PubMed:10427971 JSONTXT

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    jnlpba-st-training

    {"project":"jnlpba-st-training","denotations":[{"id":"T1","span":{"begin":24,"end":29},"obj":"protein"},{"id":"T2","span":{"begin":86,"end":104},"obj":"protein"},{"id":"T3","span":{"begin":109,"end":114},"obj":"protein"},{"id":"T4","span":{"begin":128,"end":150},"obj":"protein"},{"id":"T5","span":{"begin":154,"end":169},"obj":"cell_type"},{"id":"T6","span":{"begin":219,"end":236},"obj":"protein"},{"id":"T7","span":{"begin":245,"end":262},"obj":"protein"},{"id":"T8","span":{"begin":263,"end":287},"obj":"protein"},{"id":"T9","span":{"begin":289,"end":302},"obj":"protein"},{"id":"T10","span":{"begin":304,"end":308},"obj":"RNA"},{"id":"T11","span":{"begin":320,"end":333},"obj":"protein"},{"id":"T12","span":{"begin":343,"end":354},"obj":"protein"},{"id":"T13","span":{"begin":383,"end":420},"obj":"cell_line"},{"id":"T14","span":{"begin":422,"end":427},"obj":"cell_line"},{"id":"T15","span":{"begin":458,"end":467},"obj":"cell_type"},{"id":"T16","span":{"begin":507,"end":512},"obj":"protein"},{"id":"T17","span":{"begin":554,"end":563},"obj":"protein"},{"id":"T18","span":{"begin":588,"end":598},"obj":"cell_line"},{"id":"T19","span":{"begin":599,"end":604},"obj":"cell_line"},{"id":"T20","span":{"begin":609,"end":614},"obj":"cell_line"},{"id":"T21","span":{"begin":643,"end":651},"obj":"protein"},{"id":"T22","span":{"begin":656,"end":669},"obj":"protein"},{"id":"T23","span":{"begin":682,"end":687},"obj":"protein"},{"id":"T24","span":{"begin":701,"end":706},"obj":"protein"},{"id":"T25","span":{"begin":710,"end":744},"obj":"cell_line"},{"id":"T26","span":{"begin":756,"end":809},"obj":"cell_line"},{"id":"T27","span":{"begin":811,"end":816},"obj":"protein"},{"id":"T28","span":{"begin":831,"end":836},"obj":"protein"},{"id":"T29","span":{"begin":852,"end":857},"obj":"cell_line"},{"id":"T30","span":{"begin":895,"end":900},"obj":"protein"},{"id":"T31","span":{"begin":923,"end":927},"obj":"protein"},{"id":"T32","span":{"begin":932,"end":944},"obj":"protein"},{"id":"T33","span":{"begin":968,"end":981},"obj":"protein"},{"id":"T34","span":{"begin":1009,"end":1014},"obj":"protein"},{"id":"T35","span":{"begin":1030,"end":1035},"obj":"protein"},{"id":"T36","span":{"begin":1085,"end":1090},"obj":"cell_line"},{"id":"T37","span":{"begin":1121,"end":1134},"obj":"protein"},{"id":"T38","span":{"begin":1139,"end":1147},"obj":"protein"},{"id":"T39","span":{"begin":1149,"end":1154},"obj":"protein"},{"id":"T40","span":{"begin":1190,"end":1206},"obj":"protein"},{"id":"T41","span":{"begin":1210,"end":1215},"obj":"cell_line"},{"id":"T42","span":{"begin":1257,"end":1268},"obj":"protein"},{"id":"T43","span":{"begin":1330,"end":1352},"obj":"protein"},{"id":"T44","span":{"begin":1356,"end":1361},"obj":"cell_line"}],"text":"Diminished responses to IL-13 by human monocytes differentiated in vitro: role of the IL-13Ralpha1 chain and STAT6.\nThe primary IL-13 receptor complex on human monocytes is believed to be a heterodimer comprised of the IL-4R alpha chain and the IL-2R gamma chain (gamma(c))-like molecule, IL-13R alpha1. mRNA levels for IL-13R alpha1, but not IL-4R alpha, were markedly decreased in in vitro monocyte-derived macrophages (MDMac), and with increasing time of monocytes in culture correlated with the loss of IL-13 regulation of lipopolysaccharide-induced TNF-alpha production. Analysis of cell lines Daudi and THP-1 that differentially express gamma(c) and IL-13R alpha1 showed that IL-13 can activate STAT6 in IL-13R alpha1-positive THP-1 cells but not in gamma(c)-positive, IL-13R alpha1-negative Daudi cells. IL-13 activation of STAT6 was reduced in MDMac which was associated with diminished IL-13-induced expression of CD23 and MHC class II. However, with reduced IL-13R alpha1 expression and low nuclear STAT6 activity, some IL-13-induced responses were unaltered in magnitude in MDMac. In the absence of functional IL-13R alpha1 and gamma(c), IL-13 must signal through an alternative receptor complex on MDMac. Experiments with a blocking antibody to IL-4R alpha showed that this chain remains an essential component of the IL-13 receptor complex on MDMac."}

