PubMed:28138013
Annnotations
GlyCosmos6-Glycan-Motif-Image
Id | Subject | Object | Predicate | Lexical cue | image |
---|---|---|---|---|---|
T1 | 0-10 | Glycan_Motif | denotes | Hyaluronan | https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00017MO |
T2 | 30-40 | Glycan_Motif | denotes | hyaluronan | https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00017MO |
T3 | 88-98 | Glycan_Motif | denotes | hyaluronan | https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00017MO |
T4 | 178-188 | Glycan_Motif | denotes | hyaluronan | https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00017MO |
GlyCosmos6-Glycan-Motif-Structure
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
T1 | 0-10 | https://glytoucan.org/Structures/Glycans/G00017MO | denotes | Hyaluronan |
T2 | 30-40 | https://glytoucan.org/Structures/Glycans/G00017MO | denotes | hyaluronan |
T3 | 88-98 | https://glytoucan.org/Structures/Glycans/G00017MO | denotes | hyaluronan |
T4 | 178-188 | https://glytoucan.org/Structures/Glycans/G00017MO | denotes | hyaluronan |
sentences
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
TextSentencer_T1 | 0-169 | Sentence | denotes | Hyaluronan synthase assembles hyaluronan on a [GlcNAc(β1,4)]n-GlcNAc(α1→)UDP primer and hyaluronan retains this residual chitin oligomer as a cap at the nonreducing end. |
TextSentencer_T2 | 170-286 | Sentence | denotes | Class I hyaluronan synthases (HAS) assemble [GlcNAc(β1,4)GlcUA(β1,3)]n-UDP at the reducing end and also make chitin. |
TextSentencer_T3 | 287-415 | Sentence | denotes | Streptococcus equisimilis HAS (SeHAS) also synthesizes chitin-UDP oligosaccharides, (GlcNAc-β1,4)n-GlcNAc(α1→)UDP (Weigel et al. |
TextSentencer_T4 | 416-422 | Sentence | denotes | 2015). |
TextSentencer_T5 | 423-557 | Sentence | denotes | Here we determined if HAS uses chitin-UDPs as primers to initiate HA synthesis, leaving the non-HA primer at the nonreducing (NR) end. |
TextSentencer_T6 | 558-728 | Sentence | denotes | HA made by SeHAS membranes was purified, digested with streptomyces lyase, and hydrophobic oligomers were enriched by solid phase extraction and analyzed by MALDI-TOF MS. |
TextSentencer_T7 | 729-937 | Sentence | denotes | Jack bean hexosaminidase (JBH) and MS/MS were used to analyze 19 m/z species of possible GnHn ions with clustered GlcNAc (G) residues attached to disaccharide units (H): (GlcNAcβ1,4)2-5[GlcUA(β1,3)GlcNAc]2-6. |
TextSentencer_T8 | 938-1068 | Sentence | denotes | JBH digestion sequentially removed GlcNAc from the NR-end of GnHn oligomers, producing successively smaller GnH2-3 series members. |
TextSentencer_T9 | 1069-1167 | Sentence | denotes | Since lyase releases dehydro-oligos (dHn; M-18), only the unique NR-end oligo lacks dehydro-GlcUA. |
TextSentencer_T10 | 1168-1307 | Sentence | denotes | Hn oligomers were undetectable in lyase digests, whereas JBH treatment created new H2-6m/z peaks (i.e. HA tetra- through dodeca-oligomers). |
TextSentencer_T11 | 1308-1436 | Sentence | denotes | MS/MS of larger GnHn species produced chitin (2-5 GlcNAcs), HA oligomers and multiple smaller series members with fewer GlcNAcs. |
