc), SLn (Neu5Ac alpha 2-3Gal beta 1-4GlcNAc) and corresponding BSA-conjugated forms--displaying different ratios of SLeX and SLn to protein--were tested for their ability to inhibit binding of HL-60 cells to immobilized E-selectin. Free SLeX and conjugated SLeX-BSA inhibited cell binding in a dose-dependent manner. SLn and SLn-BSA did not inhibit binding. SLeX16BSA (16 mol tetrasaccharide/mol BSA) and monovalent SLeX inhibited cell binding with measured inhibitory concentrations (IC50S) of 1 microM and 1 mM, respectively, demonstrating a three-order-of-magnitude enhancement of inhibitory activity with the multivalent form of SLeX. A SLex7BSA conjugate was 10-fold less potent than those with 11 or 16 mol SLeX/mol BSA. An assay which measured neutrophil rolling on interleukin (IL)-1 beta-activated human umbilical vein endothelial cells (HUVECs) showed 50% reduction in the number of rolling neutrophils in the presence of 1 microM SLeX16BSA, whereas the level of free, monovalent SLeX oligosaccharide required to produce the same effect was approximately 0.3 mM. SLeX-BSA was found to be an excellent reagent for staining endothelial cells expressing E-selectin. Biotinylated SLeX-BSA in conjunction with Texas red avidin-stained lipopolysaccharide (LPS)-activated HUVECs, and co-incubation of activated cells with anti-E-selectin, specifically blocked staining. The distribution of E-selectin, as determined by binding of SLeX-BSA, was virtually identical with that obtained by binding of anti-E-selectin antibody.(ABSTRACT TRUNCATED AT 250 WORDS)"}

{"project":"GlyCosmos15-CL","denotations":[{"id":"T1","span":{"begin":111,"end":128},"obj":"Cell"},{"id":"T2","span":{"begin":954,"end":964},"obj":"Cell"},{"id":"T3","span":{"begin":1026,"end":1048},"obj":"Cell"},{"id":"T4","span":{"begin":1104,"end":1115},"obj":"Cell"},{"id":"T5","span":{"begin":1335,"end":1352},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000115"},{"id":"A2","pred":"cl_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL:0000775"},{"id":"A3","pred":"cl_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CL:0002543"},{"id":"A4","pred":"cl_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/CL:0000775"},{"id":"A5","pred":"cl_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/CL:0000115"}],"text":"Multivalent sialyl-LeX: potent inhibitors of E-selectin-mediated cell adhesion; reagent for staining activated endothelial cells.\nFree, monovalent, SLeX (Neu5Ac alpha 2-3Gal beta 1-4(Fuc alpha 1-3)-GlcNAc), SLn (Neu5Ac alpha 2-3Gal beta 1-4GlcNAc) and corresponding BSA-conjugated forms--displaying different ratios of SLeX and SLn to protein--were tested for their ability to inhibit binding of HL-60 cells to immobilized E-selectin. Free SLeX and conjugated SLeX-BSA inhibited cell binding in a dose-dependent manner. SLn and SLn-BSA did not inhibit binding. SLeX16BSA (16 mol tetrasaccharide/mol BSA) and monovalent SLeX inhibited cell binding with measured inhibitory concentrations (IC50S) of 1 microM and 1 mM, respectively, demonstrating a three-order-of-magnitude enhancement of inhibitory activity with the multivalent form of SLeX. A SLex7BSA conjugate was 10-fold less potent than those with 11 or 16 mol SLeX/mol BSA. An assay which measured neutrophil rolling on interleukin (IL)-1 beta-activated human umbilical vein endothelial cells (HUVECs) showed 50% reduction in the number of rolling neutrophils in the presence of 1 microM SLeX16BSA, whereas the level of free, monovalent SLeX oligosaccharide required to produce the same effect was approximately 0.3 mM. SLeX-BSA was found to be an excellent reagent for staining endothelial cells expressing E-selectin. Biotinylated SLeX-BSA in conjunction with Texas red avidin-stained lipopolysaccharide (LPS)-activated HUVECs, and co-incubation of activated cells with anti-E-selectin, specifically blocked staining. The distribution of E-selectin, as determined by binding of SLeX-BSA, was virtually identical with that obtained by binding of anti-E-selectin antibody.(ABSTRACT TRUNCATED AT 250 WORDS)"}

