PubMed:23193180 JSONTXT

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    sentences

    {"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":111},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":112,"end":324},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":325,"end":555},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":556,"end":895},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":896,"end":1328},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":1329,"end":1334},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":1335,"end":1351},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":1352,"end":1365},"obj":"Sentence"},{"id":"TextSentencer_T9","span":{"begin":1366,"end":1673},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":111},"obj":"Sentence"},{"id":"T2","span":{"begin":112,"end":324},"obj":"Sentence"},{"id":"T3","span":{"begin":325,"end":555},"obj":"Sentence"},{"id":"T4","span":{"begin":556,"end":895},"obj":"Sentence"},{"id":"T5","span":{"begin":896,"end":1334},"obj":"Sentence"},{"id":"T6","span":{"begin":1335,"end":1365},"obj":"Sentence"},{"id":"T7","span":{"begin":1366,"end":1673},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":111},"obj":"Sentence"},{"id":"T2","span":{"begin":112,"end":324},"obj":"Sentence"},{"id":"T3","span":{"begin":325,"end":555},"obj":"Sentence"},{"id":"T4","span":{"begin":556,"end":895},"obj":"Sentence"},{"id":"T5","span":{"begin":896,"end":1328},"obj":"Sentence"},{"id":"T6","span":{"begin":1329,"end":1334},"obj":"Sentence"},{"id":"T7","span":{"begin":1335,"end":1351},"obj":"Sentence"},{"id":"T8","span":{"begin":1352,"end":1365},"obj":"Sentence"},{"id":"T9","span":{"begin":1366,"end":1673},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Structural studies of the O-antigen polysaccharide from Escherichia coli O115 and biosynthetic aspects thereof.\nThe structure of the O-antigen polysaccharide (PS) of Escherichia coli O115 has been investigated using a combination of component analysis and 1D and 2D nuclear magnetic resonance (NMR) spectroscopy experiments. The repeating unit of the O-antigen was elucidated using the O-deacetylated PS and has the following branched pentasaccharide structure: →3)[β-L-Rhap-(1 → 4)]-β-D-GlcpNAc-(1 → 4)-α-D-GalpA-(1 → 3)-α-D-Manp-(1 → 3)-β-D-GlcpNAc-(1→. Cross-peaks of low intensity, corresponding to a β-L-Rhap-(1 → 4)-β-D-GlcpNAc-(1→ structural element, were present in the NMR spectra and attributed to the terminal part of the PS; this information defines the biological repeating unit of the O-antigen by having a 3-substituted N-acetyl-D-glucosamine (GlcNAc) residue at its reducing end. Analysis of the NMR spectra of the native PS revealed O-acetyl groups distributed over different positions of the l-Rhap residue (∼0.70 per repeating unit) as well as at O-2 and O-3 of the D-GalpA residue (∼0.03 and ∼0.25 per repeating unit, respectively), which is in agreement with the presence of two acetyltransferases previously identified in the O-antigen gene cluster (Wang Q, Ruan X, Wei D, Hu Z, Wu L, Yu T, Feng L, Wang L. 2010. Mol Cell Probes. 24:286-290.). In addition, the four glycosyltransferases initially identified in the O-antigen gene cluster of E. coli O115 were analyzed using BLAST, and the function of two of them predicted on the basis of similarities with glycosyltransferases from Shigella dysenteriae type 5 and 12, as well as E. coli O58 and O152."}