TextSentencer_T12 | 1437-1603 | Sentence | denotes | All NR-ends (97%) started with GlcNAc, as a chitin trimer (three GlcNAcs), indicating that GlcNAc(β1,4)2GlcNAc(α1→)-UDP may be optimal for initiation of HA synthesis. |
TextSentencer_T13 | 1604-1674 | Sentence | denotes | Also, HA made by live S. pyogenes cells had G4Hn chitin-oligo NR-ends. |
TextSentencer_T14 | 1675-1887 | Sentence | denotes | We conclude that chitin-UDP functions in vitro and in live cells as a primer to initiate synthesis of all HA chains and these primers remain at the NR-ends of HA chains as residual chitin caps [(GlcNAc-β1,4)3-4]. |
T1 | 0-169 | Sentence | denotes | Hyaluronan synthase assembles hyaluronan on a [GlcNAc(β1,4)]n-GlcNAc(α1→)UDP primer and hyaluronan retains this residual chitin oligomer as a cap at the nonreducing end. |
T2 | 170-286 | Sentence | denotes | Class I hyaluronan synthases (HAS) assemble [GlcNAc(β1,4)GlcUA(β1,3)]n-UDP at the reducing end and also make chitin. |
T3 | 287-415 | Sentence | denotes | Streptococcus equisimilis HAS (SeHAS) also synthesizes chitin-UDP oligosaccharides, (GlcNAc-β1,4)n-GlcNAc(α1→)UDP (Weigel et al. |
T4 | 416-422 | Sentence | denotes | 2015). |
T5 | 423-557 | Sentence | denotes | Here we determined if HAS uses chitin-UDPs as primers to initiate HA synthesis, leaving the non-HA primer at the nonreducing (NR) end. |
T6 | 558-728 | Sentence | denotes | HA made by SeHAS membranes was purified, digested with streptomyces lyase, and hydrophobic oligomers were enriched by solid phase extraction and analyzed by MALDI-TOF MS. |
T7 | 729-937 | Sentence | denotes | Jack bean hexosaminidase (JBH) and MS/MS were used to analyze 19 m/z species of possible GnHn ions with clustered GlcNAc (G) residues attached to disaccharide units (H): (GlcNAcβ1,4)2-5[GlcUA(β1,3)GlcNAc]2-6. |
T8 | 938-1068 | Sentence | denotes | JBH digestion sequentially removed GlcNAc from the NR-end of GnHn oligomers, producing successively smaller GnH2-3 series members. |
T9 | 1069-1167 | Sentence | denotes | Since lyase releases dehydro-oligos (dHn; M-18), only the unique NR-end oligo lacks dehydro-GlcUA. |
T10 | 1168-1307 | Sentence | denotes | Hn oligomers were undetectable in lyase digests, whereas JBH treatment created new H2-6m/z peaks (i.e. HA tetra- through dodeca-oligomers). |
T11 | 1308-1436 | Sentence | denotes | MS/MS of larger GnHn species produced chitin (2-5 GlcNAcs), HA oligomers and multiple smaller series members with fewer GlcNAcs. |
T12 | 1437-1603 | Sentence | denotes | All NR-ends (97%) started with GlcNAc, as a chitin trimer (three GlcNAcs), indicating that GlcNAc(β1,4)2GlcNAc(α1→)-UDP may be optimal for initiation of HA synthesis. |
T13 | 1604-1674 | Sentence | denotes | Also, HA made by live S. pyogenes cells had G4Hn chitin-oligo NR-ends. |
T14 | 1675-1887 | Sentence | denotes | We conclude that chitin-UDP functions in vitro and in live cells as a primer to initiate synthesis of all HA chains and these primers remain at the NR-ends of HA chains as residual chitin caps [(GlcNAc-β1,4)3-4]. |
NGLY1-deficiency
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
PD-NGLY1-deficiency-B_T1 | 47-53 | chem:24139 | denotes | GlcNAc |
PD-NGLY1-deficiency-B_T2 | 62-68 | chem:24139 | denotes | GlcNAc |