{"project":"GlyCosmos15-UBERON","denotations":[{"id":"T1","span":{"begin":111,"end":128},"obj":"Body_part"},{"id":"T2","span":{"begin":954,"end":964},"obj":"Body_part"},{"id":"T3","span":{"begin":1016,"end":1030},"obj":"Body_part"},{"id":"T4","span":{"begin":1031,"end":1048},"obj":"Body_part"},{"id":"T5","span":{"begin":1104,"end":1115},"obj":"Body_part"},{"id":"T6","span":{"begin":1335,"end":1352},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL_0000115"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL_0000775"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/UBERON_0002066"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/CL_0000115"},{"id":"A5","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/CL_0000775"},{"id":"A6","pred":"uberon_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/CL_0000115"}],"text":"Multivalent sialyl-LeX: potent inhibitors of E-selectin-mediated cell adhesion; reagent for staining activated endothelial cells.\nFree, monovalent, SLeX (Neu5Ac alpha 2-3Gal beta 1-4(Fuc alpha 1-3)-GlcNAc), SLn (Neu5Ac alpha 2-3Gal beta 1-4GlcNAc) and corresponding BSA-conjugated forms--displaying different ratios of SLeX and SLn to protein--were tested for their ability to inhibit binding of HL-60 cells to immobilized E-selectin. Free SLeX and conjugated SLeX-BSA inhibited cell binding in a dose-dependent manner. SLn and SLn-BSA did not inhibit binding. SLeX16BSA (16 mol tetrasaccharide/mol BSA) and monovalent SLeX inhibited cell binding with measured inhibitory concentrations (IC50S) of 1 microM and 1 mM, respectively, demonstrating a three-order-of-magnitude enhancement of inhibitory activity with the multivalent form of SLeX. A SLex7BSA conjugate was 10-fold less potent than those with 11 or 16 mol SLeX/mol BSA. An assay which measured neutrophil rolling on interleukin (IL)-1 beta-activated human umbilical vein endothelial cells (HUVECs) showed 50% reduction in the number of rolling neutrophils in the presence of 1 microM SLeX16BSA, whereas the level of free, monovalent SLeX oligosaccharide required to produce the same effect was approximately 0.3 mM. SLeX-BSA was found to be an excellent reagent for staining endothelial cells expressing E-selectin. Biotinylated SLeX-BSA in conjunction with Texas red avidin-stained lipopolysaccharide (LPS)-activated HUVECs, and co-incubation of activated cells with anti-E-selectin, specifically blocked staining. The distribution of E-selectin, as determined by binding of SLeX-BSA, was virtually identical with that obtained by binding of anti-E-selectin antibody.(ABSTRACT TRUNCATED AT 250 WORDS)"}

{"project":"GlyCosmos15-MAT","denotations":[{"id":"T1","span":{"begin":1026,"end":1030},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000037"}],"text":"Multivalent sialyl-LeX: potent inhibitors of E-selectin-mediated cell adhesion; reagent for staining activated endothelial cells.\nFree, monovalent, SLeX (Neu5Ac alpha 2-3Gal beta 1-4(Fuc alpha 1-3)-GlcNAc), SLn (Neu5Ac alpha 2-3Gal beta 1-4GlcNAc) and corresponding BSA-conjugated forms--displaying different ratios of SLeX and SLn to protein--were tested for their ability to inhibit binding of HL-60 cells to immobilized E-selectin. Free SLeX and conjugated SLeX-BSA inhibited cell binding in a dose-dependent manner. SLn and SLn-BSA did not inhibit binding. SLeX16BSA (16 mol tetrasaccharide/mol BSA) and monovalent SLeX inhibited cell binding with measured inhibitory concentrations (IC50S) of 1 microM and 1 mM, respectively, demonstrating a three-order-of-magnitude enhancement of inhibitory activity with the multivalent form of SLeX. A SLex7BSA conjugate was 10-fold less potent than those with 11 or 16 mol SLeX/mol BSA. An assay which measured neutrophil rolling on interleukin (IL)-1 beta-activated human umbilical vein endothelial cells (HUVECs) showed 50% reduction in the number of rolling