PubMed:20798114
Annnotations
Glycan-Motif
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
T1 | 548-554 | https://glytoucan.org/Structures/Glycans/G82576YO | denotes | fucose |
T2 | 675-681 | https://glytoucan.org/Structures/Glycans/G82576YO | denotes | fucose |
GlyCosmos6-Glycan-Motif-Image
Id | Subject | Object | Predicate | Lexical cue | image |
---|---|---|---|---|---|
T1 | 548-554 | Glycan_Motif | denotes | fucose | https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G82576YO |
T2 | 675-681 | Glycan_Motif | denotes | fucose | https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G82576YO |
GlyCosmos6-Glycan-Motif-Structure
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
T1 | 548-554 | https://glytoucan.org/Structures/Glycans/G82576YO | denotes | fucose |
T2 | 675-681 | https://glytoucan.org/Structures/Glycans/G82576YO | denotes | fucose |
sentences
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
TextSentencer_T1 | 0-102 | Sentence | denotes | Production and characterization of a monomeric form and a single-site form of Aleuria aurantia lectin. |
TextSentencer_T2 | 103-195 | Sentence | denotes | Lectins have widely been used in structural and functional studies of complex carbohydrates. |
TextSentencer_T3 | 196-298 | Sentence | denotes | They usually bind carbohydrates with relatively low affinity, but compensate for this by multivalency. |
TextSentencer_T4 | 299-501 | Sentence | denotes | This multivalent nature of lectins can sometimes produce unwanted reactions such as agglutination or precipitation of target glycoproteins, when using them in different biological and analytical assays. |
TextSentencer_T5 | 502-583 | Sentence | denotes | The mushroom lectin Aleuria aurantia binds to fucose-containing oligosaccharides. |
TextSentencer_T6 | 584-682 | Sentence | denotes | It is composed of two identical subunits, and each subunit contains five binding sites for fucose. |
TextSentencer_T7 | 683-773 | Sentence | denotes | In this study, two forms of recombinant AAL were produced using site-directed mutagenesis. |
TextSentencer_T8 | 774-985 | Sentence | denotes | A monomeric form of AAL was produced by exchanging Tyr6 with Arg6, and a single-site fragment of AAL was produced by insertion of an NdeI restriction enzyme cleavage site and a stop codon in the coding sequence. |
TextSentencer_T9 | 986-1098 | Sentence | denotes | The AAL forms were expressed as His-tagged proteins in Escherichia coli and purified by affinity chromatography. |
TextSentencer_T10 | 1099-1260 | Sentence | denotes | Binding properties of the two AAL forms were performed using surface plasmon resonance, enzyme-linked lectin assay analyses and isothermal titration calorimetry. |
TextSentencer_T11 | 1261-1391 | Sentence | denotes | Both the monomeric AAL (mAAL) and the single-site AAL (S2-AAL) forms retained their capacity to bind fucosylated oligosaccharides. |
TextSentencer_T12 | 1392-1611 | Sentence | denotes | However, both constructs exhibited properties that differed from the intact recombinant AAL (rAAL). mAAL showed similar binding affinities to fucosylated oligosaccharides as rAAL, but had less hemagglutinating capacity. |
TextSentencer_T13 | 1612-1774 | Sentence | denotes | S2-AAL showed a lower binding affinity to fucosylated oligosaccharides and, in contrast to rAAL and mAAL, S2-AAL did not bind to sialylated fuco-oligosaccharides. |