PD-NGLY1-deficiency-B_T3 | 215-221 | chem:24139 | denotes | GlcNAc |
PD-NGLY1-deficiency-B_T4 | 372-378 | chem:24139 | denotes | GlcNAc |
PD-NGLY1-deficiency-B_T5 | 386-392 | chem:24139 | denotes | GlcNAc |
PD-NGLY1-deficiency-B_T6 | 843-849 | chem:24139 | denotes | GlcNAc |
PD-NGLY1-deficiency-B_T7 | 926-932 | chem:24139 | denotes | GlcNAc |
PD-NGLY1-deficiency-B_T8 | 973-979 | chem:24139 | denotes | GlcNAc |
PD-NGLY1-deficiency-B_T9 | 1358-1365 | chem:24139 | denotes | GlcNAcs |
PD-NGLY1-deficiency-B_T10 | 1428-1435 | chem:24139 | denotes | GlcNAcs |
PD-NGLY1-deficiency-B_T11 | 1468-1474 | chem:24139 | denotes | GlcNAc |
PD-NGLY1-deficiency-B_T12 | 1502-1509 | chem:24139 | denotes | GlcNAcs |
PD-NGLY1-deficiency-B_T13 | 1528-1534 | chem:24139 | denotes | GlcNAc |
PD-NGLY1-deficiency-B_T14 | 1870-1876 | chem:24139 | denotes | GlcNAc |
mondo_disease
Id | Subject | Object | Predicate | Lexical cue | mondo_id |
---|---|---|---|---|---|
T1 | 200-203 | Disease | denotes | HAS | http://purl.obolibrary.org/obo/MONDO_0019395 |
T2 | 313-316 | Disease | denotes | HAS | http://purl.obolibrary.org/obo/MONDO_0019395 |
T3 | 445-448 | Disease | denotes | HAS | http://purl.obolibrary.org/obo/MONDO_0019395 |
Glycan-GlyCosmos
Id | Subject | Object | Predicate | Lexical cue | image |
---|---|---|---|---|---|
T1 | 121-127 | Glycan | denotes | chitin | https://api.glycosmos.org/wurcs2image/latest/png/binary/G97099AY |
T2 | 279-285 | Glycan | denotes | chitin | https://api.glycosmos.org/wurcs2image/latest/png/binary/G97099AY |
T3 | 342-348 | Glycan | denotes | chitin | https://api.glycosmos.org/wurcs2image/latest/png/binary/G97099AY |
T4 | 454-460 | Glycan | denotes | chitin | https://api.glycosmos.org/wurcs2image/latest/png/binary/G97099AY |
T5 | 1346-1352 | Glycan | denotes | chitin | https://api.glycosmos.org/wurcs2image/latest/png/binary/G97099AY |
T6 | 1481-1487 | Glycan | denotes | chitin | https://api.glycosmos.org/wurcs2image/latest/png/binary/G97099AY |
T7 | 1653-1659 | Glycan | denotes | chitin | https://api.glycosmos.org/wurcs2image/latest/png/binary/G97099AY |
T8 | 1692-1698 | Glycan | denotes | chitin | https://api.glycosmos.org/wurcs2image/latest/png/binary/G97099AY |
T9 | 1856-1862 | Glycan | denotes | chitin | https://api.glycosmos.org/wurcs2image/latest/png/binary/G97099AY |
GlyCosmos15-MONDO
Id | Subject | Object | Predicate | Lexical cue | mondo_id |
---|---|---|---|---|---|
T1 | 200-203 | Disease | denotes | HAS | http://purl.obolibrary.org/obo/MONDO_0019395 |
T2 | 313-316 | Disease | denotes | HAS | http://purl.obolibrary.org/obo/MONDO_0019395 |
T3 | 445-448 | Disease | denotes | HAS | http://purl.obolibrary.org/obo/MONDO_0019395 |
GlyCosmos15-NCBITAXON
Id | Subject | Object | Predicate | Lexical cue | db_id |
---|---|---|---|---|---|
T1 | 287-312 | OrganismTaxon | denotes | Streptococcus equisimilis | 119602 |
T2 | 613-625 | OrganismTaxon | denotes | streptomyces | 1883 |
GlyCosmos15-CL
Id | Subject | Object | Predicate | Lexical cue | cl_id |
---|---|---|---|---|---|
T1 | 140-145 | Cell | denotes | a cap | http://purl.obolibrary.org/obo/CL:4028003 |
GlyCosmos15-UBERON
Id | Subject | Object | Predicate | Lexical cue | uberon_id |
---|---|---|---|---|---|
