PubMed:7895225 JSONTXT

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":200,"end":209},"obj":"Glycan_Motif"},{"id":"T3","span":{"begin":408,"end":417},"obj":"Glycan_Motif"},{"id":"T5","span":{"begin":498,"end":507},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G68158BT"},{"id":"A2","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G65889KE"},{"id":"A3","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G68158BT"},{"id":"A4","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G65889KE"},{"id":"A5","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G68158BT"},{"id":"A6","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G65889KE"}],"text":"Structural and functional-group tuning in the design of neuraminidase inhibitors.\nAnalogues of the disaccharide alpha-NeuAc-(2--\u003e6)-beta-D-Gal-OR have been made by modifications at C-1 and C-6 of the galactose and at C-4 of the NeuAc unit, for structure-activity relationship studies with influenza virus neuraminidase. These studies indicate that for the influenza neuraminidase, a larger aglycon at C-1 of galactose is less preferred, whereas the restriction of the rotamer orientation at C-6 of galactose in the \"tg\" mode favors enzyme binding. Substitution at C-4 of the NeuAc unit has the most profound effect in the influenza neuraminidase hydrolysis and inhibition. For example, azido and acetamido groups at C-4 of the NeuAc units render the sialosides resistant to neuraminidase hydrolysis. However, these derivatives are not inhibitors of the neuraminidase, indicating their lack of binding. On the other hand, a 4-amino substitution of the NeuAc unit not only renders the corresponding sialosides neuraminidase-resistant, but also makes them potent neuraminidase inhibitors. This potent inhibition indicates that the 4-amino groups in these sialosides may engage in favorable interaction with amino acids at the neuraminidase active-site. The conclusion is also supported by docking studies of the carbohydrate structures at the neuraminidase active-site."}

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":200,"end":209},"obj":"https://glytoucan.org/Structures/Glycans/G65889KE"},{"id":"T2","span":{"begin":200,"end":209},"obj":"https://glytoucan.org/Structures/Glycans/G68158BT"},{"id":"T3","span":{"begin":408,"end":417},"obj":"https://glytoucan.org/Structures/Glycans/G65889KE"},{"id":"T4","span":{"begin":408,"end":417},"obj":"https://glytoucan.org/Structures/Glycans/G68158BT"},{"id":"T5","span":{"begin":498,"end":507},"obj":"https://glytoucan.org/Structures/Glycans/G65889KE"},{"id":"T6","span":{"begin":498,"end":507},"obj":"https://glytoucan.org/Structures/Glycans/G68158BT"}],"text":"Structural and functional-group tuning in the design of neuraminidase inhibitors.\nAnalogues of the disaccharide alpha-NeuAc-(2--\u003e6)-beta-D-Gal-OR have been made by modifications at C-1 and C-6 of the galactose and at C-4 of the NeuAc unit, for structure-activity relationship studies with influenza virus neuraminidase. These studies indicate that for the influenza neuraminidase, a larger aglycon at C-1 of galactose is less preferred, whereas the restriction of the rotamer orientation at C-6 of galactose in the \"tg\" mode favors enzyme binding. Substitution at C-4 of the NeuAc unit has the most profound effect in the influenza neuraminidase hydrolysis and inhibition. For example, azido and acetamido groups at C-4 of the NeuAc units render the sialosides resistant to neuraminidase hydrolysis. However, these derivatives are not inhibitors of the neuraminidase, indicating their lack of binding. On the other hand, a 4-amino substitution of the NeuAc unit not only renders the corresponding sialosides neuraminidase-resistant, but also makes them potent neuraminidase inhibitors. This potent inhibition indicates that the 4-amino groups in these sialosides may engage in favorable interaction with amino acids at the neuraminidase active-site. The conclusion is also supported by docking studies of the carbohydrate structures at the neuraminidase active-site."}

