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Glycan-Motif

{"project":"Glycan-Motif","denotations":[{"id":"T1","span":{"begin":609,"end":623},"obj":"https://glytoucan.org/Structures/Glycans/G93424OB"}],"text":"Binding of polysaccharides to human galectin-3 at a noncanonical site in its carbohydrate recognition domain.\nGalectin-3 (Gal-3) is a multifunctional lectin, unique to galectins by the presence of a long N-terminal tail (NT) off of its carbohydrate recognition domain (CRD). Many previous studies have investigated binding of small carbohydrates to its CRD. Here, we used nuclear magnetic resonance spectroscopy ((15)N-(1)H heteronuclear single quantum coherence data) to assess binding of (15)N-Gal-3 (and truncated (15)N-Gal-3 CRD) to several, relatively large polysaccharides, including eight varieties of galactomannans (GMs), as well as a β(1 → 4)-polymannan and an α-branched mannan. Overall, we found that these polysaccharides with a larger carbohydrate footprint interact primarily with a noncanonical carbohydrate-binding site on the F-face of the Gal-3 CRD β-sandwich, and to a less extent, if at all, with the canonical carbohydrate-binding site on the S-face. While there is no evidence for interaction with the NT itself, it does appear that the NT somehow mediates stronger interactions between the Gal-3 CRD and the GMs. Significant Gal-3 resonance broadening observed during polysaccharide titrations indicates that interactions occur in the intermediate exchange regime, and analysis of these data allows estimation of affinities and stoichiometries that range from 4 × 10(4) to 12 × 10(4) M(-1) per site and multiple sites per polysaccharide, respectively. We also found that lactose can still bind to the CRD S-face of GM-bound Gal-3, with the binding of one ligand attenuating affinity of the other. These data are compared with previous results on Gal-1, revealing differences and similarities. They also provide research direction to the development of these polysaccharides as galectin-targeting therapeutics in the clinic."}

GlyCosmos6-Glycan-Motif-Image

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":609,"end":623},"obj":"Glycan_Motif"},{"id":"T2","span":{"begin":625,"end":628},"obj":"Glycan_Motif"},{"id":"T3","span":{"begin":1132,"end":1135},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G93424OB"},{"id":"A2","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G93424OB"},{"id":"A3","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G93424OB"}],"text":"Binding of polysaccharides to human galectin-3 at a noncanonical site in its carbohydrate recognition domain.\nGalectin-3 (Gal-3) is a multifunctional lectin, unique to galectins by the presence of a long N-terminal tail (NT) off of its carbohydrate recognition domain (CRD). Many previous studies have investigated binding of small carbohydrates to its CRD. Here, we used nuclear magnetic resonance spectroscopy ((15)N-(1)H heteronuclear single quantum coherence data) to assess binding of (15)N-Gal-3 (and truncated (15)N-Gal-3 CRD) to several, relatively large polysaccharides, including eight varieties of galactomannans (GMs), as well as a β(1 → 4)-polymannan and an α-branched mannan. Overall, we found that these polysaccharides with a larger carbohydrate footprint interact primarily with a noncanonical carbohydrate-binding site on the F-face of the Gal-3 CRD β-sandwich, and to a less extent, if at all, with the canonical carbohydrate-binding site on the S-face. While there is no evidence for interaction with the NT itself, it does appear that the NT somehow mediates stronger interactions between the Gal-3 CRD and the GMs. Significant Gal-3 resonance broadening observed during polysaccharide titrations indicates that interactions occur in the intermediate exchange regime, and analysis of these data allows estimation of affinities and stoichiometries that range from 4 × 10(4) to 12 × 10(4) M(-1) per site and multiple sites per polysaccharide, respectively. We also found that lactose can still bind to the CRD S-face of GM-bound Gal-3, with the binding of one ligand attenuating affinity of the other. These data are compared with previous results on Gal-1, revealing differences and similarities. They also provide research direction to the development of these polysaccharides as galectin-targeting therapeutics in the clinic."}

sentences

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":109},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":110,"end":274},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":275,"end":357},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":358,"end":689},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":690,"end":972},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":973,"end":1475},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":1476,"end":1620},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":1621,"end":1716},"obj":"Sentence"},{"id":"TextSentencer_T9","span":{"begin":1717,"end":1847},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":109},"obj":"Sentence"},{"id":"T2","span":{"begin":110,"end":274},"obj":"Sentence"},{"id":"T3","span":{"begin":275,"end":357},"obj":"Sentence"},{"id":"T4","span":{"begin":358,"end":689},"obj":"Sentence"},{"id":"T5","span":{"begin":690,"end":972},"obj":"Sentence"},{"id":"T6","span":{"begin":973,"end":1475},"obj":"Sentence"},{"id":"T7","span":{"begin":1476,"end":1620},"obj":"Sentence"},{"id":"T8","span":{"begin":1621,"end":1716},"obj":"Sentence"},{"id":"T9","span":{"begin":1717,"end":1847},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":109},"obj":"Sentence"},{"id":"T2","span":{"begin":110,"end":274},"obj":"Sentence"},{"id":"T3","span":{"begin":275,"end":357},"obj":"Sentence"},{"id":"T4","span":{"begin":358,"end":689},"obj":"Sentence"},{"id":"T5","span":{"begin":690,"end":972},"obj":"Sentence"},{"id":"T6","span":{"begin":973,"end":1475},"obj":"Sentence"},{"id":"T7","span":{"begin":1476,"end":1620},"obj":"Sentence"},{"id":"T8","span":{"begin":1621,"end":1716},"obj":"Sentence"},{"id":"T9","span":{"begin":1717,"end":1847},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Binding of polysaccharides to human galectin-3 at a noncanonical site in its carbohydrate recognition domain.\nGalectin-3 (Gal-3) is a multifunctional lectin, unique to galectins by the presence of a long N-terminal tail (NT) off of its carbohydrate recognition domain (CRD). Many previous studies have investigated binding of small carbohydrates to its CRD. Here, we used nuclear magnetic resonance spectroscopy ((15)N-(1)H heteronuclear single quantum coherence data) to assess binding of (15)N-Gal-3 (and truncated (15)N-Gal-3 CRD) to several, relatively large polysaccharides, including eight varieties of galactomannans (GMs), as well as a β(1 → 4)-polymannan and an α-branched mannan. Overall, we found that these polysaccharides with a larger carbohydrate footprint interact primarily with a noncanonical carbohydrate-binding site on the F-face of the Gal-3 CRD β-sandwich, and to a less extent, if at all, with the canonical carbohydrate-binding site on the S-face. While there is no evidence for interaction with the NT itself, it does appear that the NT somehow mediates stronger interactions between the Gal-3 CRD and the GMs. Significant Gal-3 resonance broadening observed during polysaccharide titrations indicates that interactions occur in the intermediate exchange regime, and analysis of these data allows estimation of affinities and stoichiometries that range from 4 × 10(4) to 12 × 10(4) M(-1) per site and multiple sites per polysaccharide, respectively. We also found that lactose can still bind to the CRD S-face of GM-bound Gal-3, with the binding of one ligand attenuating affinity of the other. These data are compared with previous results on Gal-1, revealing differences and similarities. They also provide research direction to the development of these polysaccharides as galectin-targeting therapeutics in the clinic."}