    genia-medco-coref

    {"project":"genia-medco-coref","denotations":[{"id":"C1","span":{"begin":24,"end":29},"obj":"NP"},{"id":"C2","span":{"begin":82,"end":104},"obj":"NP"},{"id":"C3","span":{"begin":109,"end":114},"obj":"NP"},{"id":"C4","span":{"begin":154,"end":169},"obj":"NP"},{"id":"C5","span":{"begin":215,"end":236},"obj":"NP"},{"id":"C6","span":{"begin":241,"end":287},"obj":"NP"},{"id":"C7","span":{"begin":289,"end":302},"obj":"NP"},{"id":"C8","span":{"begin":320,"end":333},"obj":"NP"},{"id":"C9","span":{"begin":458,"end":467},"obj":"NP"},{"id":"C10","span":{"begin":588,"end":614},"obj":"NP"},{"id":"C11","span":{"begin":615,"end":619},"obj":"NP"},{"id":"C12","span":{"begin":656,"end":669},"obj":"NP"},{"id":"C13","span":{"begin":682,"end":687},"obj":"NP"},{"id":"C14","span":{"begin":831,"end":836},"obj":"NP"},{"id":"C16","span":{"begin":852,"end":857},"obj":"NP"},{"id":"C17","span":{"begin":858,"end":863},"obj":"NP"},{"id":"C15","span":{"begin":852,"end":944},"obj":"NP"},{"id":"C18","span":{"begin":1085,"end":1090},"obj":"NP"},{"id":"C19","span":{"begin":1149,"end":1154},"obj":"NP"},{"id":"C20","span":{"begin":1210,"end":1215},"obj":"NP"},{"id":"C21","span":{"begin":1257,"end":1268},"obj":"NP"},{"id":"C22","span":{"begin":1281,"end":1291},"obj":"NP"},{"id":"C23","span":{"begin":1356,"end":1361},"obj":"NP"}],"relations":[{"id":"R1","pred":"coref-ident","subj":"C6","obj":"C2"},{"id":"R2","pred":"coref-appos","subj":"C7","obj":"C6"},{"id":"R3","pred":"coref-ident","subj":"C8","obj":"C6"},{"id":"R4","pred":"coref-ident","subj":"C9","obj":"C4"},{"id":"R5","pred":"coref-relat","subj":"C11","obj":"C10"},{"id":"R6","pred":"coref-ident","subj":"C12","obj":"C8"},{"id":"R7","pred":"coref-ident","subj":"C13","obj":"C1"},{"id":"R8","pred":"coref-ident","subj":"C14","obj":"C3"},{"id":"R9","pred":"coref-relat","subj":"C17","obj":"C16"},{"id":"R10","pred":"coref-ident","subj":"C18","obj":"C15"},{"id":"R11","pred":"coref-ident","subj":"C19","obj":"C13"},{"id":"R12","pred":"coref-ident","subj":"C20","obj":"C18"},{"id":"R13","pred":"coref-ident","subj":"C21","obj":"C5"},{"id":"R14","pred":"coref-ident","subj":"C22","obj":"C21"},{"id":"R15","pred":"coref-ident","subj":"C23","obj":"C20"}],"text":"Diminished responses to IL-13 by human monocytes differentiated in vitro: role of the IL-13Ralpha1 chain and STAT6.\nThe primary IL-13 receptor complex on human monocytes is believed to be a heterodimer comprised of the IL-4R alpha chain and the IL-2R gamma chain (gamma(c))-like molecule, IL-13R alpha1. mRNA levels for IL-13R alpha1, but not IL-4R alpha, were markedly decreased in in vitro monocyte-derived macrophages (MDMac), and with increasing time of monocytes in culture correlated with the loss of IL-13 regulation of lipopolysaccharide-induced TNF-alpha production. Analysis of cell lines Daudi and THP-1 that differentially express gamma(c) and IL-13R alpha1 showed that IL-13 can activate STAT6 in IL-13R alpha1-positive THP-1 cells but not in gamma(c)-positive, IL-13R alpha1-negative Daudi cells. IL-13 activation of STAT6 was reduced in MDMac which was associated with diminished IL-13-induced expression of CD23 and MHC class II. However, with reduced IL-13R alpha1 expression and low nuclear STAT6 activity, some IL-13-induced responses were unaltered in magnitude in MDMac. In the absence of functional IL-13R alpha1 and gamma(c), IL-13 must signal through an alternative receptor complex on MDMac. Experiments with a blocking antibody to IL-4R alpha showed that this chain remains an essential component of the IL-13 receptor complex on MDMac."}