{"project":"Glycosmos6-MAT","denotations":[{"id":"T1","span":{"begin":915,"end":919},"obj":"http://purl.obolibrary.org/obo/MAT_0000091"}],"text":"Structural and functional-group tuning in the design of neuraminidase inhibitors.\nAnalogues of the disaccharide alpha-NeuAc-(2--\u003e6)-beta-D-Gal-OR have been made by modifications at C-1 and C-6 of the galactose and at C-4 of the NeuAc unit, for structure-activity relationship studies with influenza virus neuraminidase. These studies indicate that for the influenza neuraminidase, a larger aglycon at C-1 of galactose is less preferred, whereas the restriction of the rotamer orientation at C-6 of galactose in the \"tg\" mode favors enzyme binding. Substitution at C-4 of the NeuAc unit has the most profound effect in the influenza neuraminidase hydrolysis and inhibition. For example, azido and acetamido groups at C-4 of the NeuAc units render the sialosides resistant to neuraminidase hydrolysis. However, these derivatives are not inhibitors of the neuraminidase, indicating their lack of binding. On the other hand, a 4-amino substitution of the NeuAc unit not only renders the corresponding sialosides neuraminidase-resistant, but also makes them potent neuraminidase inhibitors. This potent inhibition indicates that the 4-amino groups in these sialosides may engage in favorable interaction with amino acids at the neuraminidase active-site. The conclusion is also supported by docking studies of the carbohydrate structures at the neuraminidase active-site."}

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":81},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":82,"end":319},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":320,"end":547},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":548,"end":672},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":673,"end":799},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":800,"end":901},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":902,"end":1085},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":1086,"end":1249},"obj":"Sentence"},{"id":"TextSentencer_T9","span":{"begin":1250,"end":1366},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":81},"obj":"Sentence"},{"id":"T2","span":{"begin":82,"end":319},"obj":"Sentence"},{"id":"T3","span":{"begin":320,"end":547},"obj":"Sentence"},{"id":"T4","span":{"begin":548,"end":672},"obj":"Sentence"},{"id":"T5","span":{"begin":673,"end":799},"obj":"Sentence"},{"id":"T6","span":{"begin":800,"end":901},"obj":"Sentence"},{"id":"T7","span":{"begin":902,"end":1085},"obj":"Sentence"},{"id":"T8","span":{"begin":1086,"end":1249},"obj":"Sentence"},{"id":"T9","span":{"begin":1250,"end":1366},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Structural and functional-group tuning in the design of neuraminidase inhibitors.\nAnalogues of the disaccharide alpha-NeuAc-(2--\u003e6)-beta-D-Gal-OR have been made by modifications at C-1 and C-6 of the galactose and at C-4 of the NeuAc unit, for structure-activity relationship studies with influenza virus neuraminidase. These studies indicate that for the influenza neuraminidase, a larger aglycon at C-1 of galactose is less preferred, whereas the restriction of the rotamer orientation at C-6 of galactose in the \"tg\" mode favors enzyme binding. Substitution at C-4 of the NeuAc unit has the most profound effect in the influenza neuraminidase hydrolysis and inhibition. For example, azido and acetamido groups at C-4 of the NeuAc units render the sialosides resistant to neuraminidase hydrolysis. However, these derivatives are not inhibitors of the neuraminidase, indicating their lack of binding. On the other hand, a 4-amino substitution of the NeuAc unit not only renders the corresponding sialosides neuraminidase-resistant, but also makes them potent neuraminidase inhibitors. This potent inhibition indicates that the 4-amino groups in these sialosides may engage in favorable interaction with amino acids at the neuraminidase active-site. The conclusion is also supported by docking studies of the carbohydrate structures at the neuraminidase active-site."}

