PubMed:20864568 JSONTXT

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":88},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":89,"end":195},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":196,"end":431},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":432,"end":613},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":614,"end":767},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":768,"end":884},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":885,"end":1264},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":1265,"end":1650},"obj":"Sentence"},{"id":"TextSentencer_T9","span":{"begin":1651,"end":1953},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":88},"obj":"Sentence"},{"id":"T2","span":{"begin":89,"end":195},"obj":"Sentence"},{"id":"T3","span":{"begin":196,"end":431},"obj":"Sentence"},{"id":"T4","span":{"begin":432,"end":613},"obj":"Sentence"},{"id":"T5","span":{"begin":614,"end":767},"obj":"Sentence"},{"id":"T6","span":{"begin":768,"end":884},"obj":"Sentence"},{"id":"T7","span":{"begin":885,"end":1264},"obj":"Sentence"},{"id":"T8","span":{"begin":1265,"end":1650},"obj":"Sentence"},{"id":"T9","span":{"begin":1651,"end":1953},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":88},"obj":"Sentence"},{"id":"T2","span":{"begin":89,"end":195},"obj":"Sentence"},{"id":"T3","span":{"begin":196,"end":431},"obj":"Sentence"},{"id":"T4","span":{"begin":432,"end":613},"obj":"Sentence"},{"id":"T5","span":{"begin":614,"end":767},"obj":"Sentence"},{"id":"T6","span":{"begin":768,"end":884},"obj":"Sentence"},{"id":"T7","span":{"begin":885,"end":1264},"obj":"Sentence"},{"id":"T8","span":{"begin":1265,"end":1650},"obj":"Sentence"},{"id":"T9","span":{"begin":1651,"end":1953},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Galectin multimerization and lattice formation are regulated by linker region structure.\nGalectins regulate cellular functions by binding to glycan ligands on cell surface glycoprotein receptors. Prototype galectins, such as galectin-1, are one carbohydrate recognition domain (CRD) monomers that noncovalently dimerize, whereas tandem-repeat galectins, such as galectin-9, have two non-identical CRDs connected by a linker domain. Dimerization of prototype galectins, or both CRDs in tandem-repeat galectins, is typically required for the crosslinking of glycoprotein receptors and subsequent cellular signaling. Several studies have found that tandem-repeat galectins are more potent than prototype galectins in triggering many cell responses, including cell death. These differences could be due to CRD specificity, the presence or absence of a linker domain between CRDs, or both. To interrogate the basis for the increased potency of tandem-repeat galectins compared with prototype galectins in triggering cell death, we created three tandem-repeat galectin constructs with different linker regions joining identical galectin-1 CRDs, so that any differences we observed would be due to the contribution of the linker region rather than due to CRD specificity. We found that random-coil or rigid α-helical linkers that permit separation of the two galectin-1 CRDs facilitated the formation of higher-order galectin multimers and that these galectins were more potent in binding to glycan ligands and cell surface glycoprotein receptors, as well as triggering T cell death, compared with native galectin-1 or a construct with a short rigid linker. Thus, the increased potency of tandem-repeat galectins compared with prototype galectins is likely due to the ability of the linker domain to permit intermolecular CRD interactions, resulting in the formation of higher-order multimers with increased valency, rather than differences in CRD specificity."}

{"project":"GlycoBiology-FMA","denotations":[{"id":"_T1","span":{"begin":159,"end":171},"obj":"FMAID:212684"},{"id":"_T2","span":{"begin":159,"end":171},"obj":"FMAID:200942"},{"id":"_T3","span":{"begin":164,"end":171},"obj":"FMAID:146300"},{"id":"_T4","span":{"begin":164,"end":171},"obj":"FMAID:50594"},{"id":"_T5","span":{"begin":172,"end":184},"obj":"FMAID:167256"},{"id":"_T6","span":{"begin":172,"end":184},"obj":"FMAID:62925"},{"id":"_T7","span":{"begin":245,"end":257},"obj":"FMAID:82737"},{"id":"_T8","span":{"begin":245,"end":257},"obj":"FMAID:197276"},{"id":"_T9","span":{"begin":556,"end":568},"obj":"FMAID:167256"},{"id":"_T10","span":{"begin":556,"end":568},"obj":"FMAID:62925"},{"id":"_T11","span":{"begin":1504,"end":1516},"obj":"FMAID:200942"},{"id":"_T12","span":{"begin":1504,"end":1516},"obj":"FMAID:212684"},{"id":"_T13","span":{"begin":1509,"end":1516},"obj":"FMAID:146300"},{"id":"_T14","span":{"begin":1509,"end":1516},"obj":"FMAID:50594"},{"id":"_T15","span":{"begin":1517,"end":1529},"obj":"FMAID:167256"},{"id":"_T16","span":{"begin":1517,"end":1529},"obj":"FMAID:62925"},{"id":"_T17","span":{"begin":1800,"end":1818},"obj":"FMAID:85706"},{"id":"_T18","span":{"begin":1800,"end":1818},"obj":"FMAID:202234"}],"namespaces":[{"prefix":"FMAID","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"Galectin multimerization and lattice formation are regulated by linker region structure.\nGalectins regulate cellular functions by binding to glycan ligands on cell surface glycoprotein receptors. Prototype galectins, such as galectin-1, are one carbohydrate recognition domain (CRD) monomers that noncovalently dimerize, whereas tandem-repeat galectins, such as galectin-9, have two non-identical CRDs connected by a linker domain. Dimerization of prototype galectins, or both CRDs in tandem-repeat galectins, is typically required for the crosslinking of glycoprotein receptors and subsequent cellular signaling. Several studies have found that tandem-repeat galectins are more potent than prototype galectins in triggering many cell responses, including cell death. These differences could be due to CRD specificity, the presence or absence of a linker domain between CRDs, or both. To interrogate the basis for the increased potency of tandem-repeat galectins compared with prototype galectins in triggering cell death, we created three tandem-repeat galectin constructs with different linker regions joining identical galectin-1 CRDs, so that any differences we observed would be due to the contribution of the linker region rather than due to CRD specificity. We found that random-coil or rigid α-helical linkers that permit separation of the two galectin-1 CRDs facilitated the formation of higher-order galectin multimers and that these galectins were more potent in binding to glycan ligands and cell surface glycoprotein receptors, as well as triggering T cell death, compared with native galectin-1 or a construct with a short rigid linker. Thus, the increased potency of tandem-repeat galectins compared with prototype galectins is likely due to the ability of the linker domain to permit intermolecular CRD interactions, resulting in the formation of higher-order multimers with increased valency, rather than differences in CRD specificity."}

