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inhibitors were used to demonstrate that the transcription factor sites within the IL-1RA promoter are relevant for the induction of IL-1RA by GP. As expected, an inhibition of NFκB via CAPE [35] and CyA, NFAT via CyA and NFIL-6 via CHX [36] could not be overruled by GP, leading to a down-regulated binding activity of the transcription factors to the IL-1RA sites, and a reduction of IL-1RA mRNA and IL-1RA protein levels (Fig. 7). The extent of reduction in NFATP2/3 binding is exemplarily shown in an autoradiogram (Fig. 7A, left side) and graphically summarized (n = 4, Fig. 7A, right side). The results for the NFκB and NFIL-6 binding sites were similar (data not shown). Because the highest IL-1RA amount was found at 24 h, mRNA was examined following 1 h inhibition and 18 h of GP. A representative gel demonstrating a decrease in IL-1RA mRNA after inhibition with CAPE, CyA and CHX is displayed in Fig. 7B (n = 4). In addition, corresponding IL-1RA protein levels after 24 h of GP are shown in Fig. 7C (n = 3). Altogether, NFκB inhibition by CAPE was more pronounced at the binding activity and the transcription, whereas CyA and CHX mainly led to a decreased IL-1RA release."}

{"project":"bionlp-st-ge-2016-test-proteins","denotations":[{"id":"T10514","span":{"begin":1185,"end":1191},"obj":"Protein"},{"id":"T10513","span":{"begin":967,"end":973},"obj":"Protein"},{"id":"T10512","span":{"begin":855,"end":861},"obj":"Protein"},{"id":"T10511","span":{"begin":714,"end":720},"obj":"Protein"},{"id":"T10510","span":{"begin":418,"end":424},"obj":"Protein"},{"id":"T10509","span":{"begin":402,"end":408},"obj":"Protein"},{"id":"T10508","span":{"begin":369,"end":375},"obj":"Protein"},{"id":"T10507","span":{"begin":238,"end":244},"obj":"Protein"},{"id":"T10506","span":{"begin":221,"end":225},"obj":"Protein"},{"id":"T10505","span":{"begin":149,"end":155},"obj":"Protein"},{"id":"T10504","span":{"begin":99,"end":105},"obj":"Protein"}],"namespaces":[{"prefix":"_base","uri":"http://bionlp.dbcls.jp/ontology/ge.owl#"}],"text":"Pharmacological inhibitors were used to demonstrate that the transcription factor sites within the IL-1RA promoter are relevant for the induction of IL-1RA by GP. As expected, an inhibition of NFκB via CAPE [35] and CyA, NFAT via CyA and NFIL-6 via CHX [36] could not be overruled by GP, leading to a down-regulated binding activity of the transcription factors to the IL-1RA sites, and a reduction of IL-1RA mRNA and IL-1RA protein levels (Fig. 7). The extent of reduction in NFATP2/3 binding is exemplarily shown in an autoradiogram (Fig. 7A, left side) and graphically summarized (n = 4, Fig. 7A, right side). The results for the NFκB and NFIL-6 binding sites were similar (data not shown). Because the highest IL-1RA amount was found at 24 h, mRNA was examined following 1 h inhibition and 18 h of GP. A representative gel demonstrating a decrease in IL-1RA mRNA after inhibition with CAPE, CyA and CHX is displayed in Fig. 7B (n = 4). In addition, corresponding IL-1RA protein levels after 24 h of GP are shown in Fig. 7C (n = 3). Altogether, NFκB inhibition by CAPE was more pronounced at the binding activity and the transcription, whereas CyA and CHX mainly led to a decreased IL-1RA release."}

{"project":"bionlp-st-ge-2016-uniprot","denotations":[{"id":"T10789","span":{"begin":1185,"end":1191},"obj":"http://www.uniprot.org/uniprot/P18510"},{"id":"T10788","span":{"begin":967,"end":973},"obj":"http://www.uniprot.org/uniprot/P18510"},{"id":"T10787","span":{"begin":855,"end":861},"obj":"http://www.uniprot.org/uniprot/P18510"},{"id":"T10786","span":{"begin":714,"end":720},"obj":"http://www.uniprot.org/uniprot/P18510"},{"id":"T10785","span":{"begin":418,"end":424},"obj":"http://www.uniprot.org/uniprot/P18510"},{"id":"T10784","span":{"begin":402,"end":408},"obj":"http://www.uniprot.org/uniprot/P18510"},{"id":"T10783","span":{"begin":369,"end":375},"obj":"http://www.uniprot.org/uniprot/P18510"},{"id":"T10782","span":{"begin":149,"end":155},"obj":"http://www.uniprot.org/uniprot/P18510"},{"id":"T10781","span":{"begin":99,"end":105},"obj":"http://www.uniprot.org/uniprot/P18510"}],"namespaces":[{"prefix":"_base","uri":"http://www.uniprot.org/uniprot/"}],"text":"Pharmacological inhibitors were used to demonstrate that the transcription factor sites within the IL-1RA promoter are relevant for the induction of IL-1RA by GP. As expected, an inhibition of NFκB via CAPE [35] and CyA, NFAT via CyA and NFIL-6 via CHX [36] could not be overruled by