PubMed:16540530 / 1450-2150 JSONTXT

{"project":"Glycan-Motif","denotations":[{"id":"T6","span":{"begin":456,"end":469},"obj":"https://glytoucan.org/Structures/Glycans/G00067MO"},{"id":"T7","span":{"begin":456,"end":469},"obj":"https://glytoucan.org/Structures/Glycans/G26934CO"},{"id":"T8","span":{"begin":456,"end":469},"obj":"https://glytoucan.org/Structures/Glycans/G41865GQ"},{"id":"T9","span":{"begin":456,"end":469},"obj":"https://glytoucan.org/Structures/Glycans/G60395SO"},{"id":"T10","span":{"begin":456,"end":469},"obj":"https://glytoucan.org/Structures/Glycans/G65112QB"},{"id":"T11","span":{"begin":665,"end":674},"obj":"https://glytoucan.org/Structures/Glycans/G65889KE"},{"id":"T12","span":{"begin":665,"end":674},"obj":"https://glytoucan.org/Structures/Glycans/G68158BT"}],"text":"It is concluded that (1) Galbeta1-3/4GlcNAc and other Galbeta1-related oligosaccharides with alpha1-3 extensions are essential for binding, their polyvalent form in cellular glycoconjugates being a key recognition force for galectin-5; (2) the combining site of galectin-5 appears to be of a shallow-groove type sufficiently large to accommodate a substituted beta-galactoside, especially with alpha-anomeric extension at the non-reducing end (e.g., human blood group B-active II and B-active IIbeta1-3L); (3) the preference within beta-anomeric positioning is Galbeta1-4 \u003e or = Galbeta1-3 \u003e Galbeta1-6; and (4) hydrophobic interactions in the vicinity of the core galactose unit can enhance binding."}

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T6","span":{"begin":456,"end":469},"obj":"Glycan_Motif"},{"id":"T11","span":{"begin":665,"end":674},"obj":"Glycan_Motif"}],"attributes":[{"id":"A6","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G65112QB"},{"id":"A7","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G60395SO"},{"id":"A8","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G41865GQ"},{"id":"A9","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G26934CO"},{"id":"A10","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00067MO"},{"id":"A11","pred":"image","subj":"T11","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G68158BT"},{"id":"A12","pred":"image","subj":"T11","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G65889KE"}],"text":"It is concluded that (1) Galbeta1-3/4GlcNAc and other Galbeta1-related oligosaccharides with alpha1-3 extensions are essential for binding, their polyvalent form in cellular glycoconjugates being a key recognition force for galectin-5; (2) the combining site of galectin-5 appears to be of a shallow-groove type sufficiently large to accommodate a substituted beta-galactoside, especially with alpha-anomeric extension at the non-reducing end (e.g., human blood group B-active II and B-active IIbeta1-3L); (3) the preference within beta-anomeric positioning is Galbeta1-4 \u003e or = Galbeta1-3 \u003e Galbeta1-6; and (4) hydrophobic interactions in the vicinity of the core galactose unit can enhance binding."}

{"project":"Glycosmos6-MAT","denotations":[{"id":"T5","span":{"begin":456,"end":461},"obj":"http://purl.obolibrary.org/obo/MAT_0000083"},{"id":"T6","span":{"begin":456,"end":461},"obj":"http://purl.obolibrary.org/obo/MAT_0000315"}],"text":"It is concluded that (1) Galbeta1-3/4GlcNAc and other Galbeta1-related oligosaccharides with alpha1-3 extensions are essential for binding, their polyvalent form in cellular glycoconjugates being a key recognition force for galectin-5; (2) the combining site of galectin-5 appears to be of a shallow-groove type sufficiently large to accommodate a substituted beta-galactoside, especially with alpha-anomeric extension at the non-reducing end (e.g., human blood group B-active II and B-active IIbeta1-3L); (3) the preference within beta-anomeric positioning is Galbeta1-4 \u003e or = Galbeta1-3 \u003e Galbeta1-6; and (4) hydrophobic interactions in the vicinity of the core galactose unit can enhance binding."}

