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PubMed:1629216 JSONTXT

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CL-cell

Id Subject Object Predicate Lexical cue cl_id
T1 133-140 Cell denotes epsilon http://purl.obolibrary.org/obo/CL:0003025
T2 665-672 Cell denotes epsilon http://purl.obolibrary.org/obo/CL:0003025
T3 751-758 Cell denotes epsilon http://purl.obolibrary.org/obo/CL:0003025
T4 812-819 Cell denotes epsilon http://purl.obolibrary.org/obo/CL:0003025
T5 878-885 Cell denotes epsilon http://purl.obolibrary.org/obo/CL:0003025
T6 893-900 Cell denotes epsilon http://purl.obolibrary.org/obo/CL:0003025
T7 1128-1135 Cell denotes epsilon http://purl.obolibrary.org/obo/CL:0003025
T8 1142-1149 Cell denotes epsilon http://purl.obolibrary.org/obo/CL:0003025
T9 1245-1252 Cell denotes epsilon http://purl.obolibrary.org/obo/CL:0003025
T10 1296-1303 Cell denotes epsilon http://purl.obolibrary.org/obo/CL:0003025
T11 1340-1347 Cell denotes epsilon http://purl.obolibrary.org/obo/CL:0003025
T12 1395-1402 Cell denotes epsilon http://purl.obolibrary.org/obo/CL:0003025
T13 1424-1431 Cell denotes epsilon http://purl.obolibrary.org/obo/CL:0003025
T14 1502-1509 Cell denotes epsilon http://purl.obolibrary.org/obo/CL:0003025
T15 1581-1588 Cell denotes epsilon http://purl.obolibrary.org/obo/CL:0003025
T16 1655-1662 Cell denotes epsilon http://purl.obolibrary.org/obo/CL:0003025
T17 1712-1724 Cell denotes erythrocytes http://purl.obolibrary.org/obo/CL:0000232
T18 1734-1741 Cell denotes epsilon http://purl.obolibrary.org/obo/CL:0003025
T19 1842-1849 Cell denotes epsilon http://purl.obolibrary.org/obo/CL:0003025
T20 1889-1896 Cell denotes epsilon http://purl.obolibrary.org/obo/CL:0003025

