| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-101 |
Sentence |
denotes |
Structural elucidation of an α-1,2-mannosidase resistant oligosaccharide produced in Pichia pastoris. |
| T1 |
0-101 |
Sentence |
denotes |
Structural elucidation of an α-1,2-mannosidase resistant oligosaccharide produced in Pichia pastoris. |
| T1 |
0-101 |
Sentence |
denotes |
Structural elucidation of an α-1,2-mannosidase resistant oligosaccharide produced in Pichia pastoris. |
| TextSentencer_T2 |
102-346 |
Sentence |
denotes |
The N-glycosylation pathway in Pichia pastoris has been humanized by the deletion of genes responsible for fungal-type glycosylation (high mannose) as well as the introduction of heterologous genes capable of forming human-like N-glycosylation. |
| T2 |
102-346 |
Sentence |
denotes |
The N-glycosylation pathway in Pichia pastoris has been humanized by the deletion of genes responsible for fungal-type glycosylation (high mannose) as well as the introduction of heterologous genes capable of forming human-like N-glycosylation. |
| T2 |
102-346 |
Sentence |
denotes |
The N-glycosylation pathway in Pichia pastoris has been humanized by the deletion of genes responsible for fungal-type glycosylation (high mannose) as well as the introduction of heterologous genes capable of forming human-like N-glycosylation. |
| TextSentencer_T3 |
347-432 |
Sentence |
denotes |
This results in a yeast host that is capable of expressing therapeutic glycoproteins. |
| T3 |
347-432 |
Sentence |
denotes |
This results in a yeast host that is capable of expressing therapeutic glycoproteins. |
| T3 |
347-432 |
Sentence |
denotes |
This results in a yeast host that is capable of expressing therapeutic glycoproteins. |
| TextSentencer_T4 |
433-611 |
Sentence |
denotes |
A thorough investigation was performed to examine whether glycoproteins expressed in glycoengineered P. pastoris strains may contain residual fungal-type high-mannose structures. |
| T4 |
433-611 |
Sentence |
denotes |
A thorough investigation was performed to examine whether glycoproteins expressed in glycoengineered P. pastoris strains may contain residual fungal-type high-mannose structures. |
| T4 |
433-611 |
Sentence |
denotes |
A thorough investigation was performed to examine whether glycoproteins expressed in glycoengineered P. pastoris strains may contain residual fungal-type high-mannose structures. |
| TextSentencer_T5 |
612-883 |
Sentence |
denotes |
In a pool of N-linked glycans enzymatically released by protein N-glycosidase from a reporter glycoprotein expressed in a developmental glycoengineered P. pastoris strain, an oligosaccharide with a mass consistent with a Hexose(9)GlcNAc(2) oligosaccharide was identified. |
| T5 |
612-883 |
Sentence |
denotes |
In a pool of N-linked glycans enzymatically released by protein N-glycosidase from a reporter glycoprotein expressed in a developmental glycoengineered P. pastoris strain, an oligosaccharide with a mass consistent with a Hexose(9)GlcNAc(2) oligosaccharide was identified. |
| T5 |
612-883 |
Sentence |
denotes |
In a pool of N-linked glycans enzymatically released by protein N-glycosidase from a reporter glycoprotein expressed in a developmental glycoengineered P. pastoris strain, an oligosaccharide with a mass consistent with a Hexose(9)GlcNAc(2) oligosaccharide was identified. |
| TextSentencer_T6 |
884-1045 |
Sentence |
denotes |
When this structure was analyzed by a normal-phase high-performance liquid chromatography (HPLC), its retention time was identical to a Man(9)GlcNAc(2) standard. |
| T6 |
884-1045 |
Sentence |
denotes |
