PubMed:7895225
Annnotations
GlyCosmos6-Glycan-Motif-Image
| Id | Subject | Object | Predicate | Lexical cue | image |
|---|---|---|---|---|---|
| T1 | 200-209 | Glycan_Motif | denotes | galactose | https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G68158BT|https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G65889KE |
| T3 | 408-417 | Glycan_Motif | denotes | galactose | https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G68158BT|https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G65889KE |
| T5 | 498-507 | Glycan_Motif | denotes | galactose | https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G68158BT|https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G65889KE |
GlyCosmos6-Glycan-Motif-Structure
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| T1 | 200-209 | https://glytoucan.org/Structures/Glycans/G65889KE | denotes | galactose |
| T2 | 200-209 | https://glytoucan.org/Structures/Glycans/G68158BT | denotes | galactose |
| T3 | 408-417 | https://glytoucan.org/Structures/Glycans/G65889KE | denotes | galactose |
| T4 | 408-417 | https://glytoucan.org/Structures/Glycans/G68158BT | denotes | galactose |
| T5 | 498-507 | https://glytoucan.org/Structures/Glycans/G65889KE | denotes | galactose |
| T6 | 498-507 | https://glytoucan.org/Structures/Glycans/G68158BT | denotes | galactose |
Glycosmos6-MAT
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| T1 | 915-919 | http://purl.obolibrary.org/obo/MAT_0000091 | denotes | hand |
sentences
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| TextSentencer_T1 | 0-81 | Sentence | denotes | Structural and functional-group tuning in the design of neuraminidase inhibitors. |
| TextSentencer_T2 | 82-319 | Sentence | denotes | Analogues of the disaccharide alpha-NeuAc-(2-->6)-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. |
| TextSentencer_T3 | 320-547 | Sentence | denotes | 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. |
| TextSentencer_T4 | 548-672 | Sentence | denotes | Substitution at C-4 of the NeuAc unit has the most profound effect in the influenza neuraminidase hydrolysis and inhibition. |
| TextSentencer_T5 | 673-799 | Sentence | denotes | For example, azido and acetamido groups at C-4 of the NeuAc units render the sialosides resistant to neuraminidase hydrolysis. |
| TextSentencer_T6 | 800-901 | Sentence | denotes | However, these derivatives are not inhibitors of the neuraminidase, indicating their lack of binding. |
| TextSentencer_T7 | 902-1085 | Sentence | denotes | 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. |
| TextSentencer_T8 | 1086-1249 | Sentence | denotes | 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. |
| TextSentencer_T9 | 1250-1366 | Sentence | denotes | The conclusion is also supported by docking studies of the carbohydrate structures at the neuraminidase active-site. |
| T1 | 0-81 | Sentence | denotes | Structural and functional-group tuning in the design of neuraminidase inhibitors. |
| T2 | 82-319 | Sentence | denotes | Analogues of the disaccharide alpha-NeuAc-(2-->6)-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. |
| T3 | 320-547 | Sentence | denotes | 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. |
| T4 | 548-672 | Sentence | denotes | Substitution at C-4 of the NeuAc unit has the most profound effect in the influenza neuraminidase hydrolysis and inhibition. |
| T5 | 673-799 | Sentence | denotes | For example, azido and acetamido groups at C-4 of the NeuAc units render the sialosides resistant to neuraminidase hydrolysis. |
| T6 | 800-901 | Sentence | denotes | However, these derivatives are not inhibitors of the neuraminidase, indicating their lack of binding. |
| T7 | 902-1085 | Sentence | denotes | 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. |
| T8 | 1086-1249 | Sentence | denotes | 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. |
| T9 | 1250-1366 | Sentence | denotes | The conclusion is also supported by docking studies of the carbohydrate structures at the neuraminidase active-site. |
GlyCosmos15-Glycan
| Id | Subject | Object | Predicate | Lexical cue | image |