{"project":"uniprot-human","denotations":[{"id":"T1","span":{"begin":225,"end":235},"obj":"http://www.uniprot.org/uniprot/P09382"},{"id":"T2","span":{"begin":1122,"end":1132},"obj":"http://www.uniprot.org/uniprot/P09382"},{"id":"T3","span":{"begin":1352,"end":1362},"obj":"http://www.uniprot.org/uniprot/P09382"},{"id":"T4","span":{"begin":1598,"end":1608},"obj":"http://www.uniprot.org/uniprot/P09382"},{"id":"T5","span":{"begin":362,"end":372},"obj":"http://www.uniprot.org/uniprot/Q9NQ58"}],"text":"Galectin multimerization and lattice formation are regulated by linker region structure.\nGalectins regulate cellular functions by binding to glycan ligands on cell surface glycoprotein receptors. Prototype galectins, such as galectin-1, are one carbohydrate recognition domain (CRD) monomers that noncovalently dimerize, whereas tandem-repeat galectins, such as galectin-9, have two non-identical CRDs connected by a linker domain. Dimerization of prototype galectins, or both CRDs in tandem-repeat galectins, is typically required for the crosslinking of glycoprotein receptors and subsequent cellular signaling. Several studies have found that tandem-repeat galectins are more potent than prototype galectins in triggering many cell responses, including cell death. These differences could be due to CRD specificity, the presence or absence of a linker domain between CRDs, or both. To interrogate the basis for the increased potency of tandem-repeat galectins compared with prototype galectins in triggering cell death, we created three tandem-repeat galectin constructs with different linker regions joining identical galectin-1 CRDs, so that any differences we observed would be due to the contribution of the linker region rather than due to CRD specificity. We found that random-coil or rigid α-helical linkers that permit separation of the two galectin-1 CRDs facilitated the formation of higher-order galectin multimers and that these galectins were more potent in binding to glycan ligands and cell surface glycoprotein receptors, as well as triggering T cell death, compared with native galectin-1 or a construct with a short rigid linker. Thus, the increased potency of tandem-repeat galectins compared with prototype galectins is likely due to the ability of the linker domain to permit intermolecular CRD interactions, resulting in the formation of higher-order multimers with increased valency, rather than differences in CRD specificity."}