GlyCosmos6-Glycan-Motif-Structure

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":609,"end":623},"obj":"https://glytoucan.org/Structures/Glycans/G93424OB"}],"text":"Binding of polysaccharides to human galectin-3 at a noncanonical site in its carbohydrate recognition domain.\nGalectin-3 (Gal-3) is a multifunctional lectin, unique to galectins by the presence of a long N-terminal tail (NT) off of its carbohydrate recognition domain (CRD). Many previous studies have investigated binding of small carbohydrates to its CRD. Here, we used nuclear magnetic resonance spectroscopy ((15)N-(1)H heteronuclear single quantum coherence data) to assess binding of (15)N-Gal-3 (and truncated (15)N-Gal-3 CRD) to several, relatively large polysaccharides, including eight varieties of galactomannans (GMs), as well as a β(1 → 4)-polymannan and an α-branched mannan. Overall, we found that these polysaccharides with a larger carbohydrate footprint interact primarily with a noncanonical carbohydrate-binding site on the F-face of the Gal-3 CRD β-sandwich, and to a less extent, if at all, with the canonical carbohydrate-binding site on the S-face. While there is no evidence for interaction with the NT itself, it does appear that the NT somehow mediates stronger interactions between the Gal-3 CRD and the GMs. Significant Gal-3 resonance broadening observed during polysaccharide titrations indicates that interactions occur in the intermediate exchange regime, and analysis of these data allows estimation of affinities and stoichiometries that range from 4 × 10(4) to 12 × 10(4) M(-1) per site and multiple sites per polysaccharide, respectively. We also found that lactose can still bind to the CRD S-face of GM-bound Gal-3, with the binding of one ligand attenuating affinity of the other. These data are compared with previous results on Gal-1, revealing differences and similarities. They also provide research direction to the development of these polysaccharides as galectin-targeting therapeutics in the clinic."}

GlycoBiology-FMA

uniprot-human

{"project":"uniprot-human","denotations":[{"id":"T1","span":{"begin":36,"end":46},"obj":"http://www.uniprot.org/uniprot/P17931"},{"id":"T2","span":{"begin":110,"end":120},"obj":"http://www.uniprot.org/uniprot/P17931"},{"id":"T3","span":{"begin":221,"end":223},"obj":"http://www.uniprot.org/uniprot/Q9P121"},{"id":"T4","span":{"begin":1025,"end":1027},"obj":"http://www.uniprot.org/uniprot/Q9P121"},{"id":"T5","span":{"begin":1060,"end":1062},"obj":"http://www.uniprot.org/uniprot/Q9P121"},{"id":"T6","span":{"begin":221,"end":223},"obj":"http://www.uniprot.org/uniprot/P30990"},{"id":"T7","span":{"begin":1025,"end":1027},"obj":"http://www.uniprot.org/uniprot/P30990"},{"id":"T8","span":{"begin":1060,"end":1062},"obj":"http://www.uniprot.org/uniprot/P30990"},{"id":"T9","span":{"begin":644,"end":647},"obj":"http://www.uniprot.org/uniprot/Q92988"},{"id":"T10","span":{"begin":1670,"end":1675},"obj":"http://www.uniprot.org/uniprot/P09382"}],"text":"Binding of polysaccharides to human galectin-3 at a noncanonical site in its carbohydrate recognition domain.\nGalectin-3 (Gal-3) is a multifunctional lectin, unique to galectins by the presence of a long N-terminal tail (NT) off of its carbohydrate recognition domain (CRD). Many previous studies have investigated binding of small carbohydrates to its CRD. Here, we used nuclear magnetic resonance spectroscopy ((15)N-(1)H heteronuclear single quantum coherence data) to assess binding of (15)N-Gal-3 (and truncated (15)N-Gal-3 CRD) to several, relatively large polysaccharides, including eight varieties of galactomannans (GMs), as well as a β(1 → 4)-polymannan and an α-branched mannan. Overall, we found that these polysaccharides with a larger carbohydrate footprint interact primarily with a noncanonical carbohydrate-binding site on the F-face of the Gal-3 CRD β-sandwich, and to a less extent, if at all, with the canonical carbohydrate-binding site on the S-face. While there is no evidence for interaction with the NT itself, it does appear that the NT somehow mediates stronger interactions between the Gal-3 CRD and the GMs. Significant Gal-3 resonance broadening observed during polysaccharide titrations indicates that interactions occur in the intermediate exchange regime, and analysis of these data allows estimation of affinities and stoichiometries that range from 4 × 10(4) to 12 × 10(4) M(-1) per site and multiple sites per polysaccharide, respectively. We also found that lactose can still bind to the CRD S-face of GM-bound Gal-3, with the binding of one ligand attenuating affinity of the other. These data are compared with previous results on Gal-1, revealing differences and similarities. They also provide research direction to the development of these polysaccharides as galectin-targeting therapeutics in the clinic."}