    GlycoBiology-PACDB

    {"project":"GlycoBiology-PACDB","denotations":[{"id":"_T1","span":{"begin":56,"end":72},"obj":"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"},{"id":"_T2","span":{"begin":56,"end":72},"obj":"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"},{"id":"_T3","span":{"begin":56,"end":72},"obj":"http://acgg.asia/db/diseases/pacdb/lec?ids=LEC157,LEC407"},{"id":"_T4","span":{"begin":56,"end":72},"obj":"http://acgg.asia/db/diseases/pacdb/lec?ids=LEC244,LEC256,LEC354"},{"id":"_T5","span":{"begin":56,"end":72},"obj":"http://acgg.asia/db/diseases/pacdb/lec?ids=LEC754"},{"id":"_T6","span":{"begin":56,"end":72},"obj":"http://acgg.asia/db/diseases/pacdb/lec?ids=LEC295,LEC417"},{"id":"_T7","span":{"begin":56,"end":72},"obj":"http://acgg.asia/db/diseases/pacdb/lec?ids=LEC243,LEC640"},{"id":"_T8","span":{"begin":56,"end":72},"obj":"http://acgg.asia/db/diseases/pacdb/lec?ids=LEC636"},{"id":"_T9","span":{"begin":56,"end":72},"obj":"http://acgg.asia/db/diseases/pacdb/lec?ids=LEC487"},{"id":"_T10","span":{"begin":56,"end":77},"obj":"http://acgg.asia/db/diseases/pacdb/lec?ids=LEC267,LEC475"},{"id":"_T11","span":{"begin":166,"end":182},"obj":"http://acgg.asia/db/diseases/pacdb/lec?ids=LEC295,LEC417"},{"id":"_T12","span":{"begin":166,"end":182},"obj":"http://acgg.asia/db/diseases/pacdb/lec?ids=LEC243,LEC640"},{"id":"_T13","span":{"begin":166,"end":182},"obj":"http://acgg.asia/db/diseases/pacdb/lec?ids=LEC754"},{"id":"_T14","span":{"begin":166,"end":182},"obj":"http://acgg.asia/db/diseases/pacdb/lec?ids=LEC636"},{"id":"_T15","span":{"begin":166,"end":182},"obj":"http://acgg.asia/db/diseases/pacdb/lec?ids=LEC157,LEC407"},{"id":"_T16","span":{"begin":166,"end":182},"obj":"http://acgg.asia/db/diseases/pacdb/lec?ids=LEC244,LEC256,LEC354"},{"id":"_T17","span":{"begin":166,"end":182},"obj":"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"},{"id":"_T18","span":{"begin":166,"end":182},"obj":"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"},{"id":"_T19","span":{"begin":166,"end":182},"obj":"http://acgg.asia/db/diseases/pacdb/lec?ids=LEC487"},{"id":"_T20","span":{"begin":166,"end":187},"obj":"http://acgg.asia/db/diseases/pacdb/lec?ids=LEC267,LEC475"},{"id":"_T21","span":{"begin":1605,"end":1625},"obj":"http://acgg.asia/db/diseases/pacdb/lec?ids=LEC240,LEC496,LEC580"},{"id":"_T22","span":{"begin":1605,"end":1632},"obj":"http://acgg.asia/db/diseases/pacdb/lec?ids=LEC542"}],"text":"Structural studies of the O-antigen polysaccharide from Escherichia coli O115 and biosynthetic aspects thereof.\nThe structure of the O-antigen polysaccharide (PS) of Escherichia coli O115 has been investigated using a combination of component analysis and 1D and 2D nuclear magnetic resonance (NMR) spectroscopy experiments. The repeating unit of the O-antigen was elucidated using the O-deacetylated PS and has the following branched pentasaccharide structure: →3)[β-L-Rhap-(1 → 4)]-β-D-GlcpNAc-(1 → 4)-α-D-GalpA-(1 → 3)-α-D-Manp-(1 → 3)-β-D-GlcpNAc-(1→. Cross-peaks of low intensity, corresponding to a β-L-Rhap-(1 → 4)-β-D-GlcpNAc-(1→ structural element, were present in the NMR spectra and attributed to the terminal part of the PS; this information defines the biological repeating unit of the O-antigen by having a 3-substituted N-acetyl-D-glucosamine (GlcNAc) residue at its reducing end. Analysis of the NMR spectra of the native PS revealed O-acetyl groups distributed over different positions of the l-Rhap residue (∼0.70 per repeating unit) as well as at O-2 and O-3 of the D-GalpA residue (∼0.03 and ∼0.25 per repeating unit, respectively), which is in agreement with the presence of two acetyltransferases previously identified in the O-antigen gene cluster (Wang Q, Ruan X, Wei D, Hu Z, Wu L, Yu T, Feng L, Wang L. 2010. Mol Cell Probes. 24:286-290.). In addition, the four glycosyltransferases initially identified in the O-antigen gene cluster of E. coli O115 were analyzed using BLAST, and the function of two of them predicted on the basis of similarities with glycosyltransferases from Shigella dysenteriae type 5 and 12, as well as E. coli O58 and O152."}