T1 | 575-584 | Body_part | denotes | membranes | http://purl.obolibrary.org/obo/GO_0016020|http://purl.obolibrary.org/obo/UBERON_0000094|http://purl.obolibrary.org/obo/UBERON_0000158 |
sentences
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
TextSentencer_T1 | 0-169 | Sentence | denotes | Hyaluronan synthase assembles hyaluronan on a [GlcNAc(β1,4)]n-GlcNAc(α1→)UDP primer and hyaluronan retains this residual chitin oligomer as a cap at the nonreducing end. |
TextSentencer_T2 | 170-286 | Sentence | denotes | Class I hyaluronan synthases (HAS) assemble [GlcNAc(β1,4)GlcUA(β1,3)]n-UDP at the reducing end and also make chitin. |
TextSentencer_T3 | 287-415 | Sentence | denotes | Streptococcus equisimilis HAS (SeHAS) also synthesizes chitin-UDP oligosaccharides, (GlcNAc-β1,4)n-GlcNAc(α1→)UDP (Weigel et al. |
TextSentencer_T4 | 416-422 | Sentence | denotes | 2015). |
TextSentencer_T5 | 423-557 | Sentence | denotes | Here we determined if HAS uses chitin-UDPs as primers to initiate HA synthesis, leaving the non-HA primer at the nonreducing (NR) end. |
TextSentencer_T6 | 558-728 | Sentence | denotes | HA made by SeHAS membranes was purified, digested with streptomyces lyase, and hydrophobic oligomers were enriched by solid phase extraction and analyzed by MALDI-TOF MS. |
TextSentencer_T7 | 729-937 | Sentence | denotes | Jack bean hexosaminidase (JBH) and MS/MS were used to analyze 19 m/z species of possible GnHn ions with clustered GlcNAc (G) residues attached to disaccharide units (H): (GlcNAcβ1,4)2-5[GlcUA(β1,3)GlcNAc]2-6. |
TextSentencer_T8 | 938-1068 | Sentence | denotes | JBH digestion sequentially removed GlcNAc from the NR-end of GnHn oligomers, producing successively smaller GnH2-3 series members. |
TextSentencer_T9 | 1069-1167 | Sentence | denotes | Since lyase releases dehydro-oligos (dHn; M-18), only the unique NR-end oligo lacks dehydro-GlcUA. |
TextSentencer_T10 | 1168-1307 | Sentence | denotes | Hn oligomers were undetectable in lyase digests, whereas JBH treatment created new H2-6m/z peaks (i.e. HA tetra- through dodeca-oligomers). |
TextSentencer_T11 | 1308-1436 | Sentence | denotes | MS/MS of larger GnHn species produced chitin (2-5 GlcNAcs), HA oligomers and multiple smaller series members with fewer GlcNAcs. |
TextSentencer_T12 | 1437-1603 | Sentence | denotes | All NR-ends (97%) started with GlcNAc, as a chitin trimer (three GlcNAcs), indicating that GlcNAc(β1,4)2GlcNAc(α1→)-UDP may be optimal for initiation of HA synthesis. |
TextSentencer_T13 | 1604-1674 | Sentence | denotes | Also, HA made by live S. pyogenes cells had G4Hn chitin-oligo NR-ends. |
TextSentencer_T14 | 1675-1887 | Sentence | denotes | We conclude that chitin-UDP functions in vitro and in live cells as a primer to initiate synthesis of all HA chains and these primers remain at the NR-ends of HA chains as residual chitin caps [(GlcNAc-β1,4)3-4]. |
T1 | 0-169 | Sentence | denotes | Hyaluronan synthase assembles hyaluronan on a [GlcNAc(β1,4)]n-GlcNAc(α1→)UDP primer and hyaluronan retains this residual chitin oligomer as a cap at the nonreducing end. |
T2 | 170-286 | Sentence | denotes | Class I hyaluronan synthases (HAS) assemble [GlcNAc(β1,4)GlcUA(β1,3)]n-UDP at the reducing end and also make chitin. |
