PMC:3291650 / 37520-38829 JSON TXT

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pmc-enju-pas

bionlp-st-ge-2016-uniprot

{"project":"bionlp-st-ge-2016-uniprot","denotations":[{"id":"T17723","span":{"begin":1042,"end":1046},"obj":"http://www.uniprot.org/uniprot/Q14653"},{"id":"T17722","span":{"begin":1010,"end":1014},"obj":"http://www.uniprot.org/uniprot/Q14653"},{"id":"T17721","span":{"begin":967,"end":970},"obj":"http://www.uniprot.org/uniprot/P21579"},{"id":"T17720","span":{"begin":967,"end":970},"obj":"http://www.uniprot.org/uniprot/Q04206"},{"id":"T17719","span":{"begin":946,"end":949},"obj":"http://www.uniprot.org/uniprot/P21580"}],"namespaces":[{"prefix":"_base","uri":"http://www.uniprot.org/uniprot/"}],"text":"For total lysates, cells were lysed at 4°C for 15 min in lysis buffer (200 mM NaCl, 1% NP-40, 10 mM Tris-HCl pH 7.5, 5 mM EDTA, 2 mM DTT) supplemented with protease and phosphatase inhibitors. Nuclear and cytoplasmic lysates were prepared by resuspending cells in B1 (10 mM Hepes pH 7.5, 10 mM KCl, 1 mM MgCl2, 5% glycerol, 0.5 mM EDTA and 0.1 mM EGTA supplemented with protease and phosphatase inhibitors) for 15 min at 4°C. Next, NP-40 detergent was added to a final concentration of 0.65% and cells were centrifuged at 500 g for 5 min. The nuclear fraction containing pellet was lyzed in B2 (20 mM Hepes pH 7.5, 1% NP-40, 400 mM NaCl, 10 mM KCl, 1 mM MgCl2, 20% glycerol, 0.5 mM EDTA and 0.1 mM EGTA supplemented with protease and phosphatase inhibitors) for 15 min at 4°C. The lysates were subsequently separated by SDS-PAGE and analyzed by western blotting and ECL detection (Perkin Elmer Life Sciences). Immunoblots were revealed with anti-A20, anti-IκBα, anti-p65, and anti-histon H1 (Santa Cruz), anti-IRF3 (Invitrogen), anti-phospho-IRF3 and anti-phospho-IκBα (Cell Signaling) and anti-actin (MP Biomedicals). The density of the bands was quantified (fold induction) with the ImageJ (http://rsbweb.nih.gov/ij) Gel analyzer tool. All intensities were calculated relative to the first lane ( = time 0)."}

GO-BP

{"project":"GO-BP","denotations":[{"id":"T17170","span":{"begin":734,"end":745},"obj":"http://purl.obolibrary.org/obo/GO_0016791"},{"id":"T17169","span":{"begin":383,"end":394},"obj":"http://purl.obolibrary.org/obo/GO_0016791"},{"id":"T17168","span":{"begin":169,"end":180},"obj":"http://purl.obolibrary.org/obo/GO_0016791"},{"id":"T17167","span":{"begin":57,"end":62},"obj":"http://purl.obolibrary.org/obo/GO_0019835"}],"text":"For total lysates, cells were lysed at 4°C for 15 min in lysis buffer (200 mM NaCl, 1% NP-40, 10 mM Tris-HCl pH 7.5, 5 mM EDTA, 2 mM DTT) supplemented with protease and phosphatase inhibitors. Nuclear and cytoplasmic lysates were prepared by resuspending cells in B1 (10 mM Hepes pH 7.5, 10 mM KCl, 1 mM MgCl2, 5% glycerol, 0.5 mM EDTA and 0.1 mM EGTA supplemented with protease and phosphatase inhibitors) for 15 min at 4°C. Next, NP-40 detergent was added to a final concentration of 0.65% and cells were centrifuged at 500 g for 5 min. The nuclear fraction containing pellet was lyzed in B2 (20 mM Hepes pH 7.5, 1% NP-40, 400 mM NaCl, 10 mM KCl, 1 mM MgCl2, 20% glycerol, 0.5 mM EDTA and 0.1 mM EGTA supplemented with protease and phosphatase inhibitors) for 15 min at 4°C. The lysates were subsequently separated by SDS-PAGE and analyzed by western blotting and ECL detection (Perkin Elmer Life Sciences). Immunoblots were revealed with anti-A20, anti-IκBα, anti-p65, and anti-histon H1 (Santa Cruz), anti-IRF3 (Invitrogen), anti-phospho-IRF3 and anti-phospho-IκBα (Cell Signaling) and anti-actin (MP Biomedicals). The density of the bands was quantified (fold induction) with the ImageJ (http://rsbweb.nih.gov/ij) Gel analyzer tool. All intensities were calculated relative to the first lane ( = time 0)."}

