| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-131 |
Sentence |
denotes |
Kinetic and spatial interrelationships between ganglioside glycosyltransferases and O-acetyltransferase(s) in human melanoma cells. |
| T1 |
0-131 |
Sentence |
denotes |
Kinetic and spatial interrelationships between ganglioside glycosyltransferases and O-acetyltransferase(s) in human melanoma cells. |
| T2 |
132-258 |
Sentence |
denotes |
The melanoma-associated disialogangliosides 9(7)-O-acetyl-GD3 and 9(7)-O-acetyl-GD2 have been structurally well characterized. |
| T2 |
132-258 |
Sentence |
denotes |
The melanoma-associated disialogangliosides 9(7)-O-acetyl-GD3 and 9(7)-O-acetyl-GD2 have been structurally well characterized. |
| T3 |
259-407 |
Sentence |
denotes |
However, the compartmentalization and sequence of action of the biosynthetic activities responsible for synthesizing these molecules remain obscure. |
| T3 |
259-407 |
Sentence |
denotes |
However, the compartmentalization and sequence of action of the biosynthetic activities responsible for synthesizing these molecules remain obscure. |
| T4 |
408-617 |
Sentence |
denotes |
Here, we have studied the spatial and temporal interrelationships among the activities responsible for the later stages of ganglioside biosynthesis and those for O-acetylation in cultured human melanoma cells. |
| T4 |
408-617 |
Sentence |
denotes |
Here, we have studied the spatial and temporal interrelationships among the activities responsible for the later stages of ganglioside biosynthesis and those for O-acetylation in cultured human melanoma cells. |
| T5 |
618-767 |
Sentence |
denotes |
First, brefeldin A treatment was used to separate biosynthetic steps into compartments distal or proximal to the transport block imposed by the drug. |
| T5 |
618-767 |
Sentence |
denotes |
First, brefeldin A treatment was used to separate biosynthetic steps into compartments distal or proximal to the transport block imposed by the drug. |
| T6 |
768-884 |
Sentence |
denotes |
In keeping with prior reports, GM2/GD2 synthase was consistently rendered inaccessible to its acceptors GM3 and GD3. |
| T6 |
768-884 |
Sentence |
denotes |
In keeping with prior reports, GM2/GD2 synthase was consistently rendered inaccessible to its acceptors GM3 and GD3. |
| T7 |
885-952 |
Sentence |
denotes |
In contrast, the effect on GD3 biosynthesis was cell line-specific. |
| T7 |
885-952 |
Sentence |
denotes |
In contrast, the effect on GD3 biosynthesis was cell line-specific. |
| T8 |
953-1042 |
Sentence |
denotes |
Synthesis of GD3 was nearly abrogated in two lines, while it accumulated in a third line. |
| T8 |
953-1042 |
Sentence |
denotes |
Synthesis of GD3 was nearly abrogated in two lines, while it accumulated in a third line. |
| T9 |
1043-1166 |
Sentence |
denotes |
This indicates that the spatial organization of ganglioside processing activities can vary even between similar cell lines. |
| T9 |
1043-1166 |
Sentence |
denotes |
This indicates that the spatial organization of ganglioside processing activities can vary even between similar cell lines. |
| T10 |
1167-1429 |
Sentence |
denotes |
However, in all cell lines studied, the ratio of 9(7)-O-acetyl-GD3 to GD3 was not changed by brefeldin A, indicating that the majority of ganglioside O-acetyltransferase activity is co-localized with GD3 biosynthetic activity in the same Golgi subcompartment(s). |
| T10 |
1167-1429 |
Sentence |
denotes |
However, in all cell lines studied, the ratio of 9(7)-O-acetyl-GD3 to GD3 was not changed by brefeldin A, indicating that the majority of ganglioside O-acetyltransferase activity is co-localized with GD3 biosynthetic activity in the same Golgi subcompartment(s). |
| T11 |
1430-1583 |
Sentence |
denotes |
As an alternative approach, Golgi-enriched fractions from melanoma cells were incubated with radiolabeled and nonlabeled nucleotide sugars or acetyl-CoA. |
| T11 |
1430-1583 |
Sentence |
denotes |
As an alternative approach, Golgi-enriched fractions from melanoma cells were incubated with radiolabeled and nonlabeled nucleotide sugars or acetyl-CoA. |
| T12 |
1584-1819 |
Sentence |
denotes |
In these preparations, biosynthesis is dependent upon the co-localization of appropriate sugar nucleotide transporters, glycosyltransferases, and acceptors that are endogenously present within intact topologically correct compartments. |
| T12 |
1584-1819 |
Sentence |
denotes |
In these preparations, biosynthesis is dependent upon the co-localization of appropriate sugar nucleotide transporters, glycosyltransferases, and acceptors that are endogenously present within intact topologically correct compartments. |
| T13 |
1820-2012 |
Sentence |
denotes |
Incubations with CMP-Neu5Ac and acetyl-CoA corroborated the results with brefeldin A, co-localizing ganglioside O-acetyltransferase activity in compartments where GD3 biosynthesis takes place. |
| T13 |
1820-2012 |
Sentence |
denotes |
Incubations with CMP-Neu5Ac and acetyl-CoA corroborated the results with brefeldin A, co-localizing ganglioside O-acetyltransferase activity in compartments where GD3 biosynthesis takes place. |
| T14 |
2013-2131 |
Sentence |
denotes |
Analyses with CMP-Neu5Ac and UDP-GalNAc showed that GD2 and GD3 synthesis occur in partially overlapping compartments. |
| T14 |
2013-2131 |
Sentence |
denotes |
Analyses with CMP-Neu5Ac and UDP-GalNAc showed that GD2 and GD3 synthesis occur in partially overlapping compartments. |
| T15 |
2132-2381 |
Sentence |
denotes |
Labeling with acetyl-CoA and UDP-GalNAc indicated that although labeled acetate can be transferred from acetyl-CoA directly to GD2, ganglioside O-acetyltransferase activity does not substantially overlap with the biosynthetic compartment(s) for GD2. |
| T15 |
2132-2381 |
Sentence |
denotes |
Labeling with acetyl-CoA and UDP-GalNAc indicated that although labeled acetate can be transferred from acetyl-CoA directly to GD2, ganglioside O-acetyltransferase activity does not substantially overlap with the biosynthetic compartment(s) for GD2. |
| T16 |
2382-2515 |
Sentence |
denotes |
Instead, O-acetyl-GD3 appears to be co-localized with the compartment of GD2 biosynthesis and serves as an acceptor for GD2 synthase. |
| T16 |
2382-2515 |
Sentence |
denotes |
Instead, O-acetyl-GD3 appears to be co-localized with the compartment of GD2 biosynthesis and serves as an acceptor for GD2 synthase. |
| T17 |
2516-2627 |
Sentence |
denotes |
Thus, both 9-O-acetyl-GD3 and GD2 can be precursors of 9-O-acetyl-GD2, but apparently in distinct compartments. |
| T17 |
2516-2627 |
Sentence |
denotes |
Thus, both 9-O-acetyl-GD3 and GD2 can be precursors of 9-O-acetyl-GD2, but apparently in distinct compartments. |