| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-80 |
Sentence |
denotes |
Asparagine-linked protein glycosylation: from eukaryotic to prokaryotic systems. |
| T1 |
0-80 |
Sentence |
denotes |
Asparagine-linked protein glycosylation: from eukaryotic to prokaryotic systems. |
| T1 |
0-80 |
Sentence |
denotes |
Asparagine-linked protein glycosylation: from eukaryotic to prokaryotic systems. |
| TextSentencer_T2 |
81-188 |
Sentence |
denotes |
Asparagine-linked protein glycosylation is a prevalent protein modification reaction in eukaryotic systems. |
| T2 |
81-188 |
Sentence |
denotes |
Asparagine-linked protein glycosylation is a prevalent protein modification reaction in eukaryotic systems. |
| T2 |
81-188 |
Sentence |
denotes |
Asparagine-linked protein glycosylation is a prevalent protein modification reaction in eukaryotic systems. |
| TextSentencer_T3 |
189-408 |
Sentence |
denotes |
This process involves the co-translational transfer of a pre-assembled tetradecasaccharide from a dolichyl-pyrophosphate donor to the asparagine side chain of nascent proteins at the endoplasmic reticulum (ER) membrane. |
| T3 |
189-408 |
Sentence |
denotes |
This process involves the co-translational transfer of a pre-assembled tetradecasaccharide from a dolichyl-pyrophosphate donor to the asparagine side chain of nascent proteins at the endoplasmic reticulum (ER) membrane. |
| T3 |
189-408 |
Sentence |
denotes |
This process involves the co-translational transfer of a pre-assembled tetradecasaccharide from a dolichyl-pyrophosphate donor to the asparagine side chain of nascent proteins at the endoplasmic reticulum (ER) membrane. |
| TextSentencer_T4 |
409-535 |
Sentence |
denotes |
Recently, the first such system of N-linked glycosylation was discovered in the Gram-negative bacterium, Campylobacter jejuni. |
| T4 |
409-535 |
Sentence |
denotes |
Recently, the first such system of N-linked glycosylation was discovered in the Gram-negative bacterium, Campylobacter jejuni. |
| T4 |
409-535 |
Sentence |
denotes |
Recently, the first such system of N-linked glycosylation was discovered in the Gram-negative bacterium, Campylobacter jejuni. |
| TextSentencer_T5 |
536-730 |
Sentence |
denotes |
Glycosylation in this organism involves the transfer of a heptasaccharide from an undecaprenyl-pyrophosphate donor to the asparagine side chain of proteins at the bacterial periplasmic membrane. |
| T5 |
536-730 |
Sentence |
denotes |
Glycosylation in this organism involves the transfer of a heptasaccharide from an undecaprenyl-pyrophosphate donor to the asparagine side chain of proteins at the bacterial periplasmic membrane. |
| T5 |
536-730 |
Sentence |
denotes |
Glycosylation in this organism involves the transfer of a heptasaccharide from an undecaprenyl-pyrophosphate donor to the asparagine side chain of proteins at the bacterial periplasmic membrane. |
| TextSentencer_T6 |
731-956 |
Sentence |
denotes |
Here we provide a detailed comparison of the machinery involved in the N-linked glycosylation systems of eukaryotic organisms, exemplified by the yeast Saccharomyces cerevisiae, with that of the bacterial system in C. jejuni. |
| T6 |
731-956 |
Sentence |
denotes |
Here we provide a detailed comparison of the machinery involved in the N-linked glycosylation systems of eukaryotic organisms, exemplified by the yeast Saccharomyces cerevisiae, with that of the bacterial system in C. jejuni. |
| T6 |
731-956 |
Sentence |
denotes |
Here we provide a detailed comparison of the machinery involved in the N-linked glycosylation systems of eukaryotic organisms, exemplified by the yeast Saccharomyces cerevisiae, with that of the bacterial system in C. jejuni. |
| TextSentencer_T7 |
957-1178 |
Sentence |
denotes |
The two systems display significant similarities and the relative simplicity of the bacterial glycosylation process could provide a model system that can be used to decipher the complex eukaryotic glycosylation machinery. |
| T7 |
957-1178 |
Sentence |
denotes |
The two systems display significant similarities and the relative simplicity of the bacterial glycosylation process could provide a model system that can be used to decipher the complex eukaryotic glycosylation machinery. |
| T7 |
957-1178 |
Sentence |
denotes |
The two systems display significant similarities and the relative simplicity of the bacterial glycosylation process could provide a model system that can be used to decipher the complex eukaryotic glycosylation machinery. |