PMC:3333881 / 1664-2005 JSONTXT

Annnotations TAB JSON ListView MergeView

    2_test

    {"project":"2_test","denotations":[{"id":"22187158-19302050-77584394","span":{"begin":224,"end":225},"obj":"19302050"},{"id":"22187158-12360211-77584395","span":{"begin":326,"end":327},"obj":"12360211"}],"text":"tero-dimerization and DNA-binding. The transcriptional activity of the NF-κB complex depends on dimer composition since C-terminal unrelated transcriptional activation domains are present exclusively in p65, RelB and c-Rel (2).\nInhibitors of NF-κB (IκB) associate with the NF-κB complex and interfere with its binding to DNA (3). In the cano"}

    pmc-enju-pas

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and DNA-binding. The transcriptional activity of the NF-κB complex depends on dimer composition since C-terminal unrelated transcriptional activation domains are present exclusively in p65, RelB and c-Rel (2).\nInhibitors of NF-κB (IκB) associate with the NF-κB complex and interfere with its binding to DNA (3). In the cano"}

    bionlp-st-ge-2016-spacy-parsed

    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and DNA-binding. The transcriptional activity of the NF-κB complex depends on dimer composition since C-terminal unrelated transcriptional activation domains are present exclusively in p65, RelB and c-Rel (2).\nInhibitors of NF-κB (IκB) associate with the NF-κB complex and interfere with its binding to DNA (3). In the cano"}

    GO-MF

    {"project":"GO-MF","denotations":[{"id":"T3224","span":{"begin":22,"end":33},"obj":"http://purl.obolibrary.org/obo/GO_0003677"},{"id":"T3225","span":{"begin":310,"end":324},"obj":"http://purl.obolibrary.org/obo/GO_0003677"},{"id":"T3228","span":{"begin":26,"end":33},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T3229","span":{"begin":310,"end":317},"obj":"http://purl.obolibrary.org/obo/GO_0005488"}],"text":"tero-dimerization and DNA-binding. The transcriptional activity of the NF-κB complex depends on dimer composition since C-terminal unrelated transcriptional activation domains are present exclusively in p65, RelB and c-Rel (2).\nInhibitors of NF-κB (IκB) associate with the NF-κB complex and interfere with its binding to DNA (3). In the cano"}

    GO-CC

    {"project":"GO-CC","denotations":[{"id":"T3205","span":{"begin":71,"end":84},"obj":"http://purl.obolibrary.org/obo/GO_0071159"},{"id":"T3206","span":{"begin":273,"end":286},"obj":"http://purl.obolibrary.org/obo/GO_0071159"}],"text":"tero-dimerization and DNA-binding. The transcriptional activity of the NF-κB complex depends on dimer composition since C-terminal unrelated transcriptional activation domains are present exclusively in p65, RelB and c-Rel (2).\nInhibitors of NF-κB (IκB) associate with the NF-κB complex and interfere with its binding to DNA (3). In the cano"}

    sentences

    {"project":"sentences","denotations":[{"id":"T1431","span":{"begin":35,"end":227},"obj":"Sentence"},{"id":"T1432","span":{"begin":228,"end":329},"obj":"Sentence"},{"id":"T13","span":{"begin":35,"end":227},"obj":"Sentence"},{"id":"T14","span":{"begin":228,"end":329},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"tero-dimerization and DNA-binding. The transcriptional activity of the NF-κB complex depends on dimer composition since C-terminal unrelated transcriptional activation domains are present exclusively in p65, RelB and c-Rel (2).\nInhibitors of NF-κB (IκB) associate with the NF-κB complex and interfere with its binding to DNA (3). In the cano"}

    events-check-again

    {"project":"events-check-again","denotations":[{"id":"T4055","span":{"begin":5,"end":17},"obj":"Binding"},{"id":"T4056","span":{"begin":5,"end":17},"obj":"Binding"},{"id":"T4057","span":{"begin":5,"end":17},"obj":"Binding"},{"id":"T4058","span":{"begin":5,"end":17},"obj":"Binding"},{"id":"T4059","span":{"begin":5,"end":17},"obj":"Binding"},{"id":"T4060","span":{"begin":26,"end":33},"obj":"Binding"},{"id":"T4061","span":{"begin":26,"end":33},"obj":"Binding"},{"id":"T4062","span":{"begin":26,"end":33},"obj":"Binding"},{"id":"T4063","span":{"begin":26,"end":33},"obj":"Binding"},{"id":"T4064","span":{"begin":26,"end":33},"obj":"Binding"},{"id":"T4065","span":{"begin":203,"end":206},"obj":"Protein"},{"id":"T4066","span":{"begin":208,"end":212},"obj":"Protein"},{"id":"T4067","span":{"begin":217,"end":222},"obj":"Protein"}],"text":"tero-dimerization and DNA-binding. The transcriptional activity of the NF-κB complex depends on dimer composition since C-terminal unrelated transcriptional activation domains are present exclusively in p65, RelB and c-Rel (2).\nInhibitors of NF-κB (IκB) associate with the NF-κB complex and interfere with its binding to DNA (3). In the cano"}

