PMC:2674207 / 15127-16052 JSON TXT

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2_test

{"project":"2_test","denotations":[{"id":"19436703-11395507-86274489","span":{"begin":140,"end":142},"obj":"11395507"},{"id":"T8362","span":{"begin":140,"end":142},"obj":"11395507"}],"text":"Cell Fractionation, Immunoprecipitation, and Western Blot Analysis\nNuclear and cytoplasmic fractions were prepared as previously described [35]. Whole cell lysates were prepared in NP-40 lysis buffer (0.5% Nonidet P-40, 20 mM Tris-HCl [pH 7.5], 150 mM NaCl) in the presence of complete protease cocktail inhibitor. Lysates were centrifuged at 4°C for 10 min at 12,000 rpm in an Eppendorf microcentrifuge to remove cellular debris. Samples were then immunoprecipitated with either 10 µl of antibody against GATA-3 or importin-α using A/G agarose slurry in the presence of protease inhibitor using the Catch and Release methodology (Upstate Biotechnology, Lake Placid, New York, USA). Western blot analysis was performed using anti-GATA-3, anti-importin-α, anti-GR, anti-p-p38 MAP kinase, anti-p-ATF-2, and anti-p-serine. Immunoreactive proteins were detected using an enhanced chemiluminescence ECL kit (Amersham Biosciences)."}

pmc-enju-pas

bionlp-st-ge-2016-spacy-parsed

GO-BP

{"project":"GO-BP","denotations":[{"id":"T5179","span":{"begin":187,"end":192},"obj":"http://purl.obolibrary.org/obo/GO_0019835"},{"id":"T5180","span":{"begin":414,"end":422},"obj":"http://purl.obolibrary.org/obo/GO_0007349"}],"text":"Cell Fractionation, Immunoprecipitation, and Western Blot Analysis\nNuclear and cytoplasmic fractions were prepared as previously described [35]. Whole cell lysates were prepared in NP-40 lysis buffer (0.5% Nonidet P-40, 20 mM Tris-HCl [pH 7.5], 150 mM NaCl) in the presence of complete protease cocktail inhibitor. Lysates were centrifuged at 4°C for 10 min at 12,000 rpm in an Eppendorf microcentrifuge to remove cellular debris. Samples were then immunoprecipitated with either 10 µl of antibody against GATA-3 or importin-α using A/G agarose slurry in the presence of protease inhibitor using the Catch and Release methodology (Upstate Biotechnology, Lake Placid, New York, USA). Western blot analysis was performed using anti-GATA-3, anti-importin-α, anti-GR, anti-p-p38 MAP kinase, anti-p-ATF-2, and anti-p-serine. Immunoreactive proteins were detected using an enhanced chemiluminescence ECL kit (Amersham Biosciences)."}

GO-MF

{"project":"GO-MF","denotations":[{"id":"T5181","span":{"begin":489,"end":497},"obj":"http://purl.obolibrary.org/obo/GO_0003823"}],"text":"Cell Fractionation, Immunoprecipitation, and Western Blot Analysis\nNuclear and cytoplasmic fractions were prepared as previously described [35]. Whole cell lysates were prepared in NP-40 lysis buffer (0.5% Nonidet P-40, 20 mM Tris-HCl [pH 7.5], 150 mM NaCl) in the presence of complete protease cocktail inhibitor. Lysates were centrifuged at 4°C for 10 min at 12,000 rpm in an Eppendorf microcentrifuge to remove cellular debris. Samples were then immunoprecipitated with either 10 µl of antibody against GATA-3 or importin-α using A/G agarose slurry in the presence of protease inhibitor using the Catch and Release methodology (Upstate Biotechnology, Lake Placid, New York, USA). Western blot analysis was performed using anti-GATA-3, anti-importin-α, anti-GR, anti-p-p38 MAP kinase, anti-p-ATF-2, and anti-p-serine. Immunoreactive proteins were detected using an enhanced chemiluminescence ECL kit (Amersham Biosciences)."}

