PubMed:10814697 JSON TXT

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sentences

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":99},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":100,"end":219},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":220,"end":337},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":338,"end":607},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":608,"end":752},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":753,"end":832},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":833,"end":892},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":893,"end":1105},"obj":"Sentence"},{"id":"TextSentencer_T9","span":{"begin":1106,"end":1200},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":99},"obj":"Sentence"},{"id":"T2","span":{"begin":100,"end":219},"obj":"Sentence"},{"id":"T3","span":{"begin":220,"end":337},"obj":"Sentence"},{"id":"T4","span":{"begin":338,"end":607},"obj":"Sentence"},{"id":"T5","span":{"begin":608,"end":752},"obj":"Sentence"},{"id":"T6","span":{"begin":753,"end":832},"obj":"Sentence"},{"id":"T7","span":{"begin":833,"end":892},"obj":"Sentence"},{"id":"T8","span":{"begin":893,"end":1105},"obj":"Sentence"},{"id":"T9","span":{"begin":1106,"end":1200},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":99},"obj":"Sentence"},{"id":"T2","span":{"begin":100,"end":219},"obj":"Sentence"},{"id":"T3","span":{"begin":220,"end":337},"obj":"Sentence"},{"id":"T4","span":{"begin":338,"end":607},"obj":"Sentence"},{"id":"T5","span":{"begin":608,"end":752},"obj":"Sentence"},{"id":"T6","span":{"begin":753,"end":832},"obj":"Sentence"},{"id":"T7","span":{"begin":833,"end":892},"obj":"Sentence"},{"id":"T8","span":{"begin":893,"end":1105},"obj":"Sentence"},{"id":"T9","span":{"begin":1106,"end":1200},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Characterization of the interaction between galectin-1 and lymphocyte glycoproteins CD45 and Thy-1.\nGalectin-1 is a sugar binding protein specific for beta-galactosides and not requiring metal ions for binding activity. It exists as a soluble protein which forms a noncovalent homodimer and is expressed with a broad tissue distribution. Recently, galectin-1 has been shown to play a possible role in the immune system mediating apoptosis of activated T cells with indirect evidence suggesting that galectin-1 interacts with the heavily glycosylated, transmembrane, protein phosphotyrosine phosphatase CD45. The interaction of galectin-1 with purified lymphocyte cell surface proteins was studied using surface plasmon resonance in a BIAcoretrade mark. Galectin-1 was shown to bind CD45 and Thy-1 in a carbohydrate-dependent manner. Several galectin-1 molecules could bind each CD45 molecule. The dissociation constant of dimeric galectin-1 binding to CD45 was measured at approximately 5 microM, indicating the concentration at which cross-linking of cell surface glycoproteins by galectin-1 would occur. A possible role for galectin-1 in the organization of cell surface glycoproteins is discussed."}

GlycoBiology-FMA

uniprot-human

{"project":"uniprot-human","denotations":[{"id":"T1","span":{"begin":44,"end":54},"obj":"http://www.uniprot.org/uniprot/P09382"},{"id":"T2","span":{"begin":348,"end":358},"obj":"http://www.uniprot.org/uniprot/P09382"},{"id":"T3","span":{"begin":499,"end":509},"obj":"http://www.uniprot.org/uniprot/P09382"},{"id":"T4","span":{"begin":627,"end":637},"obj":"http://www.uniprot.org/uniprot/P09382"},{"id":"T5","span":{"begin":841,"end":851},"obj":"http://www.uniprot.org/uniprot/P09382"},{"id":"T6","span":{"begin":930,"end":940},"obj":"http://www.uniprot.org/uniprot/P09382"},{"id":"T7","span":{"begin":1082,"end":1092},"obj":"http://www.uniprot.org/uniprot/P09382"},{"id":"T8","span":{"begin":1126,"end":1136},"obj":"http://www.uniprot.org/uniprot/P09382"},{"id":"T9","span":{"begin":84,"end":88},"obj":"http://www.uniprot.org/uniprot/P08575"},{"id":"T10","span":{"begin":602,"end":606},"obj":"http://www.uniprot.org/uniprot/P08575"},{"id":"T11","span":{"begin":782,"end":786},"obj":"http://www.uniprot.org/uniprot/P08575"},{"id":"T12","span":{"begin":878,"end":882},"obj":"http://www.uniprot.org/uniprot/P08575"},{"id":"T13","span":{"begin":952,"end":956},"obj":"http://www.uniprot.org/uniprot/P08575"}],"text":"Characterization of the interaction between galectin-1 and lymphocyte glycoproteins CD45 and Thy-1.\nGalectin-1 is a sugar binding protein specific for beta-galactosides and not requiring metal ions for binding activity. It exists as a soluble protein which forms a noncovalent homodimer and is expressed with a broad tissue distribution. Recently, galectin-1 has been shown to play a possible role in the immune system mediating apoptosis of activated T cells with indirect evidence suggesting that galectin-1 interacts with the heavily glycosylated, transmembrane, protein phosphotyrosine phosphatase CD45. The interaction of galectin-1 with purified lymphocyte cell surface proteins was studied using surface plasmon resonance in a BIAcoretrade mark. Galectin-1 was shown to bind CD45 and Thy-1 in a carbohydrate-dependent manner. Several galectin-1 molecules could bind each CD45 molecule. The dissociation constant of dimeric galectin-1 binding to CD45 was measured at approximately 5 microM, indicating the concentration at which cross-linking of cell surface glycoproteins by galectin-1 would occur. A possible role for galectin-1 in the organization of cell surface glycoproteins is discussed."}