{"project":"GlyCosmos15-Glycan","denotations":[{"id":"T1","span":{"begin":118,"end":123},"obj":"Glycan"},{"id":"T2","span":{"begin":228,"end":233},"obj":"Glycan"},{"id":"T3","span":{"begin":575,"end":580},"obj":"Glycan"},{"id":"T4","span":{"begin":727,"end":732},"obj":"Glycan"},{"id":"T5","span":{"begin":951,"end":956},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G76685HR"},{"id":"A6","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":"A7","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR"},{"id":"A3","pred":"glycosmos_id","subj":"T3","obj":"https://glycosmos.org/glycans/show/G76685HR"},{"id":"A8","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR"},{"id":"A4","pred":"glycosmos_id","subj":"T4","obj":"https://glycosmos.org/glycans/show/G76685HR"},{"id":"A9","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR"},{"id":"A5","pred":"glycosmos_id","subj":"T5","obj":"https://glycosmos.org/glycans/show/G76685HR"},{"id":"A10","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR"}],"text":"Structural and functional-group tuning in the design of neuraminidase inhibitors.\nAnalogues of the disaccharide alpha-NeuAc-(2--\u003e6)-beta-D-Gal-OR have been made by modifications at C-1 and C-6 of the galactose and at C-4 of the NeuAc unit, for structure-activity relationship studies with influenza virus neuraminidase. These studies indicate that for the influenza neuraminidase, a larger aglycon at C-1 of galactose is less preferred, whereas the restriction of the rotamer orientation at C-6 of galactose in the \"tg\" mode favors enzyme binding. Substitution at C-4 of the NeuAc unit has the most profound effect in the influenza neuraminidase hydrolysis and inhibition. For example, azido and acetamido groups at C-4 of the NeuAc units render the sialosides resistant to neuraminidase hydrolysis. However, these derivatives are not inhibitors of the neuraminidase, indicating their lack of binding. On the other hand, a 4-amino substitution of the NeuAc unit not only renders the corresponding sialosides neuraminidase-resistant, but also makes them potent neuraminidase inhibitors. This potent inhibition indicates that the 4-amino groups in these sialosides may engage in favorable interaction with amino acids at the neuraminidase active-site. The conclusion is also supported by docking studies of the carbohydrate structures at the neuraminidase active-site."}

{"project":"mondo_disease","denotations":[{"id":"T1","span":{"begin":289,"end":298},"obj":"Disease"},{"id":"T2","span":{"begin":356,"end":365},"obj":"Disease"},{"id":"T3","span":{"begin":622,"end":631},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0005812"},{"id":"A2","pred":"mondo_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MONDO_0005812"},{"id":"A3","pred":"mondo_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MONDO_0005812"}],"text":"Structural and functional-group tuning in the design of neuraminidase inhibitors.\nAnalogues of the disaccharide alpha-NeuAc-(2--\u003e6)-beta-D-Gal-OR have been made by modifications at C-1 and C-6 of the galactose and at C-4 of the NeuAc unit, for structure-activity relationship studies with influenza virus neuraminidase. These studies indicate that for the influenza neuraminidase, a larger aglycon at C-1 of galactose is less preferred, whereas the restriction of the rotamer orientation at C-6 of galactose in the \"tg\" mode favors enzyme binding. Substitution at C-4 of the NeuAc unit has the most profound effect in the influenza neuraminidase hydrolysis and inhibition. For example, azido and acetamido groups at C-4 of the NeuAc units render the sialosides resistant to neuraminidase hydrolysis. However, these derivatives are not inhibitors of the neuraminidase, indicating their lack of binding. On the other hand, a 4-amino substitution of the NeuAc unit not only renders the corresponding sialosides neuraminidase-resistant, but also makes them potent neuraminidase inhibitors. This potent inhibition indicates that the 4-amino groups in these sialosides may engage in favorable interaction with amino acids at the neuraminidase active-site. The conclusion is also supported by docking studies of the carbohydrate structures at the neuraminidase active-site."}