GO-CC

{"project":"GO-CC","denotations":[{"id":"T5182","span":{"begin":0,"end":4},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T5183","span":{"begin":151,"end":155},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T5184","span":{"begin":489,"end":497},"obj":"http://purl.obolibrary.org/obo/GO_0019815"},{"id":"T5185","span":{"begin":489,"end":497},"obj":"http://purl.obolibrary.org/obo/GO_0042571"}],"text":"Cell Fractionation, Immunoprecipitation, and Western Blot Analysis\nNuclear and cytoplasmic fractions were prepared as previously described [35]. Whole cell lysates were prepared in NP-40 lysis buffer (0.5% Nonidet P-40, 20 mM Tris-HCl [pH 7.5], 150 mM NaCl) in the presence of complete protease cocktail inhibitor. Lysates were centrifuged at 4°C for 10 min at 12,000 rpm in an Eppendorf microcentrifuge to remove cellular debris. Samples were then immunoprecipitated with either 10 µl of antibody against GATA-3 or importin-α using A/G agarose slurry in the presence of protease inhibitor using the Catch and Release methodology (Upstate Biotechnology, Lake Placid, New York, USA). Western blot analysis was performed using anti-GATA-3, anti-importin-α, anti-GR, anti-p-p38 MAP kinase, anti-p-ATF-2, and anti-p-serine. Immunoreactive proteins were detected using an enhanced chemiluminescence ECL kit (Amersham Biosciences)."}

sentences

{"project":"sentences","denotations":[{"id":"T4846","span":{"begin":0,"end":66},"obj":"Sentence"},{"id":"T4847","span":{"begin":67,"end":144},"obj":"Sentence"},{"id":"T4848","span":{"begin":145,"end":314},"obj":"Sentence"},{"id":"T4849","span":{"begin":315,"end":430},"obj":"Sentence"},{"id":"T4850","span":{"begin":431,"end":682},"obj":"Sentence"},{"id":"T4851","span":{"begin":683,"end":819},"obj":"Sentence"},{"id":"T4852","span":{"begin":820,"end":925},"obj":"Sentence"},{"id":"T102","span":{"begin":0,"end":66},"obj":"Sentence"},{"id":"T103","span":{"begin":67,"end":144},"obj":"Sentence"},{"id":"T104","span":{"begin":145,"end":314},"obj":"Sentence"},{"id":"T105","span":{"begin":315,"end":430},"obj":"Sentence"},{"id":"T106","span":{"begin":431,"end":682},"obj":"Sentence"},{"id":"T107","span":{"begin":683,"end":819},"obj":"Sentence"},{"id":"T108","span":{"begin":820,"end":925},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Cell Fractionation, Immunoprecipitation, and Western Blot Analysis\nNuclear and cytoplasmic fractions were prepared as previously described [35]. Whole cell lysates were prepared in NP-40 lysis buffer (0.5% Nonidet P-40, 20 mM Tris-HCl [pH 7.5], 150 mM NaCl) in the presence of complete protease cocktail inhibitor. Lysates were centrifuged at 4°C for 10 min at 12,000 rpm in an Eppendorf microcentrifuge to remove cellular debris. Samples were then immunoprecipitated with either 10 µl of antibody against GATA-3 or importin-α using A/G agarose slurry in the presence of protease inhibitor using the Catch and Release methodology (Upstate Biotechnology, Lake Placid, New York, USA). Western blot analysis was performed using anti-GATA-3, anti-importin-α, anti-GR, anti-p-p38 MAP kinase, anti-p-ATF-2, and anti-p-serine. Immunoreactive proteins were detected using an enhanced chemiluminescence ECL kit (Amersham Biosciences)."}