uniprot-mouse

{"project":"uniprot-mouse","denotations":[{"id":"T1","span":{"begin":44,"end":54},"obj":"http://www.uniprot.org/uniprot/P16045"},{"id":"T2","span":{"begin":348,"end":358},"obj":"http://www.uniprot.org/uniprot/P16045"},{"id":"T3","span":{"begin":499,"end":509},"obj":"http://www.uniprot.org/uniprot/P16045"},{"id":"T4","span":{"begin":627,"end":637},"obj":"http://www.uniprot.org/uniprot/P16045"},{"id":"T5","span":{"begin":841,"end":851},"obj":"http://www.uniprot.org/uniprot/P16045"},{"id":"T6","span":{"begin":930,"end":940},"obj":"http://www.uniprot.org/uniprot/P16045"},{"id":"T7","span":{"begin":1082,"end":1092},"obj":"http://www.uniprot.org/uniprot/P16045"},{"id":"T8","span":{"begin":1126,"end":1136},"obj":"http://www.uniprot.org/uniprot/P16045"},{"id":"T9","span":{"begin":84,"end":88},"obj":"http://www.uniprot.org/uniprot/P06800"},{"id":"T10","span":{"begin":602,"end":606},"obj":"http://www.uniprot.org/uniprot/P06800"},{"id":"T11","span":{"begin":782,"end":786},"obj":"http://www.uniprot.org/uniprot/P06800"},{"id":"T12","span":{"begin":878,"end":882},"obj":"http://www.uniprot.org/uniprot/P06800"},{"id":"T13","span":{"begin":952,"end":956},"obj":"http://www.uniprot.org/uniprot/P06800"},{"id":"T14","span":{"begin":93,"end":98},"obj":"http://www.uniprot.org/uniprot/P01831"},{"id":"T15","span":{"begin":791,"end":796},"obj":"http://www.uniprot.org/uniprot/P01831"}],"text":"Characterization of the interaction between galectin-1 and lymphocyte glycoproteins CD45 and Thy-1.\nGalectin-1 is a sugar binding protein specific for beta-galactosides and not requiring metal ions for binding activity. It exists as a soluble protein which forms a noncovalent homodimer and is expressed with a broad tissue distribution. Recently, galectin-1 has been shown to play a possible role in the immune system mediating apoptosis of activated T cells with indirect evidence suggesting that galectin-1 interacts with the heavily glycosylated, transmembrane, protein phosphotyrosine phosphatase CD45. The interaction of galectin-1 with purified lymphocyte cell surface proteins was studied using surface plasmon resonance in a BIAcoretrade mark. Galectin-1 was shown to bind CD45 and Thy-1 in a carbohydrate-dependent manner. Several galectin-1 molecules could bind each CD45 molecule. The dissociation constant of dimeric galectin-1 binding to CD45 was measured at approximately 5 microM, indicating the concentration at which cross-linking of cell surface glycoproteins by galectin-1 would occur. A possible role for galectin-1 in the organization of cell surface glycoproteins is discussed."}

