| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-194 |
Sentence |
denotes |
Characterization of exogenous bacterial oligosaccharyltransferases in Escherichia coli reveals the potential for O-linked protein glycosylation in Vibrio cholerae and Burkholderia thailandensis. |
| T1 |
0-194 |
Sentence |
denotes |
Characterization of exogenous bacterial oligosaccharyltransferases in Escherichia coli reveals the potential for O-linked protein glycosylation in Vibrio cholerae and Burkholderia thailandensis. |
| T1 |
0-194 |
Sentence |
denotes |
Characterization of exogenous bacterial oligosaccharyltransferases in Escherichia coli reveals the potential for O-linked protein glycosylation in Vibrio cholerae and Burkholderia thailandensis. |
| TextSentencer_T2 |
195-313 |
Sentence |
denotes |
Bacterial protein glycosylation systems from varying species have been functionally reconstituted in Escherichia coli. |
| T2 |
195-313 |
Sentence |
denotes |
Bacterial protein glycosylation systems from varying species have been functionally reconstituted in Escherichia coli. |
| T2 |
195-313 |
Sentence |
denotes |
Bacterial protein glycosylation systems from varying species have been functionally reconstituted in Escherichia coli. |
| TextSentencer_T3 |
314-544 |
Sentence |
denotes |
Both N- and O-linked glycosylation pathways, in which the glycans are first assembled onto lipid carriers and subsequently transferred to acceptor proteins by an oligosaccharyltransferase (OTase), have been documented in bacteria. |
| T3 |
314-544 |
Sentence |
denotes |
Both N- and O-linked glycosylation pathways, in which the glycans are first assembled onto lipid carriers and subsequently transferred to acceptor proteins by an oligosaccharyltransferase (OTase), have been documented in bacteria. |
| T3 |
314-544 |
Sentence |
denotes |
Both N- and O-linked glycosylation pathways, in which the glycans are first assembled onto lipid carriers and subsequently transferred to acceptor proteins by an oligosaccharyltransferase (OTase), have been documented in bacteria. |
| TextSentencer_T4 |
545-708 |
Sentence |
denotes |
The identification and characterization of novel OTases with different properties may provide new tools for engineering glycoproteins of biotechnological interest. |
| T4 |
545-708 |
Sentence |
denotes |
The identification and characterization of novel OTases with different properties may provide new tools for engineering glycoproteins of biotechnological interest. |
| T4 |
545-708 |
Sentence |
denotes |
The identification and characterization of novel OTases with different properties may provide new tools for engineering glycoproteins of biotechnological interest. |
| TextSentencer_T5 |
709-854 |
Sentence |
denotes |
In the case of OTases involved in O-glycosylation (O-OTases), there is very low sequence homology between those from different bacterial species. |
| T5 |
709-854 |
Sentence |
denotes |
In the case of OTases involved in O-glycosylation (O-OTases), there is very low sequence homology between those from different bacterial species. |
| T5 |
709-854 |
Sentence |
denotes |
In the case of OTases involved in O-glycosylation (O-OTases), there is very low sequence homology between those from different bacterial species. |
| TextSentencer_T6 |
855-991 |
Sentence |
denotes |
The Wzy_C signature domain common to these enzymes is also present in WaaL ligases; enzymes involved in lipopolysaccharide biosynthesis. |
| T6 |
855-991 |
Sentence |
denotes |
The Wzy_C signature domain common to these enzymes is also present in WaaL ligases; enzymes involved in lipopolysaccharide biosynthesis. |
| T6 |
855-991 |
Sentence |
denotes |
The Wzy_C signature domain common to these enzymes is also present in WaaL ligases; enzymes involved in lipopolysaccharide biosynthesis. |
| TextSentencer_T7 |
992-1084 |
Sentence |
denotes |
Therefore, the identification of O-OTases using solely bioinformatic methods is problematic. |