TextSentencer_T14 | 1775-1960 | Sentence | denotes | The study shows that molecular engineering is a highly useful tool for producing lectins with more defined properties such as decreased valency and defined specificities and affinities. |
TextSentencer_T15 | 1961-2082 | Sentence | denotes | Thus, this approach has high potential in developing reliable diagnostic and biological assays for carbohydrate analysis. |
T1 | 0-102 | Sentence | denotes | Production and characterization of a monomeric form and a single-site form of Aleuria aurantia lectin. |
T2 | 103-195 | Sentence | denotes | Lectins have widely been used in structural and functional studies of complex carbohydrates. |
T3 | 196-298 | Sentence | denotes | They usually bind carbohydrates with relatively low affinity, but compensate for this by multivalency. |
T4 | 299-501 | Sentence | denotes | This multivalent nature of lectins can sometimes produce unwanted reactions such as agglutination or precipitation of target glycoproteins, when using them in different biological and analytical assays. |
T5 | 502-583 | Sentence | denotes | The mushroom lectin Aleuria aurantia binds to fucose-containing oligosaccharides. |
T6 | 584-682 | Sentence | denotes | It is composed of two identical subunits, and each subunit contains five binding sites for fucose. |
T7 | 683-773 | Sentence | denotes | In this study, two forms of recombinant AAL were produced using site-directed mutagenesis. |
T8 | 774-985 | Sentence | denotes | A monomeric form of AAL was produced by exchanging Tyr6 with Arg6, and a single-site fragment of AAL was produced by insertion of an NdeI restriction enzyme cleavage site and a stop codon in the coding sequence. |
T9 | 986-1098 | Sentence | denotes | The AAL forms were expressed as His-tagged proteins in Escherichia coli and purified by affinity chromatography. |
T10 | 1099-1260 | Sentence | denotes | Binding properties of the two AAL forms were performed using surface plasmon resonance, enzyme-linked lectin assay analyses and isothermal titration calorimetry. |
T11 | 1261-1391 | Sentence | denotes | Both the monomeric AAL (mAAL) and the single-site AAL (S2-AAL) forms retained their capacity to bind fucosylated oligosaccharides. |
T12 | 1392-1611 | Sentence | denotes | However, both constructs exhibited properties that differed from the intact recombinant AAL (rAAL). mAAL showed similar binding affinities to fucosylated oligosaccharides as rAAL, but had less hemagglutinating capacity. |
T13 | 1612-1774 | Sentence | denotes | S2-AAL showed a lower binding affinity to fucosylated oligosaccharides and, in contrast to rAAL and mAAL, S2-AAL did not bind to sialylated fuco-oligosaccharides. |
T14 | 1775-1960 | Sentence | denotes | The study shows that molecular engineering is a highly useful tool for producing lectins with more defined properties such as decreased valency and defined specificities and affinities. |
T15 | 1961-2082 | Sentence | denotes | Thus, this approach has high potential in developing reliable diagnostic and biological assays for carbohydrate analysis. |
T1 | 0-102 | Sentence | denotes | Production and characterization of a monomeric form and a single-site form of Aleuria aurantia lectin. |
T2 | 103-195 | Sentence | denotes | Lectins have widely been used in structural and functional studies of complex carbohydrates. |
T3 | 196-298 | Sentence | denotes | They usually bind carbohydrates with relatively low affinity, but compensate for this by multivalency. |