neutrophils in the presence of 1 microM SLeX16BSA, whereas the level of free, monovalent SLeX oligosaccharide required to produce the same effect was approximately 0.3 mM. SLeX-BSA was found to be an excellent reagent for staining endothelial cells expressing E-selectin. Biotinylated SLeX-BSA in conjunction with Texas red avidin-stained lipopolysaccharide (LPS)-activated HUVECs, and co-incubation of activated cells with anti-E-selectin, specifically blocked staining. The distribution of E-selectin, as determined by binding of SLeX-BSA, was virtually identical with that obtained by binding of anti-E-selectin antibody.(ABSTRACT TRUNCATED AT 250 WORDS)"}

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":129},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":130,"end":434},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":435,"end":519},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":520,"end":560},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":561,"end":841},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":842,"end":929},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":930,"end":1275},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":1276,"end":1375},"obj":"Sentence"},{"id":"TextSentencer_T9","span":{"begin":1376,"end":1575},"obj":"Sentence"},{"id":"TextSentencer_T10","span":{"begin":1576,"end":1761},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":129},"obj":"Sentence"},{"id":"T2","span":{"begin":130,"end":434},"obj":"Sentence"},{"id":"T3","span":{"begin":435,"end":519},"obj":"Sentence"},{"id":"T4","span":{"begin":520,"end":560},"obj":"Sentence"},{"id":"T5","span":{"begin":561,"end":841},"obj":"Sentence"},{"id":"T6","span":{"begin":842,"end":929},"obj":"Sentence"},{"id":"T7","span":{"begin":930,"end":1275},"obj":"Sentence"},{"id":"T8","span":{"begin":1276,"end":1375},"obj":"Sentence"},{"id":"T9","span":{"begin":1376,"end":1575},"obj":"Sentence"},{"id":"T10","span":{"begin":1576,"end":1761},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":129},"obj":"Sentence"},{"id":"T2","span":{"begin":130,"end":434},"obj":"Sentence"},{"id":"T3","span":{"begin":435,"end":519},"obj":"Sentence"},{"id":"T4","span":{"begin":520,"end":560},"obj":"Sentence"},{"id":"T5","span":{"begin":561,"end":841},"obj":"Sentence"},{"id":"T6","span":{"begin":842,"end":929},"obj":"Sentence"},{"id":"T7","span":{"begin":930,"end":1275},"obj":"Sentence"},{"id":"T8","span":{"begin":1276,"end":1375},"obj":"Sentence"},{"id":"T9","span":{"begin":1376,"end":1575},"obj":"Sentence"},{"id":"T10","span":{"begin":1576,"end":1761},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Multivalent sialyl-LeX: potent inhibitors of E-selectin-mediated cell adhesion; reagent for staining activated endothelial cells.\nFree, monovalent, SLeX (Neu5Ac alpha 2-3Gal beta 1-4(Fuc alpha 1-3)-GlcNAc), SLn (Neu5Ac alpha 2-3Gal beta 1-4GlcNAc) and corresponding BSA-conjugated forms--displaying different ratios of SLeX and SLn to protein--were tested for their ability to inhibit binding of HL-60 cells to immobilized E-selectin. Free SLeX and conjugated SLeX-BSA inhibited cell binding in a dose-dependent manner. SLn and SLn-BSA did not inhibit binding. SLeX16BSA (16 mol tetrasaccharide/mol BSA) and monovalent SLeX inhibited cell binding with measured inhibitory concentrations (IC50S) of 1 microM and 1 mM, respectively, demonstrating a three-order-of-magnitude enhancement of inhibitory activity with the multivalent form of SLeX. A SLex7BSA conjugate was 10-fold less potent than those with 11 or 16 mol SLeX/mol BSA. An assay which measured neutrophil rolling on interleukin (IL)-1 beta-activated human umbilical vein endothelial cells (HUVECs) showed 50% reduction in the number of rolling neutrophils in the presence of 1 microM SLeX16BSA, whereas the level of free, monovalent SLeX oligosaccharide required to produce the same effect was approximately 0.3 mM. SLeX-BSA was found to be an excellent reagent for staining endothelial cells expressing E-selectin. Biotinylated SLeX-BSA in conjunction with Texas red avidin-stained lipopolysaccharide (LPS)-activated HUVECs, and co-incubation of activated cells with anti-E-selectin, specifically blocked staining. The distribution of E-selectin, as determined by binding of SLeX-BSA, was virtually identical with that obtained by binding of anti-E-selectin antibody.(ABSTRACT TRUNCATED AT 250 WORDS)"}

