PubMed:21084405
Annnotations
GlycoBiology-FMA
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| _T1 | 113-129 | FMAID:196731 | denotes | oligosaccharides |
| _T2 | 113-129 | FMAID:82742 | denotes | oligosaccharides |
| _T3 | 161-177 | FMAID:196731 | denotes | oligosaccharides |
| _T4 | 161-177 | FMAID:82742 | denotes | oligosaccharides |
| _T5 | 257-264 | FMAID:178661 | denotes | testing |
| _T6 | 363-379 | FMAID:82742 | denotes | oligosaccharides |
| _T7 | 363-379 | FMAID:196731 | denotes | oligosaccharides |
| _T8 | 463-479 | FMAID:196731 | denotes | oligosaccharides |
| _T9 | 463-479 | FMAID:82742 | denotes | oligosaccharides |
| _T10 | 1003-1019 | FMAID:196731 | denotes | oligosaccharides |
| _T11 | 1003-1019 | FMAID:82742 | denotes | oligosaccharides |
| _T12 | 1123-1136 | FMAID:196789 | denotes | galactosidase |
| _T13 | 1123-1136 | FMAID:82794 | denotes | galactosidase |
| _T14 | 1292-1308 | FMAID:196731 | denotes | oligosaccharides |
| _T15 | 1292-1308 | FMAID:82742 | denotes | oligosaccharides |
uniprot-mouse
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| T1 | 192-196 | http://www.uniprot.org/uniprot/O35111 | denotes | task |
GlycoBiology-NCBITAXON
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| T1 | 37-47 | http://purl.bioontology.org/ontology/NCBITAXON/188709 | denotes | Thermotoga |
| T2 | 37-47 | http://purl.bioontology.org/ontology/NCBITAXON/200918 | denotes | Thermotoga |
| T3 | 37-47 | http://purl.bioontology.org/ontology/NCBITAXON/188708 | denotes | Thermotoga |
| T4 | 37-47 | http://purl.bioontology.org/ontology/NCBITAXON/2335 | denotes | Thermotoga |
| T5 | 37-56 | http://purl.bioontology.org/ontology/NCBITAXON/2336 | denotes | Thermotoga maritima |
| T6 | 66-70 | http://purl.bioontology.org/ontology/NCBITAXON/158455 | denotes | beta |
| T7 | 66-70 | http://purl.bioontology.org/ontology/NCBITAXON/3554 | denotes | beta |
| T8 | 1146-1173 | http://purl.bioontology.org/ontology/NCBITAXON/198711 | denotes | hyperthermophilic bacterium |
| T9 | 1164-1173 | http://purl.bioontology.org/ontology/NCBITAXON/336400 | denotes | bacterium |
| T10 | 1164-1173 | http://purl.bioontology.org/ontology/NCBITAXON/538104 | denotes | bacterium |
| T11 | 1164-1173 | http://purl.bioontology.org/ontology/NCBITAXON/1368069 | denotes | bacterium |
| T12 | 1164-1173 | http://purl.bioontology.org/ontology/NCBITAXON/538107 | denotes | bacterium |
| T13 | 1164-1173 | http://purl.bioontology.org/ontology/NCBITAXON/538108 | denotes | bacterium |
| T14 | 1164-1173 | http://purl.bioontology.org/ontology/NCBITAXON/538113 | denotes | bacterium |
| T15 | 1164-1173 | http://purl.bioontology.org/ontology/NCBITAXON/538117 | denotes | bacterium |
| T16 | 1164-1173 | http://purl.bioontology.org/ontology/NCBITAXON/538101 | denotes | bacterium |
| T17 | 1164-1173 | http://purl.bioontology.org/ontology/NCBITAXON/138290 | denotes | bacterium |
| T18 | 1164-1173 | http://purl.bioontology.org/ontology/NCBITAXON/336403 | denotes | bacterium |
| T19 | 1164-1173 | http://purl.bioontology.org/ontology/NCBITAXON/538099 | denotes | bacterium |
| T20 | 1164-1173 | http://purl.bioontology.org/ontology/NCBITAXON/1144558 | denotes | bacterium |
| T21 | 1164-1173 | http://purl.bioontology.org/ontology/NCBITAXON/336405 | denotes | bacterium |
| T22 | 1164-1173 | http://purl.bioontology.org/ontology/NCBITAXON/674166 | denotes | bacterium |
| T23 | 1164-1173 | http://purl.bioontology.org/ontology/NCBITAXON/400048 | denotes | bacterium |
| T24 | 1164-1173 | http://purl.bioontology.org/ontology/NCBITAXON/538097 | denotes | bacterium |
| T25 | 1164-1173 | http://purl.bioontology.org/ontology/NCBITAXON/538091 | denotes | bacterium |
| T26 | 1164-1173 | http://purl.bioontology.org/ontology/NCBITAXON/1730 | denotes | bacterium |
| T27 | 1164-1173 | http://purl.bioontology.org/ontology/NCBITAXON/538085 | denotes | bacterium |
| T28 | 1164-1173 | http://purl.bioontology.org/ontology/NCBITAXON/538084 | denotes | bacterium |