{"project":"sentences","denotations":[{"id":"TextSentencer_T10","span":{"begin":0,"end":700},"obj":"Sentence"},{"id":"T10","span":{"begin":0,"end":700},"obj":"Sentence"},{"id":"T10","span":{"begin":0,"end":700},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"It is concluded that (1) Galbeta1-3/4GlcNAc and other Galbeta1-related oligosaccharides with alpha1-3 extensions are essential for binding, their polyvalent form in cellular glycoconjugates being a key recognition force for galectin-5; (2) the combining site of galectin-5 appears to be of a shallow-groove type sufficiently large to accommodate a substituted beta-galactoside, especially with alpha-anomeric extension at the non-reducing end (e.g., human blood group B-active II and B-active IIbeta1-3L); (3) the preference within beta-anomeric positioning is Galbeta1-4 \u003e or = Galbeta1-3 \u003e Galbeta1-6; and (4) hydrophobic interactions in the vicinity of the core galactose unit can enhance binding."}

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T6","span":{"begin":456,"end":469},"obj":"https://glytoucan.org/Structures/Glycans/G00067MO"},{"id":"T7","span":{"begin":456,"end":469},"obj":"https://glytoucan.org/Structures/Glycans/G26934CO"},{"id":"T8","span":{"begin":456,"end":469},"obj":"https://glytoucan.org/Structures/Glycans/G41865GQ"},{"id":"T9","span":{"begin":456,"end":469},"obj":"https://glytoucan.org/Structures/Glycans/G60395SO"},{"id":"T10","span":{"begin":456,"end":469},"obj":"https://glytoucan.org/Structures/Glycans/G65112QB"},{"id":"T11","span":{"begin":665,"end":674},"obj":"https://glytoucan.org/Structures/Glycans/G65889KE"},{"id":"T12","span":{"begin":665,"end":674},"obj":"https://glytoucan.org/Structures/Glycans/G68158BT"}],"text":"It is concluded that (1) Galbeta1-3/4GlcNAc and other Galbeta1-related oligosaccharides with alpha1-3 extensions are essential for binding, their polyvalent form in cellular glycoconjugates being a key recognition force for galectin-5; (2) the combining site of galectin-5 appears to be of a shallow-groove type sufficiently large to accommodate a substituted beta-galactoside, especially with alpha-anomeric extension at the non-reducing end (e.g., human blood group B-active II and B-active IIbeta1-3L); (3) the preference within beta-anomeric positioning is Galbeta1-4 \u003e or = Galbeta1-3 \u003e Galbeta1-6; and (4) hydrophobic interactions in the vicinity of the core galactose unit can enhance binding."}

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T4","span":{"begin":63,"end":70},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/353209"},{"id":"T5","span":{"begin":360,"end":364},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"},{"id":"T6","span":{"begin":360,"end":364},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T7","span":{"begin":426,"end":429},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/604139"},{"id":"T8","span":{"begin":462,"end":467},"obj":"http://purl.bioontology.org/ontology/STY/T096"},{"id":"T9","span":{"begin":532,"end":536},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"},{"id":"T10","span":{"begin":532,"end":536},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"}],"text":"It is concluded that (1) Galbeta1-3/4GlcNAc and other Galbeta1-related oligosaccharides with alpha1-3 extensions are essential for binding, their polyvalent form in cellular glycoconjugates being a key recognition force for galectin-5; (2) the combining site of galectin-5 appears to be of a shallow-groove type sufficiently large to accommodate a substituted beta-galactoside, especially with alpha-anomeric extension at the non-reducing end (e.g., human blood group B-active II and B-active IIbeta1-3L); (3) the preference within beta-anomeric positioning is Galbeta1-4 \u003e or = Galbeta1-3 \u003e Galbeta1-6; and (4) hydrophobic interactions in the vicinity of the core galactose unit can enhance binding."}

{"project":"GO-BP","denotations":[{"id":"T5","span":{"begin":468,"end":476},"obj":"http://purl.obolibrary.org/obo/GO_0004066"},{"id":"T6","span":{"begin":484,"end":492},"obj":"http://purl.obolibrary.org/obo/GO_0004066"},{"id":"T7","span":{"begin":165,"end":173},"obj":"http://purl.obolibrary.org/obo/GO_0007349"}],"text":"It is concluded that (1) Galbeta1-3/4GlcNAc and other Galbeta1-related oligosaccharides with alpha1-3 extensions are essential for binding, their polyvalent form in cellular glycoconjugates being a key recognition force for galectin-5; (2) the combining site of galectin-5 appears to be of a shallow-groove type sufficiently large to accommodate a substituted beta-galactoside, especially with alpha-anomeric extension at the non-reducing end (e.g., human blood group B-active II and B-active IIbeta1-3L); (3) the preference within beta-anomeric positioning is Galbeta1-4 \u003e or = Galbeta1-3 \u003e Galbeta1-6; and (4) hydrophobic interactions in the vicinity of the core galactose unit can enhance binding."}