GP, leading to a down-regulated binding activity of the transcription factors to the IL-1RA sites, and a reduction of IL-1RA mRNA and IL-1RA protein levels (Fig. 7). The extent of reduction in NFATP2/3 binding is exemplarily shown in an autoradiogram (Fig. 7A, left side) and graphically summarized (n = 4, Fig. 7A, right side). The results for the NFκB and NFIL-6 binding sites were similar (data not shown). Because the highest IL-1RA amount was found at 24 h, mRNA was examined following 1 h inhibition and 18 h of GP. A representative gel demonstrating a decrease in IL-1RA mRNA after inhibition with CAPE, CyA and CHX is displayed in Fig. 7B (n = 4). In addition, corresponding IL-1RA protein levels after 24 h of GP are shown in Fig. 7C (n = 3). Altogether, NFκB inhibition by CAPE was more pronounced at the binding activity and the transcription, whereas CyA and CHX mainly led to a decreased IL-1RA release."}

{"project":"GO-BP","denotations":[{"id":"T10460","span":{"begin":324,"end":361},"obj":"http://purl.obolibrary.org/obo/GO_0051090"},{"id":"T10459","span":{"begin":324,"end":361},"obj":"http://purl.obolibrary.org/obo/GO_0006352"},{"id":"T10458","span":{"begin":324,"end":361},"obj":"http://purl.obolibrary.org/obo/GO_0034246"},{"id":"T10457","span":{"begin":324,"end":361},"obj":"http://purl.obolibrary.org/obo/GO_0003700"},{"id":"T10456","span":{"begin":324,"end":361},"obj":"http://purl.obolibrary.org/obo/GO_0001071"},{"id":"T10455","span":{"begin":324,"end":361},"obj":"http://purl.obolibrary.org/obo/GO_0001070"},{"id":"T10454","span":{"begin":324,"end":361},"obj":"http://purl.obolibrary.org/obo/GO_0000988"},{"id":"T10453","span":{"begin":324,"end":361},"obj":"http://purl.obolibrary.org/obo/GO_0051091"},{"id":"T10452","span":{"begin":1124,"end":1137},"obj":"http://purl.obolibrary.org/obo/GO_0006351"},{"id":"T10451","span":{"begin":340,"end":353},"obj":"http://purl.obolibrary.org/obo/GO_0006351"},{"id":"T10450","span":{"begin":61,"end":74},"obj":"http://purl.obolibrary.org/obo/GO_0006351"},{"id":"T10447","span":{"begin":324,"end":361},"obj":"http://purl.obolibrary.org/obo/GO_0043433"}],"text":"Pharmacological inhibitors were used to demonstrate that the transcription factor sites within the IL-1RA promoter are relevant for the induction of IL-1RA by GP. As expected, an inhibition of NFκB via CAPE [35] and CyA, NFAT via CyA and NFIL-6 via CHX [36] could not be overruled by GP, leading to a down-regulated binding activity of the transcription factors to the IL-1RA sites, and a reduction of IL-1RA mRNA and IL-1RA protein levels (Fig. 7). The extent of reduction in NFATP2/3 binding is exemplarily shown in an autoradiogram (Fig. 7A, left side) and graphically summarized (n = 4, Fig. 7A, right side). The results for the NFκB and NFIL-6 binding sites were similar (data not shown). Because the highest IL-1RA amount was found at 24 h, mRNA was examined following 1 h inhibition and 18 h of GP. A representative gel demonstrating a decrease in IL-1RA mRNA after inhibition with CAPE, CyA and CHX is displayed in Fig. 7B (n = 4). In addition, corresponding IL-1RA protein levels after 24 h of GP are shown in Fig. 7C (n = 3). Altogether, NFκB inhibition by CAPE was more pronounced at the binding activity and the transcription, whereas CyA and CHX mainly led to a decreased IL-1RA release."}

{"project":"GO-MF","denotations":[{"id":"T10523","span":{"begin":324,"end":361},"obj":"http://purl.obolibrary.org/obo/GO_0034246"},{"id":"T10522","span":{"begin":324,"end":361},"obj":"http://purl.obolibrary.org/obo/GO_0003700"},{"id":"T10521","span":{"begin":324,"end":361},"obj":"http://purl.obolibrary.org/obo/GO_0001071"},{"id":"T10520","span":{"begin":324,"end":361},"obj":"http://purl.obolibrary.org/obo/GO_0001070"},{"id":"T10519","span":{"begin":324,"end":361},"obj":"http://purl.obolibrary.org/obo/GO_0000988"},{"id":"T10518","span":{"begin":1099,"end":1106},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T10517","span":{"begin":649,"end":656},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T10516","span":{"begin":486,"end":493},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T10515","span":{"begin":316,"end":323},"obj":"http://purl.obolibrary.org/obo/GO_0005488"}],"text":"Pharmacological inhibitors were used to demonstrate that the transcription factor sites within the IL-1RA promoter are relevant for the induction of IL-1RA by GP. As expected, an inhibition of NFκB via CAPE [35] and CyA, NFAT via CyA and NFIL-6 via CHX [36] could not be overruled by GP, leading to a down-regulated binding