    GlycoBiology-FMA

    {"project":"GlycoBiology-FMA","denotations":[{"id":"_T1","span":{"begin":36,"end":50},"obj":"FMAID:196779"},{"id":"_T2","span":{"begin":36,"end":50},"obj":"FMAID:82785"},{"id":"_T3","span":{"begin":36,"end":50},"obj":"FMAID:196735"},{"id":"_T4","span":{"begin":36,"end":50},"obj":"FMAID:82746"},{"id":"_T5","span":{"begin":143,"end":157},"obj":"FMAID:82746"},{"id":"_T6","span":{"begin":143,"end":157},"obj":"FMAID:82785"},{"id":"_T7","span":{"begin":143,"end":157},"obj":"FMAID:196735"},{"id":"_T8","span":{"begin":143,"end":157},"obj":"FMAID:196779"},{"id":"_T9","span":{"begin":426,"end":434},"obj":"FMAID:226027"},{"id":"_T10","span":{"begin":426,"end":434},"obj":"FMAID:226028"},{"id":"_T11","span":{"begin":846,"end":857},"obj":"FMAID:196792"},{"id":"_T12","span":{"begin":846,"end":857},"obj":"FMAID:82797"},{"id":"_T13","span":{"begin":1258,"end":1262},"obj":"FMAID:198663"},{"id":"_T14","span":{"begin":1258,"end":1270},"obj":"FMAID:198017"},{"id":"_T15","span":{"begin":1258,"end":1270},"obj":"FMAID:84082"},{"id":"_T16","span":{"begin":1447,"end":1451},"obj":"FMAID:198663"},{"id":"_T17","span":{"begin":1447,"end":1459},"obj":"FMAID:198017"},{"id":"_T18","span":{"begin":1447,"end":1459},"obj":"FMAID:84082"}],"namespaces":[{"prefix":"FMAID","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"Structural studies of the O-antigen polysaccharide from Escherichia coli O115 and biosynthetic aspects thereof.\nThe structure of the O-antigen polysaccharide (PS) of Escherichia coli O115 has been investigated using a combination of component analysis and 1D and 2D nuclear magnetic resonance (NMR) spectroscopy experiments. The repeating unit of the O-antigen was elucidated using the O-deacetylated PS and has the following branched pentasaccharide structure: →3)[β-L-Rhap-(1 → 4)]-β-D-GlcpNAc-(1 → 4)-α-D-GalpA-(1 → 3)-α-D-Manp-(1 → 3)-β-D-GlcpNAc-(1→. Cross-peaks of low intensity, corresponding to a β-L-Rhap-(1 → 4)-β-D-GlcpNAc-(1→ structural element, were present in the NMR spectra and attributed to the terminal part of the PS; this information defines the biological repeating unit of the O-antigen by having a 3-substituted N-acetyl-D-glucosamine (GlcNAc) residue at its reducing end. Analysis of the NMR spectra of the native PS revealed O-acetyl groups distributed over different positions of the l-Rhap residue (∼0.70 per repeating unit) as well as at O-2 and O-3 of the D-GalpA residue (∼0.03 and ∼0.25 per repeating unit, respectively), which is in agreement with the presence of two acetyltransferases previously identified in the O-antigen gene cluster (Wang Q, Ruan X, Wei D, Hu Z, Wu L, Yu T, Feng L, Wang L. 2010. Mol Cell Probes. 24:286-290.). In addition, the four glycosyltransferases initially identified in the O-antigen gene cluster of E. coli O115 were analyzed using BLAST, and the function of two of them predicted on the basis of similarities with glycosyltransferases from Shigella dysenteriae type 5 and 12, as well as E. coli O58 and O152."}

    uniprot-human

    {"project":"uniprot-human","denotations":[{"id":"T1","span":{"begin":497,"end":505},"obj":"http://www.uniprot.org/uniprot/P13674"},{"id":"T2","span":{"begin":501,"end":505},"obj":"http://www.uniprot.org/uniprot/P78318"}],"text":"Structural studies of the O-antigen polysaccharide from Escherichia coli O115 and biosynthetic aspects thereof.\nThe structure of the O-antigen polysaccharide (PS) of Escherichia coli O115 has been investigated using a combination of component analysis and 1D and 2D nuclear magnetic resonance (NMR) spectroscopy experiments. The repeating unit of the O-antigen was elucidated using the O-deacetylated PS and has the following branched pentasaccharide structure: →3)[β-L-Rhap-(1 → 4)]-β-D-GlcpNAc-(1 → 4)-α-D-GalpA-(1 → 3)-α-D-Manp-(1 → 3)-β-D-GlcpNAc-(1→. Cross-peaks of low intensity, corresponding to a β-L-Rhap-(1 → 4)-β-D-GlcpNAc-(1→ structural element, were present in the NMR spectra and attributed to the terminal part of the PS; this information defines the biological repeating unit of the O-antigen by having a 3-substituted N-acetyl-D-glucosamine (GlcNAc) residue at its reducing end. Analysis of the NMR spectra of the native PS revealed O-acetyl groups distributed over different positions of the l-Rhap residue (∼0.70 per repeating unit) as well as at O-2 and O-3 of the D-GalpA residue (∼0.03 and ∼0.25 per repeating unit, respectively), which is in agreement with the presence of two acetyltransferases previously identified in the O-antigen gene cluster (Wang Q, Ruan X, Wei D, Hu Z, Wu L, Yu T, Feng L, Wang L. 2010. Mol Cell Probes. 24:286-290.). In addition, the four glycosyltransferases initially identified in the O-antigen gene cluster of E. coli O115 were analyzed using BLAST, and the function of two of them predicted on the basis of similarities with glycosyltransferases from Shigella dysenteriae type 5 and 12, as well as E. coli O58 and O152."}