events-check-again

{"project":"events-check-again","denotations":[{"id":"T5188","span":{"begin":506,"end":512},"obj":"Protein"}],"text":"Cell Fractionation, Immunoprecipitation, and Western Blot Analysis\nNuclear and cytoplasmic fractions were prepared as previously described [35]. Whole cell lysates were prepared in NP-40 lysis buffer (0.5% Nonidet P-40, 20 mM Tris-HCl [pH 7.5], 150 mM NaCl) in the presence of complete protease cocktail inhibitor. Lysates were centrifuged at 4°C for 10 min at 12,000 rpm in an Eppendorf microcentrifuge to remove cellular debris. Samples were then immunoprecipitated with either 10 µl of antibody against GATA-3 or importin-α using A/G agarose slurry in the presence of protease inhibitor using the Catch and Release methodology (Upstate Biotechnology, Lake Placid, New York, USA). Western blot analysis was performed using anti-GATA-3, anti-importin-α, anti-GR, anti-p-p38 MAP kinase, anti-p-ATF-2, and anti-p-serine. Immunoreactive proteins were detected using an enhanced chemiluminescence ECL kit (Amersham Biosciences)."}

bionlp-st-ge-2016-reference-tees

{"project":"bionlp-st-ge-2016-reference-tees","denotations":[{"id":"T5189","span":{"begin":277,"end":294},"obj":"Protein"},{"id":"T5190","span":{"begin":304,"end":313},"obj":"Negative_regulation"},{"id":"T5191","span":{"begin":506,"end":512},"obj":"Protein"},{"id":"T5192","span":{"begin":516,"end":526},"obj":"Protein"},{"id":"T5193","span":{"begin":725,"end":736},"obj":"Protein"},{"id":"T5194","span":{"begin":738,"end":753},"obj":"Protein"},{"id":"T5195","span":{"begin":755,"end":762},"obj":"Protein"},{"id":"T5196","span":{"begin":764,"end":774},"obj":"Protein"},{"id":"T5197","span":{"begin":775,"end":785},"obj":"Protein"},{"id":"T5198","span":{"begin":719,"end":724},"obj":"Positive_regulation"}],"relations":[{"id":"R4481","pred":"themeOf","subj":"T5189","obj":"T5190"},{"id":"R4482","pred":"themeOf","subj":"T5196","obj":"T5198"}],"text":"Cell Fractionation, Immunoprecipitation, and Western Blot Analysis\nNuclear and cytoplasmic fractions were prepared as previously described [35]. Whole cell lysates were prepared in NP-40 lysis buffer (0.5% Nonidet P-40, 20 mM Tris-HCl [pH 7.5], 150 mM NaCl) in the presence of complete protease cocktail inhibitor. Lysates were centrifuged at 4°C for 10 min at 12,000 rpm in an Eppendorf microcentrifuge to remove cellular debris. Samples were then immunoprecipitated with either 10 µl of antibody against GATA-3 or importin-α using A/G agarose slurry in the presence of protease inhibitor using the Catch and Release methodology (Upstate Biotechnology, Lake Placid, New York, USA). Western blot analysis was performed using anti-GATA-3, anti-importin-α, anti-GR, anti-p-p38 MAP kinase, anti-p-ATF-2, and anti-p-serine. Immunoreactive proteins were detected using an enhanced chemiluminescence ECL kit (Amersham Biosciences)."}

bionlp-st-ge-2016-reference

{"project":"bionlp-st-ge-2016-reference","denotations":[{"id":"T4845","span":{"begin":506,"end":512},"obj":"Protein"}],"namespaces":[{"prefix":"_base","uri":"http://bionlp.dbcls.jp/ontology/ge.owl#"}],"text":"Cell Fractionation, Immunoprecipitation, and Western Blot Analysis\nNuclear and cytoplasmic fractions were prepared as previously described [35]. Whole cell lysates were prepared in NP-40 lysis buffer (0.5% Nonidet P-40, 20 mM Tris-HCl [pH 7.5], 150 mM NaCl) in the presence of complete protease cocktail inhibitor. Lysates were centrifuged at 4°C for 10 min at 12,000 rpm in an Eppendorf microcentrifuge to remove cellular debris. Samples were then immunoprecipitated with either 10 µl of antibody against GATA-3 or importin-α using A/G agarose slurry in the presence of protease inhibitor using the Catch and Release methodology (Upstate Biotechnology, Lake Placid, New York, USA). Western blot analysis was performed using anti-GATA-3, anti-importin-α, anti-GR, anti-p-p38 MAP kinase, anti-p-ATF-2, and anti-p-serine. Immunoreactive proteins were detected using an enhanced chemiluminescence ECL kit (Amersham Biosciences)."}