    pubmed-sentences-benchmark

    {"project":"pubmed-sentences-benchmark","denotations":[{"id":"S1","span":{"begin":0,"end":115},"obj":"Sentence"},{"id":"S2","span":{"begin":116,"end":303},"obj":"Sentence"},{"id":"S3","span":{"begin":304,"end":575},"obj":"Sentence"},{"id":"S4","span":{"begin":576,"end":810},"obj":"Sentence"},{"id":"S5","span":{"begin":811,"end":945},"obj":"Sentence"},{"id":"S6","span":{"begin":946,"end":1091},"obj":"Sentence"},{"id":"S7","span":{"begin":1092,"end":1216},"obj":"Sentence"},{"id":"S8","span":{"begin":1217,"end":1362},"obj":"Sentence"}],"text":"Diminished responses to IL-13 by human monocytes differentiated in vitro: role of the IL-13Ralpha1 chain and STAT6.\nThe primary IL-13 receptor complex on human monocytes is believed to be a heterodimer comprised of the IL-4R alpha chain and the IL-2R gamma chain (gamma(c))-like molecule, IL-13R alpha1. mRNA levels for IL-13R alpha1, but not IL-4R alpha, were markedly decreased in in vitro monocyte-derived macrophages (MDMac), and with increasing time of monocytes in culture correlated with the loss of IL-13 regulation of lipopolysaccharide-induced TNF-alpha production. Analysis of cell lines Daudi and THP-1 that differentially express gamma(c) and IL-13R alpha1 showed that IL-13 can activate STAT6 in IL-13R alpha1-positive THP-1 cells but not in gamma(c)-positive, IL-13R alpha1-negative Daudi cells. IL-13 activation of STAT6 was reduced in MDMac which was associated with diminished IL-13-induced expression of CD23 and MHC class II. However, with reduced IL-13R alpha1 expression and low nuclear STAT6 activity, some IL-13-induced responses were unaltered in magnitude in MDMac. In the absence of functional IL-13R alpha1 and gamma(c), IL-13 must signal through an alternative receptor complex on MDMac. Experiments with a blocking antibody to IL-4R alpha showed that this chain remains an essential component of the IL-13 receptor complex on MDMac."}