T4 | 299-501 | Sentence | denotes | This multivalent nature of lectins can sometimes produce unwanted reactions such as agglutination or precipitation of target glycoproteins, when using them in different biological and analytical assays. |
T5 | 502-583 | Sentence | denotes | The mushroom lectin Aleuria aurantia binds to fucose-containing oligosaccharides. |
T6 | 584-682 | Sentence | denotes | It is composed of two identical subunits, and each subunit contains five binding sites for fucose. |
T7 | 683-773 | Sentence | denotes | In this study, two forms of recombinant AAL were produced using site-directed mutagenesis. |
T8 | 774-985 | Sentence | denotes | A monomeric form of AAL was produced by exchanging Tyr6 with Arg6, and a single-site fragment of AAL was produced by insertion of an NdeI restriction enzyme cleavage site and a stop codon in the coding sequence. |
T9 | 986-1098 | Sentence | denotes | The AAL forms were expressed as His-tagged proteins in Escherichia coli and purified by affinity chromatography. |
T10 | 1099-1260 | Sentence | denotes | Binding properties of the two AAL forms were performed using surface plasmon resonance, enzyme-linked lectin assay analyses and isothermal titration calorimetry. |
T11 | 1261-1391 | Sentence | denotes | Both the monomeric AAL (mAAL) and the single-site AAL (S2-AAL) forms retained their capacity to bind fucosylated oligosaccharides. |
T12 | 1392-1611 | Sentence | denotes | However, both constructs exhibited properties that differed from the intact recombinant AAL (rAAL). mAAL showed similar binding affinities to fucosylated oligosaccharides as rAAL, but had less hemagglutinating capacity. |
T13 | 1612-1774 | Sentence | denotes | S2-AAL showed a lower binding affinity to fucosylated oligosaccharides and, in contrast to rAAL and mAAL, S2-AAL did not bind to sialylated fuco-oligosaccharides. |
T14 | 1775-1960 | Sentence | denotes | The study shows that molecular engineering is a highly useful tool for producing lectins with more defined properties such as decreased valency and defined specificities and affinities. |
T15 | 1961-2082 | Sentence | denotes | Thus, this approach has high potential in developing reliable diagnostic and biological assays for carbohydrate analysis. |
GlycoBiology-PACDB
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
_T1 | 1041-1057 | 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 | 1041-1057 | http://acgg.asia/db/diseases/pacdb/lec?ids=LEC157,LEC407 | denotes | Escherichia coli |
_T3 | 1041-1057 | http://acgg.asia/db/diseases/pacdb/lec?ids=LEC754 | denotes | Escherichia coli |
_T4 | 1041-1057 | http://acgg.asia/db/diseases/pacdb/lec?ids=LEC243,LEC640 | denotes | Escherichia coli |
_T5 | 1041-1057 | http://acgg.asia/db/diseases/pacdb/lec?ids=LEC295,LEC417 | denotes | Escherichia coli |
_T6 | 1041-1057 | http://acgg.asia/db/diseases/pacdb/lec?ids=LEC487 | denotes | Escherichia coli |
_T7 | 1041-1057 | http://acgg.asia/db/diseases/pacdb/lec?ids=LEC244,LEC256,LEC354 | denotes | Escherichia coli |
_T8 | 1041-1057 | 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 |
_T9 | 1041-1057 | http://acgg.asia/db/diseases/pacdb/lec?ids=LEC636 | denotes | Escherichia coli |
GlycoBiology-FMA
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
_T1 | 95-110 | FMAID:62931 | denotes | lectin. Lectins |
_T2 | 95-110 | FMAID:165243 | denotes | lectin. Lectins |
