PubMed:20847188
Annnotations
sentences
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| TextSentencer_T1 | 0-81 | Sentence | denotes | Relaxed acceptor site specificity of bacterial oligosaccharyltransferase in vivo. |
| TextSentencer_T2 | 82-272 | Sentence | denotes | A number of proteobacteria carry the genetic information to perform N-linked glycosylation, but only the protein glycosylation (pgl) pathway of Campylobacter jejuni has been studied to date. |
| TextSentencer_T3 | 273-432 | Sentence | denotes | Here, we report that the pgl gene cluster of Campylobacter lari encodes for a functional glycosylation machinery that can be reconstituted in Escherichia coli. |
| TextSentencer_T4 | 433-526 | Sentence | denotes | We determined that the N-glycan produced in this system consisted of a linear hexasaccharide. |
| TextSentencer_T5 | 527-729 | Sentence | denotes | We found that the oligosaccharyltransferase (OST) of C. lari conserved a predominant specificity for the primary sequence D/E-X(-1)-N-X(+1)-S/T (where X(-1) and X(+1) can be any amino acid but proline). |
| TextSentencer_T6 | 730-909 | Sentence | denotes | At the same time, we observed that this enzyme exhibited a relaxed specificity toward the acceptor site and modified asparagine residues of a protein at sequences DANSG and NNNST. |
| TextSentencer_T7 | 910-970 | Sentence | denotes | Moreover, C. lari pgl glycosylated a native E. coli protein. |
| TextSentencer_T8 | 971-1131 | Sentence | denotes | Bacterial N-glycosylation appears as a useful tool to establish a molecular description of how single-subunit OSTs perform selection of glycosyl acceptor sites. |
| T1 | 0-81 | Sentence | denotes | Relaxed acceptor site specificity of bacterial oligosaccharyltransferase in vivo. |
| T2 | 82-272 | Sentence | denotes | A number of proteobacteria carry the genetic information to perform N-linked glycosylation, but only the protein glycosylation (pgl) pathway of Campylobacter jejuni has been studied to date. |
| T3 | 273-432 | Sentence | denotes | Here, we report that the pgl gene cluster of Campylobacter lari encodes for a functional glycosylation machinery that can be reconstituted in Escherichia coli. |
| T4 | 433-526 | Sentence | denotes | We determined that the N-glycan produced in this system consisted of a linear hexasaccharide. |
| T5 | 527-729 | Sentence | denotes | We found that the oligosaccharyltransferase (OST) of C. lari conserved a predominant specificity for the primary sequence D/E-X(-1)-N-X(+1)-S/T (where X(-1) and X(+1) can be any amino acid but proline). |
| T6 | 730-909 | Sentence | denotes | At the same time, we observed that this enzyme exhibited a relaxed specificity toward the acceptor site and modified asparagine residues of a protein at sequences DANSG and NNNST. |
| T7 | 910-970 | Sentence | denotes | Moreover, C. lari pgl glycosylated a native E. coli protein. |
| T8 | 971-1131 | Sentence | denotes | Bacterial N-glycosylation appears as a useful tool to establish a molecular description of how single-subunit OSTs perform selection of glycosyl acceptor sites. |
| T1 | 0-81 | Sentence | denotes | Relaxed acceptor site specificity of bacterial oligosaccharyltransferase in vivo. |