    GENIAcorpus

    {"project":"GENIAcorpus","denotations":[{"id":"T1","span":{"begin":24,"end":29},"obj":"protein_molecule"},{"id":"T2","span":{"begin":86,"end":104},"obj":"protein_subunit"},{"id":"T3","span":{"begin":109,"end":114},"obj":"protein_molecule"},{"id":"T4","span":{"begin":128,"end":133},"obj":"protein_molecule"},{"id":"T5","span":{"begin":154,"end":169},"obj":"cell_type"},{"id":"T6","span":{"begin":219,"end":236},"obj":"protein_subunit"},{"id":"T7","span":{"begin":245,"end":262},"obj":"protein_subunit"},{"id":"T8","span":{"begin":263,"end":287},"obj":"protein_family_or_group"},{"id":"T9","span":{"begin":289,"end":302},"obj":"protein_molecule"},{"id":"T10","span":{"begin":304,"end":308},"obj":"RNA_family_or_group"},{"id":"T11","span":{"begin":320,"end":333},"obj":"protein_molecule"},{"id":"T12","span":{"begin":343,"end":354},"obj":"protein_molecule"},{"id":"T13","span":{"begin":383,"end":420},"obj":"cell_line"},{"id":"T14","span":{"begin":422,"end":427},"obj":"cell_line"},{"id":"T15","span":{"begin":458,"end":467},"obj":"cell_type"},{"id":"T16","span":{"begin":507,"end":512},"obj":"protein_molecule"},{"id":"T17","span":{"begin":527,"end":545},"obj":"lipid"},{"id":"T18","span":{"begin":554,"end":563},"obj":"protein_molecule"},{"id":"T19","span":{"begin":588,"end":598},"obj":"cell_line"},{"id":"T20","span":{"begin":599,"end":604},"obj":"cell_line"},{"id":"T21","span":{"begin":609,"end":614},"obj":"cell_line"},{"id":"T22","span":{"begin":643,"end":651},"obj":"protein_molecule"},{"id":"T23","span":{"begin":656,"end":669},"obj":"protein_molecule"},{"id":"T24","span":{"begin":682,"end":687},"obj":"protein_molecule"},{"id":"T25","span":{"begin":701,"end":706},"obj":"protein_molecule"},{"id":"T26","span":{"begin":710,"end":723},"obj":"protein_molecule"},{"id":"T27","span":{"begin":756,"end":774},"obj":"cell_line"},{"id":"T28","span":{"begin":775,"end":788},"obj":"protein_molecule"},{"id":"T29","span":{"begin":811,"end":816},"obj":"protein_molecule"},{"id":"T30","span":{"begin":831,"end":836},"obj":"protein_molecule"},{"id":"T31","span":{"begin":852,"end":857},"obj":"cell_line"},{"id":"T32","span":{"begin":895,"end":900},"obj":"protein_molecule"},{"id":"T33","span":{"begin":923,"end":927},"obj":"protein_molecule"},{"id":"T34","span":{"begin":932,"end":944},"obj":"protein_family_or_group"},{"id":"T35","span":{"begin":968,"end":981},"obj":"protein_molecule"},{"id":"T36","span":{"begin":997,"end":1008},"obj":"other_name"},{"id":"T37","span":{"begin":1009,"end":1014},"obj":"protein_molecule"},{"id":"T38","span":{"begin":1030,"end":1035},"obj":"protein_molecule"},{"id":"T39","span":{"begin":1085,"end":1090},"obj":"cell_line"},{"id":"T40","span":{"begin":1121,"end":1134},"obj":"protein_molecule"},{"id":"T41","span":{"begin":1139,"end":1147},"obj":"protein_molecule"},{"id":"T42","span":{"begin":1149,"end":1154},"obj":"protein_molecule"},{"id":"T43","span":{"begin":1190,"end":1206},"obj":"protein_complex"},{"id":"T44","span":{"begin":1210,"end":1215},"obj":"cell_line"},{"id":"T45","span":{"begin":1257,"end":1268},"obj":"protein_molecule"},{"id":"T46","span":{"begin":1330,"end":1335},"obj":"protein_molecule"},{"id":"T47","span":{"begin":1356,"end":1361},"obj":"cell_line"}],"text":"Diminished responses to IL-13 by human monocytes differentiated in vitro: role of the IL-13Ralpha1 chain and STAT6.\nThe primary IL-13 receptor complex on human monocytes is believed to be a heterodimer comprised of the IL-4R alpha chain and the IL-2R gamma chain (gamma(c))-like molecule, IL-13R alpha1. mRNA levels for IL-13R alpha1, but not IL-4R alpha, were markedly decreased in in vitro monocyte-derived macrophages (MDMac), and with increasing time of monocytes in culture correlated with the loss of IL-13 regulation of lipopolysaccharide-induced TNF-alpha production. Analysis of cell lines Daudi and THP-1 that differentially express gamma(c) and IL-13R alpha1 showed that IL-13 can activate STAT6 in IL-13R alpha1-positive THP-1 cells but not in gamma(c)-positive, IL-13R alpha1-negative Daudi cells. IL-13 activation of STAT6 was reduced in MDMac which was associated with diminished IL-13-induced expression of CD23 and MHC class II. However, with reduced IL-13R alpha1 expression and low nuclear STAT6 activity, some IL-13-induced responses were unaltered in magnitude in MDMac. In the absence of functional IL-13R alpha1 and gamma(c), IL-13 must signal through an alternative receptor complex on MDMac. Experiments with a blocking antibody to IL-4R alpha showed that this chain remains an essential component of the IL-13 receptor complex on MDMac."}