activity of the transcription factors to the IL-1RA sites, and a reduction of IL-1RA mRNA and IL-1RA protein levels (Fig. 7). The extent of reduction in NFATP2/3 binding is exemplarily shown in an autoradiogram (Fig. 7A, left side) and graphically summarized (n = 4, Fig. 7A, right side). The results for the NFκB and NFIL-6 binding sites were similar (data not shown). Because the highest IL-1RA amount was found at 24 h, mRNA was examined following 1 h inhibition and 18 h of GP. A representative gel demonstrating a decrease in IL-1RA mRNA after inhibition with CAPE, CyA and CHX is displayed in Fig. 7B (n = 4). In addition, corresponding IL-1RA protein levels after 24 h of GP are shown in Fig. 7C (n = 3). Altogether, NFκB inhibition by CAPE was more pronounced at the binding activity and the transcription, whereas CyA and CHX mainly led to a decreased IL-1RA release."}

{"project":"sentences","denotations":[{"id":"T10444","span":{"begin":1036,"end":1200},"obj":"Sentence"},{"id":"T10443","span":{"begin":940,"end":1035},"obj":"Sentence"},{"id":"T10442","span":{"begin":806,"end":939},"obj":"Sentence"},{"id":"T10441","span":{"begin":694,"end":805},"obj":"Sentence"},{"id":"T10440","span":{"begin":613,"end":693},"obj":"Sentence"},{"id":"T10439","span":{"begin":450,"end":612},"obj":"Sentence"},{"id":"T10438","span":{"begin":163,"end":449},"obj":"Sentence"},{"id":"T10437","span":{"begin":0,"end":162},"obj":"Sentence"},{"id":"T162","span":{"begin":0,"end":162},"obj":"Sentence"},{"id":"T163","span":{"begin":163,"end":449},"obj":"Sentence"},{"id":"T164","span":{"begin":450,"end":612},"obj":"Sentence"},{"id":"T165","span":{"begin":613,"end":693},"obj":"Sentence"},{"id":"T166","span":{"begin":694,"end":805},"obj":"Sentence"},{"id":"T167","span":{"begin":806,"end":939},"obj":"Sentence"},{"id":"T168","span":{"begin":940,"end":1035},"obj":"Sentence"},{"id":"T169","span":{"begin":1036,"end":1200},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Pharmacological inhibitors were used to demonstrate that the transcription factor sites within the IL-1RA promoter are relevant for the induction of IL-1RA by GP. As expected, an inhibition of NFκB via CAPE [35] and CyA, NFAT via CyA and NFIL-6 via CHX [36] could not be overruled by GP, leading to a down-regulated binding activity of the transcription factors to the IL-1RA sites, and a reduction of IL-1RA mRNA and IL-1RA protein levels (Fig. 7). The extent of reduction in NFATP2/3 binding is exemplarily shown in an autoradiogram (Fig. 7A, left side) and graphically summarized (n = 4, Fig. 7A, right side). The results for the NFκB and NFIL-6 binding sites were similar (data not shown). Because the highest IL-1RA amount was found at 24 h, mRNA was examined following 1 h inhibition and 18 h of GP. A representative gel demonstrating a decrease in IL-1RA mRNA after inhibition with CAPE, CyA and CHX is displayed in Fig. 7B (n = 4). In addition, corresponding IL-1RA protein levels after 24 h of GP are shown in Fig. 7C (n = 3). Altogether, NFκB inhibition by CAPE was more pronounced at the binding activity and the transcription, whereas CyA and CHX mainly led to a decreased IL-1RA release."}

{"project":"simple1","denotations":[{"id":"T10535","span":{"begin":1185,"end":1191},"obj":"Protein"},{"id":"T10534","span":{"begin":967,"end":973},"obj":"Protein"},{"id":"T10533","span":{"begin":855,"end":861},"obj":"Protein"},{"id":"T10532","span":{"begin":714,"end":720},"obj":"Protein"},{"id":"T10531","span":{"begin":418,"end":424},"obj":"Protein"},{"id":"T10530","span":{"begin":402,"end":408},"obj":"Protein"},{"id":"T10529","span":{"begin":369,"end":375},"obj":"Protein"},{"id":"T10528","span":{"begin":238,"end":244},"obj":"Protein"},{"id":"T10527","span":{"begin":221,"end":225},"obj":"Protein"},{"id":"T10526","span":{"begin":149,"end":155},"obj":"Protein"},{"id":"T10525","span":{"begin":99,"end":105},"obj":"Protein"}],"text":"Pharmacological inhibitors were used to demonstrate that the transcription factor sites within the IL-1RA promoter are relevant for the induction of IL-1RA by GP. As expected, an inhibition of NFκB via CAPE [35] and CyA, NFAT via CyA and NFIL-6 via CHX [36] could not be overruled by GP, leading to a down-regulated binding activity of the transcription factors to the IL-1RA sites, and a reduction of IL-1RA mRNA and IL-1RA protein levels (Fig. 7). The extent of reduction in NFATP2/3 binding is exemplarily shown in an autoradiogram (Fig. 7A, left side) and graphically summarized (n = 4, Fig. 7A, right side). The results for the NFκB and NFIL-6 binding sites were similar (data not shown). Because the highest IL-1RA amount was found at 24 h, mRNA was examined following 1 h inhibition and 18 h of GP. A representative gel demonstrating a decrease in IL-1RA mRNA after inhibition with CAPE, CyA and CHX is displayed in Fig. 7B (n = 4). In addition, corresponding IL-1RA protein levels after 24 h of GP are shown in Fig. 7C (n = 3). Altogether, NFκB inhibition by CAPE was more pronounced at the binding activity and the transcription, whereas CyA and CHX mainly led to a decreased IL-1RA release."}