{"project":"uniprot-mouse","denotations":[{"id":"T1","span":{"begin":225,"end":235},"obj":"http://www.uniprot.org/uniprot/P16045"},{"id":"T2","span":{"begin":1122,"end":1132},"obj":"http://www.uniprot.org/uniprot/P16045"},{"id":"T3","span":{"begin":1352,"end":1362},"obj":"http://www.uniprot.org/uniprot/P16045"},{"id":"T4","span":{"begin":1598,"end":1608},"obj":"http://www.uniprot.org/uniprot/P16045"},{"id":"T5","span":{"begin":362,"end":372},"obj":"http://www.uniprot.org/uniprot/O08573"},{"id":"T6","span":{"begin":1286,"end":1290},"obj":"http://www.uniprot.org/uniprot/Q5SU73"}],"text":"Galectin multimerization and lattice formation are regulated by linker region structure.\nGalectins regulate cellular functions by binding to glycan ligands on cell surface glycoprotein receptors. Prototype galectins, such as galectin-1, are one carbohydrate recognition domain (CRD) monomers that noncovalently dimerize, whereas tandem-repeat galectins, such as galectin-9, have two non-identical CRDs connected by a linker domain. Dimerization of prototype galectins, or both CRDs in tandem-repeat galectins, is typically required for the crosslinking of glycoprotein receptors and subsequent cellular signaling. Several studies have found that tandem-repeat galectins are more potent than prototype galectins in triggering many cell responses, including cell death. These differences could be due to CRD specificity, the presence or absence of a linker domain between CRDs, or both. To interrogate the basis for the increased potency of tandem-repeat galectins compared with prototype galectins in triggering cell death, we created three tandem-repeat galectin constructs with different linker regions joining identical galectin-1 CRDs, so that any differences we observed would be due to the contribution of the linker region rather than due to CRD specificity. We found that random-coil or rigid α-helical linkers that permit separation of the two galectin-1 CRDs facilitated the formation of higher-order galectin multimers and that these galectins were more potent in binding to glycan ligands and cell surface glycoprotein receptors, as well as triggering T cell death, compared with native galectin-1 or a construct with a short rigid linker. Thus, the increased potency of tandem-repeat galectins compared with prototype galectins is likely due to the ability of the linker domain to permit intermolecular CRD interactions, resulting in the formation of higher-order multimers with increased valency, rather than differences in CRD specificity."}

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":108,"end":126},"obj":"http://purl.bioontology.org/ontology/STY/T043"},{"id":"T2","span":{"begin":185,"end":194},"obj":"http://purl.bioontology.org/ontology/STY/T192"},{"id":"T3","span":{"begin":383,"end":386},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/604139"},{"id":"T4","span":{"begin":569,"end":578},"obj":"http://purl.bioontology.org/ontology/STY/T192"},{"id":"T5","span":{"begin":725,"end":729},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/9973"},{"id":"T6","span":{"begin":1302,"end":1309},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/53324"},{"id":"T7","span":{"begin":1530,"end":1539},"obj":"http://purl.bioontology.org/ontology/STY/T192"}],"text":"Galectin multimerization and lattice formation are regulated by linker region structure.\nGalectins regulate cellular functions by binding to glycan ligands on cell surface glycoprotein receptors. Prototype galectins, such as galectin-1, are one carbohydrate recognition domain (CRD) monomers that noncovalently dimerize, whereas tandem-repeat galectins, such as galectin-9, have two non-identical CRDs connected by a linker domain. Dimerization of prototype galectins, or both CRDs in tandem-repeat galectins, is typically required for the crosslinking of glycoprotein receptors and subsequent cellular signaling. Several studies have found that tandem-repeat galectins are more potent than prototype galectins in triggering many cell responses, including cell death. These differences could be due to CRD specificity, the presence or absence of a linker domain between CRDs, or both. To interrogate the basis for the increased potency of tandem-repeat galectins compared with prototype galectins in triggering cell death, we created three tandem-repeat galectin constructs with different linker regions joining identical galectin-1 CRDs, so that any differences we observed would be due to the contribution of the linker region rather than due to CRD specificity. We found that random-coil or rigid α-helical linkers that permit separation of the two galectin-1 CRDs facilitated the formation of higher-order galectin multimers and that these galectins were more potent in binding to glycan ligands and cell surface glycoprotein receptors, as well as triggering T cell death, compared with native galectin-1 or a construct with a short rigid linker. Thus, the increased potency of tandem-repeat galectins compared with prototype galectins is likely due to the ability of the linker domain to permit intermolecular CRD interactions, resulting in the formation of higher-order multimers with increased valency, rather than differences in CRD specificity."}