    bionlp-st-ge-2016-reference-tees

    {"project":"bionlp-st-ge-2016-reference-tees","denotations":[{"id":"T4193","span":{"begin":71,"end":84},"obj":"Protein"},{"id":"T4194","span":{"begin":203,"end":206},"obj":"Protein"},{"id":"T4195","span":{"begin":208,"end":212},"obj":"Protein"},{"id":"T4196","span":{"begin":242,"end":247},"obj":"Protein"},{"id":"T4197","span":{"begin":249,"end":252},"obj":"Protein"},{"id":"T4198","span":{"begin":273,"end":278},"obj":"Protein"},{"id":"T4199","span":{"begin":228,"end":238},"obj":"Negative_regulation"},{"id":"T4200","span":{"begin":228,"end":238},"obj":"Negative_regulation"},{"id":"T4201","span":{"begin":254,"end":263},"obj":"Binding"},{"id":"T4202","span":{"begin":310,"end":317},"obj":"Binding"},{"id":"T4203","span":{"begin":310,"end":317},"obj":"Binding"}],"relations":[{"id":"R3781","pred":"themeOf","subj":"T4196","obj":"T4199"},{"id":"R3782","pred":"themeOf","subj":"T4196","obj":"T4201"},{"id":"R3783","pred":"themeOf","subj":"T4196","obj":"T4202"},{"id":"R3784","pred":"themeOf","subj":"T4197","obj":"T4200"},{"id":"R3785","pred":"themeOf","subj":"T4197","obj":"T4203"},{"id":"R3786","pred":"themeOf","subj":"T4198","obj":"T4201"}],"text":"tero-dimerization and DNA-binding. The transcriptional activity of the NF-κB complex depends on dimer composition since C-terminal unrelated transcriptional activation domains are present exclusively in p65, RelB and c-Rel (2).\nInhibitors of NF-κB (IκB) associate with the NF-κB complex and interfere with its binding to DNA (3). In the cano"}

    test2

    {"project":"test2","denotations":[{"id":"T1145","span":{"begin":26,"end":33},"obj":"Binding"},{"id":"T1146","span":{"begin":203,"end":206},"obj":"Protein"},{"id":"T1147","span":{"begin":208,"end":212},"obj":"Protein"},{"id":"T1148","span":{"begin":217,"end":222},"obj":"Protein"},{"id":"T1149","span":{"begin":310,"end":317},"obj":"Binding"}],"text":"tero-dimerization and DNA-binding. The transcriptional activity of the NF-κB complex depends on dimer composition since C-terminal unrelated transcriptional activation domains are present exclusively in p65, RelB and c-Rel (2).\nInhibitors of NF-κB (IκB) associate with the NF-κB complex and interfere with its binding to DNA (3). In the cano"}

    bionlp-st-ge-2016-reference

    {"project":"bionlp-st-ge-2016-reference","denotations":[{"id":"T1300","span":{"begin":5,"end":17},"obj":"Binding"},{"id":"T1301","span":{"begin":5,"end":17},"obj":"Binding"},{"id":"T1302","span":{"begin":5,"end":17},"obj":"Binding"},{"id":"T1303","span":{"begin":5,"end":17},"obj":"Binding"},{"id":"T1304","span":{"begin":5,"end":17},"obj":"Binding"},{"id":"T1305","span":{"begin":26,"end":33},"obj":"Binding"},{"id":"T1306","span":{"begin":26,"end":33},"obj":"Binding"},{"id":"T1307","span":{"begin":26,"end":33},"obj":"Binding"},{"id":"T1308","span":{"begin":26,"end":33},"obj":"Binding"},{"id":"T1309","span":{"begin":26,"end":33},"obj":"Binding"},{"id":"T1310","span":{"begin":203,"end":206},"obj":"Protein"},{"id":"T1311","span":{"begin":208,"end":212},"obj":"Protein"},{"id":"T1312","span":{"begin":217,"end":222},"obj":"Protein"}],"namespaces":[{"prefix":"_base","uri":"http://bionlp.dbcls.jp/ontology/ge.owl#"}],"text":"tero-dimerization and DNA-binding. The transcriptional activity of the NF-κB complex depends on dimer composition since C-terminal unrelated transcriptional activation domains are present exclusively in p65, RelB and c-Rel (2).\nInhibitors of NF-κB (IκB) associate with the NF-κB complex and interfere with its binding to DNA (3). In the cano"}

    bionlp-st-ge-2016-uniprot

    {"project":"bionlp-st-ge-2016-uniprot","denotations":[{"id":"T2254","span":{"begin":203,"end":206},"obj":"Q04206"},{"id":"T2255","span":{"begin":203,"end":206},"obj":"P21579"},{"id":"T2256","span":{"begin":208,"end":212},"obj":"Q01201"},{"id":"T2257","span":{"begin":217,"end":222},"obj":"Q04864"},{"id":"T2258","span":{"begin":219,"end":222},"obj":"Q04864"}],"namespaces":[{"prefix":"_base","uri":"http://www.uniprot.org/uniprot/"}],"text":"tero-dimerization and DNA-binding. The transcriptional activity of the NF-κB complex depends on dimer composition since C-terminal unrelated transcriptional activation domains are present exclusively in p65, RelB and c-Rel (2).\nInhibitors of NF-κB (IκB) associate with the NF-κB complex and interfere with its binding to DNA (3). In the cano"}