|---|---|---|---|---|---|
| T1 | 118-123 | Glycan | denotes | NeuAc | https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR |
| T2 | 228-233 | Glycan | denotes | NeuAc | https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR |
| T3 | 575-580 | Glycan | denotes | NeuAc | https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR |
| T4 | 727-732 | Glycan | denotes | NeuAc | https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR |
| T5 | 951-956 | Glycan | denotes | NeuAc | https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR |
mondo_disease
| Id | Subject | Object | Predicate | Lexical cue | mondo_id |
|---|---|---|---|---|---|
| T1 | 289-298 | Disease | denotes | influenza | http://purl.obolibrary.org/obo/MONDO_0005812 |
| T2 | 356-365 | Disease | denotes | influenza | http://purl.obolibrary.org/obo/MONDO_0005812 |
| T3 | 622-631 | Disease | denotes | influenza | http://purl.obolibrary.org/obo/MONDO_0005812 |
Glycan-GlyCosmos
| Id | Subject | Object | Predicate | Lexical cue | image |
|---|---|---|---|---|---|
| T1 | 118-123 | Glycan | denotes | NeuAc | https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR |
| T2 | 228-233 | Glycan | denotes | NeuAc | https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR |
| T3 | 575-580 | Glycan | denotes | NeuAc | https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR |
| T4 | 727-732 | Glycan | denotes | NeuAc | https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR |
| T5 | 951-956 | Glycan | denotes | NeuAc | https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR |
GlyCosmos15-UBERON
| Id | Subject | Object | Predicate | Lexical cue | uberon_id |
|---|---|---|---|---|---|
| T1 | 915-919 | Body_part | denotes | hand | http://purl.obolibrary.org/obo/UBERON_0002398 |
GlyCosmos15-MONDO
| Id | Subject | Object | Predicate | Lexical cue | mondo_id |
|---|---|---|---|---|---|
| T1 | 289-298 | Disease | denotes | influenza | MONDO:0005812 |
| T2 | 356-365 | Disease | denotes | influenza | MONDO:0005812 |
| T3 | 622-631 | Disease | denotes | influenza | MONDO:0005812 |
GlyCosmos15-Sentences
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| T1 | 0-81 | Sentence | denotes | Structural and functional-group tuning in the design of neuraminidase inhibitors. |
| T2 | 82-319 | Sentence | denotes | Analogues of the disaccharide alpha-NeuAc-(2-->6)-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. |
| T3 | 320-547 | Sentence | denotes | 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. |
| T4 | 548-672 | Sentence | denotes | Substitution at C-4 of the NeuAc unit has the most profound effect in the influenza neuraminidase hydrolysis and inhibition. |
| T5 | 673-799 | Sentence | denotes | For example, azido and acetamido groups at C-4 of the NeuAc units render the sialosides resistant to neuraminidase hydrolysis. |
| T6 | 800-901 | Sentence | denotes | However, these derivatives are not inhibitors of the neuraminidase, indicating their lack of binding. |
| T7 | 902-1085 | Sentence | denotes | 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. |
| T8 | 1086-1249 | Sentence | denotes | 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. |
| T9 | 1250-1366 | Sentence | denotes | The conclusion is also supported by docking studies of the carbohydrate structures at the neuraminidase active-site. |
GlyCosmos15-FMA
| Id | Subject | Object | Predicate | Lexical cue | db_id |
|---|---|---|---|---|---|
| T1 | 915-919 | Body_part | denotes | hand | FMA:9712 |
GlyCosmos15-MAT
| Id | Subject | Object | Predicate | Lexical cue | mat_id |
|---|---|---|---|---|---|
| T1 | 915-919 | Body_part | denotes | hand | http://purl.obolibrary.org/obo/MAT_0000091 |
Anatomy-UBERON
| Id | Subject | Object | Predicate | Lexical cue | uberon_id |
|---|---|---|---|---|---|
| T1 | 915-919 | Body_part | denotes | hand | http://purl.obolibrary.org/obo/UBERON_0002398 |
Anatomy-MAT
| Id | Subject | Object | Predicate | Lexical cue | mat_id |
|---|---|---|---|---|---|
| T1 | 915-919 | Body_part | denotes | hand | http://purl.obolibrary.org/obo/MAT_0000091 |