{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":37,"end":46},"obj":"http://purl.obolibrary.org/obo/GO_0009058"},{"id":"T2","span":{"begin":1384,"end":1393},"obj":"http://purl.obolibrary.org/obo/GO_0009058"},{"id":"T3","span":{"begin":1850,"end":1859},"obj":"http://purl.obolibrary.org/obo/GO_0009058"},{"id":"T4","span":{"begin":37,"end":60},"obj":"http://purl.obolibrary.org/obo/GO_0009889"},{"id":"T5","span":{"begin":51,"end":60},"obj":"http://purl.obolibrary.org/obo/GO_0065007"},{"id":"T6","span":{"begin":99,"end":107},"obj":"http://purl.obolibrary.org/obo/GO_0065007"},{"id":"T7","span":{"begin":108,"end":116},"obj":"http://purl.obolibrary.org/obo/GO_0007349"},{"id":"T8","span":{"begin":594,"end":602},"obj":"http://purl.obolibrary.org/obo/GO_0007349"},{"id":"T9","span":{"begin":603,"end":612},"obj":"http://purl.obolibrary.org/obo/GO_0023052"},{"id":"T10","span":{"begin":756,"end":766},"obj":"http://purl.obolibrary.org/obo/GO_0008219"},{"id":"T11","span":{"begin":1011,"end":1021},"obj":"http://purl.obolibrary.org/obo/GO_0008219"},{"id":"T12","span":{"begin":1565,"end":1575},"obj":"http://purl.obolibrary.org/obo/GO_0008219"},{"id":"T13","span":{"begin":761,"end":766},"obj":"http://purl.obolibrary.org/obo/GO_0016265"},{"id":"T14","span":{"begin":1016,"end":1021},"obj":"http://purl.obolibrary.org/obo/GO_0016265"},{"id":"T15","span":{"begin":1570,"end":1575},"obj":"http://purl.obolibrary.org/obo/GO_0016265"}],"text":"Galectin multimerization and lattice formation are regulated by linker region structure.\nGalectins regulate cellular functions by binding to glycan ligands on cell surface glycoprotein receptors. Prototype galectins, such as galectin-1, are one carbohydrate recognition domain (CRD) monomers that noncovalently dimerize, whereas tandem-repeat galectins, such as galectin-9, have two non-identical CRDs connected by a linker domain. Dimerization of prototype galectins, or both CRDs in tandem-repeat galectins, is typically required for the crosslinking of glycoprotein receptors and subsequent cellular signaling. Several studies have found that tandem-repeat galectins are more potent than prototype galectins in triggering many cell responses, including cell death. These differences could be due to CRD specificity, the presence or absence of a linker domain between CRDs, or both. To interrogate the basis for the increased potency of tandem-repeat galectins compared with prototype galectins in triggering cell death, we created three tandem-repeat galectin constructs with different linker regions joining identical galectin-1 CRDs, so that any differences we observed would be due to the contribution of the linker region rather than due to CRD specificity. We found that random-coil or rigid α-helical linkers that permit separation of the two galectin-1 CRDs facilitated the formation of higher-order galectin multimers and that these galectins were more potent in binding to glycan ligands and cell surface glycoprotein receptors, as well as triggering T cell death, compared with native galectin-1 or a construct with a short rigid linker. Thus, the increased potency of tandem-repeat galectins compared with prototype galectins is likely due to the ability of the linker domain to permit intermolecular CRD interactions, resulting in the formation of higher-order multimers with increased valency, rather than differences in CRD specificity."}

{"project":"GO-MF","denotations":[{"id":"T1","span":{"begin":130,"end":137},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T2","span":{"begin":1474,"end":1481},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T3","span":{"begin":130,"end":137},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T4","span":{"begin":1474,"end":1481},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T5","span":{"begin":130,"end":137},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T6","span":{"begin":1474,"end":1481},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T7","span":{"begin":130,"end":137},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T8","span":{"begin":1474,"end":1481},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T9","span":{"begin":148,"end":155},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T10","span":{"begin":1492,"end":1499},"obj":"http://purl.obolibrary.org/obo/GO_0005488"}],"text":"Galectin multimerization and lattice formation are regulated by linker region structure.\nGalectins regulate cellular functions by binding to glycan ligands on cell surface glycoprotein receptors. Prototype galectins, such as galectin-1, are one carbohydrate recognition domain (CRD) monomers that noncovalently dimerize, whereas tandem-repeat galectins, such as galectin-9, have two non-identical CRDs connected by a linker domain. Dimerization of prototype galectins, or both CRDs in tandem-repeat galectins, is typically required for the crosslinking of glycoprotein receptors and subsequent cellular signaling. Several studies have found that tandem-repeat galectins are more potent than prototype galectins in triggering many cell responses, including cell death. These differences could be due to CRD specificity, the presence or absence of a linker domain between CRDs, or both. To interrogate the basis for the increased potency of tandem-repeat galectins compared with prototype galectins in triggering cell death, we created three tandem-repeat galectin constructs with different linker regions joining identical galectin-1 CRDs, so that any differences we observed would be due to the contribution of the linker region rather than due to CRD specificity. We found that random-coil or rigid α-helical linkers that permit separation of the two galectin-1 CRDs facilitated the formation of higher-order galectin multimers and that these galectins were more potent in binding to glycan ligands and cell surface glycoprotein receptors, as well as triggering T cell death, compared with native galectin-1 or a construct with a short rigid linker. Thus, the increased potency of tandem-repeat galectins compared with prototype galectins is likely due to the ability of the linker domain to permit intermolecular CRD interactions, resulting in the formation of higher-order multimers with increased valency, rather than differences in CRD specificity."}