GlycoBiology-NCBITAXON

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":151,"end":155},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"},{"id":"T2","span":{"begin":151,"end":155},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T3","span":{"begin":317,"end":323},"obj":"http://purl.bioontology.org/ontology/STY/T024"},{"id":"T4","span":{"begin":454,"end":459},"obj":"http://purl.bioontology.org/ontology/STY/T025"}],"text":"Characterization of the interaction between galectin-1 and lymphocyte glycoproteins CD45 and Thy-1.\nGalectin-1 is a sugar binding protein specific for beta-galactosides and not requiring metal ions for binding activity. It exists as a soluble protein which forms a noncovalent homodimer and is expressed with a broad tissue distribution. Recently, galectin-1 has been shown to play a possible role in the immune system mediating apoptosis of activated T cells with indirect evidence suggesting that galectin-1 interacts with the heavily glycosylated, transmembrane, protein phosphotyrosine phosphatase CD45. The interaction of galectin-1 with purified lymphocyte cell surface proteins was studied using surface plasmon resonance in a BIAcoretrade mark. Galectin-1 was shown to bind CD45 and Thy-1 in a carbohydrate-dependent manner. Several galectin-1 molecules could bind each CD45 molecule. The dissociation constant of dimeric galectin-1 binding to CD45 was measured at approximately 5 microM, indicating the concentration at which cross-linking of cell surface glycoproteins by galectin-1 would occur. A possible role for galectin-1 in the organization of cell surface glycoproteins is discussed."}

GO-BP

{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":202,"end":218},"obj":"http://purl.obolibrary.org/obo/GO_0051099"},{"id":"T2","span":{"begin":429,"end":438},"obj":"http://purl.obolibrary.org/obo/GO_0006915"},{"id":"T3","span":{"begin":429,"end":438},"obj":"http://purl.obolibrary.org/obo/GO_0097194"},{"id":"T4","span":{"begin":429,"end":451},"obj":"http://purl.obolibrary.org/obo/GO_0006915"},{"id":"T5","span":{"begin":429,"end":451},"obj":"http://purl.obolibrary.org/obo/GO_0043065"},{"id":"T6","span":{"begin":429,"end":459},"obj":"http://purl.obolibrary.org/obo/GO_0006924"},{"id":"T7","span":{"begin":429,"end":459},"obj":"http://purl.obolibrary.org/obo/GO_0070238"},{"id":"T8","span":{"begin":429,"end":459},"obj":"http://purl.obolibrary.org/obo/GO_0070234"},{"id":"T9","span":{"begin":429,"end":459},"obj":"http://purl.obolibrary.org/obo/GO_0070235"},{"id":"T10","span":{"begin":429,"end":459},"obj":"http://purl.obolibrary.org/obo/GO_0070239"},{"id":"T11","span":{"begin":442,"end":459},"obj":"http://purl.obolibrary.org/obo/GO_0032393"},{"id":"T12","span":{"begin":442,"end":459},"obj":"http://purl.obolibrary.org/obo/GO_0032394"},{"id":"T13","span":{"begin":442,"end":459},"obj":"http://purl.obolibrary.org/obo/GO_0032395"},{"id":"T14","span":{"begin":442,"end":459},"obj":"http://purl.obolibrary.org/obo/GO_0042110"},{"id":"T15","span":{"begin":442,"end":459},"obj":"http://purl.obolibrary.org/obo/GO_0045582"},{"id":"T16","span":{"begin":442,"end":459},"obj":"http://purl.obolibrary.org/obo/GO_0050798"},{"id":"T17","span":{"begin":442,"end":459},"obj":"http://purl.obolibrary.org/obo/GO_0050863"},{"id":"T18","span":{"begin":442,"end":459},"obj":"http://purl.obolibrary.org/obo/GO_0051132"},{"id":"T19","span":{"begin":442,"end":459},"obj":"http://purl.obolibrary.org/obo/GO_1903905"},{"id":"T20","span":{"begin":442,"end":459},"obj":"http://purl.obolibrary.org/obo/GO_0042102"},{"id":"T21","span":{"begin":537,"end":549},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T22","span":{"begin":590,"end":601},"obj":"http://purl.obolibrary.org/obo/GO_0016791"},{"id":"T23","span":{"begin":663,"end":684},"obj":"http://purl.obolibrary.org/obo/GO_0034394"},{"id":"T24","span":{"begin":663,"end":684},"obj":"http://purl.obolibrary.org/obo/GO_0033575"},{"id":"T25","span":{"begin":663,"end":684},"obj":"http://purl.obolibrary.org/obo/GO_0033580"}],"text":"Characterization of the interaction between galectin-1 and lymphocyte glycoproteins CD45 and Thy-1.\nGalectin-1 is a sugar binding protein specific for beta-galactosides and not requiring metal ions for binding activity. It exists as a soluble protein which forms a noncovalent homodimer and is expressed with a broad tissue distribution. Recently, galectin-1 has been shown to play a possible role in the immune system mediating apoptosis of activated T cells with indirect evidence suggesting that galectin-1 interacts with the heavily glycosylated, transmembrane, protein phosphotyrosine phosphatase CD45. The interaction of galectin-1 with purified lymphocyte cell surface proteins was studied using surface plasmon resonance in a BIAcoretrade mark. Galectin-1 was shown to bind CD45 and Thy-1 in a carbohydrate-dependent manner. Several galectin-1 molecules could bind each CD45 molecule. The dissociation constant of dimeric galectin-1 binding to CD45 was measured at approximately 5 microM, indicating the concentration at which cross-linking of cell surface glycoproteins by galectin-1 would occur. A possible role for galectin-1 in the organization of cell surface glycoproteins is discussed."}