    GlycoBiology-NCBITAXON

    {"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":56,"end":67},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/561"},{"id":"T2","span":{"begin":166,"end":177},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/561"},{"id":"T3","span":{"begin":959,"end":965},"obj":"http://purl.bioontology.org/ontology/STY/T096"},{"id":"T4","span":{"begin":1496,"end":1501},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/298032"},{"id":"T5","span":{"begin":1605,"end":1625},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/622"}],"text":"Structural studies of the O-antigen polysaccharide from Escherichia coli O115 and biosynthetic aspects thereof.\nThe structure of the O-antigen polysaccharide (PS) of Escherichia coli O115 has been investigated using a combination of component analysis and 1D and 2D nuclear magnetic resonance (NMR) spectroscopy experiments. The repeating unit of the O-antigen was elucidated using the O-deacetylated PS and has the following branched pentasaccharide structure: →3)[β-L-Rhap-(1 → 4)]-β-D-GlcpNAc-(1 → 4)-α-D-GalpA-(1 → 3)-α-D-Manp-(1 → 3)-β-D-GlcpNAc-(1→. Cross-peaks of low intensity, corresponding to a β-L-Rhap-(1 → 4)-β-D-GlcpNAc-(1→ structural element, were present in the NMR spectra and attributed to the terminal part of the PS; this information defines the biological repeating unit of the O-antigen by having a 3-substituted N-acetyl-D-glucosamine (GlcNAc) residue at its reducing end. Analysis of the NMR spectra of the native PS revealed O-acetyl groups distributed over different positions of the l-Rhap residue (∼0.70 per repeating unit) as well as at O-2 and O-3 of the D-GalpA residue (∼0.03 and ∼0.25 per repeating unit, respectively), which is in agreement with the presence of two acetyltransferases previously identified in the O-antigen gene cluster (Wang Q, Ruan X, Wei D, Hu Z, Wu L, Yu T, Feng L, Wang L. 2010. Mol Cell Probes. 24:286-290.). In addition, the four glycosyltransferases initially identified in the O-antigen gene cluster of E. coli O115 were analyzed using BLAST, and the function of two of them predicted on the basis of similarities with glycosyltransferases from Shigella dysenteriae type 5 and 12, as well as E. coli O58 and O152."}

    GO-CC

    {"project":"GO-CC","denotations":[{"id":"T1","span":{"begin":1339,"end":1343},"obj":"http://purl.obolibrary.org/obo/GO_0005623"}],"text":"Structural studies of the O-antigen polysaccharide from Escherichia coli O115 and biosynthetic aspects thereof.\nThe structure of the O-antigen polysaccharide (PS) of Escherichia coli O115 has been investigated using a combination of component analysis and 1D and 2D nuclear magnetic resonance (NMR) spectroscopy experiments. The repeating unit of the O-antigen was elucidated using the O-deacetylated PS and has the following branched pentasaccharide structure: →3)[β-L-Rhap-(1 → 4)]-β-D-GlcpNAc-(1 → 4)-α-D-GalpA-(1 → 3)-α-D-Manp-(1 → 3)-β-D-GlcpNAc-(1→. Cross-peaks of low intensity, corresponding to a β-L-Rhap-(1 → 4)-β-D-GlcpNAc-(1→ structural element, were present in the NMR spectra and attributed to the terminal part of the PS; this information defines the biological repeating unit of the O-antigen by having a 3-substituted N-acetyl-D-glucosamine (GlcNAc) residue at its reducing end. Analysis of the NMR spectra of the native PS revealed O-acetyl groups distributed over different positions of the l-Rhap residue (∼0.70 per repeating unit) as well as at O-2 and O-3 of the D-GalpA residue (∼0.03 and ∼0.25 per repeating unit, respectively), which is in agreement with the presence of two acetyltransferases previously identified in the O-antigen gene cluster (Wang Q, Ruan X, Wei D, Hu Z, Wu L, Yu T, Feng L, Wang L. 2010. Mol Cell Probes. 24:286-290.). In addition, the four glycosyltransferases initially identified in the O-antigen gene cluster of E. coli O115 were analyzed using BLAST, and the function of two of them predicted on the basis of similarities with glycosyltransferases from Shigella dysenteriae type 5 and 12, as well as E. coli O58 and O152."}

