PubMed:8108414 JSONTXT

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    jnlpba-st-training

    {"project":"jnlpba-st-training","denotations":[{"id":"T1","span":{"begin":22,"end":47},"obj":"protein"},{"id":"T2","span":{"begin":48,"end":52},"obj":"protein"},{"id":"T3","span":{"begin":54,"end":57},"obj":"protein"},{"id":"T4","span":{"begin":71,"end":93},"obj":"protein"},{"id":"T5","span":{"begin":105,"end":119},"obj":"protein"},{"id":"T6","span":{"begin":121,"end":125},"obj":"protein"},{"id":"T7","span":{"begin":127,"end":130},"obj":"protein"},{"id":"T8","span":{"begin":191,"end":231},"obj":"protein"},{"id":"T9","span":{"begin":247,"end":273},"obj":"protein"},{"id":"T10","span":{"begin":282,"end":303},"obj":"protein"},{"id":"T11","span":{"begin":305,"end":320},"obj":"protein"},{"id":"T12","span":{"begin":349,"end":364},"obj":"protein"},{"id":"T13","span":{"begin":438,"end":448},"obj":"protein"},{"id":"T14","span":{"begin":486,"end":513},"obj":"protein"},{"id":"T15","span":{"begin":537,"end":552},"obj":"protein"},{"id":"T16","span":{"begin":556,"end":569},"obj":"cell_type"},{"id":"T17","span":{"begin":646,"end":661},"obj":"protein"},{"id":"T18","span":{"begin":746,"end":750},"obj":"protein"},{"id":"T19","span":{"begin":794,"end":810},"obj":"protein"},{"id":"T20","span":{"begin":846,"end":861},"obj":"protein"},{"id":"T21","span":{"begin":882,"end":909},"obj":"protein"},{"id":"T22","span":{"begin":940,"end":987},"obj":"DNA"},{"id":"T23","span":{"begin":1009,"end":1013},"obj":"protein"},{"id":"T24","span":{"begin":1013,"end":1029},"obj":"protein"},{"id":"T25","span":{"begin":1031,"end":1062},"obj":"protein"},{"id":"T26","span":{"begin":1093,"end":1120},"obj":"protein"},{"id":"T27","span":{"begin":1139,"end":1143},"obj":"protein"},{"id":"T28","span":{"begin":1179,"end":1183},"obj":"protein"},{"id":"T29","span":{"begin":1240,"end":1244},"obj":"protein"},{"id":"T30","span":{"begin":1249,"end":1253},"obj":"protein"},{"id":"T31","span":{"begin":1267,"end":1296},"obj":"protein"},{"id":"T32","span":{"begin":1326,"end":1353},"obj":"protein"},{"id":"T33","span":{"begin":1357,"end":1361},"obj":"protein"},{"id":"T34","span":{"begin":1385,"end":1400},"obj":"protein"},{"id":"T35","span":{"begin":1414,"end":1418},"obj":"protein"},{"id":"T36","span":{"begin":1433,"end":1437},"obj":"protein"},{"id":"T37","span":{"begin":1460,"end":1491},"obj":"protein"},{"id":"T38","span":{"begin":1533,"end":1537},"obj":"protein"},{"id":"T39","span":{"begin":1565,"end":1580},"obj":"protein"},{"id":"T40","span":{"begin":1590,"end":1594},"obj":"protein"},{"id":"T41","span":{"begin":1606,"end":1615},"obj":"RNA"},{"id":"T42","span":{"begin":1787,"end":1805},"obj":"protein"}],"text":"Autoregulation of the NF-kappa B transactivator RelA (p65) by multiple cytoplasmic inhibitors containing ankyrin motifs.\nRelA (p65) functions as the critical transactivating component of the heterodimeric p50-p65 NF-kappa B complex and contains a high-affinity binding site for its cytoplasmic inhibitor, I kappa B alpha. After cellular activation, I kappa B alpha is rapidly degraded in concert with the induced nuclear translocation of NF-kappa B. The present study demonstrates that tumor necrosis factor alpha-induced degradation of I kappa B alpha in human T cells is preceded by its rapid phosphorylation in vivo. However, these effects on I kappa B alpha result in nuclear mobilization of only a fraction of the entire cytoplasmic pool of RelA. Subsequent studies have revealed that (i) cytoplasmic RelA is stably associated not only with I kappa B alpha but also with other ankyrin motif-rich proteins including the products of the NF-kappa B2 (p100) and NF-kappa B1 (p105) genes; (ii) in contrast to RelA-I kappa B alpha, RelA-p100 cytoplasmic complexes are not dissociated following tumor necrosis factor alpha activation; (iii) p100 functions as a potent inhibitor of RelA-mediated transcription in vivo; (iv) the interaction of RelA and p100 involves the conserved Rel homology domain of both proteins but not the nuclear localization signal of RelA, which is required for I kappa B alpha binding; (v) p100 inhibition of RelA function requires the C-terminal ankyrin motif domain, which mediates cytoplasmic retention of RelA; and (vi) as observed with I kappa B alpha, nuclear RelA stimulates p100 mRNA and protein expression. These findings thus reveal the presence of a second inducible autoregulated inhibitory pathway that helps ensure the rapid but transient action of nuclear NF-kappa B."}