GO-MF

{"project":"GO-MF","denotations":[{"id":"T1","span":{"begin":116,"end":129},"obj":"http://purl.obolibrary.org/obo/GO_0030246"},{"id":"T2","span":{"begin":122,"end":129},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T3","span":{"begin":202,"end":209},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T4","span":{"begin":777,"end":781},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T5","span":{"begin":868,"end":872},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T6","span":{"begin":122,"end":129},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T7","span":{"begin":202,"end":209},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T8","span":{"begin":777,"end":781},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T9","span":{"begin":868,"end":872},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T10","span":{"begin":122,"end":129},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T11","span":{"begin":202,"end":209},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T12","span":{"begin":777,"end":781},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T13","span":{"begin":868,"end":872},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T14","span":{"begin":122,"end":129},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T15","span":{"begin":202,"end":209},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T16","span":{"begin":777,"end":781},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T17","span":{"begin":868,"end":872},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T18","span":{"begin":122,"end":137},"obj":"http://purl.obolibrary.org/obo/GO_0005515"},{"id":"T19","span":{"begin":122,"end":146},"obj":"http://purl.obolibrary.org/obo/GO_0019904"},{"id":"T20","span":{"begin":187,"end":209},"obj":"http://purl.obolibrary.org/obo/GO_0046914"},{"id":"T21","span":{"begin":187,"end":209},"obj":"http://purl.obolibrary.org/obo/GO_0031420"},{"id":"T22","span":{"begin":187,"end":209},"obj":"http://purl.obolibrary.org/obo/GO_0046872"},{"id":"T23","span":{"begin":193,"end":209},"obj":"http://purl.obolibrary.org/obo/GO_0043167"}],"text":"Characterization of the interaction between galectin-1 and lymphocyte glycoproteins CD45 and Thy-1.\nGalectin-1 is a sugar binding protein specific for beta-galactosides and not requiring metal ions for binding activity. It exists as a soluble protein which forms a noncovalent homodimer and is expressed with a broad tissue distribution. Recently, galectin-1 has been shown to play a possible role in the immune system mediating apoptosis of activated T cells with indirect evidence suggesting that galectin-1 interacts with the heavily glycosylated, transmembrane, protein phosphotyrosine phosphatase CD45. The interaction of galectin-1 with purified lymphocyte cell surface proteins was studied using surface plasmon resonance in a BIAcoretrade mark. Galectin-1 was shown to bind CD45 and Thy-1 in a carbohydrate-dependent manner. Several galectin-1 molecules could bind each CD45 molecule. The dissociation constant of dimeric galectin-1 binding to CD45 was measured at approximately 5 microM, indicating the concentration at which cross-linking of cell surface glycoproteins by galectin-1 would occur. A possible role for galectin-1 in the organization of cell surface glycoproteins is discussed."}

GO-CC

{"project":"GO-CC","denotations":[{"id":"T1","span":{"begin":454,"end":459},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T2","span":{"begin":663,"end":667},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T3","span":{"begin":1052,"end":1056},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T4","span":{"begin":1160,"end":1164},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T5","span":{"begin":551,"end":564},"obj":"http://purl.obolibrary.org/obo/GO_0016021"},{"id":"T6","span":{"begin":551,"end":564},"obj":"http://purl.obolibrary.org/obo/GO_0044214"},{"id":"T7","span":{"begin":663,"end":675},"obj":"http://purl.obolibrary.org/obo/GO_0009986"},{"id":"T8","span":{"begin":1052,"end":1064},"obj":"http://purl.obolibrary.org/obo/GO_0009986"},{"id":"T9","span":{"begin":1160,"end":1172},"obj":"http://purl.obolibrary.org/obo/GO_0009986"}],"text":"Characterization of the interaction between galectin-1 and lymphocyte glycoproteins CD45 and Thy-1.\nGalectin-1 is a sugar binding protein specific for beta-galactosides and not requiring metal ions for binding activity. It exists as a soluble protein which forms a noncovalent homodimer and is expressed with a broad tissue distribution. Recently, galectin-1 has been shown to play a possible role in the immune system mediating apoptosis of activated T cells with indirect evidence suggesting that galectin-1 interacts with the heavily glycosylated, transmembrane, protein phosphotyrosine phosphatase CD45. The interaction of galectin-1 with purified lymphocyte cell surface proteins was studied using surface plasmon resonance in a BIAcoretrade mark. Galectin-1 was shown to bind CD45 and Thy-1 in a carbohydrate-dependent manner. Several galectin-1 molecules could bind each CD45 molecule. The dissociation constant of dimeric galectin-1 binding to CD45 was measured at approximately 5 microM, indicating the concentration at which cross-linking of cell surface glycoproteins by galectin-1 would occur. A possible role for galectin-1 in the organization of cell surface glycoproteins is discussed."}