    Allie

    {"project":"Allie","denotations":[{"id":"SS1_23193180_1_0","span":{"begin":143,"end":157},"obj":"expanded"},{"id":"SS2_23193180_1_0","span":{"begin":159,"end":161},"obj":"abbr"},{"id":"SS1_23193180_1_1","span":{"begin":266,"end":292},"obj":"expanded"},{"id":"SS2_23193180_1_1","span":{"begin":294,"end":297},"obj":"abbr"},{"id":"SS1_23193180_3_0","span":{"begin":835,"end":857},"obj":"expanded"},{"id":"SS2_23193180_3_0","span":{"begin":859,"end":865},"obj":"abbr"}],"relations":[{"id":"AE1_23193180_1_0","pred":"abbreviatedTo","subj":"SS1_23193180_1_0","obj":"SS2_23193180_1_0"},{"id":"AE1_23193180_1_1","pred":"abbreviatedTo","subj":"SS1_23193180_1_1","obj":"SS2_23193180_1_1"},{"id":"AE1_23193180_3_0","pred":"abbreviatedTo","subj":"SS1_23193180_3_0","obj":"SS2_23193180_3_0"}],"text":"Structural studies of the O-antigen polysaccharide from Escherichia coli O115 and biosynthetic aspects thereof.\nThe structure of the O-antigen polysaccharide (PS) of Escherichia coli O115 has been investigated using a combination of component analysis and 1D and 2D nuclear magnetic resonance (NMR) spectroscopy experiments. The repeating unit of the O-antigen was elucidated using the O-deacetylated PS and has the following branched pentasaccharide structure: →3)[β-L-Rhap-(1 → 4)]-β-D-GlcpNAc-(1 → 4)-α-D-GalpA-(1 → 3)-α-D-Manp-(1 → 3)-β-D-GlcpNAc-(1→. Cross-peaks of low intensity, corresponding to a β-L-Rhap-(1 → 4)-β-D-GlcpNAc-(1→ structural element, were present in the NMR spectra and attributed to the terminal part of the PS; this information defines the biological repeating unit of the O-antigen by having a 3-substituted N-acetyl-D-glucosamine (GlcNAc) residue at its reducing end. Analysis of the NMR spectra of the native PS revealed O-acetyl groups distributed over different positions of the l-Rhap residue (∼0.70 per repeating unit) as well as at O-2 and O-3 of the D-GalpA residue (∼0.03 and ∼0.25 per repeating unit, respectively), which is in agreement with the presence of two acetyltransferases previously identified in the O-antigen gene cluster (Wang Q, Ruan X, Wei D, Hu Z, Wu L, Yu T, Feng L, Wang L. 2010. Mol Cell Probes. 24:286-290.). In addition, the four glycosyltransferases initially identified in the O-antigen gene cluster of E. coli O115 were analyzed using BLAST, and the function of two of them predicted on the basis of similarities with glycosyltransferases from Shigella dysenteriae type 5 and 12, as well as E. coli O58 and O152."}