    pubmed-sentences-benchmark

    {"project":"pubmed-sentences-benchmark","denotations":[{"id":"S1","span":{"begin":0,"end":120},"obj":"Sentence"},{"id":"S2","span":{"begin":121,"end":321},"obj":"Sentence"},{"id":"S3","span":{"begin":322,"end":449},"obj":"Sentence"},{"id":"S4","span":{"begin":450,"end":619},"obj":"Sentence"},{"id":"S5","span":{"begin":620,"end":751},"obj":"Sentence"},{"id":"S6","span":{"begin":752,"end":1639},"obj":"Sentence"},{"id":"S7","span":{"begin":1640,"end":1806},"obj":"Sentence"}],"text":"Autoregulation of the NF-kappa B transactivator RelA (p65) by multiple cytoplasmic inhibitors containing ankyrin motifs.\nRelA (p65) functions as the critical transactivating component of the heterodimeric p50-p65 NF-kappa B complex and contains a high-affinity binding site for its cytoplasmic inhibitor, I kappa B alpha. After cellular activation, I kappa B alpha is rapidly degraded in concert with the induced nuclear translocation of NF-kappa B. The present study demonstrates that tumor necrosis factor alpha-induced degradation of I kappa B alpha in human T cells is preceded by its rapid phosphorylation in vivo. However, these effects on I kappa B alpha result in nuclear mobilization of only a fraction of the entire cytoplasmic pool of RelA. Subsequent studies have revealed that (i) cytoplasmic RelA is stably associated not only with I kappa B alpha but also with other ankyrin motif-rich proteins including the products of the NF-kappa B2 (p100) and NF-kappa B1 (p105) genes; (ii) in contrast to RelA-I kappa B alpha, RelA-p100 cytoplasmic complexes are not dissociated following tumor necrosis factor alpha activation; (iii) p100 functions as a potent inhibitor of RelA-mediated transcription in vivo; (iv) the interaction of RelA and p100 involves the conserved Rel homology domain of both proteins but not the nuclear localization signal of RelA, which is required for I kappa B alpha binding; (v) p100 inhibition of RelA function requires the C-terminal ankyrin motif domain, which mediates cytoplasmic retention of RelA; and (vi) as observed with I kappa B alpha, nuclear RelA stimulates p100 mRNA and protein expression. These findings thus reveal the presence of a second inducible autoregulated inhibitory pathway that helps ensure the rapid but transient action of nuclear NF-kappa B."}