{"project":"GO-MF","denotations":[{"id":"T4","span":{"begin":131,"end":138},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T5","span":{"begin":692,"end":699},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T7","span":{"begin":131,"end":138},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T8","span":{"begin":692,"end":699},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T10","span":{"begin":131,"end":138},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T11","span":{"begin":692,"end":699},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T13","span":{"begin":131,"end":138},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T14","span":{"begin":692,"end":699},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T15","span":{"begin":684,"end":699},"obj":"http://purl.obolibrary.org/obo/GO_0035326"}],"text":"It is concluded that (1) Galbeta1-3/4GlcNAc and other Galbeta1-related oligosaccharides with alpha1-3 extensions are essential for binding, their polyvalent form in cellular glycoconjugates being a key recognition force for galectin-5; (2) the combining site of galectin-5 appears to be of a shallow-groove type sufficiently large to accommodate a substituted beta-galactoside, especially with alpha-anomeric extension at the non-reducing end (e.g., human blood group B-active II and B-active IIbeta1-3L); (3) the preference within beta-anomeric positioning is Galbeta1-4 \u003e or = Galbeta1-3 \u003e Galbeta1-6; and (4) hydrophobic interactions in the vicinity of the core galactose unit can enhance binding."}

{"project":"GO-CC","denotations":[{"id":"T4","span":{"begin":300,"end":306},"obj":"http://purl.obolibrary.org/obo/GO_0097610"},{"id":"T5","span":{"begin":660,"end":664},"obj":"http://purl.obolibrary.org/obo/GO_0019013"}],"text":"It is concluded that (1) Galbeta1-3/4GlcNAc and other Galbeta1-related oligosaccharides with alpha1-3 extensions are essential for binding, their polyvalent form in cellular glycoconjugates being a key recognition force for galectin-5; (2) the combining site of galectin-5 appears to be of a shallow-groove type sufficiently large to accommodate a substituted beta-galactoside, especially with alpha-anomeric extension at the non-reducing end (e.g., human blood group B-active II and B-active IIbeta1-3L); (3) the preference within beta-anomeric positioning is Galbeta1-4 \u003e or = Galbeta1-3 \u003e Galbeta1-6; and (4) hydrophobic interactions in the vicinity of the core galactose unit can enhance binding."}

{"project":"UBERON-AE","denotations":[{"id":"T4","span":{"begin":456,"end":461},"obj":"http://purl.obolibrary.org/obo/UBERON_0000178"},{"id":"T5","span":{"begin":102,"end":112},"obj":"http://purl.obolibrary.org/obo/UBERON_2000106"},{"id":"T6","span":{"begin":409,"end":418},"obj":"http://purl.obolibrary.org/obo/UBERON_2000106"}],"text":"It is concluded that (1) Galbeta1-3/4GlcNAc and other Galbeta1-related oligosaccharides with alpha1-3 extensions are essential for binding, their polyvalent form in cellular glycoconjugates being a key recognition force for galectin-5; (2) the combining site of galectin-5 appears to be of a shallow-groove type sufficiently large to accommodate a substituted beta-galactoside, especially with alpha-anomeric extension at the non-reducing end (e.g., human blood group B-active II and B-active IIbeta1-3L); (3) the preference within beta-anomeric positioning is Galbeta1-4 \u003e or = Galbeta1-3 \u003e Galbeta1-6; and (4) hydrophobic interactions in the vicinity of the core galactose unit can enhance binding."}

{"project":"GlycoBiology-MAT","denotations":[{"id":"T5","span":{"begin":456,"end":461},"obj":"http://purl.obolibrary.org/obo/MAT_0000315"},{"id":"T6","span":{"begin":456,"end":461},"obj":"http://purl.obolibrary.org/obo/MAT_0000083"}],"text":"It is concluded that (1) Galbeta1-3/4GlcNAc and other Galbeta1-related oligosaccharides with alpha1-3 extensions are essential for binding, their polyvalent form in cellular glycoconjugates being a key recognition force for galectin-5; (2) the combining site of galectin-5 appears to be of a shallow-groove type sufficiently large to accommodate a substituted beta-galactoside, especially with alpha-anomeric extension at the non-reducing end (e.g., human blood group B-active II and B-active IIbeta1-3L); (3) the preference within beta-anomeric positioning is Galbeta1-4 \u003e or = Galbeta1-3 \u003e Galbeta1-6; and (4) hydrophobic interactions in the vicinity of the core galactose unit can enhance binding."}