UBERON-AE

{"project":"UBERON-AE","denotations":[{"id":"T1","span":{"begin":317,"end":323},"obj":"http://purl.obolibrary.org/obo/UBERON_0000479"},{"id":"T2","span":{"begin":405,"end":418},"obj":"http://purl.obolibrary.org/obo/UBERON_0002405"}],"text":"Characterization of the interaction between galectin-1 and lymphocyte glycoproteins CD45 and Thy-1.\nGalectin-1 is a sugar binding protein specific for beta-galactosides and not requiring metal ions for binding activity. It exists as a soluble protein which forms a noncovalent homodimer and is expressed with a broad tissue distribution. Recently, galectin-1 has been shown to play a possible role in the immune system mediating apoptosis of activated T cells with indirect evidence suggesting that galectin-1 interacts with the heavily glycosylated, transmembrane, protein phosphotyrosine phosphatase CD45. The interaction of galectin-1 with purified lymphocyte cell surface proteins was studied using surface plasmon resonance in a BIAcoretrade mark. Galectin-1 was shown to bind CD45 and Thy-1 in a carbohydrate-dependent manner. Several galectin-1 molecules could bind each CD45 molecule. The dissociation constant of dimeric galectin-1 binding to CD45 was measured at approximately 5 microM, indicating the concentration at which cross-linking of cell surface glycoproteins by galectin-1 would occur. A possible role for galectin-1 in the organization of cell surface glycoproteins is discussed."}

EDAM-topics

{"project":"EDAM-topics","denotations":[{"id":"T1","span":{"begin":24,"end":35},"obj":"http://edamontology.org/topic_0602"},{"id":"T2","span":{"begin":130,"end":137},"obj":"http://edamontology.org/topic_0078"},{"id":"T3","span":{"begin":243,"end":250},"obj":"http://edamontology.org/topic_0078"},{"id":"T4","span":{"begin":510,"end":519},"obj":"http://edamontology.org/topic_0602"},{"id":"T5","span":{"begin":551,"end":573},"obj":"http://edamontology.org/topic_0820"},{"id":"T6","span":{"begin":566,"end":573},"obj":"http://edamontology.org/topic_0078"},{"id":"T7","span":{"begin":612,"end":623},"obj":"http://edamontology.org/topic_0602"},{"id":"T8","span":{"begin":676,"end":684},"obj":"http://edamontology.org/topic_0078"},{"id":"T9","span":{"begin":689,"end":696},"obj":"http://edamontology.org/topic_3678"},{"id":"T10","span":{"begin":802,"end":814},"obj":"http://edamontology.org/topic_0152"},{"id":"T11","span":{"begin":852,"end":861},"obj":"http://edamontology.org/topic_2839"},{"id":"T12","span":{"begin":883,"end":891},"obj":"http://edamontology.org/topic_2839"}],"text":"Characterization of the interaction between galectin-1 and lymphocyte glycoproteins CD45 and Thy-1.\nGalectin-1 is a sugar binding protein specific for beta-galactosides and not requiring metal ions for binding activity. It exists as a soluble protein which forms a noncovalent homodimer and is expressed with a broad tissue distribution. Recently, galectin-1 has been shown to play a possible role in the immune system mediating apoptosis of activated T cells with indirect evidence suggesting that galectin-1 interacts with the heavily glycosylated, transmembrane, protein phosphotyrosine phosphatase CD45. The interaction of galectin-1 with purified lymphocyte cell surface proteins was studied using surface plasmon resonance in a BIAcoretrade mark. Galectin-1 was shown to bind CD45 and Thy-1 in a carbohydrate-dependent manner. Several galectin-1 molecules could bind each CD45 molecule. The dissociation constant of dimeric galectin-1 binding to CD45 was measured at approximately 5 microM, indicating the concentration at which cross-linking of cell surface glycoproteins by galectin-1 would occur. A possible role for galectin-1 in the organization of cell surface glycoproteins is discussed."}