_T3 | 95-110 | FMAID:61795 | denotes | lectin. Lectins |
_T4 | 95-110 | FMAID:167265 | denotes | lectin. Lectins |
_T5 | 181-194 | FMAID:82737 | denotes | carbohydrates |
_T6 | 181-194 | FMAID:197276 | denotes | carbohydrates |
_T7 | 214-227 | FMAID:82737 | denotes | carbohydrates |
_T8 | 214-227 | FMAID:197276 | denotes | carbohydrates |
_T9 | 424-437 | FMAID:62925 | denotes | glycoproteins |
_T10 | 424-437 | FMAID:167256 | denotes | glycoproteins |
_T11 | 548-554 | FMAID:196784 | denotes | fucose |
_T12 | 548-554 | FMAID:82790 | denotes | fucose |
_T13 | 566-582 | FMAID:196731 | denotes | oligosaccharides |
_T14 | 566-582 | FMAID:82742 | denotes | oligosaccharides |
_T15 | 675-681 | FMAID:82790 | denotes | fucose |
_T16 | 675-681 | FMAID:196784 | denotes | fucose |
_T17 | 969-984 | FMAID:198074 | denotes | coding sequence |
_T18 | 1022-1037 | FMAID:166112 | denotes | tagged proteins |
_T19 | 1029-1037 | FMAID:67257 | denotes | proteins |
_T20 | 1029-1037 | FMAID:165447 | denotes | proteins |
_T21 | 1160-1167 | FMAID:50594 | denotes | surface |
_T22 | 1160-1167 | FMAID:146300 | denotes | surface |
_T23 | 1316-1318 | FMAID:63523 | denotes | S2 |
_T24 | 1316-1318 | FMAID:167751 | denotes | S2 |
_T25 | 1374-1390 | FMAID:82742 | denotes | oligosaccharides |
_T26 | 1374-1390 | FMAID:196731 | denotes | oligosaccharides |
_T27 | 1546-1562 | FMAID:196731 | denotes | oligosaccharides |
_T28 | 1546-1562 | FMAID:82742 | denotes | oligosaccharides |
_T29 | 1612-1614 | FMAID:63523 | denotes | S2 |
_T30 | 1612-1614 | FMAID:167751 | denotes | S2 |
_T31 | 1666-1682 | FMAID:82742 | denotes | oligosaccharides |
_T32 | 1666-1682 | FMAID:196731 | denotes | oligosaccharides |
_T33 | 1718-1720 | FMAID:167751 | denotes | S2 |
_T34 | 1718-1720 | FMAID:63523 | denotes | S2 |
_T35 | 1757-1773 | FMAID:82742 | denotes | oligosaccharides |
_T36 | 1757-1773 | FMAID:196731 | denotes | oligosaccharides |
_T37 | 2060-2072 | FMAID:197276 | denotes | carbohydrate |
_T38 | 2060-2072 | FMAID:82737 | denotes | carbohydrate |
GlycoBiology-NCBITAXON
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
T1 | 78-85 | http://purl.bioontology.org/ontology/NCBITAXON/5187 | denotes | Aleuria |
T2 | 78-94 | http://purl.bioontology.org/ontology/NCBITAXON/5188 | denotes | Aleuria aurantia |
T3 | 522-529 | http://purl.bioontology.org/ontology/NCBITAXON/5187 | denotes | Aleuria |
T4 | 522-538 | http://purl.bioontology.org/ontology/NCBITAXON/5188 | denotes | Aleuria aurantia |
T5 | 956-961 | http://purl.bioontology.org/ontology/NCBITAXON/79338 | denotes | codon |
T6 | 956-961 | http://purl.bioontology.org/ontology/NCBITAXON/722432 | denotes | codon |
T7 | 1041-1052 | http://purl.bioontology.org/ontology/NCBITAXON/561 | denotes | Escherichia |
GO-BP
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
T1 | 383-396 | http://purl.obolibrary.org/obo/GO_0000752 | denotes | agglutination |
T2 | 383-396 | http://purl.obolibrary.org/obo/GO_0007157 | denotes | agglutination |
T3 | 814-824 | http://purl.obolibrary.org/obo/GO_0015297 | denotes | exchanging |
T4 | 1362-1373 | http://purl.obolibrary.org/obo/GO_0036065 | denotes | fucosylated |
T5 | 1534-1545 | http://purl.obolibrary.org/obo/GO_0036065 | denotes | fucosylated |
T6 | 1654-1665 | http://purl.obolibrary.org/obo/GO_0036065 | denotes | fucosylated |
T7 | 1741-1751 | http://purl.obolibrary.org/obo/GO_0097503 | denotes | sialylated |