{"project":"GO-CC","denotations":[{"id":"T1","span":{"begin":159,"end":163},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T2","span":{"begin":730,"end":734},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T3","span":{"begin":756,"end":760},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T4","span":{"begin":1011,"end":1015},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T5","span":{"begin":1504,"end":1508},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T6","span":{"begin":1565,"end":1569},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T7","span":{"begin":159,"end":171},"obj":"http://purl.obolibrary.org/obo/GO_0009986"},{"id":"T8","span":{"begin":1504,"end":1516},"obj":"http://purl.obolibrary.org/obo/GO_0009986"}],"text":"Galectin multimerization and lattice formation are regulated by linker region structure.\nGalectins regulate cellular functions by binding to glycan ligands on cell surface glycoprotein receptors. Prototype galectins, such as galectin-1, are one carbohydrate recognition domain (CRD) monomers that noncovalently dimerize, whereas tandem-repeat galectins, such as galectin-9, have two non-identical CRDs connected by a linker domain. Dimerization of prototype galectins, or both CRDs in tandem-repeat galectins, is typically required for the crosslinking of glycoprotein receptors and subsequent cellular signaling. Several studies have found that tandem-repeat galectins are more potent than prototype galectins in triggering many cell responses, including cell death. These differences could be due to CRD specificity, the presence or absence of a linker domain between CRDs, or both. To interrogate the basis for the increased potency of tandem-repeat galectins compared with prototype galectins in triggering cell death, we created three tandem-repeat galectin constructs with different linker regions joining identical galectin-1 CRDs, so that any differences we observed would be due to the contribution of the linker region rather than due to CRD specificity. We found that random-coil or rigid α-helical linkers that permit separation of the two galectin-1 CRDs facilitated the formation of higher-order galectin multimers and that these galectins were more potent in binding to glycan ligands and cell surface glycoprotein receptors, as well as triggering T cell death, compared with native galectin-1 or a construct with a short rigid linker. Thus, the increased potency of tandem-repeat galectins compared with prototype galectins is likely due to the ability of the linker domain to permit intermolecular CRD interactions, resulting in the formation of higher-order multimers with increased valency, rather than differences in CRD specificity."}

{"project":"Allie","denotations":[{"id":"SS1_20864568_2_0","span":{"begin":245,"end":276},"obj":"expanded"},{"id":"SS2_20864568_2_0","span":{"begin":278,"end":281},"obj":"abbr"}],"relations":[{"id":"AE1_20864568_2_0","pred":"abbreviatedTo","subj":"SS1_20864568_2_0","obj":"SS2_20864568_2_0"}],"text":"Galectin multimerization and lattice formation are regulated by linker region structure.\nGalectins regulate cellular functions by binding to glycan ligands on cell surface glycoprotein receptors. Prototype galectins, such as galectin-1, are one carbohydrate recognition domain (CRD) monomers that noncovalently dimerize, whereas tandem-repeat galectins, such as galectin-9, have two non-identical CRDs connected by a linker domain. Dimerization of prototype galectins, or both CRDs in tandem-repeat galectins, is typically required for the crosslinking of glycoprotein receptors and subsequent cellular signaling. Several studies have found that tandem-repeat galectins are more potent than prototype galectins in triggering many cell responses, including cell death. These differences could be due to CRD specificity, the presence or absence of a linker domain between CRDs, or both. To interrogate the basis for the increased potency of tandem-repeat galectins compared with prototype galectins in triggering cell death, we created three tandem-repeat galectin constructs with different linker regions joining identical galectin-1 CRDs, so that any differences we observed would be due to the contribution of the linker region rather than due to CRD specificity. We found that random-coil or rigid α-helical linkers that permit separation of the two galectin-1 CRDs facilitated the formation of higher-order galectin multimers and that these galectins were more potent in binding to glycan ligands and cell surface glycoprotein receptors, as well as triggering T cell death, compared with native galectin-1 or a construct with a short rigid linker. Thus, the increased potency of tandem-repeat galectins compared with prototype galectins is likely due to the ability of the linker domain to permit intermolecular CRD interactions, resulting in the formation of higher-order multimers with increased valency, rather than differences in CRD specificity."}

{"project":"EDAM-topics","denotations":[{"id":"T1","span":{"begin":245,"end":257},"obj":"http://edamontology.org/topic_0152"},{"id":"T2","span":{"begin":622,"end":629},"obj":"http://edamontology.org/topic_3678"},{"id":"T3","span":{"begin":1800,"end":1831},"obj":"http://edamontology.org/topic_0602"},{"id":"T4","span":{"begin":1819,"end":1831},"obj":"http://edamontology.org/topic_0602"}],"text":"Galectin multimerization and lattice formation are regulated by linker region structure.\nGalectins regulate cellular functions by binding to glycan ligands on cell surface glycoprotein receptors. Prototype galectins, such as galectin-1, are one carbohydrate recognition domain (CRD) monomers that noncovalently dimerize, whereas tandem-repeat galectins, such as galectin-9, have two non-identical CRDs connected by a linker domain. Dimerization of prototype galectins, or both CRDs in tandem-repeat galectins, is typically required for the crosslinking of glycoprotein receptors and subsequent cellular signaling. Several studies have found that tandem-repeat galectins are more potent than prototype galectins in triggering many cell responses, including cell death. These differences could be due to CRD specificity, the presence or absence of a linker domain between CRDs, or both. To interrogate the basis for the increased potency of tandem-repeat galectins compared with prototype galectins in triggering cell death, we created three tandem-repeat galectin constructs with different linker regions joining identical galectin-1 CRDs, so that any differences we observed would be due to the contribution of the linker region rather than due to CRD specificity. We found that random-coil or rigid α-helical linkers that permit separation of the two galectin-1 CRDs facilitated the formation of higher-order galectin multimers and that these galectins were more potent in binding to glycan ligands and cell surface glycoprotein receptors, as well as triggering T cell death, compared with native galectin-1 or a construct with a short rigid linker. Thus, the increased potency of tandem-repeat galectins compared with prototype galectins is likely due to the ability of the linker domain to permit intermolecular CRD interactions, resulting in the formation of higher-order multimers with increased valency, rather than differences in CRD specificity."}