EDAM-DFO

{"project":"EDAM-DFO","denotations":[{"id":"T1","span":{"begin":130,"end":137},"obj":"http://edamontology.org/data_1467"},{"id":"T2","span":{"begin":130,"end":137},"obj":"http://edamontology.org/format_1208"},{"id":"T3","span":{"begin":243,"end":250},"obj":"http://edamontology.org/data_1467"},{"id":"T4","span":{"begin":243,"end":250},"obj":"http://edamontology.org/format_1208"},{"id":"T5","span":{"begin":566,"end":573},"obj":"http://edamontology.org/format_1208"},{"id":"T6","span":{"begin":566,"end":573},"obj":"http://edamontology.org/data_1467"},{"id":"T7","span":{"begin":676,"end":684},"obj":"http://edamontology.org/data_1467"},{"id":"T8","span":{"begin":676,"end":684},"obj":"http://edamontology.org/format_1208"},{"id":"T9","span":{"begin":961,"end":969},"obj":"http://edamontology.org/data_3108"},{"id":"T10","span":{"begin":1012,"end":1025},"obj":"http://edamontology.org/data_2140"}],"text":"Characterization of the interaction between galectin-1 and lymphocyte glycoproteins CD45 and Thy-1.\nGalectin-1 is a sugar binding protein specific for beta-galactosides and not requiring metal ions for binding activity. It exists as a soluble protein which forms a noncovalent homodimer and is expressed with a broad tissue distribution. Recently, galectin-1 has been shown to play a possible role in the immune system mediating apoptosis of activated T cells with indirect evidence suggesting that galectin-1 interacts with the heavily glycosylated, transmembrane, protein phosphotyrosine phosphatase CD45. The interaction of galectin-1 with purified lymphocyte cell surface proteins was studied using surface plasmon resonance in a BIAcoretrade mark. Galectin-1 was shown to bind CD45 and Thy-1 in a carbohydrate-dependent manner. Several galectin-1 molecules could bind each CD45 molecule. The dissociation constant of dimeric galectin-1 binding to CD45 was measured at approximately 5 microM, indicating the concentration at which cross-linking of cell surface glycoproteins by galectin-1 would occur. A possible role for galectin-1 in the organization of cell surface glycoproteins is discussed."}

