PubMed:23307905
Annnotations
Glycan-Motif
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
T1 | 188-203 | https://glytoucan.org/Structures/Glycans/G00065MO | denotes | polysialic acid |
T2 | 205-212 | https://glytoucan.org/Structures/Glycans/G00065MO | denotes | polySia |
T3 | 805-812 | https://glytoucan.org/Structures/Glycans/G00065MO | denotes | polySia |
GlyCosmos6-Glycan-Motif-Image
Id | Subject | Object | Predicate | Lexical cue | image |
---|---|---|---|---|---|
T1 | 188-203 | Glycan_Motif | denotes | polysialic acid | https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00065MO |
T2 | 205-212 | Glycan_Motif | denotes | polySia | https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00065MO |
T3 | 805-812 | Glycan_Motif | denotes | polySia | https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00065MO |
sentences
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
TextSentencer_T1 | 0-102 | Sentence | denotes | A single amino acid toggles Escherichia coli polysialyltransferases between mono- and bifunctionality. |
TextSentencer_T2 | 103-255 | Sentence | denotes | The enteropathogenic Escherichia coli K92 synthesizes a unique capsule consisting of polysialic acid (polySia) with alternating α2,8- and α2,9-linkages. |
TextSentencer_T3 | 256-450 | Sentence | denotes | The fact that a single enzyme is responsible for the synthesis of these alternating regioisomeric linkages raises questions as to how this controlled bifunctionality is achieved mechanistically. |
TextSentencer_T4 | 451-725 | Sentence | denotes | Aiming to identify the sequence elements responsible for dual regiospecificity, we have utilized a high-throughput polysialyltransferase (polyST) activity screen to explore the relevant sequence space between this enzyme and its close monofunctional homolog from E. coli K1. |
TextSentencer_T5 | 726-855 | Sentence | denotes | The linkage specificity of selected mutants was subsequently confirmed using a polySia permethylation linkage analysis technique. |
TextSentencer_T6 | 856-984 | Sentence | denotes | We have identified a single amino acid exchange at residue 52 that toggles these enzymes between mono and dual regiospecificity. |
TextSentencer_T7 | 985-1098 | Sentence | denotes | The results have implications for the mechanism by which the E. coli K92 polyST achieves bifunctional elongation. |
T1 | 0-102 | Sentence | denotes | A single amino acid toggles Escherichia coli polysialyltransferases between mono- and bifunctionality. |
T2 | 103-255 | Sentence | denotes | The enteropathogenic Escherichia coli K92 synthesizes a unique capsule consisting of polysialic acid (polySia) with alternating α2,8- and α2,9-linkages. |
T3 | 256-450 | Sentence | denotes | The fact that a single enzyme is responsible for the synthesis of these alternating regioisomeric linkages raises questions as to how this controlled bifunctionality is achieved mechanistically. |
T4 | 451-725 | Sentence | denotes | Aiming to identify the sequence elements responsible for dual regiospecificity, we have utilized a high-throughput polysialyltransferase (polyST) activity screen to explore the relevant sequence space between this enzyme and its close monofunctional homolog from E. coli K1. |
T5 | 726-855 | Sentence | denotes | The linkage specificity of selected mutants was subsequently confirmed using a polySia permethylation linkage analysis technique. |
T6 | 856-984 | Sentence | denotes | We have identified a single amino acid exchange at residue 52 that toggles these enzymes between mono and dual regiospecificity. |
T7 | 985-1098 | Sentence | denotes | The results have implications for the mechanism by which the E. coli K92 polyST achieves bifunctional elongation. |
T1 | 0-102 | Sentence | denotes | A single amino acid toggles Escherichia coli polysialyltransferases between mono- and bifunctionality. |
T2 | 103-255 | Sentence | denotes | The enteropathogenic Escherichia coli K92 synthesizes a unique capsule consisting of polysialic acid (polySia) with alternating α2,8- and α2,9-linkages. |
T3 | 256-450 | Sentence | denotes | The fact that a single enzyme is responsible for the synthesis of these alternating regioisomeric linkages raises questions as to how this controlled bifunctionality is achieved mechanistically. |
T4 | 451-725 | Sentence | denotes | Aiming to identify the sequence elements responsible for dual regiospecificity, we have utilized a high-throughput polysialyltransferase (polyST) activity screen to explore the relevant sequence space between this enzyme and its close monofunctional homolog from E. coli K1. |
T5 | 726-855 | Sentence | denotes | The linkage specificity of selected mutants was subsequently confirmed using a polySia permethylation linkage analysis technique. |
T6 | 856-984 | Sentence | denotes | We have identified a single amino acid exchange at residue 52 that toggles these enzymes between mono and dual regiospecificity. |
T7 | 985-1098 | Sentence | denotes | The results have implications for the mechanism by which the E. coli K92 polyST achieves bifunctional elongation. |