uniprot-mouse

{"project":"uniprot-mouse","denotations":[{"id":"T1","span":{"begin":36,"end":46},"obj":"http://www.uniprot.org/uniprot/P16110"},{"id":"T2","span":{"begin":110,"end":120},"obj":"http://www.uniprot.org/uniprot/P16110"},{"id":"T3","span":{"begin":221,"end":223},"obj":"http://www.uniprot.org/uniprot/Q9D3P9"},{"id":"T4","span":{"begin":1025,"end":1027},"obj":"http://www.uniprot.org/uniprot/Q9D3P9"},{"id":"T5","span":{"begin":1060,"end":1062},"obj":"http://www.uniprot.org/uniprot/Q9D3P9"},{"id":"T6","span":{"begin":1408,"end":1412},"obj":"http://www.uniprot.org/uniprot/P17717"},{"id":"T7","span":{"begin":1670,"end":1675},"obj":"http://www.uniprot.org/uniprot/P16045"}],"text":"Binding of polysaccharides to human galectin-3 at a noncanonical site in its carbohydrate recognition domain.\nGalectin-3 (Gal-3) is a multifunctional lectin, unique to galectins by the presence of a long N-terminal tail (NT) off of its carbohydrate recognition domain (CRD). Many previous studies have investigated binding of small carbohydrates to its CRD. Here, we used nuclear magnetic resonance spectroscopy ((15)N-(1)H heteronuclear single quantum coherence data) to assess binding of (15)N-Gal-3 (and truncated (15)N-Gal-3 CRD) to several, relatively large polysaccharides, including eight varieties of galactomannans (GMs), as well as a β(1 → 4)-polymannan and an α-branched mannan. Overall, we found that these polysaccharides with a larger carbohydrate footprint interact primarily with a noncanonical carbohydrate-binding site on the F-face of the Gal-3 CRD β-sandwich, and to a less extent, if at all, with the canonical carbohydrate-binding site on the S-face. While there is no evidence for interaction with the NT itself, it does appear that the NT somehow mediates stronger interactions between the Gal-3 CRD and the GMs. Significant Gal-3 resonance broadening observed during polysaccharide titrations indicates that interactions occur in the intermediate exchange regime, and analysis of these data allows estimation of affinities and stoichiometries that range from 4 × 10(4) to 12 × 10(4) M(-1) per site and multiple sites per polysaccharide, respectively. We also found that lactose can still bind to the CRD S-face of GM-bound Gal-3, with the binding of one ligand attenuating affinity of the other. These data are compared with previous results on Gal-1, revealing differences and similarities. They also provide research direction to the development of these polysaccharides as galectin-targeting therapeutics in the clinic."}

GlycoBiology-NCBITAXON

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":275,"end":279},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/9973"},{"id":"T2","span":{"begin":846,"end":850},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/1240355"},{"id":"T3","span":{"begin":967,"end":971},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/1240355"},{"id":"T4","span":{"begin":1531,"end":1535},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/1240355"}],"text":"Binding of polysaccharides to human galectin-3 at a noncanonical site in its carbohydrate recognition domain.\nGalectin-3 (Gal-3) is a multifunctional lectin, unique to galectins by the presence of a long N-terminal tail (NT) off of its carbohydrate recognition domain (CRD). Many previous studies have investigated binding of small carbohydrates to its CRD. Here, we used nuclear magnetic resonance spectroscopy ((15)N-(1)H heteronuclear single quantum coherence data) to assess binding of (15)N-Gal-3 (and truncated (15)N-Gal-3 CRD) to several, relatively large polysaccharides, including eight varieties of galactomannans (GMs), as well as a β(1 → 4)-polymannan and an α-branched mannan. Overall, we found that these polysaccharides with a larger carbohydrate footprint interact primarily with a noncanonical carbohydrate-binding site on the F-face of the Gal-3 CRD β-sandwich, and to a less extent, if at all, with the canonical carbohydrate-binding site on the S-face. While there is no evidence for interaction with the NT itself, it does appear that the NT somehow mediates stronger interactions between the Gal-3 CRD and the GMs. Significant Gal-3 resonance broadening observed during polysaccharide titrations indicates that interactions occur in the intermediate exchange regime, and analysis of these data allows estimation of affinities and stoichiometries that range from 4 × 10(4) to 12 × 10(4) M(-1) per site and multiple sites per polysaccharide, respectively. We also found that lactose can still bind to the CRD S-face of GM-bound Gal-3, with the binding of one ligand attenuating affinity of the other. These data are compared with previous results on Gal-1, revealing differences and similarities. They also provide research direction to the development of these polysaccharides as galectin-targeting therapeutics in the clinic."}

