| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-76 |
Sentence |
denotes |
CST-II's recognition domain for acceptor substrates in α-(2→8)-sialylations. |
| T1 |
0-76 |
Sentence |
denotes |
CST-II's recognition domain for acceptor substrates in α-(2→8)-sialylations. |
| TextSentencer_T2 |
77-216 |
Sentence |
denotes |
CST-II is a bacterial sialyltransferase known for its ability to perform α-(2→8)-sialylations using GM(3) related trisaccharide substrates. |
| T2 |
77-216 |
Sentence |
denotes |
CST-II is a bacterial sialyltransferase known for its ability to perform α-(2→8)-sialylations using GM(3) related trisaccharide substrates. |
| TextSentencer_T3 |
217-422 |
Sentence |
denotes |
Previously, we probed the enzyme's substrate specificity and developed an efficient synthesis for α-(2→8)-oligosialosides, and we suggested that CST-II could have a very small substrate recognition domain. |
| T3 |
217-422 |
Sentence |
denotes |
Previously, we probed the enzyme's substrate specificity and developed an efficient synthesis for α-(2→8)-oligosialosides, and we suggested that CST-II could have a very small substrate recognition domain. |
| TextSentencer_T4 |
423-511 |
Sentence |
denotes |
Here we report our full studies on CST-II's recognition feature for acceptor substrates. |
| T4 |
423-511 |
Sentence |
denotes |
Here we report our full studies on CST-II's recognition feature for acceptor substrates. |
| TextSentencer_T5 |
512-657 |
Sentence |
denotes |
The current study further demonstrates the versatility of CST-II in preparing complex oligosaccharides that contain α-(2→8)-oligosialyl moieties. |
| T5 |
512-657 |
Sentence |
denotes |
The current study further demonstrates the versatility of CST-II in preparing complex oligosaccharides that contain α-(2→8)-oligosialyl moieties. |
