| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-107 |
Sentence |
denotes |
The N-X-S/T consensus sequence is required but not sufficient for bacterial N-linked protein glycosylation. |
| T1 |
0-107 |
Sentence |
denotes |
The N-X-S/T consensus sequence is required but not sufficient for bacterial N-linked protein glycosylation. |
| T1 |
0-107 |
Sentence |
denotes |
The N-X-S/T consensus sequence is required but not sufficient for bacterial N-linked protein glycosylation. |
| TextSentencer_T2 |
108-258 |
Sentence |
denotes |
In the Gram-negative bacterium Campylobacter jejuni there is a pgl (protein glycosylation) locus-dependent general N-glycosylation system of proteins. |
| T2 |
108-258 |
Sentence |
denotes |
In the Gram-negative bacterium Campylobacter jejuni there is a pgl (protein glycosylation) locus-dependent general N-glycosylation system of proteins. |
| T2 |
108-258 |
Sentence |
denotes |
In the Gram-negative bacterium Campylobacter jejuni there is a pgl (protein glycosylation) locus-dependent general N-glycosylation system of proteins. |
| TextSentencer_T3 |
259-461 |
Sentence |
denotes |
One of the proteins encoded by pgl locus, PglB, a homolog of the eukaryotic oligosaccharyltransferase component Stt3p, is proposed to function as an oligosaccharyltransferase in this prokaryotic system. |
| T3 |
259-461 |
Sentence |
denotes |
One of the proteins encoded by pgl locus, PglB, a homolog of the eukaryotic oligosaccharyltransferase component Stt3p, is proposed to function as an oligosaccharyltransferase in this prokaryotic system. |
| T3 |
259-461 |
Sentence |
denotes |
One of the proteins encoded by pgl locus, PglB, a homolog of the eukaryotic oligosaccharyltransferase component Stt3p, is proposed to function as an oligosaccharyltransferase in this prokaryotic system. |
| TextSentencer_T4 |
462-654 |
Sentence |
denotes |
The sequence requirements of the acceptor polypeptide for N-glycosylation were analyzed by reverse genetics using the reconstituted glycosylation of the model protein AcrA in Escherichia coli. |
| T4 |
462-654 |
Sentence |
denotes |
The sequence requirements of the acceptor polypeptide for N-glycosylation were analyzed by reverse genetics using the reconstituted glycosylation of the model protein AcrA in Escherichia coli. |
| T4 |
462-654 |
Sentence |
denotes |
The sequence requirements of the acceptor polypeptide for N-glycosylation were analyzed by reverse genetics using the reconstituted glycosylation of the model protein AcrA in Escherichia coli. |
| TextSentencer_T5 |
655-776 |
Sentence |
denotes |
As in eukaryotes, the N-X-S/T sequon is an essential but not a sufficient determinant for N-linked protein glycosylation. |
| T5 |
655-776 |
Sentence |
denotes |
As in eukaryotes, the N-X-S/T sequon is an essential but not a sufficient determinant for N-linked protein glycosylation. |
| T5 |
655-776 |
Sentence |
denotes |
As in eukaryotes, the N-X-S/T sequon is an essential but not a sufficient determinant for N-linked protein glycosylation. |
| TextSentencer_T6 |
777-863 |
Sentence |
denotes |
This conclusion was supported by the analysis of a novel C. jejuni glycoprotein, HisJ. |
| T6 |
777-863 |
Sentence |
denotes |
This conclusion was supported by the analysis of a novel C. jejuni glycoprotein, HisJ. |
| T6 |
777-863 |
Sentence |
denotes |
This conclusion was supported by the analysis of a novel C. jejuni glycoprotein, HisJ. |
| TextSentencer_T7 |
864-938 |
Sentence |
denotes |
Export of the polypeptide to the periplasm was required for glycosylation. |
| T7 |
864-938 |
Sentence |
denotes |
Export of the polypeptide to the periplasm was required for glycosylation. |
| T7 |
864-938 |
Sentence |
denotes |
Export of the polypeptide to the periplasm was required for glycosylation. |
| TextSentencer_T8 |
939-1057 |
Sentence |
denotes |
Our data support the hypothesis that eukaryotic and bacterial N-linked protein glycosylation are homologous processes. |
| T8 |
939-1057 |
Sentence |
denotes |
Our data support the hypothesis that eukaryotic and bacterial N-linked protein glycosylation are homologous processes. |
| T8 |
939-1057 |
Sentence |
denotes |
Our data support the hypothesis that eukaryotic and bacterial N-linked protein glycosylation are homologous processes. |