GO-BP

{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":1272,"end":1280},"obj":"http://purl.obolibrary.org/obo/GO_0015297"},{"id":"T2","span":{"begin":1761,"end":1772},"obj":"http://purl.obolibrary.org/obo/GO_0032502"}],"text":"Binding of polysaccharides to human galectin-3 at a noncanonical site in its carbohydrate recognition domain.\nGalectin-3 (Gal-3) is a multifunctional lectin, unique to galectins by the presence of a long N-terminal tail (NT) off of its carbohydrate recognition domain (CRD). Many previous studies have investigated binding of small carbohydrates to its CRD. Here, we used nuclear magnetic resonance spectroscopy ((15)N-(1)H heteronuclear single quantum coherence data) to assess binding of (15)N-Gal-3 (and truncated (15)N-Gal-3 CRD) to several, relatively large polysaccharides, including eight varieties of galactomannans (GMs), as well as a β(1 → 4)-polymannan and an α-branched mannan. Overall, we found that these polysaccharides with a larger carbohydrate footprint interact primarily with a noncanonical carbohydrate-binding site on the F-face of the Gal-3 CRD β-sandwich, and to a less extent, if at all, with the canonical carbohydrate-binding site on the S-face. While there is no evidence for interaction with the NT itself, it does appear that the NT somehow mediates stronger interactions between the Gal-3 CRD and the GMs. Significant Gal-3 resonance broadening observed during polysaccharide titrations indicates that interactions occur in the intermediate exchange regime, and analysis of these data allows estimation of affinities and stoichiometries that range from 4 × 10(4) to 12 × 10(4) M(-1) per site and multiple sites per polysaccharide, respectively. We also found that lactose can still bind to the CRD S-face of GM-bound Gal-3, with the binding of one ligand attenuating affinity of the other. These data are compared with previous results on Gal-1, revealing differences and similarities. They also provide research direction to the development of these polysaccharides as galectin-targeting therapeutics in the clinic."}

GO-MF

UBERON-AE

{"project":"UBERON-AE","denotations":[{"id":"T1","span":{"begin":215,"end":219},"obj":"http://purl.obolibrary.org/obo/UBERON_0002415"},{"id":"T2","span":{"begin":846,"end":850},"obj":"http://purl.obolibrary.org/obo/UBERON_0001456"},{"id":"T3","span":{"begin":967,"end":971},"obj":"http://purl.obolibrary.org/obo/UBERON_0001456"},{"id":"T4","span":{"begin":1531,"end":1535},"obj":"http://purl.obolibrary.org/obo/UBERON_0001456"}],"text":"Binding of polysaccharides to human galectin-3 at a noncanonical site in its carbohydrate recognition domain.\nGalectin-3 (Gal-3) is a multifunctional lectin, unique to galectins by the presence of a long N-terminal tail (NT) off of its carbohydrate recognition domain (CRD). Many previous studies have investigated binding of small carbohydrates to its CRD. Here, we used nuclear magnetic resonance spectroscopy ((15)N-(1)H heteronuclear single quantum coherence data) to assess binding of (15)N-Gal-3 (and truncated (15)N-Gal-3 CRD) to several, relatively large polysaccharides, including eight varieties of galactomannans (GMs), as well as a β(1 → 4)-polymannan and an α-branched mannan. Overall, we found that these polysaccharides with a larger carbohydrate footprint interact primarily with a noncanonical carbohydrate-binding site on the F-face of the Gal-3 CRD β-sandwich, and to a less extent, if at all, with the canonical carbohydrate-binding site on the S-face. While there is no evidence for interaction with the NT itself, it does appear that the NT somehow mediates stronger interactions between the Gal-3 CRD and the GMs. Significant Gal-3 resonance broadening observed during polysaccharide titrations indicates that interactions occur in the intermediate exchange regime, and analysis of these data allows estimation of affinities and stoichiometries that range from 4 × 10(4) to 12 × 10(4) M(-1) per site and multiple sites per polysaccharide, respectively. We also found that lactose can still bind to the CRD S-face of GM-bound Gal-3, with the binding of one ligand attenuating affinity of the other. These data are compared with previous results on Gal-1, revealing differences and similarities. They also provide research direction to the development of these polysaccharides as galectin-targeting therapeutics in the clinic."}

performance-test

{"project":"performance-test","denotations":[{"id":"PD-UBERON-AE-B_T1","span":{"begin":215,"end":219},"obj":"http://purl.obolibrary.org/obo/UBERON_0002415"},{"id":"PD-UBERON-AE-B_T2","span":{"begin":846,"end":850},"obj":"http://purl.obolibrary.org/obo/UBERON_0001456"},{"id":"PD-UBERON-AE-B_T3","span":{"begin":967,"end":971},"obj":"http://purl.obolibrary.org/obo/UBERON_0001456"},{"id":"PD-UBERON-AE-B_T4","span":{"begin":1531,"end":1535},"obj":"http://purl.obolibrary.org/obo/UBERON_0001456"}],"text":"Binding of polysaccharides to human galectin-3 at a noncanonical site in its carbohydrate recognition domain.\nGalectin-3 (Gal-3) is a multifunctional lectin, unique to galectins by the presence of a long N-terminal tail (NT) off of its carbohydrate recognition domain (CRD). Many previous studies have investigated binding of small carbohydrates to its CRD. Here, we used nuclear magnetic resonance spectroscopy ((15)N-(1)H heteronuclear single quantum coherence data) to assess binding of (15)N-Gal-3 (and truncated (15)N-Gal-3 CRD) to several, relatively large polysaccharides, including eight varieties of galactomannans (GMs), as well as a β(1 → 4)-polymannan and an α-branched mannan. Overall, we found that these polysaccharides with a larger carbohydrate footprint interact primarily with a noncanonical carbohydrate-binding site on the F-face of the Gal-3 CRD β-sandwich, and to a less extent, if at all, with the canonical carbohydrate-binding site on the S-face. While there is no evidence for interaction with the NT itself, it does appear that the NT somehow mediates stronger interactions between the Gal-3 CRD and the GMs. Significant Gal-3 resonance broadening observed during polysaccharide titrations indicates that interactions occur in the intermediate exchange regime, and analysis of these data allows estimation of affinities and stoichiometries that range from 4 × 10(4) to 12 × 10(4) M(-1) per site and multiple sites per polysaccharide, respectively. We also found that lactose can still bind to the CRD S-face of GM-bound Gal-3, with the binding of one ligand attenuating affinity of the other. These data are compared with previous results on Gal-1, revealing differences and similarities. They also provide research direction to the development of these polysaccharides as galectin-targeting therapeutics in the clinic."}