{"project":"BioNLP16_DUT","denotations":[{"id":"T11196","span":{"begin":1192,"end":1199},"obj":"Localization"},{"id":"T11195","span":{"begin":1175,"end":1184},"obj":"Negative_regulation"},{"id":"T11194","span":{"begin":843,"end":851},"obj":"Negative_regulation"},{"id":"T11193","span":{"begin":389,"end":398},"obj":"Negative_regulation"},{"id":"T11192","span":{"begin":119,"end":127},"obj":"Positive_regulation"},{"id":"T11191","span":{"begin":136,"end":145},"obj":"Positive_regulation"},{"id":"T11189","span":{"begin":1185,"end":1191},"obj":"Protein"},{"id":"T11188","span":{"begin":967,"end":973},"obj":"Protein"},{"id":"T11187","span":{"begin":855,"end":861},"obj":"Protein"},{"id":"T11186","span":{"begin":714,"end":720},"obj":"Protein"},{"id":"T11185","span":{"begin":418,"end":424},"obj":"Protein"},{"id":"T11184","span":{"begin":402,"end":408},"obj":"Protein"},{"id":"T11183","span":{"begin":369,"end":375},"obj":"Protein"},{"id":"T11182","span":{"begin":238,"end":244},"obj":"Protein"},{"id":"T11181","span":{"begin":221,"end":225},"obj":"Protein"},{"id":"T11180","span":{"begin":149,"end":155},"obj":"Protein"},{"id":"T11179","span":{"begin":99,"end":105},"obj":"Protein"}],"relations":[{"id":"R7412","pred":"themeOf","subj":"T11180","obj":"T11191"},{"id":"R7413","pred":"themeOf","subj":"T11184","obj":"T11193"},{"id":"R7414","pred":"themeOf","subj":"T11185","obj":"T11193"},{"id":"R7415","pred":"themeOf","subj":"T11187","obj":"T11194"},{"id":"R7416","pred":"themeOf","subj":"T11189","obj":"T11196"},{"id":"R7417","pred":"themeOf","subj":"T11191","obj":"T11192"},{"id":"R7418","pred":"themeOf","subj":"T11196","obj":"T11195"}],"text":"Pharmacological inhibitors were used to demonstrate that the transcription factor sites within the IL-1RA promoter are relevant for the induction of IL-1RA by GP. As expected, an inhibition of NFκB via CAPE [35] and CyA, NFAT via CyA and NFIL-6 via CHX [36] could not be overruled by GP, leading to a down-regulated binding activity of the transcription factors to the IL-1RA sites, and a reduction of IL-1RA mRNA and IL-1RA protein levels (Fig. 7). The extent of reduction in NFATP2/3 binding is exemplarily shown in an autoradiogram (Fig. 7A, left side) and graphically summarized (n = 4, Fig. 7A, right side). The results for the NFκB and NFIL-6 binding sites were similar (data not shown). Because the highest IL-1RA amount was found at 24 h, mRNA was examined following 1 h inhibition and 18 h of GP. A representative gel demonstrating a decrease in IL-1RA mRNA after inhibition with CAPE, CyA and CHX is displayed in Fig. 7B (n = 4). In addition, corresponding IL-1RA protein levels after 24 h of GP are shown in Fig. 7C (n = 3). Altogether, NFκB inhibition by CAPE was more pronounced at the binding activity and the transcription, whereas CyA and CHX mainly led to a decreased IL-1RA release."}

{"project":"BioNLP16_Messiy","denotations":[{"id":"T10808","span":{"begin":1175,"end":1184},"obj":"Negative_regulation"},{"id":"T10807","span":{"begin":1192,"end":1199},"obj":"Localization"},{"id":"T10806","span":{"begin":843,"end":851},"obj":"Negative_regulation"},{"id":"T10805","span":{"begin":389,"end":398},"obj":"Negative_regulation"},{"id":"T10804","span":{"begin":136,"end":145},"obj":"Positive_regulation"},{"id":"T10801","span":{"begin":1185,"end":1191},"obj":"Protein"},{"id":"T10800","span":{"begin":967,"end":973},"obj":"Protein"},{"id":"T10799","span":{"begin":855,"end":861},"obj":"Protein"},{"id":"T10798","span":{"begin":714,"end":720},"obj":"Protein"},{"id":"T10797","span":{"begin":418,"end":424},"obj":"Protein"},{"id":"T10796","span":{"begin":402,"end":408},"obj":"Protein"},{"id":"T10795","span":{"begin":369,"end":375},"obj":"Protein"},{"id":"T10794","span":{"begin":238,"end":244},"obj":"Protein"},{"id":"T10793","span":{"begin":221,"end":225},"obj":"Protein"},{"id":"T10792","span":{"begin":149,"end":155},"obj":"Protein"},{"id":"T10791","span":{"begin":99,"end":105},"obj":"Protein"}],"relations":[{"id":"R7109","pred":"themeOf","subj":"T10792","obj":"T10804"},{"id":"R7110","pred":"themeOf","subj":"T10796","obj":"T10805"},{"id":"R7111","pred":"themeOf","subj":"T10797","obj":"T10805"},{"id":"R7112","pred":"themeOf","subj":"T10799","obj":"T10806"},{"id":"R7113","pred":"themeOf","subj":"T10801","obj":"T10807"},{"id":"R7114","pred":"themeOf","subj":"T10807","obj":"T10808"}],"text":"Pharmacological