| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-144 |
Sentence |
denotes |
Characterization of an N-acetylglucosaminyltransferase involved in Aspergillus fumigatus zwitterionic glycoinositolphosphoceramide biosynthesis. |
| T1 |
0-144 |
Sentence |
denotes |
Characterization of an N-acetylglucosaminyltransferase involved in Aspergillus fumigatus zwitterionic glycoinositolphosphoceramide biosynthesis. |
| T1 |
0-144 |
Sentence |
denotes |
Characterization of an N-acetylglucosaminyltransferase involved in Aspergillus fumigatus zwitterionic glycoinositolphosphoceramide biosynthesis. |
| TextSentencer_T2 |
145-302 |
Sentence |
denotes |
Glycoinositolphosphoceramides (GIPCs) are complex sphingolipids present at the plasma membrane of various eukaryotes with the important exception of mammals. |
| T2 |
145-302 |
Sentence |
denotes |
Glycoinositolphosphoceramides (GIPCs) are complex sphingolipids present at the plasma membrane of various eukaryotes with the important exception of mammals. |
| T2 |
145-302 |
Sentence |
denotes |
Glycoinositolphosphoceramides (GIPCs) are complex sphingolipids present at the plasma membrane of various eukaryotes with the important exception of mammals. |
| TextSentencer_T3 |
303-419 |
Sentence |
denotes |
In fungi, these glycosphingolipids commonly contain an α-mannose residue (Man) linked at position 2 of the inositol. |
| T3 |
303-419 |
Sentence |
denotes |
In fungi, these glycosphingolipids commonly contain an α-mannose residue (Man) linked at position 2 of the inositol. |
| T3 |
303-419 |
Sentence |
denotes |
In fungi, these glycosphingolipids commonly contain an α-mannose residue (Man) linked at position 2 of the inositol. |
| TextSentencer_T4 |
420-555 |
Sentence |
denotes |
However, several pathogenic fungi additionally synthesize zwitterionic GIPCs carrying an α-glucosamine residue (GlcN) at this position. |
| T4 |
420-555 |
Sentence |
denotes |
However, several pathogenic fungi additionally synthesize zwitterionic GIPCs carrying an α-glucosamine residue (GlcN) at this position. |
| T4 |
420-555 |
Sentence |
denotes |
However, several pathogenic fungi additionally synthesize zwitterionic GIPCs carrying an α-glucosamine residue (GlcN) at this position. |
| TextSentencer_T5 |
556-763 |
Sentence |
denotes |
In the human pathogen Aspergillus fumigatus, the GlcNα1,2IPC core (where IPC is inositolphosphoceramide) is elongated to Manα1,3Manα1,6GlcNα1,2IPC, which is the most abundant GIPC synthesized by this fungus. |
| T5 |
556-763 |
Sentence |
denotes |
In the human pathogen Aspergillus fumigatus, the GlcNα1,2IPC core (where IPC is inositolphosphoceramide) is elongated to Manα1,3Manα1,6GlcNα1,2IPC, which is the most abundant GIPC synthesized by this fungus. |
| T5 |
556-763 |
Sentence |
denotes |
In the human pathogen Aspergillus fumigatus, the GlcNα1,2IPC core (where IPC is inositolphosphoceramide) is elongated to Manα1,3Manα1,6GlcNα1,2IPC, which is the most abundant GIPC synthesized by this fungus. |
| TextSentencer_T6 |
764-938 |
Sentence |
denotes |
In this study, we identified an A. fumigatus N-acetylglucosaminyltransferase, named GntA, and demonstrate its involvement in the initiation of zwitterionic GIPC biosynthesis. |
| T6 |
764-938 |
Sentence |
denotes |
In this study, we identified an A. fumigatus N-acetylglucosaminyltransferase, named GntA, and demonstrate its involvement in the initiation of zwitterionic GIPC biosynthesis. |
| T6 |
764-938 |
Sentence |
denotes |
In this study, we identified an A. fumigatus N-acetylglucosaminyltransferase, named GntA, and demonstrate its involvement in the initiation of zwitterionic GIPC biosynthesis. |
| TextSentencer_T7 |
939-1130 |
Sentence |
denotes |
Targeted deletion of the gene encoding GntA in A. fumigatus resulted in complete absence of zwitterionic GIPC; a phenotype that could be reverted by episomal expression of GntA in the mutant. |
| T7 |
939-1130 |
Sentence |
denotes |
Targeted deletion of the gene encoding GntA in A. fumigatus resulted in complete absence of zwitterionic GIPC; a phenotype that could be reverted by episomal expression of GntA in the mutant. |
| T7 |
939-1130 |
Sentence |
denotes |
Targeted deletion of the gene encoding GntA in A. fumigatus resulted in complete absence of zwitterionic GIPC; a phenotype that could be reverted by episomal expression of GntA in the mutant. |
| TextSentencer_T8 |
1131-1300 |
Sentence |
denotes |
The N-acetylhexosaminyltransferase activity of GntA was substantiated by production of N-acetylhexosamine-IPC in the yeast Saccharomyces cerevisiae upon GntA expression. |
| T8 |
1131-1300 |
Sentence |
denotes |
The N-acetylhexosaminyltransferase activity of GntA was substantiated by production of N-acetylhexosamine-IPC in the yeast Saccharomyces cerevisiae upon GntA expression. |
| T8 |
1131-1300 |
Sentence |
denotes |
The N-acetylhexosaminyltransferase activity of GntA was substantiated by production of N-acetylhexosamine-IPC in the yeast Saccharomyces cerevisiae upon GntA expression. |
| TextSentencer_T9 |
1301-1551 |
Sentence |
denotes |
Using an in vitro assay, GntA was furthermore shown to use UDP-N-acetylglucosamine as donor substrate to generate a glycolipid product resistant to saponification and to digestion by phosphatidylinositol-phospholipase C as expected for GlcNAcα1,2IPC. |
| T9 |
1301-1551 |
Sentence |
denotes |
Using an in vitro assay, GntA was furthermore shown to use UDP-N-acetylglucosamine as donor substrate to generate a glycolipid product resistant to saponification and to digestion by phosphatidylinositol-phospholipase C as expected for GlcNAcα1,2IPC. |
| T9 |
1301-1551 |
Sentence |
denotes |
Using an in vitro assay, GntA was furthermore shown to use UDP-N-acetylglucosamine as donor substrate to generate a glycolipid product resistant to saponification and to digestion by phosphatidylinositol-phospholipase C as expected for GlcNAcα1,2IPC. |
| TextSentencer_T10 |
1552-1679 |
Sentence |
denotes |
Finally, as the enzymes involved in mannosylation of IPC, GntA was localized to the Golgi apparatus, the site of IPC synthesis. |
| T10 |
1552-1679 |
Sentence |
denotes |
Finally, as the enzymes involved in mannosylation of IPC, GntA was localized to the Golgi apparatus, the site of IPC synthesis. |
| T10 |
1552-1679 |
Sentence |
denotes |
Finally, as the enzymes involved in mannosylation of IPC, GntA was localized to the Golgi apparatus, the site of IPC synthesis. |