Lectin

{"project":"Lectin","denotations":[{"id":"Lectin_T1","span":{"begin":110,"end":118},"obj":"https://acgg.asia/db/lfdb/LfDB0270"},{"id":"Lectin_T2","span":{"begin":110,"end":118},"obj":"https://acgg.asia/db/lfdb/LfDB0272"},{"id":"Lectin_T3","span":{"begin":110,"end":118},"obj":"https://acgg.asia/db/lfdb/LfDB0274"},{"id":"Lectin_T4","span":{"begin":122,"end":127},"obj":"https://acgg.asia/db/lfdb/LfDB0065"},{"id":"Lectin_T5","span":{"begin":496,"end":501},"obj":"https://acgg.asia/db/lfdb/LfDB0065"},{"id":"Lectin_T6","span":{"begin":523,"end":528},"obj":"https://acgg.asia/db/lfdb/LfDB0065"},{"id":"Lectin_T7","span":{"begin":858,"end":863},"obj":"https://acgg.asia/db/lfdb/LfDB0065"},{"id":"Lectin_T8","span":{"begin":1114,"end":1119},"obj":"https://acgg.asia/db/lfdb/LfDB0065"},{"id":"Lectin_T9","span":{"begin":1149,"end":1154},"obj":"https://acgg.asia/db/lfdb/LfDB0065"},{"id":"Lectin_T10","span":{"begin":1548,"end":1553},"obj":"https://acgg.asia/db/lfdb/LfDB0065"}],"text":"Binding of polysaccharides to human galectin-3 at a noncanonical site in its carbohydrate recognition domain.\nGalectin-3 (Gal-3) is a multifunctional lectin, unique to galectins by the presence of a long N-terminal tail (NT) off of its carbohydrate recognition domain (CRD). Many previous studies have investigated binding of small carbohydrates to its CRD. Here, we used nuclear magnetic resonance spectroscopy ((15)N-(1)H heteronuclear single quantum coherence data) to assess binding of (15)N-Gal-3 (and truncated (15)N-Gal-3 CRD) to several, relatively large polysaccharides, including eight varieties of galactomannans (GMs), as well as a β(1 → 4)-polymannan and an α-branched mannan. Overall, we found that these polysaccharides with a larger carbohydrate footprint interact primarily with a noncanonical carbohydrate-binding site on the F-face of the Gal-3 CRD β-sandwich, and to a less extent, if at all, with the canonical carbohydrate-binding site on the S-face. While there is no evidence for interaction with the NT itself, it does appear that the NT somehow mediates stronger interactions between the Gal-3 CRD and the GMs. Significant Gal-3 resonance broadening observed during polysaccharide titrations indicates that interactions occur in the intermediate exchange regime, and analysis of these data allows estimation of affinities and stoichiometries that range from 4 × 10(4) to 12 × 10(4) M(-1) per site and multiple sites per polysaccharide, respectively. We also found that lactose can still bind to the CRD S-face of GM-bound Gal-3, with the binding of one ligand attenuating affinity of the other. These data are compared with previous results on Gal-1, revealing differences and similarities. They also provide research direction to the development of these polysaccharides as galectin-targeting therapeutics in the clinic."}

GlycoBiology-Epitope

{"project":"GlycoBiology-Epitope","denotations":[{"id":"PD-GlycoEpitope-B_T1","span":{"begin":609,"end":623},"obj":"http://www.glycoepitope.jp/epitopes/EP0510"}],"text":"Binding of polysaccharides to human galectin-3 at a noncanonical site in its carbohydrate recognition domain.\nGalectin-3 (Gal-3) is a multifunctional lectin, unique to galectins by the presence of a long N-terminal tail (NT) off of its carbohydrate recognition domain (CRD). Many previous studies have investigated binding of small carbohydrates to its CRD. Here, we used nuclear magnetic resonance spectroscopy ((15)N-(1)H heteronuclear single quantum coherence data) to assess binding of (15)N-Gal-3 (and truncated (15)N-Gal-3 CRD) to several, relatively large polysaccharides, including eight varieties of galactomannans (GMs), as well as a β(1 → 4)-polymannan and an α-branched mannan. Overall, we found that these polysaccharides with a larger carbohydrate footprint interact primarily with a noncanonical carbohydrate-binding site on the F-face of the Gal-3 CRD β-sandwich, and to a less extent, if at all, with the canonical carbohydrate-binding site on the S-face. While there is no evidence for interaction with the NT itself, it does appear that the NT somehow mediates stronger interactions between the Gal-3 CRD and the GMs. Significant Gal-3 resonance broadening observed during polysaccharide titrations indicates that interactions occur in the intermediate exchange regime, and analysis of these data allows estimation of affinities and stoichiometries that range from 4 × 10(4) to 12 × 10(4) M(-1) per site and multiple sites per polysaccharide, respectively. We also found that lactose can still bind to the CRD S-face of GM-bound Gal-3, with the binding of one ligand attenuating affinity of the other. These data are compared with previous results on Gal-1, revealing differences and similarities. They also provide research direction to the development of these polysaccharides as galectin-targeting therapeutics in the clinic."}