bionlp-st-ge-2016-uniprot

{"project":"bionlp-st-ge-2016-uniprot","denotations":[{"id":"T5004","span":{"begin":236,"end":238},"obj":"P0A7Z4"},{"id":"T5005","span":{"begin":506,"end":512},"obj":"P23771"},{"id":"T5006","span":{"begin":730,"end":736},"obj":"P23771"},{"id":"T5007","span":{"begin":760,"end":762},"obj":"P04150"},{"id":"T5008","span":{"begin":771,"end":774},"obj":"Q16539"},{"id":"T5009","span":{"begin":771,"end":774},"obj":"Q15759"},{"id":"T5010","span":{"begin":771,"end":774},"obj":"P53778"},{"id":"T5011","span":{"begin":771,"end":774},"obj":"O15264"},{"id":"T5012","span":{"begin":794,"end":799},"obj":"P15336"}],"namespaces":[{"prefix":"_base","uri":"http://www.uniprot.org/uniprot/"}],"text":"Cell Fractionation, Immunoprecipitation, and Western Blot Analysis\nNuclear and cytoplasmic fractions were prepared as previously described [35]. Whole cell lysates were prepared in NP-40 lysis buffer (0.5% Nonidet P-40, 20 mM Tris-HCl [pH 7.5], 150 mM NaCl) in the presence of complete protease cocktail inhibitor. Lysates were centrifuged at 4°C for 10 min at 12,000 rpm in an Eppendorf microcentrifuge to remove cellular debris. Samples were then immunoprecipitated with either 10 µl of antibody against GATA-3 or importin-α using A/G agarose slurry in the presence of protease inhibitor using the Catch and Release methodology (Upstate Biotechnology, Lake Placid, New York, USA). Western blot analysis was performed using anti-GATA-3, anti-importin-α, anti-GR, anti-p-p38 MAP kinase, anti-p-ATF-2, and anti-p-serine. Immunoreactive proteins were detected using an enhanced chemiluminescence ECL kit (Amersham Biosciences)."}

test2

{"project":"test2","denotations":[{"id":"T4844","span":{"begin":506,"end":512},"obj":"Protein"}],"text":"Cell Fractionation, Immunoprecipitation, and Western Blot Analysis\nNuclear and cytoplasmic fractions were prepared as previously described [35]. Whole cell lysates were prepared in NP-40 lysis buffer (0.5% Nonidet P-40, 20 mM Tris-HCl [pH 7.5], 150 mM NaCl) in the presence of complete protease cocktail inhibitor. Lysates were centrifuged at 4°C for 10 min at 12,000 rpm in an Eppendorf microcentrifuge to remove cellular debris. Samples were then immunoprecipitated with either 10 µl of antibody against GATA-3 or importin-α using A/G agarose slurry in the presence of protease inhibitor using the Catch and Release methodology (Upstate Biotechnology, Lake Placid, New York, USA). Western blot analysis was performed using anti-GATA-3, anti-importin-α, anti-GR, anti-p-p38 MAP kinase, anti-p-ATF-2, and anti-p-serine. Immunoreactive proteins were detected using an enhanced chemiluminescence ECL kit (Amersham Biosciences)."}

PMC:2674207 / 15127-16052 JSONTXT

Annnotations TAB JSON ListView MergeView

PMC:2674207 / 15127-16052 JSON TXT