{"project":"GlycoBiology-Motifs","denotations":[{"id":"T4","span":{"begin":456,"end":467},"obj":"http://rdf.glycoinfo.org/glycan/G00066MO"},{"id":"T8","span":{"begin":456,"end":469},"obj":"http://rdf.glycoinfo.org/glycan/G00067MO"}],"text":"It is concluded that (1) Galbeta1-3/4GlcNAc and other Galbeta1-related oligosaccharides with alpha1-3 extensions are essential for binding, their polyvalent form in cellular glycoconjugates being a key recognition force for galectin-5; (2) the combining site of galectin-5 appears to be of a shallow-groove type sufficiently large to accommodate a substituted beta-galactoside, especially with alpha-anomeric extension at the non-reducing end (e.g., human blood group B-active II and B-active IIbeta1-3L); (3) the preference within beta-anomeric positioning is Galbeta1-4 \u003e or = Galbeta1-3 \u003e Galbeta1-6; and (4) hydrophobic interactions in the vicinity of the core galactose unit can enhance binding."}

{"project":"GlyTouCan-IUPAC","denotations":[{"id":"GlycanIUPAC_T617","span":{"begin":426,"end":429},"obj":"\"http://rdf.glycoinfo.org/glycan/G02780QX\""},{"id":"GlycanIUPAC_T618","span":{"begin":426,"end":429},"obj":"\"http://rdf.glycoinfo.org/glycan/G18425DX\""},{"id":"GlycanIUPAC_T619","span":{"begin":426,"end":429},"obj":"\"http://rdf.glycoinfo.org/glycan/G18630JE\""},{"id":"GlycanIUPAC_T620","span":{"begin":426,"end":429},"obj":"\"http://rdf.glycoinfo.org/glycan/G01004IT\""},{"id":"GlycanIUPAC_T621","span":{"begin":426,"end":429},"obj":"\"http://rdf.glycoinfo.org/glycan/G87301QZ\""},{"id":"GlycanIUPAC_T622","span":{"begin":426,"end":429},"obj":"\"http://rdf.glycoinfo.org/glycan/G39790GW\""},{"id":"GlycanIUPAC_T623","span":{"begin":426,"end":429},"obj":"\"http://rdf.glycoinfo.org/glycan/G42928BB\""},{"id":"GlycanIUPAC_T624","span":{"begin":426,"end":429},"obj":"\"http://rdf.glycoinfo.org/glycan/G51134HC\""},{"id":"GlycanIUPAC_T625","span":{"begin":426,"end":429},"obj":"\"http://rdf.glycoinfo.org/glycan/G68183GR\""},{"id":"GlycanIUPAC_T626","span":{"begin":426,"end":429},"obj":"\"http://rdf.glycoinfo.org/glycan/G46883FA\""},{"id":"GlycanIUPAC_T627","span":{"begin":426,"end":429},"obj":"\"http://rdf.glycoinfo.org/glycan/G54702VY\""}],"text":"It is concluded that (1) Galbeta1-3/4GlcNAc and other Galbeta1-related oligosaccharides with alpha1-3 extensions are essential for binding, their polyvalent form in cellular glycoconjugates being a key recognition force for galectin-5; (2) the combining site of galectin-5 appears to be of a shallow-groove type sufficiently large to accommodate a substituted beta-galactoside, especially with alpha-anomeric extension at the non-reducing end (e.g., human blood group B-active II and B-active IIbeta1-3L); (3) the preference within beta-anomeric positioning is Galbeta1-4 \u003e or = Galbeta1-3 \u003e Galbeta1-6; and (4) hydrophobic interactions in the vicinity of the core galactose unit can enhance binding."}

{"project":"performance-test","denotations":[{"id":"PD-UBERON-AE-B_T4","span":{"begin":456,"end":461},"obj":"http://purl.obolibrary.org/obo/UBERON_0000178"},{"id":"PD-UBERON-AE-B_T5","span":{"begin":102,"end":112},"obj":"http://purl.obolibrary.org/obo/UBERON_2000106"},{"id":"PD-UBERON-AE-B_T6","span":{"begin":409,"end":418},"obj":"http://purl.obolibrary.org/obo/UBERON_2000106"}],"text":"It is concluded that (1) Galbeta1-3/4GlcNAc and other Galbeta1-related oligosaccharides with alpha1-3 extensions are essential for binding, their polyvalent form in cellular glycoconjugates being a key recognition force for galectin-5; (2) the combining site of galectin-5 appears to be of a shallow-groove type sufficiently large to accommodate a substituted beta-galactoside, especially with alpha-anomeric extension at the non-reducing end (e.g., human blood group B-active II and B-active IIbeta1-3L); (3) the preference within beta-anomeric positioning is Galbeta1-4 \u003e or = Galbeta1-3 \u003e Galbeta1-6; and (4) hydrophobic interactions in the vicinity of the core galactose unit can enhance binding."}