When this structure was analyzed by a normal-phase high-performance liquid chromatography (HPLC), its retention time was identical to a Man(9)GlcNAc(2) standard. |
| T6 |
884-1045 |
Sentence |
denotes |
When this structure was analyzed by a normal-phase high-performance liquid chromatography (HPLC), its retention time was identical to a Man(9)GlcNAc(2) standard. |
| TextSentencer_T7 |
1046-1279 |
Sentence |
denotes |
However, this Hexose(9)GlcNAc(2) oligosaccharide was found to be resistant to α-1,2-mannosidase as well as endomannosidase, which preferentially catabolizes endoplasmic reticulum oligosaccharides containing terminal α-linked glucose. |
| T7 |
1046-1279 |
Sentence |
denotes |
However, this Hexose(9)GlcNAc(2) oligosaccharide was found to be resistant to α-1,2-mannosidase as well as endomannosidase, which preferentially catabolizes endoplasmic reticulum oligosaccharides containing terminal α-linked glucose. |
| T7 |
1046-1279 |
Sentence |
denotes |
However, this Hexose(9)GlcNAc(2) oligosaccharide was found to be resistant to α-1,2-mannosidase as well as endomannosidase, which preferentially catabolizes endoplasmic reticulum oligosaccharides containing terminal α-linked glucose. |
| TextSentencer_T8 |
1280-1633 |
Sentence |
denotes |
To further characterize this oligosaccharide, we purified the Hexose(9)GlcNAc(2) oligosaccharide by HPLC and analyzed the structure by high-field one-dimensional (1D) and two-dimensional (2D) (1)H NMR (nuclear magnetic resonance) spectroscopy followed by structural elucidation by homonuclear and heteronuclear 1D and 2D (1)H and (13)C NMR spectroscopy. |
| T8 |
1280-1633 |
Sentence |
denotes |
To further characterize this oligosaccharide, we purified the Hexose(9)GlcNAc(2) oligosaccharide by HPLC and analyzed the structure by high-field one-dimensional (1D) and two-dimensional (2D) (1)H NMR (nuclear magnetic resonance) spectroscopy followed by structural elucidation by homonuclear and heteronuclear 1D and 2D (1)H and (13)C NMR spectroscopy. |
| T8 |
1280-1633 |
Sentence |
denotes |
To further characterize this oligosaccharide, we purified the Hexose(9)GlcNAc(2) oligosaccharide by HPLC and analyzed the structure by high-field one-dimensional (1D) and two-dimensional (2D) (1)H NMR (nuclear magnetic resonance) spectroscopy followed by structural elucidation by homonuclear and heteronuclear 1D and 2D (1)H and (13)C NMR spectroscopy. |
| TextSentencer_T9 |
1634-1816 |
Sentence |
denotes |
The results of these experiments lead to the identification of an oligosaccharide α-Man-(1 → 2)-β-Man-(1 → 2)-β-Man-(1 → 2)-α-Man-(1 → 2) moiety as part of a tri-antennary structure. |
| T9 |
1634-1816 |
Sentence |
denotes |
The results of these experiments lead to the identification of an oligosaccharide α-Man-(1 → 2)-β-Man-(1 → 2)-β-Man-(1 → 2)-α-Man-(1 → 2) moiety as part of a tri-antennary structure. |
| T9 |
1634-1816 |
Sentence |
denotes |
The results of these experiments lead to the identification of an oligosaccharide α-Man-(1 → 2)-β-Man-(1 → 2)-β-Man-(1 → 2)-α-Man-(1 → 2) moiety as part of a tri-antennary structure. |
| TextSentencer_T10 |
1817-1953 |
Sentence |
denotes |
The difference in enzymatic reactivity can be attributed to multiple β-linkages on the α-1,3 arm of the Man(9)GlcNAc(2) oligosaccharide. |
| T10 |
1817-1953 |
Sentence |
denotes |
The difference in enzymatic reactivity can be attributed to multiple β-linkages on the α-1,3 arm of the Man(9)GlcNAc(2) oligosaccharide. |
| T10 |
1817-1953 |
Sentence |
denotes |
The difference in enzymatic reactivity can be attributed to multiple β-linkages on the α-1,3 arm of the Man(9)GlcNAc(2) oligosaccharide. |