GlyCosmos6-Glycan-Motif-Structure
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
T1 | 188-203 | https://glytoucan.org/Structures/Glycans/G00065MO | denotes | polysialic acid |
GlycoBiology-PACDB
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
_T1 | 28-44 | 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 |
_T2 | 28-44 | http://acgg.asia/db/diseases/pacdb/lec?ids=LEC636 | denotes | Escherichia coli |
_T3 | 28-44 | http://acgg.asia/db/diseases/pacdb/lec?ids=LEC157,LEC407 | denotes | Escherichia coli |
_T4 | 28-44 | 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 |
_T5 | 28-44 | http://acgg.asia/db/diseases/pacdb/lec?ids=LEC754 | denotes | Escherichia coli |
_T6 | 28-44 | http://acgg.asia/db/diseases/pacdb/lec?ids=LEC244,LEC256,LEC354 | denotes | Escherichia coli |
_T7 | 28-44 | http://acgg.asia/db/diseases/pacdb/lec?ids=LEC243,LEC640 | denotes | Escherichia coli |
_T8 | 28-44 | http://acgg.asia/db/diseases/pacdb/lec?ids=LEC487 | denotes | Escherichia coli |
_T9 | 28-44 | http://acgg.asia/db/diseases/pacdb/lec?ids=LEC295,LEC417 | denotes | Escherichia coli |
_T10 | 124-140 | http://acgg.asia/db/diseases/pacdb/lec?ids=LEC295,LEC417 | denotes | Escherichia coli |
_T11 | 124-140 | http://acgg.asia/db/diseases/pacdb/lec?ids=LEC243,LEC640 | denotes | Escherichia coli |
_T12 | 124-140 | http://acgg.asia/db/diseases/pacdb/lec?ids=LEC636 | denotes | Escherichia coli |
_T13 | 124-140 | 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 |
_T14 | 124-140 | http://acgg.asia/db/diseases/pacdb/lec?ids=LEC754 | denotes | Escherichia coli |
_T15 | 124-140 | 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 |
_T16 | 124-140 | http://acgg.asia/db/diseases/pacdb/lec?ids=LEC157,LEC407 | denotes | Escherichia coli |
_T17 | 124-140 | http://acgg.asia/db/diseases/pacdb/lec?ids=LEC244,LEC256,LEC354 | denotes | Escherichia coli |
_T18 | 124-144 | http://acgg.asia/db/diseases/pacdb/lec?ids=LEC720 | denotes | Escherichia coli K92 |
_T19 | 124-144 | http://acgg.asia/db/diseases/pacdb/lec?ids=LEC487 | denotes | Escherichia coli K92 |
ICD10
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
T1 | 107-140 | http://purl.bioontology.org/ontology/ICD10/A04.0 | denotes | enteropathogenic Escherichia coli |
GlycoBiology-FMA
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
_T1 | 9-19 | FMAID:82739 | denotes | amino acid |
_T2 | 9-19 | FMAID:196728 | denotes | amino acid |
_T3 | 166-173 | FMAID:85272 | denotes | capsule |
_T4 | 166-173 | FMAID:199625 | denotes | capsule |
_T5 | 884-894 | FMAID:82739 | denotes | amino acid |
_T6 | 884-894 | FMAID:196728 | denotes | amino acid |
uniprot-human
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
T1 | 722-724 | http://www.uniprot.org/uniprot/P04264 | denotes | K1 |
uniprot-mouse
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
T1 | 722-724 | http://www.uniprot.org/uniprot/P04104 | denotes | K1 |
GlycoBiology-NCBITAXON
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
T1 | 28-39 | http://purl.bioontology.org/ontology/NCBITAXON/561 | denotes | Escherichia |
T2 | 124-135 | http://purl.bioontology.org/ontology/NCBITAXON/561 | denotes | Escherichia |
T3 | 1023-1032 | http://purl.bioontology.org/ontology/NCBITAXON/127244 | denotes | mechanism |
GO-BP
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
T1 | 309-318 | http://purl.obolibrary.org/obo/GO_0009058 | denotes | synthesis |
T2 | 895-903 | http://purl.obolibrary.org/obo/GO_0015297 | denotes | exchange |
UBERON-AE
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
T1 | 166-173 | http://purl.obolibrary.org/obo/UBERON_0003893 | denotes | capsule |
Allie
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
SS1_23307905_1_0 | 188-203 | expanded | denotes | polysialic acid |
SS2_23307905_1_0 | 205-212 | abbr | denotes | polySia |
SS1_23307905_3_0 | 566-587 | expanded | denotes | polysialyltransferase |
SS2_23307905_3_0 | 589-595 | abbr | denotes | polyST |
AE1_23307905_1_0 | SS1_23307905_1_0 | SS2_23307905_1_0 | abbreviatedTo | polysialic acid,polySia |
AE1_23307905_3_0 | SS1_23307905_3_0 | SS2_23307905_3_0 | abbreviatedTo | polysialyltransferase,polyST |
GlycoBiology-Epitope
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
PD-GlycoEpitope-B_T1 | 915-917 | http://www.glycoepitope.jp/epitopes/AN0785 | denotes | 52 |
performance-test
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
PD-UBERON-AE-B_T1 | 166-173 | http://purl.obolibrary.org/obo/UBERON_0003893 | denotes | capsule |
NCBITAXON
Id | Subject | Object | Predicate | Lexical cue | db_id |
---|---|---|---|---|---|
T1 | 28-44 | OrganismTaxon | denotes | Escherichia coli | 562 |
T2 | 124-140 | OrganismTaxon | denotes | Escherichia coli | 562 |
T3 | 714-721 | OrganismTaxon | denotes | E. coli | 562 |
T4 | 1046-1053 | OrganismTaxon | denotes | E. coli | 562 |
Anatomy-UBERON
Id | Subject | Object | Predicate | Lexical cue | uberon_id |
---|---|---|---|---|---|
T1 | 646-651 | Body_part | denotes | space | http://purl.obolibrary.org/obo/UBERON_0000464 |