GlyTouCan-IUPAC

Glycan-GlyCosmos

{"project":"Glycan-GlyCosmos","denotations":[{"id":"T1","span":{"begin":1495,"end":1502},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G15541SE"},{"id":"A2","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G15541SE"}],"text":"Binding of polysaccharides to human galectin-3 at a noncanonical site in its carbohydrate recognition domain.\nGalectin-3 (Gal-3) is a multifunctional lectin, unique to galectins by the presence of a long N-terminal tail (NT) off of its carbohydrate recognition domain (CRD). Many previous studies have investigated binding of small carbohydrates to its CRD. Here, we used nuclear magnetic resonance spectroscopy ((15)N-(1)H heteronuclear single quantum coherence data) to assess binding of (15)N-Gal-3 (and truncated (15)N-Gal-3 CRD) to several, relatively large polysaccharides, including eight varieties of galactomannans (GMs), as well as a β(1 → 4)-polymannan and an α-branched mannan. Overall, we found that these polysaccharides with a larger carbohydrate footprint interact primarily with a noncanonical carbohydrate-binding site on the F-face of the Gal-3 CRD β-sandwich, and to a less extent, if at all, with the canonical carbohydrate-binding site on the S-face. While there is no evidence for interaction with the NT itself, it does appear that the NT somehow mediates stronger interactions between the Gal-3 CRD and the GMs. Significant Gal-3 resonance broadening observed during polysaccharide titrations indicates that interactions occur in the intermediate exchange regime, and analysis of these data allows estimation of affinities and stoichiometries that range from 4 × 10(4) to 12 × 10(4) M(-1) per site and multiple sites per polysaccharide, respectively. We also found that lactose can still bind to the CRD S-face of GM-bound Gal-3, with the binding of one ligand attenuating affinity of the other. These data are compared with previous results on Gal-1, revealing differences and similarities. They also provide research direction to the development of these polysaccharides as galectin-targeting therapeutics in the clinic."}

GlyCosmos15-NCBITAXON

{"project":"GlyCosmos15-NCBITAXON","denotations":[{"id":"T1","span":{"begin":30,"end":35},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9606"}],"text":"Binding of polysaccharides to human galectin-3 at a noncanonical site in its carbohydrate recognition domain.\nGalectin-3 (Gal-3) is a multifunctional lectin, unique to galectins by the presence of a long N-terminal tail (NT) off of its carbohydrate recognition domain (CRD). Many previous studies have investigated binding of small carbohydrates to its CRD. Here, we used nuclear magnetic resonance spectroscopy ((15)N-(1)H heteronuclear single quantum coherence data) to assess binding of (15)N-Gal-3 (and truncated (15)N-Gal-3 CRD) to several, relatively large polysaccharides, including eight varieties of galactomannans (GMs), as well as a β(1 → 4)-polymannan and an α-branched mannan. Overall, we found that these polysaccharides with a larger carbohydrate footprint interact primarily with a noncanonical carbohydrate-binding site on the F-face of the Gal-3 CRD β-sandwich, and to a less extent, if at all, with the canonical carbohydrate-binding site on the S-face. While there is no evidence for interaction with the NT itself, it does appear that the NT somehow mediates stronger interactions between the Gal-3 CRD and the GMs. Significant Gal-3 resonance broadening observed during polysaccharide titrations indicates that interactions occur in the intermediate exchange regime, and analysis of these data allows estimation of affinities and stoichiometries that range from 4 × 10(4) to 12 × 10(4) M(-1) per site and multiple sites per polysaccharide, respectively. We also found that lactose can still bind to the CRD S-face of GM-bound Gal-3, with the binding of one ligand attenuating affinity of the other. These data are compared with previous results on Gal-1, revealing differences and similarities. They also provide research direction to the development of these polysaccharides as galectin-targeting therapeutics in the clinic."}

GlyCosmos15-UBERON

{"project":"GlyCosmos15-UBERON","denotations":[{"id":"T1","span":{"begin":215,"end":219},"obj":"Body_part"},{"id":"T3","span":{"begin":846,"end":850},"obj":"Body_part"},{"id":"T4","span":{"begin":967,"end":971},"obj":"Body_part"},{"id":"T5","span":{"begin":1531,"end":1535},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0002415"},{"id":"A2","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_4000164"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/UBERON_0001456"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/UBERON_0001456"},{"id":"A5","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/UBERON_0001456"}],"text":"Binding of polysaccharides to human galectin-3 at a noncanonical site in its carbohydrate recognition domain.\nGalectin-3 (Gal-3) is a multifunctional lectin, unique to galectins by the presence of a long N-terminal tail (NT) off of its carbohydrate recognition domain (CRD). Many previous studies have investigated binding of small carbohydrates to its CRD. Here, we used nuclear magnetic resonance spectroscopy ((15)N-(1)H heteronuclear single quantum coherence data) to assess binding of (15)N-Gal-3 (and truncated (15)N-Gal-3 CRD) to several, relatively large polysaccharides, including eight varieties of galactomannans (GMs), as well as a β(1 → 4)-polymannan and an α-branched mannan. Overall, we found that these polysaccharides with a larger carbohydrate footprint interact primarily with a noncanonical carbohydrate-binding site on the F-face of the Gal-3 CRD β-sandwich, and to a less extent, if at all, with the canonical carbohydrate-binding site on the S-face. While there is no evidence for interaction with the NT itself, it does appear that the NT somehow mediates stronger interactions between the Gal-3 CRD and the GMs. Significant Gal-3 resonance broadening observed during polysaccharide titrations indicates that interactions occur in the intermediate exchange regime, and analysis of these data allows estimation of affinities and stoichiometries that range from 4 × 10(4) to 12 × 10(4) M(-1) per site and multiple sites per polysaccharide, respectively. We also found that lactose can still bind to the CRD S-face of GM-bound Gal-3, with the binding of one ligand attenuating affinity of the other. These data are compared with previous results on Gal-1, revealing differences and similarities. They also provide research direction to the development of these polysaccharides as galectin-targeting therapeutics in the clinic."}