GO-MF

{"project":"GO-MF","denotations":[{"id":"T17173","span":{"begin":734,"end":745},"obj":"http://purl.obolibrary.org/obo/GO_0016791"},{"id":"T17172","span":{"begin":383,"end":394},"obj":"http://purl.obolibrary.org/obo/GO_0016791"},{"id":"T17171","span":{"begin":169,"end":180},"obj":"http://purl.obolibrary.org/obo/GO_0016791"}],"text":"For total lysates, cells were lysed at 4°C for 15 min in lysis buffer (200 mM NaCl, 1% NP-40, 10 mM Tris-HCl pH 7.5, 5 mM EDTA, 2 mM DTT) supplemented with protease and phosphatase inhibitors. Nuclear and cytoplasmic lysates were prepared by resuspending cells in B1 (10 mM Hepes pH 7.5, 10 mM KCl, 1 mM MgCl2, 5% glycerol, 0.5 mM EDTA and 0.1 mM EGTA supplemented with protease and phosphatase inhibitors) for 15 min at 4°C. Next, NP-40 detergent was added to a final concentration of 0.65% and cells were centrifuged at 500 g for 5 min. The nuclear fraction containing pellet was lyzed in B2 (20 mM Hepes pH 7.5, 1% NP-40, 400 mM NaCl, 10 mM KCl, 1 mM MgCl2, 20% glycerol, 0.5 mM EDTA and 0.1 mM EGTA supplemented with protease and phosphatase inhibitors) for 15 min at 4°C. The lysates were subsequently separated by SDS-PAGE and analyzed by western blotting and ECL detection (Perkin Elmer Life Sciences). Immunoblots were revealed with anti-A20, anti-IκBα, anti-p65, and anti-histon H1 (Santa Cruz), anti-IRF3 (Invitrogen), anti-phospho-IRF3 and anti-phospho-IκBα (Cell Signaling) and anti-actin (MP Biomedicals). The density of the bands was quantified (fold induction) with the ImageJ (http://rsbweb.nih.gov/ij) Gel analyzer tool. All intensities were calculated relative to the first lane ( = time 0)."}

GO-CC

{"project":"GO-CC","denotations":[{"id":"T17176","span":{"begin":496,"end":501},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T17175","span":{"begin":255,"end":260},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T17174","span":{"begin":19,"end":24},"obj":"http://purl.obolibrary.org/obo/GO_0005623"}],"text":"For total lysates, cells were lysed at 4°C for 15 min in lysis buffer (200 mM NaCl, 1% NP-40, 10 mM Tris-HCl pH 7.5, 5 mM EDTA, 2 mM DTT) supplemented with protease and phosphatase inhibitors. Nuclear and cytoplasmic lysates were prepared by resuspending cells in B1 (10 mM Hepes pH 7.5, 10 mM KCl, 1 mM MgCl2, 5% glycerol, 0.5 mM EDTA and 0.1 mM EGTA supplemented with protease and phosphatase inhibitors) for 15 min at 4°C. Next, NP-40 detergent was added to a final concentration of 0.65% and cells were centrifuged at 500 g for 5 min. The nuclear fraction containing pellet was lyzed in B2 (20 mM Hepes pH 7.5, 1% NP-40, 400 mM NaCl, 10 mM KCl, 1 mM MgCl2, 20% glycerol, 0.5 mM EDTA and 0.1 mM EGTA supplemented with protease and phosphatase inhibitors) for 15 min at 4°C. The lysates were subsequently separated by SDS-PAGE and analyzed by western blotting and ECL detection (Perkin Elmer Life Sciences). Immunoblots were revealed with anti-A20, anti-IκBα, anti-p65, and anti-histon H1 (Santa Cruz), anti-IRF3 (Invitrogen), anti-phospho-IRF3 and anti-phospho-IκBα (Cell Signaling) and anti-actin (MP Biomedicals). The density of the bands was quantified (fold induction) with the ImageJ (http://rsbweb.nih.gov/ij) Gel analyzer tool. All intensities were calculated relative to the first lane ( = time 0)."}