{"project":"EDAM-DFO","denotations":[{"id":"T1","span":{"begin":37,"end":46},"obj":"http://edamontology.org/format_1915"},{"id":"T2","span":{"begin":37,"end":46},"obj":"http://edamontology.org/operation_0335"},{"id":"T3","span":{"begin":78,"end":87},"obj":"http://edamontology.org/data_0883"},{"id":"T4","span":{"begin":117,"end":126},"obj":"http://edamontology.org/operation_0004"},{"id":"T5","span":{"begin":258,"end":269},"obj":"http://edamontology.org/operation_2423"},{"id":"T6","span":{"begin":1063,"end":1073},"obj":"http://edamontology.org/operation_3429"},{"id":"T7","span":{"begin":1384,"end":1393},"obj":"http://edamontology.org/format_1915"},{"id":"T8","span":{"begin":1384,"end":1393},"obj":"http://edamontology.org/operation_0335"},{"id":"T9","span":{"begin":1614,"end":1623},"obj":"http://edamontology.org/operation_3429"},{"id":"T10","span":{"begin":1850,"end":1859},"obj":"http://edamontology.org/format_1915"},{"id":"T11","span":{"begin":1850,"end":1859},"obj":"http://edamontology.org/operation_0335"}],"text":"Galectin multimerization and lattice formation are regulated by linker region structure.\nGalectins regulate cellular functions by binding to glycan ligands on cell surface glycoprotein receptors. Prototype galectins, such as galectin-1, are one carbohydrate recognition domain (CRD) monomers that noncovalently dimerize, whereas tandem-repeat galectins, such as galectin-9, have two non-identical CRDs connected by a linker domain. Dimerization of prototype galectins, or both CRDs in tandem-repeat galectins, is typically required for the crosslinking of glycoprotein receptors and subsequent cellular signaling. Several studies have found that tandem-repeat galectins are more potent than prototype galectins in triggering many cell responses, including cell death. These differences could be due to CRD specificity, the presence or absence of a linker domain between CRDs, or both. To interrogate the basis for the increased potency of tandem-repeat galectins compared with prototype galectins in triggering cell death, we created three tandem-repeat galectin constructs with different linker regions joining identical galectin-1 CRDs, so that any differences we observed would be due to the contribution of the linker region rather than due to CRD specificity. We found that random-coil or rigid α-helical linkers that permit separation of the two galectin-1 CRDs facilitated the formation of higher-order galectin multimers and that these galectins were more potent in binding to glycan ligands and cell surface glycoprotein receptors, as well as triggering T cell death, compared with native galectin-1 or a construct with a short rigid linker. Thus, the increased potency of tandem-repeat galectins compared with prototype galectins is likely due to the ability of the linker domain to permit intermolecular CRD interactions, resulting in the formation of higher-order multimers with increased valency, rather than differences in CRD specificity."}

{"project":"PubmedHPO","denotations":[{"id":"T1","span":{"begin":1294,"end":1299},"obj":"HP_0002063"},{"id":"T2","span":{"begin":1637,"end":1642},"obj":"HP_0002063"}],"text":"Galectin multimerization and lattice formation are regulated by linker region structure.\nGalectins regulate cellular functions by binding to glycan ligands on cell surface glycoprotein receptors. Prototype galectins, such as galectin-1, are one carbohydrate recognition domain (CRD) monomers that noncovalently dimerize, whereas tandem-repeat galectins, such as galectin-9, have two non-identical CRDs connected by a linker domain. Dimerization of prototype galectins, or both CRDs in tandem-repeat galectins, is typically required for the crosslinking of glycoprotein receptors and subsequent cellular signaling. Several studies have found that tandem-repeat galectins are more potent than prototype galectins in triggering many cell responses, including cell death. These differences could be due to CRD specificity, the presence or absence of a linker domain between CRDs, or both. To interrogate the basis for the increased potency of tandem-repeat galectins compared with prototype galectins in triggering cell death, we created three tandem-repeat galectin constructs with different linker regions joining identical galectin-1 CRDs, so that any differences we observed would be due to the contribution of the linker region rather than due to CRD specificity. We found that random-coil or rigid α-helical linkers that permit separation of the two galectin-1 CRDs facilitated the formation of higher-order galectin multimers and that these galectins were more potent in binding to glycan ligands and cell surface glycoprotein receptors, as well as triggering T cell death, compared with native galectin-1 or a construct with a short rigid linker. Thus, the increased potency of tandem-repeat galectins compared with prototype galectins is likely due to the ability of the linker domain to permit intermolecular CRD interactions, resulting in the formation of higher-order multimers with increased valency, rather than differences in CRD specificity."}