inhibitors were used to demonstrate that the transcription factor sites within the IL-1RA promoter are relevant for the induction of IL-1RA by GP. As expected, an inhibition of NFκB via CAPE [35] and CyA, NFAT via CyA and NFIL-6 via CHX [36] could not be overruled by GP, leading to a down-regulated binding activity of the transcription factors to the IL-1RA sites, and a reduction of IL-1RA mRNA and IL-1RA protein levels (Fig. 7). The extent of reduction in NFATP2/3 binding is exemplarily shown in an autoradiogram (Fig. 7A, left side) and graphically summarized (n = 4, Fig. 7A, right side). The results for the NFκB and NFIL-6 binding sites were similar (data not shown). Because the highest IL-1RA amount was found at 24 h, mRNA was examined following 1 h inhibition and 18 h of GP. A representative gel demonstrating a decrease in IL-1RA mRNA after inhibition with CAPE, CyA and CHX is displayed in Fig. 7B (n = 4). In addition, corresponding IL-1RA protein levels after 24 h of GP are shown in Fig. 7C (n = 3). Altogether, NFκB inhibition by CAPE was more pronounced at the binding activity and the transcription, whereas CyA and CHX mainly led to a decreased IL-1RA release."}

{"project":"DLUT931","denotations":[{"id":"T10876","span":{"begin":1175,"end":1184},"obj":"Negative_regulation"},{"id":"T10875","span":{"begin":1166,"end":1169},"obj":"Positive_regulation"},{"id":"T10874","span":{"begin":1192,"end":1199},"obj":"Localization"},{"id":"T10873","span":{"begin":389,"end":398},"obj":"Negative_regulation"},{"id":"T10872","span":{"begin":179,"end":189},"obj":"Negative_regulation"},{"id":"T10871","span":{"begin":119,"end":127},"obj":"Positive_regulation"},{"id":"T10870","span":{"begin":136,"end":145},"obj":"Positive_regulation"},{"id":"T10867","span":{"begin":1185,"end":1191},"obj":"Protein"},{"id":"T10866","span":{"begin":967,"end":973},"obj":"Protein"},{"id":"T10865","span":{"begin":855,"end":861},"obj":"Protein"},{"id":"T10864","span":{"begin":714,"end":720},"obj":"Protein"},{"id":"T10863","span":{"begin":418,"end":424},"obj":"Protein"},{"id":"T10862","span":{"begin":402,"end":408},"obj":"Protein"},{"id":"T10861","span":{"begin":369,"end":375},"obj":"Protein"},{"id":"T10860","span":{"begin":238,"end":244},"obj":"Protein"},{"id":"T10859","span":{"begin":221,"end":225},"obj":"Protein"},{"id":"T10858","span":{"begin":149,"end":155},"obj":"Protein"},{"id":"T10857","span":{"begin":99,"end":105},"obj":"Protein"}],"relations":[{"id":"R7132","pred":"themeOf","subj":"T10858","obj":"T10870"},{"id":"R7133","pred":"themeOf","subj":"T10859","obj":"T10872"},{"id":"R7134","pred":"themeOf","subj":"T10862","obj":"T10873"},{"id":"R7135","pred":"themeOf","subj":"T10863","obj":"T10873"},{"id":"R7136","pred":"themeOf","subj":"T10867","obj":"T10874"},{"id":"R7138","pred":"themeOf","subj":"T10870","obj":"T10871"},{"id":"R7139","pred":"themeOf","subj":"T10874","obj":"T10875"},{"id":"R7140","pred":"themeOf","subj":"T10874","obj":"T10876"}],"text":"Pharmacological inhibitors were used to demonstrate that the transcription factor sites within the IL-1RA promoter are relevant for the induction of IL-1RA by GP. As expected, an inhibition of NFκB via CAPE [35] and CyA, NFAT via CyA and NFIL-6 via CHX [36] could not be overruled by GP, leading to a down-regulated binding activity of the transcription factors to the IL-1RA sites, and a reduction of IL-1RA mRNA and IL-1RA protein levels (Fig. 7). The extent of reduction in NFATP2/3 binding is exemplarily shown in an autoradiogram (Fig. 7A, left side) and graphically summarized (n = 4, Fig. 7A, right side). The results for the NFκB and NFIL-6 binding sites were similar (data not shown). Because the highest IL-1RA amount was found at 24 h, mRNA was examined following 1 h inhibition and 18 h of GP. A representative gel demonstrating a decrease in IL-1RA mRNA after inhibition with CAPE, CyA and CHX is displayed in Fig. 7B (n = 4). In addition, corresponding IL-1RA protein levels after 24 h of GP are shown in Fig. 7C (n = 3). Altogether, NFκB inhibition by CAPE was more pronounced at the binding activity and the transcription, whereas CyA and CHX mainly led to a decreased IL-1RA release."}