sentences

GlyCosmos15-Sentences

{"project":"GlyCosmos15-Sentences","blocks":[{"id":"T1","span":{"begin":0,"end":109},"obj":"Sentence"},{"id":"T2","span":{"begin":110,"end":274},"obj":"Sentence"},{"id":"T3","span":{"begin":275,"end":357},"obj":"Sentence"},{"id":"T4","span":{"begin":358,"end":689},"obj":"Sentence"},{"id":"T5","span":{"begin":690,"end":972},"obj":"Sentence"},{"id":"T6","span":{"begin":973,"end":1475},"obj":"Sentence"},{"id":"T7","span":{"begin":1476,"end":1620},"obj":"Sentence"},{"id":"T8","span":{"begin":1621,"end":1716},"obj":"Sentence"},{"id":"T9","span":{"begin":1717,"end":1847},"obj":"Sentence"}],"text":"Binding of polysaccharides to human galectin-3 at a noncanonical site in its carbohydrate recognition domain.\nGalectin-3 (Gal-3) is a multifunctional lectin, unique to galectins by the presence of a long N-terminal tail (NT) off of its carbohydrate recognition domain (CRD). Many previous studies have investigated binding of small carbohydrates to its CRD. Here, we used nuclear magnetic resonance spectroscopy ((15)N-(1)H heteronuclear single quantum coherence data) to assess binding of (15)N-Gal-3 (and truncated (15)N-Gal-3 CRD) to several, relatively large polysaccharides, including eight varieties of galactomannans (GMs), as well as a β(1 → 4)-polymannan and an α-branched mannan. Overall, we found that these polysaccharides with a larger carbohydrate footprint interact primarily with a noncanonical carbohydrate-binding site on the F-face of the Gal-3 CRD β-sandwich, and to a less extent, if at all, with the canonical carbohydrate-binding site on the S-face. While there is no evidence for interaction with the NT itself, it does appear that the NT somehow mediates stronger interactions between the Gal-3 CRD and the GMs. Significant Gal-3 resonance broadening observed during polysaccharide titrations indicates that interactions occur in the intermediate exchange regime, and analysis of these data allows estimation of affinities and stoichiometries that range from 4 × 10(4) to 12 × 10(4) M(-1) per site and multiple sites per polysaccharide, respectively. We also found that lactose can still bind to the CRD S-face of GM-bound Gal-3, with the binding of one ligand attenuating affinity of the other. These data are compared with previous results on Gal-1, revealing differences and similarities. They also provide research direction to the development of these polysaccharides as galectin-targeting therapeutics in the clinic."}

GlyCosmos15-Glycan

{"project":"GlyCosmos15-Glycan","denotations":[{"id":"T1","span":{"begin":1495,"end":1502},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G15541SE"},{"id":"A2","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G15541SE"}],"text":"Binding of polysaccharides to human galectin-3 at a noncanonical site in its carbohydrate recognition domain.\nGalectin-3 (Gal-3) is a multifunctional lectin, unique to galectins by the presence of a long N-terminal tail (NT) off of its carbohydrate recognition domain (CRD). Many previous studies have investigated binding of small carbohydrates to its CRD. Here, we used nuclear magnetic resonance spectroscopy ((15)N-(1)H heteronuclear single quantum coherence data) to assess binding of (15)N-Gal-3 (and truncated (15)N-Gal-3 CRD) to several, relatively large polysaccharides, including eight varieties of galactomannans (GMs), as well as a β(1 → 4)-polymannan and an α-branched mannan. Overall, we found that these polysaccharides with a larger carbohydrate footprint interact primarily with a noncanonical carbohydrate-binding site on the F-face of the Gal-3 CRD β-sandwich, and to a less extent, if at all, with the canonical carbohydrate-binding site on the S-face. While there is no evidence for interaction with the NT itself, it does appear that the NT somehow mediates stronger interactions between the Gal-3 CRD and the GMs. Significant Gal-3 resonance broadening observed during polysaccharide titrations indicates that interactions occur in the intermediate exchange regime, and analysis of these data allows estimation of affinities and stoichiometries that range from 4 × 10(4) to 12 × 10(4) M(-1) per site and multiple sites per polysaccharide, respectively. We also found that lactose can still bind to the CRD S-face of GM-bound Gal-3, with the binding of one ligand attenuating affinity of the other. These data are compared with previous results on Gal-1, revealing differences and similarities. They also provide research direction to the development of these polysaccharides as galectin-targeting therapeutics in the clinic."}