{"project":"GlyTouCan-IUPAC","denotations":[{"id":"GlycanIUPAC_T1","span":{"begin":383,"end":386},"obj":"\"http://rdf.glycoinfo.org/glycan/G02780QX\""},{"id":"GlycanIUPAC_T2","span":{"begin":383,"end":386},"obj":"\"http://rdf.glycoinfo.org/glycan/G18425DX\""},{"id":"GlycanIUPAC_T3","span":{"begin":383,"end":386},"obj":"\"http://rdf.glycoinfo.org/glycan/G18630JE\""},{"id":"GlycanIUPAC_T4","span":{"begin":383,"end":386},"obj":"\"http://rdf.glycoinfo.org/glycan/G01004IT\""},{"id":"GlycanIUPAC_T5","span":{"begin":383,"end":386},"obj":"\"http://rdf.glycoinfo.org/glycan/G87301QZ\""},{"id":"GlycanIUPAC_T6","span":{"begin":383,"end":386},"obj":"\"http://rdf.glycoinfo.org/glycan/G39790GW\""},{"id":"GlycanIUPAC_T7","span":{"begin":383,"end":386},"obj":"\"http://rdf.glycoinfo.org/glycan/G42928BB\""},{"id":"GlycanIUPAC_T8","span":{"begin":383,"end":386},"obj":"\"http://rdf.glycoinfo.org/glycan/G51134HC\""},{"id":"GlycanIUPAC_T9","span":{"begin":383,"end":386},"obj":"\"http://rdf.glycoinfo.org/glycan/G68183GR\""},{"id":"GlycanIUPAC_T10","span":{"begin":383,"end":386},"obj":"\"http://rdf.glycoinfo.org/glycan/G46883FA\""},{"id":"GlycanIUPAC_T11","span":{"begin":383,"end":386},"obj":"\"http://rdf.glycoinfo.org/glycan/G54702VY\""}],"text":"Galectin multimerization and lattice formation are regulated by linker region structure.\nGalectins regulate cellular functions by binding to glycan ligands on cell surface glycoprotein receptors. Prototype galectins, such as galectin-1, are one carbohydrate recognition domain (CRD) monomers that noncovalently dimerize, whereas tandem-repeat galectins, such as galectin-9, have two non-identical CRDs connected by a linker domain. Dimerization of prototype galectins, or both CRDs in tandem-repeat galectins, is typically required for the crosslinking of glycoprotein receptors and subsequent cellular signaling. Several studies have found that tandem-repeat galectins are more potent than prototype galectins in triggering many cell responses, including cell death. These differences could be due to CRD specificity, the presence or absence of a linker domain between CRDs, or both. To interrogate the basis for the increased potency of tandem-repeat galectins compared with prototype galectins in triggering cell death, we created three tandem-repeat galectin constructs with different linker regions joining identical galectin-1 CRDs, so that any differences we observed would be due to the contribution of the linker region rather than due to CRD specificity. We found that random-coil or rigid α-helical linkers that permit separation of the two galectin-1 CRDs facilitated the formation of higher-order galectin multimers and that these galectins were more potent in binding to glycan ligands and cell surface glycoprotein receptors, as well as triggering T cell death, compared with native galectin-1 or a construct with a short rigid linker. Thus, the increased potency of tandem-repeat galectins compared with prototype galectins is likely due to the ability of the linker domain to permit intermolecular CRD interactions, resulting in the formation of higher-order multimers with increased valency, rather than differences in CRD specificity."}