{"project":"GlyCosmos15-Sentences","blocks":[{"id":"T1","span":{"begin":0,"end":129},"obj":"Sentence"},{"id":"T2","span":{"begin":130,"end":434},"obj":"Sentence"},{"id":"T3","span":{"begin":435,"end":519},"obj":"Sentence"},{"id":"T4","span":{"begin":520,"end":560},"obj":"Sentence"},{"id":"T5","span":{"begin":561,"end":841},"obj":"Sentence"},{"id":"T6","span":{"begin":842,"end":929},"obj":"Sentence"},{"id":"T7","span":{"begin":930,"end":1275},"obj":"Sentence"},{"id":"T8","span":{"begin":1276,"end":1375},"obj":"Sentence"},{"id":"T9","span":{"begin":1376,"end":1575},"obj":"Sentence"},{"id":"T10","span":{"begin":1576,"end":1761},"obj":"Sentence"}],"text":"Multivalent sialyl-LeX: potent inhibitors of E-selectin-mediated cell adhesion; reagent for staining activated endothelial cells.\nFree, monovalent, SLeX (Neu5Ac alpha 2-3Gal beta 1-4(Fuc alpha 1-3)-GlcNAc), SLn (Neu5Ac alpha 2-3Gal beta 1-4GlcNAc) and corresponding BSA-conjugated forms--displaying different ratios of SLeX and SLn to protein--were tested for their ability to inhibit binding of HL-60 cells to immobilized E-selectin. Free SLeX and conjugated SLeX-BSA inhibited cell binding in a dose-dependent manner. SLn and SLn-BSA did not inhibit binding. SLeX16BSA (16 mol tetrasaccharide/mol BSA) and monovalent SLeX inhibited cell binding with measured inhibitory concentrations (IC50S) of 1 microM and 1 mM, respectively, demonstrating a three-order-of-magnitude enhancement of inhibitory activity with the multivalent form of SLeX. A SLex7BSA conjugate was 10-fold less potent than those with 11 or 16 mol SLeX/mol BSA. An assay which measured neutrophil rolling on interleukin (IL)-1 beta-activated human umbilical vein endothelial cells (HUVECs) showed 50% reduction in the number of rolling neutrophils in the presence of 1 microM SLeX16BSA, whereas the level of free, monovalent SLeX oligosaccharide required to produce the same effect was approximately 0.3 mM. SLeX-BSA was found to be an excellent reagent for staining endothelial cells expressing E-selectin. Biotinylated SLeX-BSA in conjunction with Texas red avidin-stained lipopolysaccharide (LPS)-activated HUVECs, and co-incubation of activated cells with anti-E-selectin, specifically blocked staining. The distribution of E-selectin, as determined by binding of SLeX-BSA, was virtually identical with that obtained by binding of anti-E-selectin antibody.(ABSTRACT TRUNCATED AT 250 WORDS)"}

{"project":"GlyCosmos15-Glycan","denotations":[{"id":"T1","span":{"begin":154,"end":160},"obj":"Glycan"},{"id":"T2","span":{"begin":212,"end":218},"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/G76685HR"},{"id":"A4","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR"}],"text":"Multivalent sialyl-LeX: potent inhibitors of E-selectin-mediated cell adhesion; reagent for staining activated endothelial cells.\nFree, monovalent, SLeX (Neu5Ac alpha 2-3Gal beta 1-4(Fuc alpha 1-3)-GlcNAc), SLn (Neu5Ac alpha 2-3Gal beta 1-4GlcNAc) and corresponding BSA-conjugated forms--displaying different ratios of SLeX and SLn to protein--were tested for their ability to inhibit binding of HL-60 cells to immobilized E-selectin. Free SLeX and conjugated SLeX-BSA inhibited cell binding in a dose-dependent manner. SLn and SLn-BSA did not inhibit binding. SLeX16BSA (16 mol tetrasaccharide/mol BSA) and monovalent SLeX inhibited cell binding with measured inhibitory concentrations (IC50S) of 1 microM and 1 mM, respectively, demonstrating a three-order-of-magnitude enhancement of inhibitory activity with the