    genia-medco-coref

    {"project":"genia-medco-coref","denotations":[{"id":"C1","span":{"begin":18,"end":58},"obj":"NP"},{"id":"C2","span":{"begin":121,"end":131},"obj":"NP"},{"id":"C3","span":{"begin":187,"end":231},"obj":"NP"},{"id":"C5","span":{"begin":278,"end":281},"obj":"NP"},{"id":"C4","span":{"begin":278,"end":303},"obj":"NP"},{"id":"C6","span":{"begin":305,"end":320},"obj":"NP"},{"id":"C7","span":{"begin":349,"end":364},"obj":"NP"},{"id":"C8","span":{"begin":537,"end":569},"obj":"NP"},{"id":"C9","span":{"begin":585,"end":588},"obj":"NP"},{"id":"C10","span":{"begin":646,"end":661},"obj":"NP"},{"id":"C11","span":{"begin":746,"end":750},"obj":"NP"},{"id":"C12","span":{"begin":846,"end":861},"obj":"NP"},{"id":"C13","span":{"begin":936,"end":958},"obj":"NP"},{"id":"C14","span":{"begin":1009,"end":1014},"obj":"NP"},{"id":"C15","span":{"begin":1031,"end":1036},"obj":"NP"},{"id":"C16","span":{"begin":1139,"end":1143},"obj":"NP"},{"id":"C17","span":{"begin":1179,"end":1184},"obj":"NP"},{"id":"C18","span":{"begin":1240,"end":1244},"obj":"NP"},{"id":"C19","span":{"begin":1249,"end":1253},"obj":"NP"},{"id":"C20","span":{"begin":1357,"end":1361},"obj":"NP"},{"id":"C21","span":{"begin":1363,"end":1368},"obj":"NP"},{"id":"C22","span":{"begin":1433,"end":1437},"obj":"NP"},{"id":"C23","span":{"begin":1456,"end":1491},"obj":"NP"},{"id":"C24","span":{"begin":1493,"end":1498},"obj":"NP"},{"id":"C25","span":{"begin":1533,"end":1538},"obj":"NP"},{"id":"C26","span":{"begin":1565,"end":1580},"obj":"NP"},{"id":"C27","span":{"begin":1683,"end":1734},"obj":"NP"},{"id":"C28","span":{"begin":1735,"end":1739},"obj":"NP"}],"relations":[{"id":"R1","pred":"coref-ident","subj":"C2","obj":"C1"},{"id":"R2","pred":"coref-pron","subj":"C4","obj":"C3"},{"id":"R3","pred":"coref-ident","subj":"C7","obj":"C6"},{"id":"R4","pred":"coref-ident","subj":"C8","obj":"C7"},{"id":"R5","pred":"coref-pron","subj":"C9","obj":"C8"},{"id":"R6","pred":"coref-ident","subj":"C10","obj":"C8"},{"id":"R7","pred":"coref-other","subj":"C11","obj":"C2"},{"id":"R8","pred":"coref-ident","subj":"C12","obj":"C10"},{"id":"R9","pred":"coref-ident","subj":"C14","obj":"C11"},{"id":"R10","pred":"coref-ident","subj":"C15","obj":"C14"},{"id":"R11","pred":"coref-ident","subj":"C16","obj":"C13"},{"id":"R12","pred":"coref-ident","subj":"C17","obj":"C15"},{"id":"R13","pred":"coref-ident","subj":"C18","obj":"C17"},{"id":"R14","pred":"coref-ident","subj":"C19","obj":"C16"},{"id":"R15","pred":"coref-ident","subj":"C20","obj":"C18"},{"id":"R16","pred":"coref-relat","subj":"C21","obj":"C20"},{"id":"R17","pred":"coref-ident","subj":"C22","obj":"C20"},{"id":"R18","pred":"coref-relat","subj":"C24","obj":"C23"},{"id":"R19","pred":"coref-ident","subj":"C25","obj":"C22"},{"id":"R20","pred":"coref-ident","subj":"C26","obj":"C12"},{"id":"R21","pred":"coref-relat","subj":"C28","obj":"C27"}],"text":"Autoregulation of the NF-kappa B transactivator RelA (p65) by multiple cytoplasmic inhibitors containing ankyrin motifs.\nRelA (p65) functions as the critical transactivating component of the heterodimeric p50-p65 NF-kappa B complex and contains a high-affinity binding site for its cytoplasmic inhibitor, I kappa B alpha. After cellular activation, I kappa B alpha is rapidly degraded in concert with the induced nuclear translocation of NF-kappa B. The present study demonstrates that tumor necrosis factor alpha-induced degradation of I kappa B alpha in human T cells is preceded by its rapid phosphorylation in vivo. However, these effects on I kappa B alpha result in nuclear mobilization of only a fraction of the entire cytoplasmic pool of RelA. Subsequent studies have revealed that (i) cytoplasmic RelA is stably associated not only with I kappa B alpha but also with other ankyrin motif-rich proteins including the products of the NF-kappa B2 (p100) and NF-kappa B1 (p105) genes; (ii) in contrast to RelA-I kappa B alpha, RelA-p100 cytoplasmic complexes are not dissociated following tumor necrosis factor alpha activation; (iii) p100 functions as a potent inhibitor of RelA-mediated transcription in vivo; (iv) the interaction of RelA and p100 involves the conserved Rel homology domain of both proteins but not the nuclear localization signal of RelA, which is required for I kappa B alpha binding; (v) p100 inhibition of RelA function requires the C-terminal ankyrin motif domain, which mediates cytoplasmic retention of RelA; and (vi) as observed with I kappa B alpha, nuclear RelA stimulates p100 mRNA and protein expression. These findings thus reveal the presence of a second inducible autoregulated inhibitory pathway that helps ensure the rapid but transient action of nuclear NF-kappa B."}