| T7 |
992-1084 |
Sentence |
denotes |
Therefore, the identification of O-OTases using solely bioinformatic methods is problematic. |
| T7 |
992-1084 |
Sentence |
denotes |
Therefore, the identification of O-OTases using solely bioinformatic methods is problematic. |
| TextSentencer_T8 |
1085-1222 |
Sentence |
denotes |
The hypothetical proteins BTH_I0650 from Burkholderia thailandensis E264 and VC0393 from Vibrio cholerae N16961 contain the Wzy_C domain. |
| T8 |
1085-1222 |
Sentence |
denotes |
The hypothetical proteins BTH_I0650 from Burkholderia thailandensis E264 and VC0393 from Vibrio cholerae N16961 contain the Wzy_C domain. |
| T8 |
1085-1222 |
Sentence |
denotes |
The hypothetical proteins BTH_I0650 from Burkholderia thailandensis E264 and VC0393 from Vibrio cholerae N16961 contain the Wzy_C domain. |
| TextSentencer_T9 |
1223-1408 |
Sentence |
denotes |
In this work, we demonstrate that both proteins have O-OTase activity and renamed them PglL(Bt) and PglL(Vc), respectively, similar to the Neisseria meningitidis counterpart (PglL(Nm)). |
| T9 |
1223-1408 |
Sentence |
denotes |
In this work, we demonstrate that both proteins have O-OTase activity and renamed them PglL(Bt) and PglL(Vc), respectively, similar to the Neisseria meningitidis counterpart (PglL(Nm)). |
| T9 |
1223-1408 |
Sentence |
denotes |
In this work, we demonstrate that both proteins have O-OTase activity and renamed them PglL(Bt) and PglL(Vc), respectively, similar to the Neisseria meningitidis counterpart (PglL(Nm)). |
| TextSentencer_T10 |
1409-1490 |
Sentence |
denotes |
In E. coli, PglL(Bt) and PglL(Vc) display relaxed glycan and protein specificity. |
| T10 |
1409-1490 |
Sentence |
denotes |
In E. coli, PglL(Bt) and PglL(Vc) display relaxed glycan and protein specificity. |
| T10 |
1409-1490 |
Sentence |
denotes |
In E. coli, PglL(Bt) and PglL(Vc) display relaxed glycan and protein specificity. |
| TextSentencer_T11 |
1491-1613 |
Sentence |
denotes |
However, effective glycosylation depends upon a specific combination of the protein acceptor, glycan and O-OTase analyzed. |
| T11 |
1491-1613 |
Sentence |
denotes |
However, effective glycosylation depends upon a specific combination of the protein acceptor, glycan and O-OTase analyzed. |
| T11 |
1491-1613 |
Sentence |
denotes |
However, effective glycosylation depends upon a specific combination of the protein acceptor, glycan and O-OTase analyzed. |
| TextSentencer_T12 |
1614-1755 |
Sentence |
denotes |
This knowledge has important implications in the design of glycoconjugates and provides novel tools for use in glycoengineering applications. |
| T12 |
1614-1755 |
Sentence |
denotes |
This knowledge has important implications in the design of glycoconjugates and provides novel tools for use in glycoengineering applications. |
| T12 |
1614-1755 |
Sentence |
denotes |
This knowledge has important implications in the design of glycoconjugates and provides novel tools for use in glycoengineering applications. |
| TextSentencer_T13 |
1756-2008 |
Sentence |
denotes |
The codification of enzymatically active O-OTase in the genomes of members of the Vibrio and Burkholderia genera suggests the presence of still unknown O-glycoproteins in these organisms, which might have a role in bacterial physiology or pathogenesis. |
| T13 |
1756-2008 |
Sentence |
denotes |
The codification of enzymatically active O-OTase in the genomes of members of the Vibrio and Burkholderia genera suggests the presence of still unknown O-glycoproteins in these organisms, which might have a role in bacterial physiology or pathogenesis. |
| T13 |
1756-2008 |
Sentence |
denotes |
The codification of enzymatically active O-OTase in the genomes of members of the Vibrio and Burkholderia genera suggests the presence of still unknown O-glycoproteins in these organisms, which might have a role in bacterial physiology or pathogenesis. |