| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-84 |
Sentence |
denotes |
Selective biochemical labeling of Campylobacter jejuni cell-surface glycoconjugates. |
| T1 |
0-84 |
Sentence |
denotes |
Selective biochemical labeling of Campylobacter jejuni cell-surface glycoconjugates. |
| TextSentencer_T2 |
85-252 |
Sentence |
denotes |
The display of cell-surface glycolipids and glycoproteins is essential for the motility, adhesion and colonization of pathogenic bacteria such as Campylobacter jejuni. |
| T2 |
85-252 |
Sentence |
denotes |
The display of cell-surface glycolipids and glycoproteins is essential for the motility, adhesion and colonization of pathogenic bacteria such as Campylobacter jejuni. |
| TextSentencer_T3 |
253-516 |
Sentence |
denotes |
Recently, the cell-surface display of C. jejuni glycoconjugates has been the focus of considerable attention; however, our understanding of the roles that glycosylation plays in bacteria still pales in comparison with our understanding of mammalian glycosylation. |
| T3 |
253-516 |
Sentence |
denotes |
Recently, the cell-surface display of C. jejuni glycoconjugates has been the focus of considerable attention; however, our understanding of the roles that glycosylation plays in bacteria still pales in comparison with our understanding of mammalian glycosylation. |
| TextSentencer_T4 |
517-724 |
Sentence |
denotes |
One of the reasons for this is that carbohydrate metabolic labeling, a powerful tool for studying mammalian glycans, is difficult to establish in bacterial systems and has a significantly more limited scope. |
| T4 |
517-724 |
Sentence |
denotes |
One of the reasons for this is that carbohydrate metabolic labeling, a powerful tool for studying mammalian glycans, is difficult to establish in bacterial systems and has a significantly more limited scope. |
| TextSentencer_T5 |
725-851 |
Sentence |
denotes |
Herein, we report the development of an alternative strategy that can be used to study bacterial cell-surface glycoconjugates. |
| T5 |
725-851 |
Sentence |
denotes |
Herein, we report the development of an alternative strategy that can be used to study bacterial cell-surface glycoconjugates. |
| TextSentencer_T6 |
852-965 |
Sentence |
denotes |
Galactose oxidase (GalO) is used to generate an aldehyde at C-6 of terminal GalNAc residues of C. jejuni glycans. |
| T6 |
852-965 |
Sentence |
denotes |
Galactose oxidase (GalO) is used to generate an aldehyde at C-6 of terminal GalNAc residues of C. jejuni glycans. |
| TextSentencer_T7 |
966-1077 |
Sentence |
denotes |
This newly generated aldehyde can be conjugated with aminooxy-functionalized purification tags or fluorophores. |
| T7 |
966-1077 |
Sentence |
denotes |
This newly generated aldehyde can be conjugated with aminooxy-functionalized purification tags or fluorophores. |
| TextSentencer_T8 |
1078-1230 |
Sentence |
denotes |
The label can be targeted towards specific glycoconjugates using C. jejuni mutant strains with N-glycan or lipo-oligosaccharides (LOS) assembly defects. |
| T8 |
1078-1230 |
Sentence |
denotes |
The label can be targeted towards specific glycoconjugates using C. jejuni mutant strains with N-glycan or lipo-oligosaccharides (LOS) assembly defects. |
| TextSentencer_T9 |
1231-1456 |
Sentence |
denotes |
GalO-catalyzed labeling of cell-surface glycoproteins with biotin, allowed for the purification and identification of known extracellular N-linked glycoproteins as well as a recently identified O-linked glycan modifying PorA. |
| T9 |
1231-1456 |
Sentence |
denotes |
GalO-catalyzed labeling of cell-surface glycoproteins with biotin, allowed for the purification and identification of known extracellular N-linked glycoproteins as well as a recently identified O-linked glycan modifying PorA. |
| TextSentencer_T10 |
1457-1652 |
Sentence |
denotes |
To expand the scope of the GalO reaction, live-cell fluorescent labeling of C. jejuni was used to compare the levels of surface-exposed LOS to the levels of N-glycosylated, cell-surface proteins. |
| T10 |
1457-1652 |
Sentence |
denotes |
To expand the scope of the GalO reaction, live-cell fluorescent labeling of C. jejuni was used to compare the levels of surface-exposed LOS to the levels of N-glycosylated, cell-surface proteins. |
| TextSentencer_T11 |
1653-1841 |
Sentence |
denotes |
While this study focuses on the GalO-catalyzed labeling of C. jejuni, it can in principle be used to evaluate glycosylation patterns and identify glycoproteins of interest in any bacteria. |
| T11 |
1653-1841 |
Sentence |
denotes |
While this study focuses on the GalO-catalyzed labeling of C. jejuni, it can in principle be used to evaluate glycosylation patterns and identify glycoproteins of interest in any bacteria. |