multivalent form of SLeX. A SLex7BSA conjugate was 10-fold less potent than those with 11 or 16 mol SLeX/mol BSA. An assay which measured neutrophil rolling on interleukin (IL)-1 beta-activated human umbilical vein endothelial cells (HUVECs) showed 50% reduction in the number of rolling neutrophils in the presence of 1 microM SLeX16BSA, whereas the level of free, monovalent SLeX oligosaccharide required to produce the same effect was approximately 0.3 mM. SLeX-BSA was found to be an excellent reagent for staining endothelial cells expressing E-selectin. Biotinylated SLeX-BSA in conjunction with Texas red avidin-stained lipopolysaccharide (LPS)-activated HUVECs, and co-incubation of activated cells with anti-E-selectin, specifically blocked staining. The distribution of E-selectin, as determined by binding of SLeX-BSA, was virtually identical with that obtained by binding of anti-E-selectin antibody.(ABSTRACT TRUNCATED AT 250 WORDS)"}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":1010,"end":1015},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9606"}],"text":"Multivalent sialyl-LeX: potent inhibitors of E-selectin-mediated cell adhesion; reagent for staining activated endothelial cells.\nFree, monovalent, SLeX (Neu5Ac alpha 2-3Gal beta 1-4(Fuc alpha 1-3)-GlcNAc), SLn (Neu5Ac alpha 2-3Gal beta 1-4GlcNAc) and corresponding BSA-conjugated forms--displaying different ratios of SLeX and SLn to protein--were tested for their ability to inhibit binding of HL-60 cells to immobilized E-selectin. Free SLeX and conjugated SLeX-BSA inhibited cell binding in a dose-dependent manner. SLn and SLn-BSA did not inhibit binding. SLeX16BSA (16 mol tetrasaccharide/mol BSA) and monovalent SLeX inhibited cell binding with measured inhibitory concentrations (IC50S) of 1 microM and 1 mM, respectively, demonstrating a three-order-of-magnitude enhancement of inhibitory activity with the multivalent form of SLeX. A SLex7BSA conjugate was 10-fold less potent than those with 11 or 16 mol SLeX/mol BSA. An assay which measured neutrophil rolling on interleukin (IL)-1 beta-activated human umbilical vein endothelial cells (HUVECs) showed 50% reduction in the number of rolling neutrophils in the presence of 1 microM SLeX16BSA, whereas the level of free, monovalent SLeX oligosaccharide required to produce the same effect was approximately 0.3 mM. SLeX-BSA was found to be an excellent reagent for staining endothelial cells expressing E-selectin. Biotinylated SLeX-BSA in conjunction with Texas red avidin-stained lipopolysaccharide (LPS)-activated HUVECs, and co-incubation of activated cells with anti-E-selectin, specifically blocked staining. The distribution of E-selectin, as determined by binding of SLeX-BSA, was virtually identical with that obtained by binding of anti-E-selectin antibody.(ABSTRACT TRUNCATED AT 250 WORDS)"}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":111,"end":128},"obj":"Body_part"},{"id":"T2","span":{"begin":954,"end":964},"obj":"Body_part"},{"id":"T3","span":{"begin":1016,"end":1030},"obj":"Body_part"},{"id":"T4","span":{"begin":1031,"end":1048},"obj":"Body_part"},{"id":"T5","span":{"begin":1104,"end":1115},"obj":"Body_part"},{"id":"T6","span":{"begin":1335,"end":1352},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL_0000115"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL_0000775"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/UBERON_0002066"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/CL_0000115"},{"id":"A5","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/CL_0000775"},{"id":"A6","pred":"uberon_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/CL_0000115"}],"text":"Multivalent sialyl-LeX: potent inhibitors of E-selectin-mediated cell adhesion; reagent for staining activated endothelial cells.