sentences

{"project":"sentences","denotations":[{"id":"T17166","span":{"begin":1238,"end":1309},"obj":"Sentence"},{"id":"T17165","span":{"begin":1119,"end":1237},"obj":"Sentence"},{"id":"T17164","span":{"begin":910,"end":1118},"obj":"Sentence"},{"id":"T17163","span":{"begin":539,"end":909},"obj":"Sentence"},{"id":"T17162","span":{"begin":193,"end":538},"obj":"Sentence"},{"id":"T17161","span":{"begin":0,"end":192},"obj":"Sentence"},{"id":"T241","span":{"begin":0,"end":192},"obj":"Sentence"},{"id":"T242","span":{"begin":193,"end":425},"obj":"Sentence"},{"id":"T243","span":{"begin":426,"end":538},"obj":"Sentence"},{"id":"T244","span":{"begin":539,"end":776},"obj":"Sentence"},{"id":"T245","span":{"begin":777,"end":909},"obj":"Sentence"},{"id":"T246","span":{"begin":910,"end":1118},"obj":"Sentence"},{"id":"T247","span":{"begin":1119,"end":1237},"obj":"Sentence"},{"id":"T248","span":{"begin":1238,"end":1309},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"For total lysates, cells were lysed at 4°C for 15 min in lysis buffer (200 mM NaCl, 1% NP-40, 10 mM Tris-HCl pH 7.5, 5 mM EDTA, 2 mM DTT) supplemented with protease and phosphatase inhibitors. Nuclear and cytoplasmic lysates were prepared by resuspending cells in B1 (10 mM Hepes pH 7.5, 10 mM KCl, 1 mM MgCl2, 5% glycerol, 0.5 mM EDTA and 0.1 mM EGTA supplemented with protease and phosphatase inhibitors) for 15 min at 4°C. Next, NP-40 detergent was added to a final concentration of 0.65% and cells were centrifuged at 500 g for 5 min. The nuclear fraction containing pellet was lyzed in B2 (20 mM Hepes pH 7.5, 1% NP-40, 400 mM NaCl, 10 mM KCl, 1 mM MgCl2, 20% glycerol, 0.5 mM EDTA and 0.1 mM EGTA supplemented with protease and phosphatase inhibitors) for 15 min at 4°C. The lysates were subsequently separated by SDS-PAGE and analyzed by western blotting and ECL detection (Perkin Elmer Life Sciences). Immunoblots were revealed with anti-A20, anti-IκBα, anti-p65, and anti-histon H1 (Santa Cruz), anti-IRF3 (Invitrogen), anti-phospho-IRF3 and anti-phospho-IκBα (Cell Signaling) and anti-actin (MP Biomedicals). The density of the bands was quantified (fold induction) with the ImageJ (http://rsbweb.nih.gov/ij) Gel analyzer tool. All intensities were calculated relative to the first lane ( = time 0)."}

bionlp-st-ge-2016-test-ihmc

bionlp-st-ge-2016-spacy-parsed

bionlp-st-ge-2016-test-tees

{"project":"bionlp-st-ge-2016-test-tees","denotations":[{"id":"T17734","span":{"begin":1090,"end":1100},"obj":"Protein"},{"id":"T17733","span":{"begin":1051,"end":1085},"obj":"Protein"},{"id":"T17732","span":{"begin":1029,"end":1046},"obj":"Protein"},{"id":"T17731","span":{"begin":976,"end":990},"obj":"Protein"},{"id":"T17730","span":{"begin":962,"end":970},"obj":"Protein"},{"id":"T17729","span":{"begin":951,"end":960},"obj":"Protein"},{"id":"T17728","span":{"begin":941,"end":949},"obj":"Protein"},{"id":"T17727","span":{"begin":695,"end":745},"obj":"Protein"},{"id":"T17726","span":{"begin":344,"end":394},"obj":"Protein"},{"id":"T17725","span":{"begin":181,"end":191},"obj":"Negative_regulation"},{"id":"T17724","span":{"begin":156,"end":180},"obj":"Protein"}],"relations":[{"id":"R13503","pred":"themeOf","subj":"T17724","obj":"T17725"}],"text":"For total lysates, cells were lysed at 4°C for 15 min in lysis buffer (200 mM NaCl, 1% NP-40, 10 mM Tris-HCl pH 7.5, 5 mM EDTA, 2 mM DTT) supplemented with protease and phosphatase inhibitors. Nuclear and cytoplasmic lysates were prepared by resuspending cells in B1 (10 mM Hepes pH 7.5, 10 mM KCl, 1 mM MgCl2, 5% glycerol, 0.5 mM EDTA and 0.1 mM EGTA supplemented with protease and phosphatase inhibitors) for 15 min at 4°C. Next, NP-40 detergent was added to a final concentration of 0.65% and cells were centrifuged at 500 g for 5 min. The nuclear fraction containing pellet was lyzed in B2 (20 mM Hepes pH 7.5, 1% NP-40, 400 mM NaCl, 10 mM KCl, 1 mM MgCl2, 20% glycerol, 0.5 mM EDTA and 0.1 mM EGTA supplemented with protease and phosphatase inhibitors) for 15 min at 4°C. The lysates were subsequently separated by SDS-PAGE and analyzed by western blotting and ECL detection (Perkin Elmer Life Sciences). Immunoblots were revealed with anti-A20, anti-IκBα, anti-p65, and anti-histon H1 (Santa Cruz), anti-IRF3 (Invitrogen), anti-phospho-IRF3 and anti-phospho-IκBα (Cell Signaling) and anti-actin (MP Biomedicals). The density of the bands was quantified (fold induction) with the ImageJ (http://rsbweb.nih.gov/ij) Gel analyzer tool. All intensities were calculated relative to the first lane ( = time 0)."}

PMC:3291650 / 37520-38829 JSONTXT

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PMC:3291650 / 37520-38829 JSON TXT