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inhibitors were used to demonstrate that the transcription factor sites within the IL-1RA promoter are relevant for the induction of IL-1RA by GP. As expected, an inhibition of NFκB via CAPE [35] and CyA, NFAT via CyA and NFIL-6 via CHX [36] could not be overruled by GP, leading to a down-regulated binding activity of the transcription factors to the IL-1RA sites, and a reduction of IL-1RA mRNA and IL-1RA protein levels (Fig. 7). The extent of reduction in NFATP2/3 binding is exemplarily shown in an autoradiogram (Fig. 7A, left side) and graphically summarized (n = 4, Fig. 7A, right side). The results for the NFκB and NFIL-6 binding sites were similar (data not shown). Because the highest IL-1RA amount was found at 24 h, mRNA was examined following 1 h inhibition and 18 h of GP. A representative gel demonstrating a decrease in IL-1RA mRNA after inhibition with CAPE, CyA and CHX is displayed in Fig. 7B (n = 4). In addition, corresponding IL-1RA protein levels after 24 h of GP are shown in Fig. 7C (n = 3). Altogether, NFκB inhibition by CAPE was more pronounced at the binding activity and the transcription, whereas CyA and CHX mainly led to a decreased IL-1RA release."}

{"project":"bionlp-st-ge-2016-test-tees","denotations":[{"id":"T10855","span":{"begin":1175,"end":1184},"obj":"Negative_regulation"},{"id":"T10831","span":{"begin":238,"end":244},"obj":"Protein"},{"id":"T10830","span":{"begin":221,"end":233},"obj":"Protein"},{"id":"T10829","span":{"begin":202,"end":219},"obj":"Protein"},{"id":"T10828","span":{"begin":193,"end":197},"obj":"Protein"},{"id":"T10827","span":{"begin":119,"end":127},"obj":"Positive_regulation"},{"id":"T10826","span":{"begin":136,"end":145},"obj":"Positive_regulation"},{"id":"T10825","span":{"begin":159,"end":161},"obj":"Protein"},{"id":"T10824","span":{"begin":149,"end":155},"obj":"Protein"},{"id":"T10823","span":{"begin":99,"end":114},"obj":"Protein"},{"id":"T10854","span":{"begin":1081,"end":1091},"obj":"Positive_regulation"},{"id":"T10853","span":{"begin":1192,"end":1199},"obj":"Localization"},{"id":"T10852","span":{"begin":1099,"end":1106},"obj":"Binding"},{"id":"T10851","span":{"begin":1053,"end":1063},"obj":"Negative_regulation"},{"id":"T10850","span":{"begin":1185,"end":1191},"obj":"Protein"},{"id":"T10849","span":{"begin":1048,"end":1052},"obj":"Protein"},{"id":"T10848","span":{"begin":982,"end":988},"obj":"Gene_expression"},{"id":"T10847","span":{"begin":982,"end":988},"obj":"Gene_expression"},{"id":"T10846","span":{"begin":1019,"end":1022},"obj":"Protein"},{"id":"T10845","span":{"begin":1003,"end":1005},"obj":"Protein"},{"id":"T10844","span":{"begin":967,"end":981},"obj":"Protein"},{"id":"T10843","span":{"begin":843,"end":851},"obj":"Negative_regulation"},{"id":"T10842","span":{"begin":923,"end":926},"obj":"Protein"},{"id":"T10841","span":{"begin":855,"end":861},"obj":"Protein"},{"id":"T10840","span":{"begin":706,"end":720},"obj":"Protein"},{"id":"T10839","span":{"begin":642,"end":662},"obj":"Protein"},{"id":"T10838","span":{"begin":633,"end":637},"obj":"Protein"},{"id":"T10837","span":{"begin":389,"end":398},"obj":"Negative_regulation"},{"id":"T10836","span":{"begin":389,"end":398},"obj":"Negative_regulation"},{"id":"T10835","span":{"begin":179,"end":189},"obj":"Negative_regulation"},{"id":"T10834","span":{"begin":179,"end":189},"obj":"Negative_regulation"},{"id":"T10833","span":{"begin":418,"end":432},"obj":"Protein"},{"id":"T10832","span":{"begin":402,"end":413},"obj":"Protein"}],"relations":[{"id":"R7116","pred":"themeOf","subj":"T10824","obj":"T10826"},{"id":"R7117","pred":"causeOf","subj":"T10825","obj":"T10826"},{"id":"R7118","pred":"themeOf","subj":"T10826","obj":"T10827"},{"id":"R7119","pred":"themeOf","subj":"T10828","obj":"T10834"},{"id":"R7120","pred":"themeOf","subj":"T10829","obj":"T10835"},{"id":"R7121","pred":"themeOf","subj":"T10832","obj":"T10836"},{"id":"R7122","pred":"themeOf","subj":"T10833","obj":"T10837"},{"id":"R7123","pred":"themeOf","subj":"T10841","obj":"T10843"},{"id":"R7124","pred":"themeOf","subj":"T10844","obj":"T10847"},{"id":"R7125","pred":"themeOf","subj":"T10845","obj":"T10848"},{"id":"R7126","pred":"themeOf","subj":"T10849","obj":"T10851"},{"id":"R7127","pred":"themeOf","subj":"T10849","obj":"T10852"},{"id":"R7128","pred":"themeOf","subj":"T10850","obj":"T10853"},{"id":"R7129","pred":"themeOf","subj":"T10852","obj":"T10854"},{"id":"R7130","pred":"themeOf","subj":"T10853","obj":"T10855"}],"text":"Pharmacological inhibitors were used to demonstrate