{"project":"Anatomy-MAT","denotations":[{"id":"T5","span":{"begin":456,"end":461},"obj":"Body_part"}],"attributes":[{"id":"A5","pred":"mat_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/MAT_0000083"},{"id":"A6","pred":"mat_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/MAT_0000315"}],"text":"It is concluded that (1) Galbeta1-3/4GlcNAc and other Galbeta1-related oligosaccharides with alpha1-3 extensions are essential for binding, their polyvalent form in cellular glycoconjugates being a key recognition force for galectin-5; (2) the combining site of galectin-5 appears to be of a shallow-groove type sufficiently large to accommodate a substituted beta-galactoside, especially with alpha-anomeric extension at the non-reducing end (e.g., human blood group B-active II and B-active IIbeta1-3L); (3) the preference within beta-anomeric positioning is Galbeta1-4 \u003e or = Galbeta1-3 \u003e Galbeta1-6; and (4) hydrophobic interactions in the vicinity of the core galactose unit can enhance binding."}

{"project":"Lectin-Jamboree-Sentence","blocks":[{"id":"T10","span":{"begin":0,"end":700},"obj":"Sentence"}],"text":"It is concluded that (1) Galbeta1-3/4GlcNAc and other Galbeta1-related oligosaccharides with alpha1-3 extensions are essential for binding, their polyvalent form in cellular glycoconjugates being a key recognition force for galectin-5; (2) the combining site of galectin-5 appears to be of a shallow-groove type sufficiently large to accommodate a substituted beta-galactoside, especially with alpha-anomeric extension at the non-reducing end (e.g., human blood group B-active II and B-active IIbeta1-3L); (3) the preference within beta-anomeric positioning is Galbeta1-4 \u003e or = Galbeta1-3 \u003e Galbeta1-6; and (4) hydrophobic interactions in the vicinity of the core galactose unit can enhance binding."}

{"project":"NCBITAXON","denotations":[{"id":"T3","span":{"begin":450,"end":455},"obj":"OrganismTaxon"}],"attributes":[{"id":"A3","pred":"db_id","subj":"T3","obj":"9606"}],"text":"It is concluded that (1) Galbeta1-3/4GlcNAc and other Galbeta1-related oligosaccharides with alpha1-3 extensions are essential for binding, their polyvalent form in cellular glycoconjugates being a key recognition force for galectin-5; (2) the combining site of galectin-5 appears to be of a shallow-groove type sufficiently large to accommodate a substituted beta-galactoside, especially with alpha-anomeric extension at the non-reducing end (e.g., human blood group B-active II and B-active IIbeta1-3L); (3) the preference within beta-anomeric positioning is Galbeta1-4 \u003e or = Galbeta1-3 \u003e Galbeta1-6; and (4) hydrophobic interactions in the vicinity of the core galactose unit can enhance binding."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T4","span":{"begin":102,"end":112},"obj":"Body_part"},{"id":"T5","span":{"begin":300,"end":306},"obj":"Body_part"},{"id":"T8","span":{"begin":409,"end":418},"obj":"Body_part"},{"id":"T9","span":{"begin":456,"end":461},"obj":"Body_part"}],"attributes":[{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/UBERON_2000106"},{"id":"A5","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/UBERON_0004704"},{"id":"A6","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/UBERON_0006846"},{"id":"A7","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/UBERON_0014764"},{"id":"A8","pred":"uberon_id","subj":"T8","obj":"http://purl.obolibrary.org/obo/UBERON_2000106"},{"id":"A9","pred":"uberon_id","subj":"T9","obj":"http://purl.obolibrary.org/obo/UBERON_0000178"}],"text":"It is concluded that (1) Galbeta1-3/4GlcNAc and other Galbeta1-related oligosaccharides with alpha1-3 extensions are essential for binding, their polyvalent form in cellular glycoconjugates being a key recognition force for galectin-5; (2) the combining site of galectin-5 appears to be of a shallow-groove type sufficiently large to accommodate a substituted beta-galactoside, especially with alpha-anomeric extension at the non-reducing end (e.g., human blood group B-active II and B-active IIbeta1-3L); (3) the preference within beta-anomeric positioning is Galbeta1-4 \u003e or = Galbeta1-3 \u003e Galbeta1-6; and (4) hydrophobic interactions in the vicinity of the core galactose unit can enhance binding."}