    GlyTouCan-IUPAC

    {"project":"GlyTouCan-IUPAC","denotations":[{"id":"GlycanIUPAC_T1","span":{"begin":859,"end":865},"obj":"\"http://rdf.glycoinfo.org/glycan/G26693XF\""},{"id":"GlycanIUPAC_T2","span":{"begin":859,"end":865},"obj":"\"http://rdf.glycoinfo.org/glycan/G01864SU\""},{"id":"GlycanIUPAC_T3","span":{"begin":859,"end":865},"obj":"\"http://rdf.glycoinfo.org/glycan/G17605FD\""},{"id":"GlycanIUPAC_T4","span":{"begin":859,"end":865},"obj":"\"http://rdf.glycoinfo.org/glycan/G41950LU\""},{"id":"GlycanIUPAC_T5","span":{"begin":859,"end":865},"obj":"\"http://rdf.glycoinfo.org/glycan/G57195RJ\""},{"id":"GlycanIUPAC_T6","span":{"begin":859,"end":865},"obj":"\"http://rdf.glycoinfo.org/glycan/G85391SA\""},{"id":"GlycanIUPAC_T7","span":{"begin":859,"end":865},"obj":"\"http://rdf.glycoinfo.org/glycan/G89565QL\""},{"id":"GlycanIUPAC_T8","span":{"begin":859,"end":865},"obj":"\"http://rdf.glycoinfo.org/glycan/G80869MR\""},{"id":"GlycanIUPAC_T9","span":{"begin":859,"end":865},"obj":"\"http://rdf.glycoinfo.org/glycan/G55978NL\""},{"id":"GlycanIUPAC_T10","span":{"begin":859,"end":865},"obj":"\"http://rdf.glycoinfo.org/glycan/G54644LT\""},{"id":"GlycanIUPAC_T11","span":{"begin":859,"end":865},"obj":"\"http://rdf.glycoinfo.org/glycan/G25694UG\""},{"id":"GlycanIUPAC_T12","span":{"begin":859,"end":865},"obj":"\"http://rdf.glycoinfo.org/glycan/G25126RB\""},{"id":"GlycanIUPAC_T13","span":{"begin":859,"end":865},"obj":"\"http://rdf.glycoinfo.org/glycan/G51848AD\""},{"id":"GlycanIUPAC_T14","span":{"begin":859,"end":865},"obj":"\"http://rdf.glycoinfo.org/glycan/G94667GM\""},{"id":"GlycanIUPAC_T15","span":{"begin":859,"end":865},"obj":"\"http://rdf.glycoinfo.org/glycan/G30124BO\""},{"id":"GlycanIUPAC_T16","span":{"begin":859,"end":865},"obj":"\"http://rdf.glycoinfo.org/glycan/G82777EZ\""},{"id":"GlycanIUPAC_T17","span":{"begin":859,"end":865},"obj":"\"http://rdf.glycoinfo.org/glycan/G10151YZ\""},{"id":"GlycanIUPAC_T18","span":{"begin":859,"end":865},"obj":"\"http://rdf.glycoinfo.org/glycan/G17585ZM\""},{"id":"GlycanIUPAC_T19","span":{"begin":859,"end":865},"obj":"\"http://rdf.glycoinfo.org/glycan/G04411CJ\""},{"id":"GlycanIUPAC_T20","span":{"begin":859,"end":865},"obj":"\"http://rdf.glycoinfo.org/glycan/G38254HJ\""},{"id":"GlycanIUPAC_T21","span":{"begin":859,"end":865},"obj":"\"http://rdf.glycoinfo.org/glycan/G75188FS\""},{"id":"GlycanIUPAC_T22","span":{"begin":859,"end":865},"obj":"\"http://rdf.glycoinfo.org/glycan/G70374VG\""},{"id":"GlycanIUPAC_T23","span":{"begin":859,"end":865},"obj":"\"http://rdf.glycoinfo.org/glycan/G45176LJ\""},{"id":"GlycanIUPAC_T24","span":{"begin":859,"end":865},"obj":"\"http://rdf.glycoinfo.org/glycan/G30874VW\""},{"id":"GlycanIUPAC_T25","span":{"begin":859,"end":865},"obj":"\"http://rdf.glycoinfo.org/glycan/G69333MI\""},{"id":"GlycanIUPAC_T26","span":{"begin":859,"end":865},"obj":"\"http://rdf.glycoinfo.org/glycan/G10676XO\""},{"id":"GlycanIUPAC_T27","span":{"begin":859,"end":865},"obj":"\"http://rdf.glycoinfo.org/glycan/G14843DJ\""},{"id":"GlycanIUPAC_T28","span":{"begin":859,"end":865},"obj":"\"http://rdf.glycoinfo.org/glycan/G47546FR\""},{"id":"GlycanIUPAC_T29","span":{"begin":859,"end":865},"obj":"\"http://rdf.glycoinfo.org/glycan/G73695ZM\""},{"id":"GlycanIUPAC_T30","span":{"begin":859,"end":865},"obj":"\"http://rdf.glycoinfo.org/glycan/G31923TJ\