Id |
Subject |
Object |
Predicate |
Lexical cue |
TextSentencer_T1 |
0-170 |
Sentence |
denotes |
Desulfovibrio desulfuricans PglB homolog possesses oligosaccharyltransferase activity with relaxed glycan specificity and distinct protein acceptor sequence requirements. |
T1 |
0-170 |
Sentence |
denotes |
Desulfovibrio desulfuricans PglB homolog possesses oligosaccharyltransferase activity with relaxed glycan specificity and distinct protein acceptor sequence requirements. |
T1 |
0-170 |
Sentence |
denotes |
Desulfovibrio desulfuricans PglB homolog possesses oligosaccharyltransferase activity with relaxed glycan specificity and distinct protein acceptor sequence requirements. |
TextSentencer_T2 |
171-337 |
Sentence |
denotes |
Oligosaccharyltransferases (OTases) are responsible for the transfer of carbohydrates from lipid carriers to acceptor proteins and are present in all domains of life. |
T2 |
171-337 |
Sentence |
denotes |
Oligosaccharyltransferases (OTases) are responsible for the transfer of carbohydrates from lipid carriers to acceptor proteins and are present in all domains of life. |
T2 |
171-337 |
Sentence |
denotes |
Oligosaccharyltransferases (OTases) are responsible for the transfer of carbohydrates from lipid carriers to acceptor proteins and are present in all domains of life. |
TextSentencer_T3 |
338-435 |
Sentence |
denotes |
In bacteria, the most studied member of this family is PglB from Campylobacter jejuni (PglB(Cj)). |
T3 |
338-435 |
Sentence |
denotes |
In bacteria, the most studied member of this family is PglB from Campylobacter jejuni (PglB(Cj)). |
T3 |
338-435 |
Sentence |
denotes |
In bacteria, the most studied member of this family is PglB from Campylobacter jejuni (PglB(Cj)). |
TextSentencer_T4 |
436-624 |
Sentence |
denotes |
This enzyme is functional in Escherichia coli and, contrary to its eukaryotic counterparts, has the ability to transfer a variety of oligo- and polysaccharides to protein carriers in vivo. |
T4 |
436-624 |
Sentence |
denotes |
This enzyme is functional in Escherichia coli and, contrary to its eukaryotic counterparts, has the ability to transfer a variety of oligo- and polysaccharides to protein carriers in vivo. |
T4 |
436-624 |
Sentence |
denotes |
This enzyme is functional in Escherichia coli and, contrary to its eukaryotic counterparts, has the ability to transfer a variety of oligo- and polysaccharides to protein carriers in vivo. |
TextSentencer_T5 |
625-822 |
Sentence |
denotes |
Phylogenetic analysis revealed that in the delta proteobacteria Desulfovibrio sp., the PglB homolog is more closely related to eukaryotic and archaeal OTases than to its Campylobacter counterparts. |
T5 |
625-822 |
Sentence |
denotes |
Phylogenetic analysis revealed that in the delta proteobacteria Desulfovibrio sp., the PglB homolog is more closely related to eukaryotic and archaeal OTases than to its Campylobacter counterparts. |
T5 |
625-822 |
Sentence |
denotes |
Phylogenetic analysis revealed that in the delta proteobacteria Desulfovibrio sp., the PglB homolog is more closely related to eukaryotic and archaeal OTases than to its Campylobacter counterparts. |
TextSentencer_T6 |
823-973 |
Sentence |
denotes |
Genetic analysis revealed the presence of a putative operon that might encode all enzymes required for N-glycosylation in Desulfovibrio desulfuricans. |
T6 |
823-973 |
Sentence |
denotes |
Genetic analysis revealed the presence of a putative operon that might encode all enzymes required for N-glycosylation in Desulfovibrio desulfuricans. |
T6 |
823-973 |
Sentence |
denotes |
Genetic analysis revealed the presence of a putative operon that might encode all enzymes required for N-glycosylation in Desulfovibrio desulfuricans. |
