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PubMed:1629216
Annnotations
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 |
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-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 |
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 |
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. |
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 |
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 |
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 |