\nFree, monovalent, SLeX (Neu5Ac alpha 2-3Gal beta 1-4(Fuc alpha 1-3)-GlcNAc), SLn (Neu5Ac alpha 2-3Gal beta 1-4GlcNAc) and corresponding BSA-conjugated forms--displaying different ratios of SLeX and SLn to protein--were tested for their ability to inhibit binding of HL-60 cells to immobilized E-selectin. Free SLeX and conjugated SLeX-BSA inhibited cell binding in a dose-dependent manner. SLn and SLn-BSA did not inhibit binding. SLeX16BSA (16 mol tetrasaccharide/mol BSA) and monovalent SLeX inhibited cell binding with measured inhibitory concentrations (IC50S) of 1 microM and 1 mM, respectively, demonstrating a three-order-of-magnitude enhancement of inhibitory activity with the multivalent form of SLeX. A SLex7BSA conjugate was 10-fold less potent than those with 11 or 16 mol SLeX/mol BSA. An assay which measured neutrophil rolling on interleukin (IL)-1 beta-activated human umbilical vein endothelial cells (HUVECs) showed 50% reduction in the number of rolling neutrophils in the presence of 1 microM SLeX16BSA, whereas the level of free, monovalent SLeX oligosaccharide required to produce the same effect was approximately 0.3 mM. SLeX-BSA was found to be an excellent reagent for staining endothelial cells expressing E-selectin. Biotinylated SLeX-BSA in conjunction with Texas red avidin-stained lipopolysaccharide (LPS)-activated HUVECs, and co-incubation of activated cells with anti-E-selectin, specifically blocked staining. The distribution of E-selectin, as determined by binding of SLeX-BSA, was virtually identical with that obtained by binding of anti-E-selectin antibody.(ABSTRACT TRUNCATED AT 250 WORDS)"}

{"project":"CL-cell","denotations":[{"id":"T1","span":{"begin":111,"end":128},"obj":"Cell"},{"id":"T2","span":{"begin":954,"end":964},"obj":"Cell"},{"id":"T3","span":{"begin":1026,"end":1048},"obj":"Cell"},{"id":"T4","span":{"begin":1104,"end":1115},"obj":"Cell"},{"id":"T5","span":{"begin":1335,"end":1352},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000115"},{"id":"A2","pred":"cl_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL:0000775"},{"id":"A3","pred":"cl_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CL:0002543"},{"id":"A4","pred":"cl_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/CL:0000775"},{"id":"A5","pred":"cl_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/CL:0000115"}],"text":"Multivalent sialyl-LeX: potent inhibitors of E-selectin-mediated cell adhesion; reagent for staining activated endothelial cells.\nFree, monovalent, SLeX (Neu5Ac alpha 2-3Gal beta 1-4(Fuc alpha 1-3)-GlcNAc), SLn (Neu5Ac alpha 2-3Gal beta 1-4GlcNAc) and corresponding BSA-conjugated forms--displaying different ratios of SLeX and SLn to protein--were tested for their ability to inhibit binding of HL-60 cells to immobilized E-selectin. Free SLeX and conjugated SLeX-BSA inhibited cell binding in a dose-dependent manner. SLn and SLn-BSA did not inhibit binding. SLeX16BSA (16 mol tetrasaccharide/mol BSA) and monovalent SLeX inhibited cell binding with measured inhibitory concentrations (IC50S) of 1 microM and 1 mM, respectively, demonstrating a three-order-of-magnitude enhancement of inhibitory activity with the multivalent form of SLeX. A SLex7BSA conjugate was 10-fold less potent than those with 11 or 16 mol SLeX/mol BSA. An assay which measured neutrophil rolling on interleukin (IL)-1 beta-activated human umbilical vein endothelial cells (HUVECs) showed 50% reduction in the number of rolling neutrophils in the presence of 1 microM SLeX16BSA, whereas the level of free, monovalent SLeX oligosaccharide required to produce the same effect was approximately 0.3 mM. SLeX-BSA was found to be an excellent reagent for staining endothelial cells expressing E-selectin. Biotinylated SLeX-BSA in conjunction with Texas red avidin-stained lipopolysaccharide (LPS)-activated HUVECs, and co-incubation of activated cells with anti-E-selectin, specifically blocked staining. The distribution of E-selectin, as determined by binding of SLeX-BSA, was virtually identical with that obtained by binding of anti-E-selectin antibody.(ABSTRACT TRUNCATED AT 250 WORDS)"}