{"project":"Glycan-GlyCosmos","denotations":[{"id":"T1","span":{"begin":118,"end":123},"obj":"Glycan"},{"id":"T2","span":{"begin":228,"end":233},"obj":"Glycan"},{"id":"T3","span":{"begin":575,"end":580},"obj":"Glycan"},{"id":"T4","span":{"begin":727,"end":732},"obj":"Glycan"},{"id":"T5","span":{"begin":951,"end":956},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G76685HR"},{"id":"A6","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":"A7","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR"},{"id":"A3","pred":"glycosmos_id","subj":"T3","obj":"https://glycosmos.org/glycans/show/G76685HR"},{"id":"A8","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR"},{"id":"A4","pred":"glycosmos_id","subj":"T4","obj":"https://glycosmos.org/glycans/show/G76685HR"},{"id":"A9","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR"},{"id":"A5","pred":"glycosmos_id","subj":"T5","obj":"https://glycosmos.org/glycans/show/G76685HR"},{"id":"A10","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR"}],"text":"Structural and functional-group tuning in the design of neuraminidase inhibitors.\nAnalogues of the disaccharide alpha-NeuAc-(2--\u003e6)-beta-D-Gal-OR have been made by modifications at C-1 and C-6 of the galactose and at C-4 of the NeuAc unit, for structure-activity relationship studies with influenza virus neuraminidase. These studies indicate that for the influenza neuraminidase, a larger aglycon at C-1 of galactose is less preferred, whereas the restriction of the rotamer orientation at C-6 of galactose in the \"tg\" mode favors enzyme binding. Substitution at C-4 of the NeuAc unit has the most profound effect in the influenza neuraminidase hydrolysis and inhibition. For example, azido and acetamido groups at C-4 of the NeuAc units render the sialosides resistant to neuraminidase hydrolysis. However, these derivatives are not inhibitors of the neuraminidase, indicating their lack of binding. On the other hand, a 4-amino substitution of the NeuAc unit not only renders the corresponding sialosides neuraminidase-resistant, but also makes them potent neuraminidase inhibitors. This potent inhibition indicates that the 4-amino groups in these sialosides may engage in favorable interaction with amino acids at the neuraminidase active-site. The conclusion is also supported by docking studies of the carbohydrate structures at the neuraminidase active-site."}

{"project":"GlyCosmos15-UBERON","denotations":[{"id":"T1","span":{"begin":915,"end":919},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0002398"}],"text":"Structural and functional-group tuning in the design of neuraminidase inhibitors.\nAnalogues of the disaccharide alpha-NeuAc-(2--\u003e6)-beta-D-Gal-OR have been made by modifications at C-1 and C-6 of the galactose and at C-4 of the NeuAc unit, for structure-activity relationship studies with influenza virus neuraminidase. These studies indicate that for the influenza neuraminidase, a larger aglycon at C-1 of galactose is less preferred, whereas the restriction of the rotamer orientation at C-6 of galactose in the \"tg\" mode favors enzyme binding. Substitution at C-4 of the NeuAc unit has the most profound effect in the influenza neuraminidase hydrolysis and inhibition. For example, azido and acetamido groups at C-4 of the NeuAc units render the sialosides resistant to neuraminidase hydrolysis. However, these derivatives are not inhibitors of the neuraminidase, indicating their lack of binding. On the other hand, a 4-amino substitution of the NeuAc unit not only renders the corresponding sialosides neuraminidase-resistant, but also makes them potent neuraminidase inhibitors. This potent inhibition indicates that the 4-amino groups in these sialosides may engage in favorable interaction with amino acids at the neuraminidase active-site. The conclusion is also supported by docking studies of the carbohydrate structures at the neuraminidase active-site."}

{"project":"GlyCosmos15-MONDO","denotations":[{"id":"T1","span":{"begin":289,"end":298},"obj":"Disease"},{"id":"T2","span":{"begin":356,"end":365},"obj":"Disease"},{"id":"T3","span":{"begin":622,"end":631},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"MONDO:0005812"},{"id":"A2","pred":"mondo_id","subj":"T2","obj":"MONDO:0005812"},{"id":"A3","pred":"mondo_id","subj":"T3","obj":"MONDO:0005812"}],"namespaces":[{"prefix":"MONDO","uri":"http://purl.obolibrary.org/obo/MONDO_"}],"text":"Structural and functional-group tuning in the design of neuraminidase inhibitors.\nAnalogues of the disaccharide alpha-NeuAc-(2--\u003e6)-beta-D-Gal-OR have been made by modifications at C-1 and C-6 of the galactose and at C-4 of the NeuAc unit, for structure-activity relationship studies with influenza virus neuraminidase. These studies indicate that for the influenza neuraminidase, a larger aglycon at C-1 of galactose is less preferred, whereas the restriction of the rotamer orientation at C-6 of galactose in the \"tg\" mode favors enzyme binding. Substitution at C-4 of the NeuAc unit has the most profound effect in the influenza neuraminidase hydrolysis and inhibition. For example, azido and acetamido groups at C-4 of the NeuAc units render the sialosides resistant to neuraminidase hydrolysis. However, these derivatives are not inhibitors of the neuraminidase, indicating their lack of binding. On the other hand, a 4-amino substitution of the NeuAc unit not only renders the corresponding sialosides neuraminidase-resistant, but also makes them potent neuraminidase inhibitors. This potent inhibition indicates that the 4-amino groups in these sialosides may engage in favorable interaction with amino acids at the neuraminidase active-site. The conclusion is also supported by docking studies of the carbohydrate structures at the neuraminidase active-site."}

