| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-90 |
Sentence |
denotes |
Structural basis for the resistance of Tay-Sachs ganglioside GM2 to enzymatic degradation. |
| T2 |
91-454 |
Sentence |
denotes |
To understand the reason why, in the absence of GM2 activator protein, the GalNAc and the NeuAc in GM2 (GalNAcbeta1-->4(NeuAcalpha2-->3)Galbeta1-->4Glcbet a1-1'Cer) are refractory to beta-hexosaminidase A and sialidase, respectively, we have recently synthesized a linkage analogue of GM2 named 6'GM2 (GalNAcbeta1-->6(NeuAcalpha2-->3)Galbeta1-->4Glcbet a1-1'Cer). |
| T3 |
455-627 |
Sentence |
denotes |
While GM2 has GalNAcbeta1-->4Gal linkage, 6'-GM2 has GalNAcbeta1-->6Gal linkage (Ishida, H., Ito, Y., Tanahashi, E., Li, Y.-T., Kiso, M., and Hasegawa, A. (1997) Carbohydr. |
| T4 |
628-632 |
Sentence |
denotes |
Res. |
| T5 |
633-647 |
Sentence |
denotes |
302, 223-227). |
| T6 |
648-837 |
Sentence |
denotes |
We have studied the enzymatic susceptibilities of GM2 and 6'GM2, as well as that of the oligosaccharides derived from GM2, asialo-GM2 (GalNAcbeta1-->4Galbeta1--> 4Glcbeta1-1'Cer) and 6'GM2. |
| T7 |
838-976 |
Sentence |
denotes |
In addition, the conformational properties of both GM2 and 6'GM2 were analyzed using NMR spectroscopy and molecular mechanics computation. |
| T8 |
977-1138 |
Sentence |
denotes |
In sharp contrast to GM2, the GalNAc and the Neu5Ac of 6'GM2 were readily hydrolyzed by beta-hexosaminidase A and sialidase, respectively, without GM2 activator. |
| T9 |
1139-1280 |
Sentence |
denotes |
Among the oligosaccharides derived from GM2, asialo-GM2, and 6'GM2, only the oligosaccharide from GM2 was resistant to beta-hexosaminidase A. |
| T10 |
1281-1513 |
Sentence |
denotes |
Conformational analyses revealed that while GM2 has a compact and rigid oligosaccharide head group, 6'GM2 has an open spatial arrangement of the sugar units, with the GalNAc and the Neu5Ac freely accessible to external interactions. |
| T11 |
1514-1670 |
Sentence |
denotes |
These results strongly indicate that the resistance of GM2 to enzymatic hydrolysis is because of the specific rigid conformation of the GM2 oligosaccharide. |