{"project":"Lectin","denotations":[{"id":"Lectin_T1","span":{"begin":0,"end":8},"obj":"https://acgg.asia/db/lfdb/LfDB0270"},{"id":"Lectin_T2","span":{"begin":225,"end":235},"obj":"https://acgg.asia/db/lfdb/LfDB0270"},{"id":"Lectin_T3","span":{"begin":1122,"end":1132},"obj":"https://acgg.asia/db/lfdb/LfDB0270"},{"id":"Lectin_T4","span":{"begin":1352,"end":1362},"obj":"https://acgg.asia/db/lfdb/LfDB0270"},{"id":"Lectin_T5","span":{"begin":1598,"end":1608},"obj":"https://acgg.asia/db/lfdb/LfDB0270"},{"id":"Lectin_T6","span":{"begin":225,"end":235},"obj":"https://acgg.asia/db/lfdb/LfDB0057"},{"id":"Lectin_T7","span":{"begin":1122,"end":1132},"obj":"https://acgg.asia/db/lfdb/LfDB0057"},{"id":"Lectin_T8","span":{"begin":1352,"end":1362},"obj":"https://acgg.asia/db/lfdb/LfDB0057"},{"id":"Lectin_T9","span":{"begin":1598,"end":1608},"obj":"https://acgg.asia/db/lfdb/LfDB0057"},{"id":"Lectin_T10","span":{"begin":0,"end":8},"obj":"https://acgg.asia/db/lfdb/LfDB0272"},{"id":"Lectin_T11","span":{"begin":0,"end":8},"obj":"https://acgg.asia/db/lfdb/LfDB0274"},{"id":"Lectin_T12","span":{"begin":362,"end":372},"obj":"https://acgg.asia/db/lfdb/LfDB0274"}],"text":"Galectin multimerization and lattice formation are regulated by linker region structure.\nGalectins regulate cellular functions by binding to glycan ligands on cell surface glycoprotein receptors. Prototype galectins, such as galectin-1, are one carbohydrate recognition domain (CRD) monomers that noncovalently dimerize, whereas tandem-repeat galectins, such as galectin-9, have two non-identical CRDs connected by a linker domain. Dimerization of prototype galectins, or both CRDs in tandem-repeat galectins, is typically required for the crosslinking of glycoprotein receptors and subsequent cellular signaling. Several studies have found that tandem-repeat galectins are more potent than prototype galectins in triggering many cell responses, including cell death. These differences could be due to CRD specificity, the presence or absence of a linker domain between CRDs, or both. To interrogate the basis for the increased potency of tandem-repeat galectins compared with prototype galectins in triggering cell death, we created three tandem-repeat galectin constructs with different linker regions joining identical galectin-1 CRDs, so that any differences we observed would be due to the contribution of the linker region rather than due to CRD specificity. We found that random-coil or rigid α-helical linkers that permit separation of the two galectin-1 CRDs facilitated the formation of higher-order galectin multimers and that these galectins were more potent in binding to glycan ligands and cell surface glycoprotein receptors, as well as triggering T cell death, compared with native galectin-1 or a construct with a short rigid linker. Thus, the increased potency of tandem-repeat galectins compared with prototype galectins is likely due to the ability of the linker domain to permit intermolecular CRD interactions, resulting in the formation of higher-order multimers with increased valency, rather than differences in CRD specificity."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":1563,"end":1569},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL_0000084"}],"text":"Galectin multimerization and lattice formation are regulated by linker region structure.\nGalectins regulate cellular functions by binding to glycan ligands on cell surface glycoprotein receptors. Prototype galectins, such as galectin-1, are one carbohydrate recognition domain (CRD) monomers that noncovalently dimerize, whereas tandem-repeat galectins, such as galectin-9, have two non-identical CRDs connected by a linker domain. Dimerization of prototype galectins, or both CRDs in tandem-repeat galectins, is typically required for the crosslinking of glycoprotein receptors and subsequent cellular signaling. Several studies have found that tandem-repeat galectins are more potent than prototype galectins in triggering many cell responses, including cell death. These differences could be due to CRD specificity, the presence or absence of a linker domain between CRDs, or both. To interrogate the basis for the increased potency of tandem-repeat galectins compared with prototype galectins in triggering cell death, we created three tandem-repeat galectin constructs with different linker regions joining identical galectin-1 CRDs, so that any differences we observed would be due to the contribution of the linker region rather than due to CRD specificity. We found that random-coil or rigid α-helical linkers that permit separation of the two galectin-1 CRDs facilitated the formation of higher-order galectin multimers and that these galectins were more potent in binding to glycan ligands and cell surface glycoprotein receptors, as well as triggering T cell death, compared with native galectin-1 or a construct with a short rigid linker. Thus, the increased potency of tandem-repeat galectins compared with prototype galectins is likely due to the ability of the linker domain to permit intermolecular CRD interactions, resulting in the formation of higher-order multimers with increased valency, rather than differences in CRD specificity."}

{"project":"CL-cell","denotations":[{"id":"T1","span":{"begin":1563,"end":1569},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000084"}],"text":"Galectin multimerization and lattice formation are regulated by linker region structure.\nGalectins regulate cellular functions by binding to glycan ligands on cell surface glycoprotein receptors. Prototype galectins, such as galectin-1, are one carbohydrate recognition domain (CRD) monomers that noncovalently dimerize, whereas tandem-repeat galectins, such as galectin-9, have two non-identical CRDs connected by a linker domain. Dimerization of prototype galectins, or both CRDs in tandem-repeat galectins, is typically required for the crosslinking of glycoprotein receptors and subsequent cellular signaling. Several studies have found that tandem-repeat galectins are more potent than prototype galectins in triggering many cell responses, including cell death. These differences could be due to CRD specificity, the presence or absence of a linker domain between CRDs, or both. To interrogate the basis for the increased potency of tandem-repeat galectins compared with prototype galectins in triggering cell death, we created three tandem-repeat galectin constructs with different linker regions joining identical galectin-1 CRDs, so that any differences we observed would be due to the contribution of the linker region rather than due to CRD specificity. We found that random-coil or rigid α-helical linkers that permit separation of the two galectin-1 CRDs facilitated the formation of higher-order galectin multimers and that these galectins were more potent in binding to glycan ligands and cell surface glycoprotein receptors, as well as triggering T cell death, compared with native galectin-1 or a construct with a short rigid linker. Thus, the increased potency of tandem-repeat galectins compared with prototype galectins is likely due to the ability of the linker domain to permit intermolecular CRD interactions, resulting in the formation of higher-order multimers with increased valency, rather than differences in CRD specificity."}