sentences

Id Subject Object Predicate Lexical cue
T1 0-111 Sentence denotes Biochemical and biophysical characterization of human recombinant IgE-binding protein, an S-type animal lectin.
T2 112-205 Sentence denotes IgE-binding protein (epsilon BP) was originally identified by virtue of its affinity for IgE.
T3 206-331 Sentence denotes It is now known to be a beta-galactoside-binding lectin with the characteristic of an S-type carbohydrate recognition domain.
T4 332-537 Sentence denotes The protein is composed of two domains: the amino-terminal domain consisting of tandem repeats and the carboxyl-terminal domain containing sequences shared by other S-type carbohydrate recognition domains.
T5 538-643 Sentence denotes The amino-terminal domain also contains a number of potential recognition sites for collagenase cleavage.
T6 644-823 Sentence denotes In this study, human epsilon BP was first expressed in Escherichia coli, and the carboxyl-terminal domain (epsilon BP-C) was then generated by collagenase digestion of epsilon BP.
T7 824-1015 Sentence denotes By equilibrium dialysis, the association constants of epsilon BP and epsilon BP-C for lactose were found to be similar (6.0 +/- 0.70) x 10(4) M-1 and (4.7 +/- 0.27) x 10(4) M-1, respectively.
T8 1016-1081 Sentence denotes Both polypeptides contain only one lactose-binding site/molecule.
T9 1082-1307 Sentence denotes By an assay involving binding of 125I-labeled epsilon BP or epsilon BP-C to solid phase IgE, and inhibition of this binding by saccharides, it was determined that epsilon BP-C retains the saccharide specificity of epsilon BP.
T10 1308-1523 Sentence denotes Importantly, although unlabeled epsilon BP-C inhibited the binding of the radiolabeled epsilon BP to IgE, unlabeled epsilon BP caused increased binding to IgE, suggesting self-association among epsilon BP molecules.
T11 1524-1641 Sentence denotes Oligomeric structures resulting from self-association of epsilon BP were confirmed by chemical cross-linking studies.
T12 1642-1767 Sentence denotes Furthermore, epsilon BP possesses hemagglutination activity on rabbit erythrocytes, whereas epsilon BP-C lacks such activity.
T13 1768-1978 Sentence denotes Based on these results, we propose a structural model for multivalency of epsilon BP: dimerization or oligomerization of epsilon BP occurs through intermolecular interaction involving the amino-terminal domain.
T1 0-111 Sentence denotes Biochemical and biophysical characterization of human recombinant IgE-binding protein, an S-type animal lectin.
T2 112-205 Sentence denotes IgE-binding protein (epsilon BP) was originally identified by virtue of its affinity for IgE.
T3 206-331 Sentence denotes It is now known to be a beta-galactoside-binding lectin with the characteristic of an S-type carbohydrate recognition domain.
T4 332-537 Sentence denotes The protein is composed of two domains: the amino-terminal domain consisting of tandem repeats and the carboxyl-terminal domain containing sequences shared by other S-type carbohydrate recognition domains.
T5 538-643 Sentence denotes The amino-terminal domain also contains a number of potential recognition sites for collagenase cleavage.
T6 644-823 Sentence denotes In this study, human epsilon BP was first expressed in Escherichia coli, and the carboxyl-terminal domain (epsilon BP-C) was then generated by collagenase digestion of epsilon BP.
T7 824-1015 Sentence denotes By equilibrium dialysis, the association constants of epsilon BP and epsilon BP-C for lactose were found to be similar (6.0 +/- 0.70) x 10(4) M-1 and (4.7 +/- 0.27) x 10(4) M-1, respectively.
T8 1016-1081 Sentence denotes Both polypeptides contain only one lactose-binding site/molecule.
T9 1082-1307 Sentence denotes By an assay involving binding of 125I-labeled epsilon BP or epsilon BP-C to solid phase IgE, and inhibition of this binding by saccharides, it was determined that epsilon BP-C retains the saccharide specificity of epsilon BP.
T10 1308-1523 Sentence denotes Importantly, although unlabeled epsilon BP-C inhibited the binding of the radiolabeled epsilon BP to IgE, unlabeled epsilon BP caused increased binding to IgE, suggesting self-association among epsilon BP molecules.
T11 1524-1641 Sentence denotes Oligomeric structures resulting from self-association of epsilon BP were confirmed by chemical cross-linking studies.
T12 1642-1767 Sentence denotes Furthermore, epsilon BP possesses hemagglutination activity on rabbit erythrocytes, whereas epsilon BP-C lacks such activity.
T13 1768-1978 Sentence denotes Based on these results, we propose a structural model for multivalency of epsilon BP: dimerization or oligomerization of epsilon BP occurs through intermolecular interaction involving the amino-terminal domain.

PubmedHPO

Id Subject Object Predicate Lexical cue
T1 1712-1724 HP_0001901 denotes erythrocytes

GlyCosmos15-Glycan

Id Subject Object Predicate Lexical cue image
T1 910-917 Glycan denotes lactose https://api.glycosmos.org/wurcs2image/latest/png/binary/G15541SE
T2 1051-1058 Glycan denotes lactose https://api.glycosmos.org/wurcs2image/latest/png/binary/G15541SE

Glycan-GlyCosmos

Id Subject Object Predicate Lexical cue image
T1 910-917 Glycan denotes lactose https://api.glycosmos.org/wurcs2image/latest/png/binary/G15541SE
T2 1051-1058 Glycan denotes lactose https://api.glycosmos.org/wurcs2image/latest/png/binary/G15541SE