| T29 | 1164-1173 | http://purl.bioontology.org/ontology/NCBITAXON/538076 | denotes | bacterium |
| T30 | 1164-1173 | http://purl.bioontology.org/ontology/NCBITAXON/538075 | denotes | bacterium |
| T31 | 1164-1173 | http://purl.bioontology.org/ontology/NCBITAXON/538072 | denotes | bacterium |
| T32 | 1164-1173 | http://purl.bioontology.org/ontology/NCBITAXON/336404 | denotes | bacterium |
| T33 | 1174-1184 | http://purl.bioontology.org/ontology/NCBITAXON/188708 | denotes | Thermotoga |
| T34 | 1174-1184 | http://purl.bioontology.org/ontology/NCBITAXON/200918 | denotes | Thermotoga |
| T35 | 1174-1184 | http://purl.bioontology.org/ontology/NCBITAXON/2335 | denotes | Thermotoga |
| T36 | 1174-1184 | http://purl.bioontology.org/ontology/NCBITAXON/188709 | denotes | Thermotoga |
| T37 | 1174-1193 | http://purl.bioontology.org/ontology/NCBITAXON/2336 | denotes | Thermotoga maritima |
GO-BP
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| T1 | 740-748 | http://purl.obolibrary.org/obo/GO_0070085 | denotes | glycosyl |
| T2 | 797-805 | http://purl.obolibrary.org/obo/GO_0070085 | denotes | glycosyl |
| T3 | 1350-1358 | http://purl.obolibrary.org/obo/GO_0070085 | denotes | glycosyl |
| T4 | 1244-1253 | http://purl.obolibrary.org/obo/GO_0009058 | denotes | synthesis |
UBERON-AE
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| T1 | 141-146 | http://purl.obolibrary.org/obo/UBERON_0002542 | denotes | scale |
Allie
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| SS1_21084405_3_0 | 642-664 | expanded | denotes | glycoside hydrolase 29 |
| SS2_21084405_3_0 | 666-670 | abbr | denotes | GH29 |
| AE1_21084405_3_0 | SS1_21084405_3_0 | SS2_21084405_3_0 | abbreviatedTo | glycoside hydrolase 29,GH29 |
GlycoBiology-MAT
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| T1 | 1164-1173 | http://purl.obolibrary.org/obo/MAT_0000191 | denotes | bacterium |
sentences
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| TextSentencer_T1 | 0-130 | Sentence | denotes | A novel alpha-D-galactosynthase from Thermotoga maritima converts beta-D-galactopyranosyl azide to alpha-galacto-oligosaccharides. |
| TextSentencer_T2 | 131-309 | Sentence | denotes | The large-scale production of oligosaccharides is a daunting task, hampering the study of the role of glycans in vivo and the testing of the efficacy of novel glycan-based drugs. |
| TextSentencer_T3 | 310-480 | Sentence | denotes | Glycosynthases, mutated glycosidases that synthesize oligosaccharides in high yields, are becoming important chemo-enzymatic tools for the production of oligosaccharides. |
| TextSentencer_T4 | 481-822 | Sentence | denotes | However, while β-glycosynthase can be produced with a rather well-established technology, examples of α-glycosynthases are thus far limited only to enzymes from glycoside hydrolase 29 (GH29), GH31 and GH95 families. α-L-Fucosynthases from GH29 use convenient glycosyl azide derivatives as a strategic alternative to glycosyl fluoride donors. |
| TextSentencer_T5 | 823-942 | Sentence | denotes | However, the general applicability of this method to other α-glycosynthases is not trivial and remains to be confirmed. |
| TextSentencer_T6 | 943-1194 | Sentence | denotes | Here, β-D-galactopyranosyl azide was converted to α-galacto-oligosaccharides with good yields and high regioselectivity, catalyzed by a novel α-galactosynthase based on the GH36 α-galactosidase from the hyperthermophilic bacterium Thermotoga maritima. |
| TextSentencer_T7 | 1195-1444 | Sentence | denotes | These results open a new avenue to the practical synthesis of biologically interesting α-galacto-oligosaccharides and demonstrate more widespread use of β-glycosyl-azide as donors, confirming their utility to expand the repertoire of glycosynthases. |
| T1 | 0-130 | Sentence | denotes | A novel alpha-D-galactosynthase from Thermotoga maritima converts beta-D-galactopyranosyl azide to alpha-galacto-oligosaccharides. |