T3 | 287-415 | Sentence | denotes | Streptococcus equisimilis HAS (SeHAS) also synthesizes chitin-UDP oligosaccharides, (GlcNAc-β1,4)n-GlcNAc(α1→)UDP (Weigel et al. |
T4 | 416-422 | Sentence | denotes | 2015). |
T5 | 423-557 | Sentence | denotes | Here we determined if HAS uses chitin-UDPs as primers to initiate HA synthesis, leaving the non-HA primer at the nonreducing (NR) end. |
T6 | 558-728 | Sentence | denotes | HA made by SeHAS membranes was purified, digested with streptomyces lyase, and hydrophobic oligomers were enriched by solid phase extraction and analyzed by MALDI-TOF MS. |
T7 | 729-937 | Sentence | denotes | Jack bean hexosaminidase (JBH) and MS/MS were used to analyze 19 m/z species of possible GnHn ions with clustered GlcNAc (G) residues attached to disaccharide units (H): (GlcNAcβ1,4)2-5[GlcUA(β1,3)GlcNAc]2-6. |
T8 | 938-1068 | Sentence | denotes | JBH digestion sequentially removed GlcNAc from the NR-end of GnHn oligomers, producing successively smaller GnH2-3 series members. |
T9 | 1069-1167 | Sentence | denotes | Since lyase releases dehydro-oligos (dHn; M-18), only the unique NR-end oligo lacks dehydro-GlcUA. |
T10 | 1168-1307 | Sentence | denotes | Hn oligomers were undetectable in lyase digests, whereas JBH treatment created new H2-6m/z peaks (i.e. HA tetra- through dodeca-oligomers). |
T11 | 1308-1436 | Sentence | denotes | MS/MS of larger GnHn species produced chitin (2-5 GlcNAcs), HA oligomers and multiple smaller series members with fewer GlcNAcs. |
T12 | 1437-1603 | Sentence | denotes | All NR-ends (97%) started with GlcNAc, as a chitin trimer (three GlcNAcs), indicating that GlcNAc(β1,4)2GlcNAc(α1→)-UDP may be optimal for initiation of HA synthesis. |
T13 | 1604-1674 | Sentence | denotes | Also, HA made by live S. pyogenes cells had G4Hn chitin-oligo NR-ends. |
T14 | 1675-1887 | Sentence | denotes | We conclude that chitin-UDP functions in vitro and in live cells as a primer to initiate synthesis of all HA chains and these primers remain at the NR-ends of HA chains as residual chitin caps [(GlcNAc-β1,4)3-4]. |
GlyCosmos15-Sentences
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
T1 | 0-169 | Sentence | denotes | Hyaluronan synthase assembles hyaluronan on a [GlcNAc(β1,4)]n-GlcNAc(α1→)UDP primer and hyaluronan retains this residual chitin oligomer as a cap at the nonreducing end. |
T2 | 170-286 | Sentence | denotes | Class I hyaluronan synthases (HAS) assemble [GlcNAc(β1,4)GlcUA(β1,3)]n-UDP at the reducing end and also make chitin. |
T3 | 287-415 | Sentence | denotes | Streptococcus equisimilis HAS (SeHAS) also synthesizes chitin-UDP oligosaccharides, (GlcNAc-β1,4)n-GlcNAc(α1→)UDP (Weigel et al. |
T4 | 416-422 | Sentence | denotes | 2015). |
T5 | 423-557 | Sentence | denotes | Here we determined if HAS uses chitin-UDPs as primers to initiate HA synthesis, leaving the non-HA primer at the nonreducing (NR) end. |
T6 | 558-728 | Sentence | denotes | HA made by SeHAS membranes was purified, digested with streptomyces lyase, and hydrophobic oligomers were enriched by solid phase extraction and analyzed by MALDI-TOF MS. |