| T2 | 82-272 | Sentence | denotes | A number of proteobacteria carry the genetic information to perform N-linked glycosylation, but only the protein glycosylation (pgl) pathway of Campylobacter jejuni has been studied to date. |
| T3 | 273-432 | Sentence | denotes | Here, we report that the pgl gene cluster of Campylobacter lari encodes for a functional glycosylation machinery that can be reconstituted in Escherichia coli. |
| T4 | 433-526 | Sentence | denotes | We determined that the N-glycan produced in this system consisted of a linear hexasaccharide. |
| T5 | 527-729 | Sentence | denotes | We found that the oligosaccharyltransferase (OST) of C. lari conserved a predominant specificity for the primary sequence D/E-X(-1)-N-X(+1)-S/T (where X(-1) and X(+1) can be any amino acid but proline). |
| T6 | 730-909 | Sentence | denotes | At the same time, we observed that this enzyme exhibited a relaxed specificity toward the acceptor site and modified asparagine residues of a protein at sequences DANSG and NNNST. |
| T7 | 910-970 | Sentence | denotes | Moreover, C. lari pgl glycosylated a native E. coli protein. |
| T8 | 971-1131 | Sentence | denotes | Bacterial N-glycosylation appears as a useful tool to establish a molecular description of how single-subunit OSTs perform selection of glycosyl acceptor sites. |
GlycoBiology-PACDB
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| _T1 | 226-246 | http://acgg.asia/db/diseases/pacdb/lec?ids=LEC257,LEC564 | denotes | Campylobacter jejuni |
| _T2 | 415-431 | http://acgg.asia/db/diseases/pacdb/lec?ids=LEC295,LEC417 | denotes | Escherichia coli |
| _T3 | 415-431 | http://acgg.asia/db/diseases/pacdb/lec?ids=LEC157,LEC407 | denotes | Escherichia coli |
| _T4 | 415-431 | http://acgg.asia/db/diseases/pacdb/lec?ids=LEC754 | denotes | Escherichia coli |
| _T5 | 415-431 | http://acgg.asia/db/diseases/pacdb/lec?ids=LEC243,LEC640 | denotes | Escherichia coli |
| _T6 | 415-431 | http://acgg.asia/db/diseases/pacdb/lec?ids=LEC002,LEC056,LEC062,LEC069,LEC081,LEC111,LEC133,LEC171,LEC177,LEC187,LEC211,LEC242,LEC252,LEC258,LEC259,LEC260,LEC262,LEC369,LEC377,LEC422,LEC442,LEC448,LEC450,LEC451,LEC454,LEC472,LEC492,LEC620 | denotes | Escherichia coli |
| _T7 | 415-431 | http://acgg.asia/db/diseases/pacdb/lec?ids=LEC487 | denotes | Escherichia coli |
| _T8 | 415-431 | http://acgg.asia/db/diseases/pacdb/lec?ids=LEC244,LEC256,LEC354 | denotes | Escherichia coli |
| _T9 | 415-431 | http://acgg.asia/db/diseases/pacdb/lec?ids=LEC054,LEC058,LEC073,LEC082,LEC091,LEC103,LEC109,LEC110,LEC123,LEC158,LEC179,LEC198,LEC205,LEC222,LEC223,LEC224,LEC225,LEC232,LEC298,LEC357,LEC378,LEC383,LEC388,LEC389,LEC397,LEC401,LEC410,LEC452 | denotes | Escherichia coli |
| _T10 | 415-431 | http://acgg.asia/db/diseases/pacdb/lec?ids=LEC636 | denotes | Escherichia coli |
GlycoBiology-FMA
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| _T1 | 187-194 | FMAID:67257 | denotes | protein |
| _T2 | 187-194 | FMAID:165447 | denotes | protein |
| _T3 | 302-306 | FMAID:198663 | denotes | gene |
| _T4 | 302-314 | FMAID:198017 | denotes | gene cluster |
| _T5 | 302-314 | FMAID:84082 | denotes | gene cluster |
| _T6 | 705-715 | FMAID:82739 | denotes | amino acid |
| _T7 | 705-715 | FMAID:196728 | denotes | amino acid |
| _T8 | 720-727 | FMAID:196750 | denotes | proline |