""},{"id":"GlycanIUPAC_T31","span":{"begin":859,"end":865},"obj":"\"http://rdf.glycoinfo.org/glycan/G60519EP\""},{"id":"GlycanIUPAC_T32","span":{"begin":859,"end":865},"obj":"\"http://rdf.glycoinfo.org/glycan/G07933IA\""},{"id":"GlycanIUPAC_T33","span":{"begin":859,"end":865},"obj":"\"http://rdf.glycoinfo.org/glycan/G40745NH\""},{"id":"GlycanIUPAC_T34","span":{"begin":859,"end":865},"obj":"\"http://rdf.glycoinfo.org/glycan/G54496YV\""},{"id":"GlycanIUPAC_T35","span":{"begin":859,"end":865},"obj":"\"http://rdf.glycoinfo.org/glycan/G62953SQ\""},{"id":"GlycanIUPAC_T36","span":{"begin":859,"end":865},"obj":"\"http://rdf.glycoinfo.org/glycan/G70070AY\""},{"id":"GlycanIUPAC_T37","span":{"begin":859,"end":865},"obj":"\"http://rdf.glycoinfo.org/glycan/G78792WC\""},{"id":"GlycanIUPAC_T38","span":{"begin":859,"end":865},"obj":"\"http://rdf.glycoinfo.org/glycan/G25238AV\""},{"id":"GlycanIUPAC_T39","span":{"begin":859,"end":865},"obj":"\"http://rdf.glycoinfo.org/glycan/G40510DP\""},{"id":"GlycanIUPAC_T40","span":{"begin":859,"end":865},"obj":"\"http://rdf.glycoinfo.org/glycan/G61120TK\""},{"id":"GlycanIUPAC_T41","span":{"begin":859,"end":865},"obj":"\"http://rdf.glycoinfo.org/glycan/G41342KV\""},{"id":"GlycanIUPAC_T42","span":{"begin":859,"end":865},"obj":"\"http://rdf.glycoinfo.org/glycan/G90703NA\""},{"id":"GlycanIUPAC_T43","span":{"begin":859,"end":865},"obj":"\"http://rdf.glycoinfo.org/glycan/G01591HR\""},{"id":"GlycanIUPAC_T44","span":{"begin":859,"end":865},"obj":"\"http://rdf.glycoinfo.org/glycan/G56520XN\""},{"id":"GlycanIUPAC_T45","span":{"begin":859,"end":865},"obj":"\"http://rdf.glycoinfo.org/glycan/G81830JX\""}],"text":"Structural studies of the O-antigen polysaccharide from Escherichia coli O115 and biosynthetic aspects thereof.\nThe structure of the O-antigen polysaccharide (PS) of Escherichia coli O115 has been investigated using a combination of component analysis and 1D and 2D nuclear magnetic resonance (NMR) spectroscopy experiments. The repeating unit of the O-antigen was elucidated using the O-deacetylated PS and has the following branched pentasaccharide structure: →3)[β-L-Rhap-(1 → 4)]-β-D-GlcpNAc-(1 → 4)-α-D-GalpA-(1 → 3)-α-D-Manp-(1 → 3)-β-D-GlcpNAc-(1→. Cross-peaks of low intensity, corresponding to a β-L-Rhap-(1 → 4)-β-D-GlcpNAc-(1→ structural element, were present in the NMR spectra and attributed to the terminal part of the PS; this information defines the biological repeating unit of the O-antigen by having a 3-substituted N-acetyl-D-glucosamine (GlcNAc) residue at its reducing end. Analysis of the NMR spectra of the native PS revealed O-acetyl groups distributed over different positions of the l-Rhap residue (∼0.70 per repeating unit) as well as at O-2 and O-3 of the D-GalpA residue (∼0.03 and ∼0.25 per repeating unit, respectively), which is in agreement with the presence of two acetyltransferases previously identified in the O-antigen gene cluster (Wang Q, Ruan X, Wei D, Hu Z, Wu L, Yu T, Feng L, Wang L. 2010. Mol Cell Probes. 24:286-290.). In addition, the four glycosyltransferases initially identified in the O-antigen gene cluster of E. coli O115 were analyzed using BLAST, and the function of two of them predicted on the basis of similarities with glycosyltransferases from Shigella dysenteriae type 5 and 12, as well as E. coli O58 and O152."}