that the transcription factor sites within the IL-1RA promoter are relevant for the induction of IL-1RA by GP. As expected, an inhibition of NFκB via CAPE [35] and CyA, NFAT via CyA and NFIL-6 via CHX [36] could not be overruled by GP, leading to a down-regulated binding activity of the transcription factors to the IL-1RA sites, and a reduction of IL-1RA mRNA and IL-1RA protein levels (Fig. 7). The extent of reduction in NFATP2/3 binding is exemplarily shown in an autoradiogram (Fig. 7A, left side) and graphically summarized (n = 4, Fig. 7A, right side). The results for the NFκB and NFIL-6 binding sites were similar (data not shown). Because the highest IL-1RA amount was found at 24 h, mRNA was examined following 1 h inhibition and 18 h of GP. A representative gel demonstrating a decrease in IL-1RA mRNA after inhibition with CAPE, CyA and CHX is displayed in Fig. 7B (n = 4). In addition, corresponding IL-1RA protein levels after 24 h of GP are shown in Fig. 7C (n = 3). Altogether, NFκB inhibition by CAPE was more pronounced at the binding activity and the transcription, whereas CyA and CHX mainly led to a decreased IL-1RA release."}

{"project":"testone","denotations":[{"id":"T10395","span":{"begin":1192,"end":1199},"obj":"Localization"},{"id":"T10394","span":{"begin":1175,"end":1184},"obj":"Negative_regulation"},{"id":"T10393","span":{"begin":1166,"end":1169},"obj":"Positive_regulation"},{"id":"T10392","span":{"begin":1099,"end":1106},"obj":"Binding"},{"id":"T10391","span":{"begin":843,"end":851},"obj":"Negative_regulation"},{"id":"T10390","span":{"begin":486,"end":493},"obj":"Binding"},{"id":"T10389","span":{"begin":464,"end":473},"obj":"Negative_regulation"},{"id":"T10388","span":{"begin":389,"end":398},"obj":"Negative_regulation"},{"id":"T10387","span":{"begin":376,"end":381},"obj":"Entity"},{"id":"T10386","span":{"begin":316,"end":323},"obj":"Binding"},{"id":"T10385","span":{"begin":301,"end":315},"obj":"Negative_regulation"},{"id":"T10384","span":{"begin":271,"end":280},"obj":"Negative_regulation"},{"id":"T10383","span":{"begin":226,"end":229},"obj":"Positive_regulation"},{"id":"T10382","span":{"begin":136,"end":145},"obj":"Positive_regulation"},{"id":"T10381","span":{"begin":75,"end":81},"obj":"Entity"},{"id":"T10379","span":{"begin":1185,"end":1191},"obj":"Protein"},{"id":"T10378","span":{"begin":967,"end":973},"obj":"Protein"},{"id":"T10377","span":{"begin":855,"end":861},"obj":"Protein"},{"id":"T10376","span":{"begin":714,"end":720},"obj":"Protein"},{"id":"T10375","span":{"begin":418,"end":424},"obj":"Protein"},{"id":"T10374","span":{"begin":402,"end":408},"obj":"Protein"},{"id":"T10373","span":{"begin":369,"end":375},"obj":"Protein"},{"id":"T10372","span":{"begin":238,"end":244},"obj":"Protein"},{"id":"T10371","span":{"begin":221,"end":225},"obj":"Protein"},{"id":"T10370","span":{"begin":149,"end":155},"obj":"Protein"},{"id":"T10369","span":{"begin":99,"end":105},"obj":"Protein"}],"relations":[{"id":"R6805","pred":"themeOf","subj":"T10370","obj":"T10382"},{"id":"R6806","pred":"causeOf","subj":"T10372","obj":"T10383"},{"id":"R6807","pred":"themeOf","subj":"T10374","obj":"T10388"},{"id":"R6808","pred":"themeOf","subj":"T10377","obj":"T10391"},{"id":"R6809","pred":"themeOf","subj":"T10379","obj":"T10395"},{"id":"R6810","pred":"themeOf","subj":"T10386","obj":"T10385"},{"id":"R6811","pred":"themeOf","subj":"T10390","obj":"T10389"},{"id":"R6812","pred":"themeOf","subj":"T10394","obj":"T10393"},{"id":"R6813","pred":"themeOf","subj":"T10395","obj":"T10394"}],"text":"Pharmacological inhibitors were used to demonstrate that the transcription factor sites within the IL-1RA promoter are relevant for the induction of IL-1RA by GP. As expected, an inhibition of NFκB via CAPE [35] and CyA, NFAT via CyA and NFIL-6 via CHX [36] could not be overruled by GP, leading to a down-regulated binding activity of the transcription factors to the IL-1RA sites, and a reduction of IL-1RA mRNA and IL-1RA protein levels (Fig. 7). The extent of reduction in NFATP2/3 binding is exemplarily shown in an autoradiogram (Fig. 7A, left side) and graphically summarized (n = 4, Fig. 7A, right side). The results for the NFκB and NFIL-6 binding sites were similar (data not shown). Because the highest IL-1RA amount was found at 24 h, mRNA was examined following 1 h inhibition and 18 h of GP. A representative gel demonstrating a decrease in IL-1RA mRNA after inhibition with CAPE, CyA and CHX is displayed in Fig. 7B (n = 4). In addition, corresponding IL-1RA protein levels after 24 h of GP are shown in Fig. 7C (n = 3). Altogether, NFκB inhibition by CAPE was more pronounced at the binding activity and the transcription, whereas CyA and CHX mainly led to a decreased IL-1RA release."}