Lectin-Jamboree-Sentence

{"project":"Lectin-Jamboree-Sentence","blocks":[{"id":"T1","span":{"begin":0,"end":109},"obj":"Sentence"},{"id":"T2","span":{"begin":110,"end":274},"obj":"Sentence"},{"id":"T3","span":{"begin":275,"end":357},"obj":"Sentence"},{"id":"T4","span":{"begin":358,"end":689},"obj":"Sentence"},{"id":"T5","span":{"begin":690,"end":972},"obj":"Sentence"},{"id":"T6","span":{"begin":973,"end":1475},"obj":"Sentence"},{"id":"T7","span":{"begin":1476,"end":1620},"obj":"Sentence"},{"id":"T8","span":{"begin":1621,"end":1716},"obj":"Sentence"},{"id":"T9","span":{"begin":1717,"end":1847},"obj":"Sentence"}],"text":"Binding of polysaccharides to human galectin-3 at a noncanonical site in its carbohydrate recognition domain.\nGalectin-3 (Gal-3) is a multifunctional lectin, unique to galectins by the presence of a long N-terminal tail (NT) off of its carbohydrate recognition domain (CRD). Many previous studies have investigated binding of small carbohydrates to its CRD. Here, we used nuclear magnetic resonance spectroscopy ((15)N-(1)H heteronuclear single quantum coherence data) to assess binding of (15)N-Gal-3 (and truncated (15)N-Gal-3 CRD) to several, relatively large polysaccharides, including eight varieties of galactomannans (GMs), as well as a β(1 → 4)-polymannan and an α-branched mannan. Overall, we found that these polysaccharides with a larger carbohydrate footprint interact primarily with a noncanonical carbohydrate-binding site on the F-face of the Gal-3 CRD β-sandwich, and to a less extent, if at all, with the canonical carbohydrate-binding site on the S-face. While there is no evidence for interaction with the NT itself, it does appear that the NT somehow mediates stronger interactions between the Gal-3 CRD and the GMs. Significant Gal-3 resonance broadening observed during polysaccharide titrations indicates that interactions occur in the intermediate exchange regime, and analysis of these data allows estimation of affinities and stoichiometries that range from 4 × 10(4) to 12 × 10(4) M(-1) per site and multiple sites per polysaccharide, respectively. We also found that lactose can still bind to the CRD S-face of GM-bound Gal-3, with the binding of one ligand attenuating affinity of the other. These data are compared with previous results on Gal-1, revealing differences and similarities. They also provide research direction to the development of these polysaccharides as galectin-targeting therapeutics in the clinic."}

NCBITAXON

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":30,"end":35},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9606"}],"text":"Binding of polysaccharides to human galectin-3 at a noncanonical site in its carbohydrate recognition domain.\nGalectin-3 (Gal-3) is a multifunctional lectin, unique to galectins by the presence of a long N-terminal tail (NT) off of its carbohydrate recognition domain (CRD). Many previous studies have investigated binding of small carbohydrates to its CRD. Here, we used nuclear magnetic resonance spectroscopy ((15)N-(1)H heteronuclear single quantum coherence data) to assess binding of (15)N-Gal-3 (and truncated (15)N-Gal-3 CRD) to several, relatively large polysaccharides, including eight varieties of galactomannans (GMs), as well as a β(1 → 4)-polymannan and an α-branched mannan. Overall, we found that these polysaccharides with a larger carbohydrate footprint interact primarily with a noncanonical carbohydrate-binding site on the F-face of the Gal-3 CRD β-sandwich, and to a less extent, if at all, with the canonical carbohydrate-binding site on the S-face. While there is no evidence for interaction with the NT itself, it does appear that the NT somehow mediates stronger interactions between the Gal-3 CRD and the GMs. Significant Gal-3 resonance broadening observed during polysaccharide titrations indicates that interactions occur in the intermediate exchange regime, and analysis of these data allows estimation of affinities and stoichiometries that range from 4 × 10(4) to 12 × 10(4) M(-1) per site and multiple sites per polysaccharide, respectively. We also found that lactose can still bind to the CRD S-face of GM-bound Gal-3, with the binding of one ligand attenuating affinity of the other. These data are compared with previous results on Gal-1, revealing differences and similarities. They also provide research direction to the development of these polysaccharides as galectin-targeting therapeutics in the clinic."}

Anatomy-UBERON

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":215,"end":219},"obj":"Body_part"},{"id":"T3","span":{"begin":846,"end":850},"obj":"Body_part"},{"id":"T4","span":{"begin":967,"end":971},"obj":"Body_part"},{"id":"T5","span":{"begin":1531,"end":1535},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0002415"},{"id":"A2","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_4000164"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/UBERON_0001456"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/UBERON_0001456"},{"id":"A5","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/UBERON_0001456"}],"text":"Binding of polysaccharides to human galectin-3 at a noncanonical site in its carbohydrate recognition domain.\nGalectin-3 (Gal-3) is a multifunctional lectin, unique to galectins by the presence of a long N-terminal tail (NT) off of its carbohydrate recognition domain (CRD). Many previous studies have investigated binding of small carbohydrates to its CRD. Here, we used nuclear magnetic resonance spectroscopy ((15)N-(1)H heteronuclear single quantum coherence data) to assess binding of (15)N-Gal-3 (and truncated (15)N-Gal-3 CRD) to several, relatively large polysaccharides, including eight varieties of galactomannans (GMs), as well as a β(1 → 4)-polymannan and an α-branched mannan. Overall, we found that these polysaccharides with a larger carbohydrate footprint interact primarily with a noncanonical carbohydrate-binding site on the F-face of the Gal-3 CRD β-sandwich, and to a less extent, if at all, with the canonical carbohydrate-binding site on the S-face. While there is no evidence for interaction with the NT itself, it does appear that the NT somehow mediates stronger interactions between the Gal-3 CRD and the GMs. Significant Gal-3 resonance broadening observed during polysaccharide titrations indicates that interactions occur in the intermediate exchange regime, and analysis of these data allows estimation of affinities and stoichiometries that range from 4 × 10(4) to 12 × 10(4) M(-1) per site and multiple sites per polysaccharide, respectively. We also found that lactose can still bind to the CRD S-face of GM-bound Gal-3, with the binding of one ligand attenuating affinity of the other. These data are compared with previous results on Gal-1, revealing differences and similarities. They also provide research direction to the development of these polysaccharides as galectin-targeting therapeutics in the clinic."}