| _T9 | 720-727 | FMAID:82761 | denotes | proline |
| _T10 | 847-857 | FMAID:196739 | denotes | asparagine |
| _T11 | 847-857 | FMAID:82750 | denotes | asparagine |
| _T12 | 872-879 | FMAID:165447 | denotes | protein |
| _T13 | 872-879 | FMAID:67257 | denotes | protein |
| _T14 | 962-969 | FMAID:67257 | denotes | protein |
| _T15 | 962-969 | FMAID:165447 | denotes | protein |
uniprot-mouse
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| T1 | 210-213 | http://www.uniprot.org/uniprot/Q9CQ60 | denotes | pgl |
| T2 | 298-301 | http://www.uniprot.org/uniprot/Q9CQ60 | denotes | pgl |
| T3 | 928-931 | http://www.uniprot.org/uniprot/Q9CQ60 | denotes | pgl |
GlycoBiology-NCBITAXON
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| T1 | 94-108 | http://purl.bioontology.org/ontology/NCBITAXON/28216 | denotes | proteobacteria |
| T2 | 94-108 | http://purl.bioontology.org/ontology/NCBITAXON/580370 | denotes | proteobacteria |
| T3 | 94-108 | http://purl.bioontology.org/ontology/NCBITAXON/380367 | denotes | proteobacteria |
| T4 | 94-108 | http://purl.bioontology.org/ontology/NCBITAXON/1224 | denotes | proteobacteria |
| T5 | 226-246 | http://purl.bioontology.org/ontology/NCBITAXON/197 | denotes | Campylobacter jejuni |
| T6 | 415-426 | http://purl.bioontology.org/ontology/NCBITAXON/561 | denotes | Escherichia |
GO-BP
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| T1 | 159-172 | http://purl.obolibrary.org/obo/GO_0070085 | denotes | glycosylation |
| T2 | 195-208 | http://purl.obolibrary.org/obo/GO_0070085 | denotes | glycosylation |
| T3 | 362-375 | http://purl.obolibrary.org/obo/GO_0070085 | denotes | glycosylation |
| T4 | 932-944 | http://purl.obolibrary.org/obo/GO_0070085 | denotes | glycosylated |
| T5 | 1107-1115 | http://purl.obolibrary.org/obo/GO_0070085 | denotes | glycosyl |
| T6 | 187-208 | http://purl.obolibrary.org/obo/GO_0006486 | denotes | protein glycosylation |
| T7 | 210-213 | http://purl.obolibrary.org/obo/GO_0004598 | denotes | pgl |
| T8 | 298-301 | http://purl.obolibrary.org/obo/GO_0004598 | denotes | pgl |
| T9 | 928-931 | http://purl.obolibrary.org/obo/GO_0004598 | denotes | pgl |
Allie
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| SS1_20847188_1_0 | 187-208 | expanded | denotes | protein glycosylation |
| SS2_20847188_1_0 | 210-213 | abbr | denotes | pgl |
| SS1_20847188_4_0 | 545-570 | expanded | denotes | oligosaccharyltransferase |
| SS2_20847188_4_0 | 572-575 | abbr | denotes | OST |
| AE1_20847188_1_0 | SS1_20847188_1_0 | SS2_20847188_1_0 | abbreviatedTo | protein glycosylation,pgl |
| AE1_20847188_4_0 | SS1_20847188_4_0 | SS2_20847188_4_0 | abbreviatedTo | oligosaccharyltransferase,OST |
GlycoBiology-Motifs
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| T1 | 456-464 | http://rdf.glycoinfo.org/glycan/G00027MO | denotes | N-glycan |
NCBITAXON
| Id | Subject | Object | Predicate | Lexical cue | db_id |
|---|---|---|---|---|---|
| T1 | 94-108 | OrganismTaxon | denotes | proteobacteria | 1224 |
| T2 | 226-246 | OrganismTaxon | denotes | Campylobacter jejuni | 197 |
| T3 | 318-336 | OrganismTaxon | denotes | Campylobacter lari | 201 |
| T4 | 415-431 | OrganismTaxon | denotes | Escherichia coli | 562 |
| T5 | 954-961 | OrganismTaxon | denotes | E. coli | 562 |