{"project":"GlyCosmos15-Sentences","blocks":[{"id":"T1","span":{"begin":0,"end":81},"obj":"Sentence"},{"id":"T2","span":{"begin":82,"end":319},"obj":"Sentence"},{"id":"T3","span":{"begin":320,"end":547},"obj":"Sentence"},{"id":"T4","span":{"begin":548,"end":672},"obj":"Sentence"},{"id":"T5","span":{"begin":673,"end":799},"obj":"Sentence"},{"id":"T6","span":{"begin":800,"end":901},"obj":"Sentence"},{"id":"T7","span":{"begin":902,"end":1085},"obj":"Sentence"},{"id":"T8","span":{"begin":1086,"end":1249},"obj":"Sentence"},{"id":"T9","span":{"begin":1250,"end":1366},"obj":"Sentence"}],"text":"Structural and functional-group tuning in the design of neuraminidase inhibitors.\nAnalogues of the disaccharide alpha-NeuAc-(2--\u003e6)-beta-D-Gal-OR have been made by modifications at C-1 and C-6 of the galactose and at C-4 of the NeuAc unit, for structure-activity relationship studies with influenza virus neuraminidase. These studies indicate that for the influenza neuraminidase, a larger aglycon at C-1 of galactose is less preferred, whereas the restriction of the rotamer orientation at C-6 of galactose in the \"tg\" mode favors enzyme binding. Substitution at C-4 of the NeuAc unit has the most profound effect in the influenza neuraminidase hydrolysis and inhibition. For example, azido and acetamido groups at C-4 of the NeuAc units render the sialosides resistant to neuraminidase hydrolysis. However, these derivatives are not inhibitors of the neuraminidase, indicating their lack of binding. On the other hand, a 4-amino substitution of the NeuAc unit not only renders the corresponding sialosides neuraminidase-resistant, but also makes them potent neuraminidase inhibitors. This potent inhibition indicates that the 4-amino groups in these sialosides may engage in favorable interaction with amino acids at the neuraminidase active-site. The conclusion is also supported by docking studies of the carbohydrate structures at the neuraminidase active-site."}

{"project":"GlyCosmos15-FMA","denotations":[{"id":"T1","span":{"begin":915,"end":919},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"FMA:9712"}],"namespaces":[{"prefix":"FMA","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"Structural and functional-group tuning in the design of neuraminidase inhibitors.\nAnalogues of the disaccharide alpha-NeuAc-(2--\u003e6)-beta-D-Gal-OR have been made by modifications at C-1 and C-6 of the galactose and at C-4 of the NeuAc unit, for structure-activity relationship studies with influenza virus neuraminidase. These studies indicate that for the influenza neuraminidase, a larger aglycon at C-1 of galactose is less preferred, whereas the restriction of the rotamer orientation at C-6 of galactose in the \"tg\" mode favors enzyme binding. Substitution at C-4 of the NeuAc unit has the most profound effect in the influenza neuraminidase hydrolysis and inhibition. For example, azido and acetamido groups at C-4 of the NeuAc units render the sialosides resistant to neuraminidase hydrolysis. However, these derivatives are not inhibitors of the neuraminidase, indicating their lack of binding. On the other hand, a 4-amino substitution of the NeuAc unit not only renders the corresponding sialosides neuraminidase-resistant, but also makes them potent neuraminidase inhibitors. This potent inhibition indicates that the 4-amino groups in these sialosides may engage in favorable interaction with amino acids at the neuraminidase active-site. The conclusion is also supported by docking studies of the carbohydrate structures at the neuraminidase active-site."}