| T2 | 131-309 | Sentence | denotes | The large-scale production of oligosaccharides is a daunting task, hampering the study of the role of glycans in vivo and the testing of the efficacy of novel glycan-based drugs. |
| T3 | 310-480 | Sentence | denotes | Glycosynthases, mutated glycosidases that synthesize oligosaccharides in high yields, are becoming important chemo-enzymatic tools for the production of oligosaccharides. |
| T4 | 481-822 | Sentence | denotes | However, while β-glycosynthase can be produced with a rather well-established technology, examples of α-glycosynthases are thus far limited only to enzymes from glycoside hydrolase 29 (GH29), GH31 and GH95 families. α-L-Fucosynthases from GH29 use convenient glycosyl azide derivatives as a strategic alternative to glycosyl fluoride donors. |
| T5 | 823-942 | Sentence | denotes | However, the general applicability of this method to other α-glycosynthases is not trivial and remains to be confirmed. |
| T6 | 943-1194 | Sentence | denotes | Here, β-D-galactopyranosyl azide was converted to α-galacto-oligosaccharides with good yields and high regioselectivity, catalyzed by a novel α-galactosynthase based on the GH36 α-galactosidase from the hyperthermophilic bacterium Thermotoga maritima. |
| T7 | 1195-1444 | Sentence | denotes | These results open a new avenue to the practical synthesis of biologically interesting α-galacto-oligosaccharides and demonstrate more widespread use of β-glycosyl-azide as donors, confirming their utility to expand the repertoire of glycosynthases. |
| T1 | 0-130 | Sentence | denotes | A novel alpha-D-galactosynthase from Thermotoga maritima converts beta-D-galactopyranosyl azide to alpha-galacto-oligosaccharides. |
| T2 | 131-309 | Sentence | denotes | The large-scale production of oligosaccharides is a daunting task, hampering the study of the role of glycans in vivo and the testing of the efficacy of novel glycan-based drugs. |
| T3 | 310-480 | Sentence | denotes | Glycosynthases, mutated glycosidases that synthesize oligosaccharides in high yields, are becoming important chemo-enzymatic tools for the production of oligosaccharides. |
| T4 | 481-822 | Sentence | denotes | However, while β-glycosynthase can be produced with a rather well-established technology, examples of α-glycosynthases are thus far limited only to enzymes from glycoside hydrolase 29 (GH29), GH31 and GH95 families. α-L-Fucosynthases from GH29 use convenient glycosyl azide derivatives as a strategic alternative to glycosyl fluoride donors. |
| T5 | 823-942 | Sentence | denotes | However, the general applicability of this method to other α-glycosynthases is not trivial and remains to be confirmed. |
| T6 | 943-1194 | Sentence | denotes | Here, β-D-galactopyranosyl azide was converted to α-galacto-oligosaccharides with good yields and high regioselectivity, catalyzed by a novel α-galactosynthase based on the GH36 α-galactosidase from the hyperthermophilic bacterium Thermotoga maritima. |
| T7 | 1195-1444 | Sentence | denotes | These results open a new avenue to the practical synthesis of biologically interesting α-galacto-oligosaccharides and demonstrate more widespread use of β-glycosyl-azide as donors, confirming their utility to expand the repertoire of glycosynthases. |
performance-test
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| PD-UBERON-AE-B_T1 | 141-146 | http://purl.obolibrary.org/obo/UBERON_0002542 | denotes | scale |
NCBITAXON
| Id | Subject | Object | Predicate | Lexical cue | db_id |
|---|---|---|---|---|---|
| T1 | 37-56 | OrganismTaxon | denotes | Thermotoga maritima | 2336 |
| T2 | 1174-1193 | OrganismTaxon | denotes | Thermotoga maritima | 2336 |
Anatomy-UBERON
| Id | Subject | Object | Predicate | Lexical cue | uberon_id |
|---|---|---|---|---|---|
| T1 | 141-146 | Body_part | denotes | scale | http://purl.obolibrary.org/obo/UBERON_0002542 |