T8 | 2003-2013 | http://purl.obolibrary.org/obo/GO_0032502 | denotes | developing |
GO-MF
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
T1 | 209-213 | http://purl.obolibrary.org/obo/GO_0070026 | denotes | bind |
T2 | 1357-1361 | http://purl.obolibrary.org/obo/GO_0070026 | denotes | bind |
T3 | 539-544 | http://purl.obolibrary.org/obo/GO_0070026 | denotes | binds |
T4 | 657-664 | http://purl.obolibrary.org/obo/GO_0070026 | denotes | binding |
T5 | 1512-1519 | http://purl.obolibrary.org/obo/GO_0070026 | denotes | binding |
T6 | 1099-1106 | http://purl.obolibrary.org/obo/GO_0070026 | denotes | Binding |
T7 | 209-213 | http://purl.obolibrary.org/obo/GO_0003680 | denotes | bind |
T8 | 1357-1361 | http://purl.obolibrary.org/obo/GO_0003680 | denotes | bind |
T9 | 539-544 | http://purl.obolibrary.org/obo/GO_0003680 | denotes | binds |
T10 | 657-664 | http://purl.obolibrary.org/obo/GO_0003680 | denotes | binding |
T11 | 1512-1519 | http://purl.obolibrary.org/obo/GO_0003680 | denotes | binding |
T12 | 1099-1106 | http://purl.obolibrary.org/obo/GO_0003680 | denotes | Binding |
T13 | 209-213 | http://purl.obolibrary.org/obo/GO_0017091 | denotes | bind |
T14 | 1357-1361 | http://purl.obolibrary.org/obo/GO_0017091 | denotes | bind |
T15 | 539-544 | http://purl.obolibrary.org/obo/GO_0017091 | denotes | binds |
T16 | 657-664 | http://purl.obolibrary.org/obo/GO_0017091 | denotes | binding |
T17 | 1512-1519 | http://purl.obolibrary.org/obo/GO_0017091 | denotes | binding |
T18 | 1099-1106 | http://purl.obolibrary.org/obo/GO_0017091 | denotes | Binding |
T19 | 209-213 | http://purl.obolibrary.org/obo/GO_0005488 | denotes | bind |
T20 | 1357-1361 | http://purl.obolibrary.org/obo/GO_0005488 | denotes | bind |
T21 | 539-544 | http://purl.obolibrary.org/obo/GO_0005488 | denotes | binds |
T22 | 657-664 | http://purl.obolibrary.org/obo/GO_0005488 | denotes | binding |
T23 | 1512-1519 | http://purl.obolibrary.org/obo/GO_0005488 | denotes | binding |
T24 | 1099-1106 | http://purl.obolibrary.org/obo/GO_0005488 | denotes | Binding |
T25 | 209-227 | http://purl.obolibrary.org/obo/GO_0030246 | denotes | bind carbohydrates |
T26 | 539-554 | http://purl.obolibrary.org/obo/GO_0042806 | denotes | binds to fucose |
T27 | 1022-1037 | http://purl.obolibrary.org/obo/GO_0031386 | denotes | tagged proteins |
Allie
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
SS1_20798114_10_0 | 1270-1283 | expanded | denotes | monomeric AAL |
SS2_20798114_10_0 | 1285-1289 | abbr | denotes | mAAL |
SS1_20798114_11_0 | 1468-1483 | expanded | denotes | recombinant AAL |
SS2_20798114_11_0 | 1485-1489 | abbr | denotes | rAAL |
AE1_20798114_10_0 | SS1_20798114_10_0 | SS2_20798114_10_0 | abbreviatedTo | monomeric AAL,mAAL |
AE1_20798114_11_0 | SS1_20798114_11_0 | SS2_20798114_11_0 | abbreviatedTo | recombinant AAL,rAAL |
Lectin
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
Lectin_T1 | 1485-1489 | https://acgg.asia/db/lfdb/LfDB0396 | denotes | rAAL |
Lectin_T2 | 1566-1570 | https://acgg.asia/db/lfdb/LfDB0396 | denotes | rAAL |
Lectin_T3 | 1703-1707 | https://acgg.asia/db/lfdb/LfDB0396 | denotes | rAAL |
Lectin-Jamboree-small
Id | Subject | Object | Predicate | Lexical cue | glycosmos_id |
---|---|---|---|---|---|
T1 | 723-726 | Lectin | denotes | AAL | GL_001404 |
T2 | 794-797 | Lectin | denotes | AAL | GL_001404 |
T3 | 871-874 | Lectin | denotes | AAL | GL_001404 |
T4 | 990-993 | Lectin | denotes | AAL | GL_001404 |
