Id |
Subject |
Object |
Predicate |
Lexical cue |
TextSentencer_T1 |
0-127 |
Sentence |
denotes |
Sialyltransferases with enhanced legionaminic acid transferase activity for the preparation of analogs of sialoglycoconjugates. |
T1 |
0-127 |
Sentence |
denotes |
Sialyltransferases with enhanced legionaminic acid transferase activity for the preparation of analogs of sialoglycoconjugates. |
T1 |
0-127 |
Sentence |
denotes |
Sialyltransferases with enhanced legionaminic acid transferase activity for the preparation of analogs of sialoglycoconjugates. |
TextSentencer_T2 |
128-269 |
Sentence |
denotes |
Legionaminic acids (Leg) are bacterial analogs of neuraminic acid, with the same stereochemistry but different substituents at C5, C7 and C9. |
T2 |
128-269 |
Sentence |
denotes |
Legionaminic acids (Leg) are bacterial analogs of neuraminic acid, with the same stereochemistry but different substituents at C5, C7 and C9. |
T2 |
128-269 |
Sentence |
denotes |
Legionaminic acids (Leg) are bacterial analogs of neuraminic acid, with the same stereochemistry but different substituents at C5, C7 and C9. |
TextSentencer_T3 |
270-575 |
Sentence |
denotes |
Hence they may be incorporated into useful analogs of sialoglycoconjugates, and we previously reported two sialyltransferases that could utilize cytidine monophosphate (CMP)-Leg5Ac7Ac for preparation of Leg glycoconjugates, which were resistant to sialidases [Watson DC, Leclerc S, Wakarchuk WW, Young NM. |
T3 |
270-575 |
Sentence |
denotes |
Hence they may be incorporated into useful analogs of sialoglycoconjugates, and we previously reported two sialyltransferases that could utilize cytidine monophosphate (CMP)-Leg5Ac7Ac for preparation of Leg glycoconjugates, which were resistant to sialidases [Watson DC, Leclerc S, Wakarchuk WW, Young NM. |
T3 |
270-575 |
Sentence |
denotes |
Hence they may be incorporated into useful analogs of sialoglycoconjugates, and we previously reported two sialyltransferases that could utilize cytidine monophosphate (CMP)-Leg5Ac7Ac for preparation of Leg glycoconjugates, which were resistant to sialidases [Watson DC, Leclerc S, Wakarchuk WW, Young NM. |
TextSentencer_T4 |
576-581 |
Sentence |
denotes |
2011. |
T4 |
576-581 |
Sentence |
denotes |
2011. |
T4 |
576-581 |
Sentence |
denotes |
2011. |
TextSentencer_T5 |
582-696 |
Sentence |
denotes |
Enzymatic synthesis and properties of glycoconjugates with legionaminic acid as a replacement for neuraminic acid. |
T5 |
582-696 |
Sentence |
denotes |
Enzymatic synthesis and properties of glycoconjugates with legionaminic acid as a replacement for neuraminic acid. |
T5 |
582-696 |
Sentence |
denotes |
Enzymatic synthesis and properties of glycoconjugates with legionaminic acid as a replacement for neuraminic acid. |
TextSentencer_T6 |
697-710 |
Sentence |
denotes |
Glycobiology. |
T6 |
697-710 |
Sentence |
denotes |
Glycobiology. |
T6 |
697-723 |
Sentence |
denotes |
Glycobiology. 21:99-108.]. |
TextSentencer_T7 |
711-723 |
Sentence |
denotes |
21:99-108.]. |
T7 |
711-723 |
Sentence |
denotes |
21:99-108.]. |
TextSentencer_T8 |
724-800 |
Sentence |
denotes |
These were the porcine ST3Gal1 and Pasteurella multocida sialyltransferases. |
T7 |
724-800 |
Sentence |
denotes |
These were the porcine ST3Gal1 and Pasteurella multocida sialyltransferases. |
T8 |
724-800 |
Sentence |
denotes |
These were the porcine ST3Gal1 and Pasteurella multocida sialyltransferases. |
TextSentencer_T9 |
801-910 |
Sentence |
denotes |
We now report two additional sialyltransferases with superior Leg-transferase properties to the previous two. |
T8 |
801-910 |
Sentence |
denotes |
We now report two additional sialyltransferases with superior Leg-transferase properties to the previous two. |
T9 |
801-910 |
Sentence |
denotes |
We now report two additional sialyltransferases with superior Leg-transferase properties to the previous two. |
TextSentencer_T10 |
911-1216 |
Sentence |
denotes |
These are (i) a truncated form of a Photobacterium α2,6-sialyltransferase with an Ala-Met mutation in its active site, and (ii) an α2,3-sialyltransferase from Neisseria meningitidis MC58 with a higher transferase activity than the P. multocida enzyme, with either CMP-Neu5Ac or CMP-Leg5Ac7Ac as the donor. |
T9 |
911-1216 |
Sentence |
denotes |
These are (i) a truncated form of a Photobacterium α2,6-sialyltransferase with an Ala-Met mutation in its active site, and (ii) an α2,3-sialyltransferase from Neisseria meningitidis MC58 with a higher transferase activity than the P. multocida enzyme, with either CMP-Neu5Ac or CMP-Leg5Ac7Ac as the donor. |
T10 |
911-1216 |
Sentence |
denotes |
These are (i) a truncated form of a Photobacterium α2,6-sialyltransferase with an Ala-Met mutation in its active site, and (ii) an α2,3-sialyltransferase from Neisseria meningitidis MC58 with a higher transferase activity than the P. multocida enzyme, with either CMP-Neu5Ac or CMP-Leg5Ac7Ac as the donor. |
TextSentencer_T11 |
1217-1372 |
Sentence |
denotes |
These enzymes will enable the production of useful Leg5Ac7Ac glycoconjugate derivatives with either α2,6 or α2,3 linkages and unique biological properties. |
T10 |
1217-1372 |
Sentence |
denotes |
These enzymes will enable the production of useful Leg5Ac7Ac glycoconjugate derivatives with either α2,6 or α2,3 linkages and unique biological properties. |
T11 |
1217-1372 |
Sentence |
denotes |
These enzymes will enable the production of useful Leg5Ac7Ac glycoconjugate derivatives with either α2,6 or α2,3 linkages and unique biological properties. |