Lectin

{"project":"Lectin","denotations":[{"id":"Lectin_T1","span":{"begin":44,"end":54},"obj":"https://acgg.asia/db/lfdb/LfDB0270"},{"id":"Lectin_T2","span":{"begin":100,"end":110},"obj":"https://acgg.asia/db/lfdb/LfDB0270"},{"id":"Lectin_T3","span":{"begin":348,"end":358},"obj":"https://acgg.asia/db/lfdb/LfDB0270"},{"id":"Lectin_T4","span":{"begin":499,"end":509},"obj":"https://acgg.asia/db/lfdb/LfDB0270"},{"id":"Lectin_T5","span":{"begin":627,"end":637},"obj":"https://acgg.asia/db/lfdb/LfDB0270"},{"id":"Lectin_T6","span":{"begin":753,"end":763},"obj":"https://acgg.asia/db/lfdb/LfDB0270"},{"id":"Lectin_T7","span":{"begin":841,"end":851},"obj":"https://acgg.asia/db/lfdb/LfDB0270"},{"id":"Lectin_T8","span":{"begin":930,"end":940},"obj":"https://acgg.asia/db/lfdb/LfDB0270"},{"id":"Lectin_T9","span":{"begin":1082,"end":1092},"obj":"https://acgg.asia/db/lfdb/LfDB0270"},{"id":"Lectin_T10","span":{"begin":1126,"end":1136},"obj":"https://acgg.asia/db/lfdb/LfDB0270"},{"id":"Lectin_T11","span":{"begin":44,"end":54},"obj":"https://acgg.asia/db/lfdb/LfDB0057"},{"id":"Lectin_T12","span":{"begin":100,"end":110},"obj":"https://acgg.asia/db/lfdb/LfDB0057"},{"id":"Lectin_T13","span":{"begin":348,"end":358},"obj":"https://acgg.asia/db/lfdb/LfDB0057"},{"id":"Lectin_T14","span":{"begin":499,"end":509},"obj":"https://acgg.asia/db/lfdb/LfDB0057"},{"id":"Lectin_T15","span":{"begin":627,"end":637},"obj":"https://acgg.asia/db/lfdb/LfDB0057"},{"id":"Lectin_T16","span":{"begin":753,"end":763},"obj":"https://acgg.asia/db/lfdb/LfDB0057"},{"id":"Lectin_T17","span":{"begin":841,"end":851},"obj":"https://acgg.asia/db/lfdb/LfDB0057"},{"id":"Lectin_T18","span":{"begin":930,"end":940},"obj":"https://acgg.asia/db/lfdb/LfDB0057"},{"id":"Lectin_T19","span":{"begin":1082,"end":1092},"obj":"https://acgg.asia/db/lfdb/LfDB0057"},{"id":"Lectin_T20","span":{"begin":1126,"end":1136},"obj":"https://acgg.asia/db/lfdb/LfDB0057"},{"id":"Lectin_T21","span":{"begin":100,"end":108},"obj":"https://acgg.asia/db/lfdb/LfDB0272"},{"id":"Lectin_T22","span":{"begin":753,"end":761},"obj":"https://acgg.asia/db/lfdb/LfDB0272"},{"id":"Lectin_T23","span":{"begin":100,"end":108},"obj":"https://acgg.asia/db/lfdb/LfDB0274"},{"id":"Lectin_T24","span":{"begin":753,"end":761},"obj":"https://acgg.asia/db/lfdb/LfDB0274"}],"text":"Characterization of the interaction between galectin-1 and lymphocyte glycoproteins CD45 and Thy-1.\nGalectin-1 is a sugar binding protein specific for beta-galactosides and not requiring metal ions for binding activity. It exists as a soluble protein which forms a noncovalent homodimer and is expressed with a broad tissue distribution. Recently, galectin-1 has been shown to play a possible role in the immune system mediating apoptosis of activated T cells with indirect evidence suggesting that galectin-1 interacts with the heavily glycosylated, transmembrane, protein phosphotyrosine phosphatase CD45. The interaction of galectin-1 with purified lymphocyte cell surface proteins was studied using surface plasmon resonance in a BIAcoretrade mark. Galectin-1 was shown to bind CD45 and Thy-1 in a carbohydrate-dependent manner. Several galectin-1 molecules could bind each CD45 molecule. The dissociation constant of dimeric galectin-1 binding to CD45 was measured at approximately 5 microM, indicating the concentration at which cross-linking of cell surface glycoproteins by galectin-1 would occur. A possible role for galectin-1 in the organization of cell surface glycoproteins is discussed."}

GlyTouCan-IUPAC

{"project":"GlyTouCan-IUPAC","denotations":[{"id":"GlycanIUPAC_T1","span":{"begin":116,"end":121},"obj":"\"http://rdf.glycoinfo.org/glycan/G59665TO\""},{"id":"GlycanIUPAC_T2","span":{"begin":116,"end":121},"obj":"\"http://rdf.glycoinfo.org/glycan/G32915EI\""},{"id":"GlycanIUPAC_T3","span":{"begin":116,"end":121},"obj":"\"http://rdf.glycoinfo.org/glycan/G60625TS\""}],"text":"Characterization of the interaction between galectin-1 and lymphocyte glycoproteins CD45 and Thy-1.\nGalectin-1 is a sugar binding protein specific for beta-galactosides and not requiring metal ions for binding activity. It exists as a soluble protein which forms a noncovalent homodimer and is expressed with a broad tissue distribution. Recently, galectin-1 has been shown to play a possible role in the immune system mediating apoptosis of activated T cells with indirect evidence suggesting that galectin-1 interacts with the heavily glycosylated, transmembrane, protein phosphotyrosine phosphatase CD45. The interaction of galectin-1 with purified lymphocyte cell surface proteins was studied using surface plasmon resonance in a BIAcoretrade mark. Galectin-1 was shown to bind CD45 and Thy-1 in a carbohydrate-dependent manner. Several galectin-1 molecules could bind each CD45 molecule. The dissociation constant of dimeric galectin-1 binding to CD45 was measured at approximately 5 microM, indicating the concentration at which cross-linking of cell surface glycoproteins by galectin-1 would occur. A possible role for galectin-1 in the organization of cell surface glycoproteins is discussed."}