TextSentencer_T7 |
974-1171 |
Sentence |
denotes |
D. desulfuricans PglB (PglB(Dd)) was cloned and successfully expressed in E. coli, and its activity was confirmed by transferring the C. jejuni heptasaccharide onto the model protein acceptor AcrA. |
T7 |
974-1171 |
Sentence |
denotes |
D. desulfuricans PglB (PglB(Dd)) was cloned and successfully expressed in E. coli, and its activity was confirmed by transferring the C. jejuni heptasaccharide onto the model protein acceptor AcrA. |
T7 |
974-1171 |
Sentence |
denotes |
D. desulfuricans PglB (PglB(Dd)) was cloned and successfully expressed in E. coli, and its activity was confirmed by transferring the C. jejuni heptasaccharide onto the model protein acceptor AcrA. |
TextSentencer_T8 |
1172-1300 |
Sentence |
denotes |
In contrast to PglB(Cj), which adds two glycan chains to AcrA, a single oligosaccharide was attached to the protein by PglB(Dd). |
T8 |
1172-1300 |
Sentence |
denotes |
In contrast to PglB(Cj), which adds two glycan chains to AcrA, a single oligosaccharide was attached to the protein by PglB(Dd). |
T8 |
1172-1300 |
Sentence |
denotes |
In contrast to PglB(Cj), which adds two glycan chains to AcrA, a single oligosaccharide was attached to the protein by PglB(Dd). |
TextSentencer_T9 |
1301-1700 |
Sentence |
denotes |
Site-directed mutagenesis of the five putative N-X-S/T glycosylation sites in AcrA and mass spectrometry analysis showed that PglB(Dd) does not recognize the "conventional bacterial glycosylation sequon" consisting of the sequence D/E-X(1)-N-X(2)-S/T (where X(1) and X(2) are any amino acid except proline), and instead used a different site for the attachment of the oligosaccharide than PglB(Cj.). |
T9 |
1301-1700 |
Sentence |
denotes |
Site-directed mutagenesis of the five putative N-X-S/T glycosylation sites in AcrA and mass spectrometry analysis showed that PglB(Dd) does not recognize the "conventional bacterial glycosylation sequon" consisting of the sequence D/E-X(1)-N-X(2)-S/T (where X(1) and X(2) are any amino acid except proline), and instead used a different site for the attachment of the oligosaccharide than PglB(Cj.). |
T9 |
1301-1700 |
Sentence |
denotes |
Site-directed mutagenesis of the five putative N-X-S/T glycosylation sites in AcrA and mass spectrometry analysis showed that PglB(Dd) does not recognize the "conventional bacterial glycosylation sequon" consisting of the sequence D/E-X(1)-N-X(2)-S/T (where X(1) and X(2) are any amino acid except proline), and instead used a different site for the attachment of the oligosaccharide than PglB(Cj.). |
TextSentencer_T10 |
1701-1818 |
Sentence |
denotes |
Furthermore, PglB(Dd) exhibited relaxed glycan specificity, being able to transfer mono- and polysaccharides to AcrA. |
T10 |
1701-1818 |
Sentence |
denotes |
Furthermore, PglB(Dd) exhibited relaxed glycan specificity, being able to transfer mono- and polysaccharides to AcrA. |
T10 |
1701-1818 |
Sentence |
denotes |
Furthermore, PglB(Dd) exhibited relaxed glycan specificity, being able to transfer mono- and polysaccharides to AcrA. |
TextSentencer_T11 |
1819-1952 |
Sentence |
denotes |
Our analysis constitutes the first characterization of an OTase from delta-proteobacteria involved in N-linked protein glycosylation. |
T11 |
1819-1952 |
Sentence |
denotes |
Our analysis constitutes the first characterization of an OTase from delta-proteobacteria involved in N-linked protein glycosylation. |
T11 |
1819-1952 |
Sentence |
denotes |
Our analysis constitutes the first characterization of an OTase from delta-proteobacteria involved in N-linked protein glycosylation. |