GlyCosmos15-CL

Id Subject Object Predicate Lexical cue cl_id
T1 133-140 Cell denotes epsilon http://purl.obolibrary.org/obo/CL:0003025
T2 665-672 Cell denotes epsilon http://purl.obolibrary.org/obo/CL:0003025
T3 751-758 Cell denotes epsilon http://purl.obolibrary.org/obo/CL:0003025
T4 812-819 Cell denotes epsilon http://purl.obolibrary.org/obo/CL:0003025
T5 878-885 Cell denotes epsilon http://purl.obolibrary.org/obo/CL:0003025
T6 893-900 Cell denotes epsilon http://purl.obolibrary.org/obo/CL:0003025
T7 1128-1135 Cell denotes epsilon http://purl.obolibrary.org/obo/CL:0003025
T8 1142-1149 Cell denotes epsilon http://purl.obolibrary.org/obo/CL:0003025
T9 1245-1252 Cell denotes epsilon http://purl.obolibrary.org/obo/CL:0003025
T10 1296-1303 Cell denotes epsilon http://purl.obolibrary.org/obo/CL:0003025
T11 1340-1347 Cell denotes epsilon http://purl.obolibrary.org/obo/CL:0003025
T12 1395-1402 Cell denotes epsilon http://purl.obolibrary.org/obo/CL:0003025
T13 1424-1431 Cell denotes epsilon http://purl.obolibrary.org/obo/CL:0003025
T14 1502-1509 Cell denotes epsilon http://purl.obolibrary.org/obo/CL:0003025
T15 1581-1588 Cell denotes epsilon http://purl.obolibrary.org/obo/CL:0003025
T16 1655-1662 Cell denotes epsilon http://purl.obolibrary.org/obo/CL:0003025
T17 1712-1724 Cell denotes erythrocytes http://purl.obolibrary.org/obo/CL:0000232
T18 1734-1741 Cell denotes epsilon http://purl.obolibrary.org/obo/CL:0003025
T19 1842-1849 Cell denotes epsilon http://purl.obolibrary.org/obo/CL:0003025
T20 1889-1896 Cell denotes epsilon http://purl.obolibrary.org/obo/CL:0003025

GlyCosmos15-UBERON

Id Subject Object Predicate Lexical cue uberon_id
T1 1712-1724 Body_part denotes erythrocytes http://purl.obolibrary.org/obo/CL_0000232

GlyCosmos15-Taxon

Id Subject Object Predicate Lexical cue db_id
T1 48-53 Organism denotes human 9606
T2 659-664 Organism denotes human 9606
T3 699-715 Organism denotes Escherichia coli 562
T4 839-847 Organism denotes dialysis 124307

GlyCosmos15-Sentences

Id Subject Object Predicate Lexical cue
T1 0-111 Sentence denotes Biochemical and biophysical characterization of human recombinant IgE-binding protein, an S-type animal lectin.
T2 112-205 Sentence denotes IgE-binding protein (epsilon BP) was originally identified by virtue of its affinity for IgE.
T3 206-331 Sentence denotes It is now known to be a beta-galactoside-binding lectin with the characteristic of an S-type carbohydrate recognition domain.
T4 332-537 Sentence denotes The protein is composed of two domains: the amino-terminal domain consisting of tandem repeats and the carboxyl-terminal domain containing sequences shared by other S-type carbohydrate recognition domains.
T5 538-643 Sentence denotes The amino-terminal domain also contains a number of potential recognition sites for collagenase cleavage.
T6 644-823 Sentence denotes In this study, human epsilon BP was first expressed in Escherichia coli, and the carboxyl-terminal domain (epsilon BP-C) was then generated by collagenase digestion of epsilon BP.
T7 824-1015 Sentence denotes By equilibrium dialysis, the association constants of epsilon BP and epsilon BP-C for lactose were found to be similar (6.0 +/- 0.70) x 10(4) M-1 and (4.7 +/- 0.27) x 10(4) M-1, respectively.
T8 1016-1081 Sentence denotes Both polypeptides contain only one lactose-binding site/molecule.
T9 1082-1307 Sentence denotes By an assay involving binding of 125I-labeled epsilon BP or epsilon BP-C to solid phase IgE, and inhibition of this binding by saccharides, it was determined that epsilon BP-C retains the saccharide specificity of epsilon BP.
T10 1308-1523 Sentence denotes Importantly, although unlabeled epsilon BP-C inhibited the binding of the radiolabeled epsilon BP to IgE, unlabeled epsilon BP caused increased binding to IgE, suggesting self-association among epsilon BP molecules.
T11 1524-1641 Sentence denotes Oligomeric structures resulting from self-association of epsilon BP were confirmed by chemical cross-linking studies.
T12 1642-1767 Sentence denotes Furthermore, epsilon BP possesses hemagglutination activity on rabbit erythrocytes, whereas epsilon BP-C lacks such activity.
T13 1768-1978 Sentence denotes Based on these results, we propose a structural model for multivalency of epsilon BP: dimerization or oligomerization of epsilon BP occurs through intermolecular interaction involving the amino-terminal domain.