{"project":"test3","denotations":[{"id":"T10435","span":{"begin":1192,"end":1199},"obj":"Localization"},{"id":"T10434","span":{"begin":1185,"end":1191},"obj":"Protein"},{"id":"T10433","span":{"begin":1175,"end":1184},"obj":"Negative_regulation"},{"id":"T10432","span":{"begin":1166,"end":1169},"obj":"Positive_regulation"},{"id":"T10431","span":{"begin":1099,"end":1106},"obj":"Binding"},{"id":"T10430","span":{"begin":967,"end":973},"obj":"Protein"},{"id":"T10429","span":{"begin":873,"end":883},"obj":"Negative_regulation"},{"id":"T10428","span":{"begin":855,"end":861},"obj":"Protein"},{"id":"T10427","span":{"begin":843,"end":851},"obj":"Negative_regulation"},{"id":"T10426","span":{"begin":714,"end":720},"obj":"Protein"},{"id":"T10425","span":{"begin":486,"end":493},"obj":"Binding"},{"id":"T10424","span":{"begin":464,"end":473},"obj":"Negative_regulation"},{"id":"T10423","span":{"begin":418,"end":424},"obj":"Protein"},{"id":"T10422","span":{"begin":402,"end":408},"obj":"Protein"},{"id":"T10421","span":{"begin":389,"end":398},"obj":"Negative_regulation"},{"id":"T10420","span":{"begin":369,"end":375},"obj":"Protein"},{"id":"T10419","span":{"begin":316,"end":323},"obj":"Binding"},{"id":"T10418","span":{"begin":301,"end":315},"obj":"Negative_regulation"},{"id":"T10417","span":{"begin":271,"end":280},"obj":"Negative_regulation"},{"id":"T10416","span":{"begin":245,"end":248},"obj":"Positive_regulation"},{"id":"T10415","span":{"begin":238,"end":244},"obj":"Protein"},{"id":"T10414","span":{"begin":226,"end":229},"obj":"Positive_regulation"},{"id":"T10413","span":{"begin":221,"end":225},"obj":"Protein"},{"id":"T10412","span":{"begin":149,"end":155},"obj":"Protein"},{"id":"T10411","span":{"begin":136,"end":145},"obj":"Positive_regulation"},{"id":"T10410","span":{"begin":99,"end":105},"obj":"Protein"},{"id":"T10407","span":{"begin":1185,"end":1191},"obj":"Protein"},{"id":"T10406","span":{"begin":967,"end":973},"obj":"Protein"},{"id":"T10405","span":{"begin":855,"end":861},"obj":"Protein"},{"id":"T10404","span":{"begin":714,"end":720},"obj":"Protein"},{"id":"T10403","span":{"begin":418,"end":424},"obj":"Protein"},{"id":"T10402","span":{"begin":402,"end":408},"obj":"Protein"},{"id":"T10401","span":{"begin":369,"end":375},"obj":"Protein"},{"id":"T10400","span":{"begin":238,"end":244},"obj":"Protein"},{"id":"T10399","span":{"begin":221,"end":225},"obj":"Protein"},{"id":"T10398","span":{"begin":149,"end":155},"obj":"Protein"},{"id":"T10397","span":{"begin":99,"end":105},"obj":"Protein"}],"relations":[{"id":"R6815","pred":"themeOf","subj":"T10412","obj":"T10411"},{"id":"R6816","pred":"causeOf","subj":"T10415","obj":"T10414"},{"id":"R6817","pred":"themeOf","subj":"T10419","obj":"T10418"},{"id":"R6818","pred":"themeOf","subj":"T10422","obj":"T10421"},{"id":"R6819","pred":"themeOf","subj":"T10423","obj":"T10421"},{"id":"R6820","pred":"themeOf","subj":"T10425","obj":"T10424"},{"id":"R6821","pred":"themeOf","subj":"T10428","obj":"T10427"},{"id":"R6822","pred":"causeOf","subj":"T10429","obj":"T10427"},{"id":"R6823","pred":"themeOf","subj":"T10434","obj":"T10435"},{"id":"R6824","pred":"themeOf","subj":"T10435","obj":"T10433"}],"text":"Pharmacological inhibitors were used to demonstrate that the transcription factor sites within the IL-1RA promoter are relevant for the induction of IL-1RA by GP. As expected, an inhibition of NFκB via CAPE [35] and CyA, NFAT via CyA and NFIL-6 via CHX [36] could not be overruled by GP, leading to a down-regulated binding activity of the transcription factors to the IL-1RA sites, and a reduction of IL-1RA mRNA and IL-1RA protein levels (Fig. 7). The extent of reduction in NFATP2/3 binding is exemplarily shown in an autoradiogram (Fig. 7A, left side) and graphically summarized (n = 4, Fig. 7A, right side). The results for the NFκB and NFIL-6 binding sites were similar (data not shown). Because the highest IL-1RA amount was found at 24 h, mRNA was examined following 1 h inhibition and 18 h of GP. A representative gel demonstrating a decrease in IL-1RA mRNA after inhibition with CAPE, CyA and CHX is displayed in Fig. 7B (n = 4). In addition, corresponding IL-1RA protein levels after 24 h of GP are shown in Fig. 7C (n = 3). Altogether, NFκB inhibition by CAPE was more pronounced at the binding activity and the transcription, whereas CyA and CHX mainly led to a decreased IL-1RA release."}