T7 | 729-937 | Sentence | denotes | Jack bean hexosaminidase (JBH) and MS/MS were used to analyze 19 m/z species of possible GnHn ions with clustered GlcNAc (G) residues attached to disaccharide units (H): (GlcNAcβ1,4)2-5[GlcUA(β1,3)GlcNAc]2-6. |
T8 | 938-1068 | Sentence | denotes | JBH digestion sequentially removed GlcNAc from the NR-end of GnHn oligomers, producing successively smaller GnH2-3 series members. |
T9 | 1069-1167 | Sentence | denotes | Since lyase releases dehydro-oligos (dHn; M-18), only the unique NR-end oligo lacks dehydro-GlcUA. |
T10 | 1168-1307 | Sentence | denotes | Hn oligomers were undetectable in lyase digests, whereas JBH treatment created new H2-6m/z peaks (i.e. HA tetra- through dodeca-oligomers). |
T11 | 1308-1436 | Sentence | denotes | MS/MS of larger GnHn species produced chitin (2-5 GlcNAcs), HA oligomers and multiple smaller series members with fewer GlcNAcs. |
T12 | 1437-1603 | Sentence | denotes | All NR-ends (97%) started with GlcNAc, as a chitin trimer (three GlcNAcs), indicating that GlcNAc(β1,4)2GlcNAc(α1→)-UDP may be optimal for initiation of HA synthesis. |
T13 | 1604-1674 | Sentence | denotes | Also, HA made by live S. pyogenes cells had G4Hn chitin-oligo NR-ends. |
T14 | 1675-1887 | Sentence | denotes | We conclude that chitin-UDP functions in vitro and in live cells as a primer to initiate synthesis of all HA chains and these primers remain at the NR-ends of HA chains as residual chitin caps [(GlcNAc-β1,4)3-4]. |
GlyCosmos15-Glycan
Id | Subject | Object | Predicate | Lexical cue | image |
---|---|---|---|---|---|
T1 | 121-127 | Glycan | denotes | chitin | https://api.glycosmos.org/wurcs2image/latest/png/binary/G97099AY |
T2 | 279-285 | Glycan | denotes | chitin | https://api.glycosmos.org/wurcs2image/latest/png/binary/G97099AY |
T3 | 342-348 | Glycan | denotes | chitin | https://api.glycosmos.org/wurcs2image/latest/png/binary/G97099AY |
T4 | 454-460 | Glycan | denotes | chitin | https://api.glycosmos.org/wurcs2image/latest/png/binary/G97099AY |
T5 | 1346-1352 | Glycan | denotes | chitin | https://api.glycosmos.org/wurcs2image/latest/png/binary/G97099AY |
T6 | 1481-1487 | Glycan | denotes | chitin | https://api.glycosmos.org/wurcs2image/latest/png/binary/G97099AY |
T7 | 1653-1659 | Glycan | denotes | chitin | https://api.glycosmos.org/wurcs2image/latest/png/binary/G97099AY |
T8 | 1692-1698 | Glycan | denotes | chitin | https://api.glycosmos.org/wurcs2image/latest/png/binary/G97099AY |
T9 | 1856-1862 | Glycan | denotes | chitin | https://api.glycosmos.org/wurcs2image/latest/png/binary/G97099AY |
NCBITAXON
Id | Subject | Object | Predicate | Lexical cue | db_id |
---|---|---|---|---|---|
T1 | 287-312 | OrganismTaxon | denotes | Streptococcus equisimilis | 119602 |
T2 | 613-625 | OrganismTaxon | denotes | streptomyces | 1883 |
Anatomy-UBERON
Id | Subject | Object | Predicate | Lexical cue | uberon_id |
---|---|---|---|---|---|
T1 | 575-584 | Body_part | denotes | membranes | http://purl.obolibrary.org/obo/GO_0016020|http://purl.obolibrary.org/obo/UBERON_0000094|http://purl.obolibrary.org/obo/UBERON_0000158 |
CL-cell
Id | Subject | Object | Predicate | Lexical cue | cl_id |
---|---|---|---|---|---|
T1 | 140-145 | Cell | denotes | a cap | http://purl.obolibrary.org/obo/CL:4028003 |