Lectin-Jamboree-Sentence

Id Subject Object Predicate Lexical cue
T1 0-111 Sentence denotes Biochemical and biophysical characterization of human recombinant IgE-binding protein, an S-type animal lectin.
T2 112-205 Sentence denotes IgE-binding protein (epsilon BP) was originally identified by virtue of its affinity for IgE.
T3 206-331 Sentence denotes It is now known to be a beta-galactoside-binding lectin with the characteristic of an S-type carbohydrate recognition domain.
T4 332-537 Sentence denotes The protein is composed of two domains: the amino-terminal domain consisting of tandem repeats and the carboxyl-terminal domain containing sequences shared by other S-type carbohydrate recognition domains.
T5 538-643 Sentence denotes The amino-terminal domain also contains a number of potential recognition sites for collagenase cleavage.
T6 644-823 Sentence denotes In this study, human epsilon BP was first expressed in Escherichia coli, and the carboxyl-terminal domain (epsilon BP-C) was then generated by collagenase digestion of epsilon BP.
T7 824-1015 Sentence denotes By equilibrium dialysis, the association constants of epsilon BP and epsilon BP-C for lactose were found to be similar (6.0 +/- 0.70) x 10(4) M-1 and (4.7 +/- 0.27) x 10(4) M-1, respectively.
T8 1016-1081 Sentence denotes Both polypeptides contain only one lactose-binding site/molecule.
T9 1082-1307 Sentence denotes By an assay involving binding of 125I-labeled epsilon BP or epsilon BP-C to solid phase IgE, and inhibition of this binding by saccharides, it was determined that epsilon BP-C retains the saccharide specificity of epsilon BP.
T10 1308-1523 Sentence denotes Importantly, although unlabeled epsilon BP-C inhibited the binding of the radiolabeled epsilon BP to IgE, unlabeled epsilon BP caused increased binding to IgE, suggesting self-association among epsilon BP molecules.
T11 1524-1641 Sentence denotes Oligomeric structures resulting from self-association of epsilon BP were confirmed by chemical cross-linking studies.
T12 1642-1767 Sentence denotes Furthermore, epsilon BP possesses hemagglutination activity on rabbit erythrocytes, whereas epsilon BP-C lacks such activity.
T13 1768-1978 Sentence denotes Based on these results, we propose a structural model for multivalency of epsilon BP: dimerization or oligomerization of epsilon BP occurs through intermolecular interaction involving the amino-terminal domain.

GlyCosmos15-FMA

Id Subject Object Predicate Lexical cue db_id
T1 1712-1724 Body_part denotes erythrocytes FMA:62845

NCBITAXON

Id Subject Object Predicate Lexical cue db_id
T1 48-53 OrganismTaxon denotes human 9606
T2 659-664 OrganismTaxon denotes human 9606
T3 699-715 OrganismTaxon denotes Escherichia coli 562
T4 839-847 OrganismTaxon denotes dialysis 124307

Anatomy-UBERON

Id Subject Object Predicate Lexical cue uberon_id
T1 1712-1724 Body_part denotes erythrocytes http://purl.obolibrary.org/obo/CL_0000232