    NGLY1-deficiency

    {"project":"NGLY1-deficiency","denotations":[{"id":"PD-NGLY1-deficiency-B_T1","span":{"begin":859,"end":865},"obj":"chem:24139"}],"namespaces":[{"prefix":"hgnc","uri":"https://www.genenames.org/data/gene-symbol-report/#!/hgnc_id/HGNC:"},{"prefix":"omim","uri":"https://www.omim.org/entry/"},{"prefix":"chem","uri":"https://pubchem.ncbi.nlm.nih.gov/compound/"}],"text":"Structural studies of the O-antigen polysaccharide from Escherichia coli O115 and biosynthetic aspects thereof.\nThe structure of the O-antigen polysaccharide (PS) of Escherichia coli O115 has been investigated using a combination of component analysis and 1D and 2D nuclear magnetic resonance (NMR) spectroscopy experiments. The repeating unit of the O-antigen was elucidated using the O-deacetylated PS and has the following branched pentasaccharide structure: →3)[β-L-Rhap-(1 → 4)]-β-D-GlcpNAc-(1 → 4)-α-D-GalpA-(1 → 3)-α-D-Manp-(1 → 3)-β-D-GlcpNAc-(1→. Cross-peaks of low intensity, corresponding to a β-L-Rhap-(1 → 4)-β-D-GlcpNAc-(1→ structural element, were present in the NMR spectra and attributed to the terminal part of the PS; this information defines the biological repeating unit of the O-antigen by having a 3-substituted N-acetyl-D-glucosamine (GlcNAc) residue at its reducing end. Analysis of the NMR spectra of the native PS revealed O-acetyl groups distributed over different positions of the l-Rhap residue (∼0.70 per repeating unit) as well as at O-2 and O-3 of the D-GalpA residue (∼0.03 and ∼0.25 per repeating unit, respectively), which is in agreement with the presence of two acetyltransferases previously identified in the O-antigen gene cluster (Wang Q, Ruan X, Wei D, Hu Z, Wu L, Yu T, Feng L, Wang L. 2010. Mol Cell Probes. 24:286-290.). In addition, the four glycosyltransferases initially identified in the O-antigen gene cluster of E. coli O115 were analyzed using BLAST, and the function of two of them predicted on the basis of similarities with glycosyltransferases from Shigella dysenteriae type 5 and 12, as well as E. coli O58 and O152."}

    NCBITAXON

    {"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":56,"end":72},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":166,"end":182},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":1463,"end":1470},"obj":"OrganismTaxon"},{"id":"T4","span":{"begin":1605,"end":1625},"obj":"OrganismTaxon"},{"id":"T5","span":{"begin":1652,"end":1659},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"562"},{"id":"A2","pred":"db_id","subj":"T2","obj":"562"},{"id":"A3","pred":"db_id","subj":"T3","obj":"562"},{"id":"A4","pred":"db_id","subj":"T4","obj":"622"},{"id":"A5","pred":"db_id","subj":"T5","obj":"562"}],"text":"Structural studies of the O-antigen polysaccharide from Escherichia coli O115 and biosynthetic aspects thereof.\nThe structure of the O-antigen polysaccharide (PS) of Escherichia coli O115 has been investigated using a combination of component analysis and 1D and 2D nuclear magnetic resonance (NMR) spectroscopy experiments. The repeating unit of the O-antigen was elucidated using the O-deacetylated PS and has the following branched pentasaccharide structure: →3)[β-L-Rhap-(1 → 4)]-β-D-GlcpNAc-(1 → 4)-α-D-GalpA-(1 → 3)-α-D-Manp-(1 → 3)-β-D-GlcpNAc-(1→. Cross-peaks of low intensity, corresponding to a β-L-Rhap-(1 → 4)-β-D-GlcpNAc-(1→ structural element, were present in the NMR spectra and attributed to the terminal part of the PS; this information defines the biological repeating unit of the O-antigen by having a 3-substituted N-acetyl-D-glucosamine (GlcNAc) residue at its reducing end. Analysis of the NMR spectra of the native PS revealed O-acetyl groups distributed over different positions of the l-Rhap residue (∼0.70 per repeating unit) as well as at O-2 and O-3 of the D-GalpA residue (∼0.03 and ∼0.25 per repeating unit, respectively), which is in agreement with the presence of two acetyltransferases previously identified in the O-antigen gene cluster (Wang Q, Ruan X, Wei D, Hu Z, Wu L, Yu T, Feng L, Wang L. 2010. Mol Cell Probes. 24:286-290.). In addition, the four glycosyltransferases initially identified in the O-antigen gene cluster of E. coli O115 were analyzed using BLAST, and the function of two of them predicted on the basis of similarities with glycosyltransferases from Shigella dysenteriae type 5 and 12, as well as E. coli O58 and O152."}