performance-test

{"project":"performance-test","denotations":[{"id":"PD-UBERON-AE-B_T1","span":{"begin":317,"end":323},"obj":"http://purl.obolibrary.org/obo/UBERON_0000479"},{"id":"PD-UBERON-AE-B_T2","span":{"begin":1144,"end":1156},"obj":"http://purl.obolibrary.org/obo/UBERON_0000062"},{"id":"PD-UBERON-AE-B_T3","span":{"begin":405,"end":418},"obj":"http://purl.obolibrary.org/obo/UBERON_0002405"}],"text":"Characterization of the interaction between galectin-1 and lymphocyte glycoproteins CD45 and Thy-1.\nGalectin-1 is a sugar binding protein specific for beta-galactosides and not requiring metal ions for binding activity. It exists as a soluble protein which forms a noncovalent homodimer and is expressed with a broad tissue distribution. Recently, galectin-1 has been shown to play a possible role in the immune system mediating apoptosis of activated T cells with indirect evidence suggesting that galectin-1 interacts with the heavily glycosylated, transmembrane, protein phosphotyrosine phosphatase CD45. The interaction of galectin-1 with purified lymphocyte cell surface proteins was studied using surface plasmon resonance in a BIAcoretrade mark. Galectin-1 was shown to bind CD45 and Thy-1 in a carbohydrate-dependent manner. Several galectin-1 molecules could bind each CD45 molecule. The dissociation constant of dimeric galectin-1 binding to CD45 was measured at approximately 5 microM, indicating the concentration at which cross-linking of cell surface glycoproteins by galectin-1 would occur. A possible role for galectin-1 in the organization of cell surface glycoproteins is discussed."}

Anatomy-UBERON

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":59,"end":69},"obj":"Body_part"},{"id":"T2","span":{"begin":317,"end":323},"obj":"Body_part"},{"id":"T3","span":{"begin":405,"end":418},"obj":"Body_part"},{"id":"T4","span":{"begin":551,"end":564},"obj":"Body_part"},{"id":"T5","span":{"begin":652,"end":662},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL_0000542"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0000479"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/UBERON_0002405"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/GO_0016020"},{"id":"A5","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/CL_0000542"}],"text":"Characterization of the interaction between galectin-1 and lymphocyte glycoproteins CD45 and Thy-1.\nGalectin-1 is a sugar binding protein specific for beta-galactosides and not requiring metal ions for binding activity. It exists as a soluble protein which forms a noncovalent homodimer and is expressed with a broad tissue distribution. Recently, galectin-1 has been shown to play a possible role in the immune system mediating apoptosis of activated T cells with indirect evidence suggesting that galectin-1 interacts with the heavily glycosylated, transmembrane, protein phosphotyrosine phosphatase CD45. The interaction of galectin-1 with purified lymphocyte cell surface proteins was studied using surface plasmon resonance in a BIAcoretrade mark. Galectin-1 was shown to bind CD45 and Thy-1 in a carbohydrate-dependent manner. Several galectin-1 molecules could bind each CD45 molecule. The dissociation constant of dimeric galectin-1 binding to CD45 was measured at approximately 5 microM, indicating the concentration at which cross-linking of cell surface glycoproteins by galectin-1 would occur. A possible role for galectin-1 in the organization of cell surface glycoproteins is discussed."}

CL-cell

{"project":"CL-cell","denotations":[{"id":"T1","span":{"begin":59,"end":69},"obj":"Cell"},{"id":"T2","span":{"begin":452,"end":459},"obj":"Cell"},{"id":"T3","span":{"begin":652,"end":662},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000542"},{"id":"A2","pred":"cl_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL:0000084"},{"id":"A3","pred":"cl_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CL:0000542"}],"text":"Characterization of the interaction between galectin-1 and lymphocyte glycoproteins CD45 and Thy-1.\nGalectin-1 is a sugar binding protein specific for beta-galactosides and not requiring metal ions for binding activity. It exists as a soluble protein which forms a noncovalent homodimer and is expressed with a broad tissue distribution. Recently, galectin-1 has been shown to play a possible role in the immune system mediating apoptosis of activated T cells with indirect evidence suggesting that galectin-1 interacts with the heavily glycosylated, transmembrane, protein phosphotyrosine phosphatase CD45. The interaction of galectin-1 with purified lymphocyte cell surface proteins was studied using surface plasmon resonance in a BIAcoretrade mark. Galectin-1 was shown to bind CD45 and Thy-1 in a carbohydrate-dependent manner. Several galectin-1 molecules could bind each CD45 molecule. The dissociation constant of dimeric galectin-1 binding to CD45 was measured at approximately 5 microM, indicating the concentration at which cross-linking of cell surface glycoproteins by galectin-1 would occur. A possible role for galectin-1 in the organization of cell surface glycoproteins is discussed."}