{"project":"GlyCosmos15-MAT","denotations":[{"id":"T1","span":{"begin":915,"end":919},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000091"}],"text":"Structural and functional-group tuning in the design of neuraminidase inhibitors.\nAnalogues of the disaccharide alpha-NeuAc-(2--\u003e6)-beta-D-Gal-OR have been made by modifications at C-1 and C-6 of the galactose and at C-4 of the NeuAc unit, for structure-activity relationship studies with influenza virus neuraminidase. These studies indicate that for the influenza neuraminidase, a larger aglycon at C-1 of galactose is less preferred, whereas the restriction of the rotamer orientation at C-6 of galactose in the \"tg\" mode favors enzyme binding. Substitution at C-4 of the NeuAc unit has the most profound effect in the influenza neuraminidase hydrolysis and inhibition. For example, azido and acetamido groups at C-4 of the NeuAc units render the sialosides resistant to neuraminidase hydrolysis. However, these derivatives are not inhibitors of the neuraminidase, indicating their lack of binding. On the other hand, a 4-amino substitution of the NeuAc unit not only renders the corresponding sialosides neuraminidase-resistant, but also makes them potent neuraminidase inhibitors. This potent inhibition indicates that the 4-amino groups in these sialosides may engage in favorable interaction with amino acids at the neuraminidase active-site. The conclusion is also supported by docking studies of the carbohydrate structures at the neuraminidase active-site."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":915,"end":919},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0002398"}],"text":"Structural and functional-group tuning in the design of neuraminidase inhibitors.\nAnalogues of the disaccharide alpha-NeuAc-(2--\u003e6)-beta-D-Gal-OR have been made by modifications at C-1 and C-6 of the galactose and at C-4 of the NeuAc unit, for structure-activity relationship studies with influenza virus neuraminidase. These studies indicate that for the influenza neuraminidase, a larger aglycon at C-1 of galactose is less preferred, whereas the restriction of the rotamer orientation at C-6 of galactose in the \"tg\" mode favors enzyme binding. Substitution at C-4 of the NeuAc unit has the most profound effect in the influenza neuraminidase hydrolysis and inhibition. For example, azido and acetamido groups at C-4 of the NeuAc units render the sialosides resistant to neuraminidase hydrolysis. However, these derivatives are not inhibitors of the neuraminidase, indicating their lack of binding. On the other hand, a 4-amino substitution of the NeuAc unit not only renders the corresponding sialosides neuraminidase-resistant, but also makes them potent neuraminidase inhibitors. This potent inhibition indicates that the 4-amino groups in these sialosides may engage in favorable interaction with amino acids at the neuraminidase active-site. The conclusion is also supported by docking studies of the carbohydrate structures at the neuraminidase active-site."}

{"project":"Anatomy-MAT","denotations":[{"id":"T1","span":{"begin":915,"end":919},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000091"}],"text":"Structural and functional-group tuning in the design of neuraminidase inhibitors.\nAnalogues of the disaccharide alpha-NeuAc-(2--\u003e6)-beta-D-Gal-OR have been made by modifications at C-1 and C-6 of the galactose and at C-4 of the NeuAc unit, for structure-activity relationship studies with influenza virus neuraminidase. These studies indicate that for the influenza neuraminidase, a larger aglycon at C-1 of galactose is less preferred, whereas the restriction of the rotamer orientation at C-6 of galactose in the \"tg\" mode favors enzyme binding. Substitution at C-4 of the NeuAc unit has the most profound effect in the influenza neuraminidase hydrolysis and inhibition. For example, azido and acetamido groups at C-4 of the NeuAc units render the sialosides resistant to neuraminidase hydrolysis. However, these derivatives are not inhibitors of the neuraminidase, indicating their lack of binding. On the other hand, a 4-amino substitution of the NeuAc unit not only renders the corresponding sialosides neuraminidase-resistant, but also makes them potent neuraminidase inhibitors. This potent inhibition indicates that the 4-amino groups in these sialosides may engage in favorable interaction with amino acids at the neuraminidase active-site. The conclusion is also supported by docking studies of the carbohydrate structures at the neuraminidase active-site."}