T5 | 1129-1132 | Lectin | denotes | AAL | GL_001404 |
T6 | 1280-1283 | Lectin | denotes | AAL | GL_001404 |
T7 | 1311-1314 | Lectin | denotes | AAL | GL_001404 |
T8 | 1319-1322 | Lectin | denotes | AAL | GL_001404 |
T9 | 1480-1483 | Lectin | denotes | AAL | GL_001404 |
T10 | 1615-1618 | Lectin | denotes | AAL | GL_001404 |
T11 | 1721-1724 | Lectin | denotes | AAL | GL_001404 |
Lectin-Jamboree-Sentence
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
T1 | 0-102 | Sentence | denotes | Production and characterization of a monomeric form and a single-site form of Aleuria aurantia lectin. |
T2 | 103-195 | Sentence | denotes | Lectins have widely been used in structural and functional studies of complex carbohydrates. |
T3 | 196-298 | Sentence | denotes | They usually bind carbohydrates with relatively low affinity, but compensate for this by multivalency. |
T4 | 299-501 | Sentence | denotes | This multivalent nature of lectins can sometimes produce unwanted reactions such as agglutination or precipitation of target glycoproteins, when using them in different biological and analytical assays. |
T5 | 502-583 | Sentence | denotes | The mushroom lectin Aleuria aurantia binds to fucose-containing oligosaccharides. |
T6 | 584-682 | Sentence | denotes | It is composed of two identical subunits, and each subunit contains five binding sites for fucose. |
T7 | 683-773 | Sentence | denotes | In this study, two forms of recombinant AAL were produced using site-directed mutagenesis. |
T8 | 774-985 | Sentence | denotes | A monomeric form of AAL was produced by exchanging Tyr6 with Arg6, and a single-site fragment of AAL was produced by insertion of an NdeI restriction enzyme cleavage site and a stop codon in the coding sequence. |
T9 | 986-1098 | Sentence | denotes | The AAL forms were expressed as His-tagged proteins in Escherichia coli and purified by affinity chromatography. |
T10 | 1099-1260 | Sentence | denotes | Binding properties of the two AAL forms were performed using surface plasmon resonance, enzyme-linked lectin assay analyses and isothermal titration calorimetry. |
T11 | 1261-1391 | Sentence | denotes | Both the monomeric AAL (mAAL) and the single-site AAL (S2-AAL) forms retained their capacity to bind fucosylated oligosaccharides. |
T12 | 1392-1611 | Sentence | denotes | However, both constructs exhibited properties that differed from the intact recombinant AAL (rAAL). mAAL showed similar binding affinities to fucosylated oligosaccharides as rAAL, but had less hemagglutinating capacity. |
T13 | 1612-1774 | Sentence | denotes | S2-AAL showed a lower binding affinity to fucosylated oligosaccharides and, in contrast to rAAL and mAAL, S2-AAL did not bind to sialylated fuco-oligosaccharides. |
T14 | 1775-1960 | Sentence | denotes | The study shows that molecular engineering is a highly useful tool for producing lectins with more defined properties such as decreased valency and defined specificities and affinities. |
T15 | 1961-2082 | Sentence | denotes | Thus, this approach has high potential in developing reliable diagnostic and biological assays for carbohydrate analysis. |
NCBITAXON
Id | Subject | Object | Predicate | Lexical cue | db_id |
---|---|---|---|---|---|
T1 | 78-94 | OrganismTaxon | denotes | Aleuria aurantia | 5188 |
T2 | 522-538 | OrganismTaxon | denotes | Aleuria aurantia | 5188 |
T3 | 1041-1057 | OrganismTaxon | denotes | Escherichia coli | 562 |