| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-81 |
Sentence |
denotes |
Structural and functional-group tuning in the design of neuraminidase inhibitors. |
| 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. |
| 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. |
| 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. |
| 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. |
| 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. |
| 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. |
| 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. |
| 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. |
| T9 |
1250-1366 |
Sentence |
denotes |
The conclusion is also supported by docking studies of the carbohydrate structures at the neuraminidase active-site. |