    GENIAcorpus

    {"project":"GENIAcorpus","denotations":[{"id":"T1","span":{"begin":22,"end":32},"obj":"protein_complex"},{"id":"T2","span":{"begin":48,"end":52},"obj":"protein_subunit"},{"id":"T3","span":{"begin":54,"end":57},"obj":"protein_subunit"},{"id":"T4","span":{"begin":71,"end":93},"obj":"protein_family_or_group"},{"id":"T5","span":{"begin":121,"end":125},"obj":"protein_subunit"},{"id":"T6","span":{"begin":127,"end":130},"obj":"protein_subunit"},{"id":"T7","span":{"begin":191,"end":209},"obj":"protein_complex"},{"id":"T8","span":{"begin":209,"end":212},"obj":"protein_subunit"},{"id":"T9","span":{"begin":213,"end":223},"obj":"protein_complex"},{"id":"T10","span":{"begin":247,"end":273},"obj":"protein_domain_or_region"},{"id":"T11","span":{"begin":282,"end":303},"obj":"protein_family_or_group"},{"id":"T12","span":{"begin":305,"end":320},"obj":"protein_molecule"},{"id":"T13","span":{"begin":349,"end":364},"obj":"protein_molecule"},{"id":"T14","span":{"begin":438,"end":448},"obj":"protein_complex"},{"id":"T15","span":{"begin":486,"end":513},"obj":"protein_molecule"},{"id":"T16","span":{"begin":537,"end":552},"obj":"protein_molecule"},{"id":"T17","span":{"begin":556,"end":569},"obj":"cell_type"},{"id":"T18","span":{"begin":646,"end":661},"obj":"protein_molecule"},{"id":"T19","span":{"begin":726,"end":742},"obj":"other_name"},{"id":"T20","span":{"begin":746,"end":750},"obj":"protein_subunit"},{"id":"T21","span":{"begin":794,"end":805},"obj":"protein_subunit"},{"id":"T22","span":{"begin":806,"end":810},"obj":"protein_subunit"},{"id":"T23","span":{"begin":846,"end":861},"obj":"protein_molecule"},{"id":"T24","span":{"begin":882,"end":909},"obj":"protein_family_or_group"},{"id":"T25","span":{"begin":1009,"end":1013},"obj":"protein_subunit"},{"id":"T26","span":{"begin":1013,"end":1029},"obj":"protein_molecule"},{"id":"T27","span":{"begin":1031,"end":1035},"obj":"protein_subunit"},{"id":"T28","span":{"begin":1093,"end":1120},"obj":"protein_molecule"},{"id":"T29","span":{"begin":1139,"end":1143},"obj":"protein_molecule"},{"id":"T30","span":{"begin":1179,"end":1183},"obj":"protein_subunit"},{"id":"T31","span":{"begin":1240,"end":1244},"obj":"protein_subunit"},{"id":"T32","span":{"begin":1249,"end":1253},"obj":"protein_molecule"},{"id":"T33","span":{"begin":1267,"end":1296},"obj":"protein_domain_or_region"},{"id":"T34","span":{"begin":1326,"end":1353},"obj":"protein_domain_or_region"},{"id":"T35","span":{"begin":1357,"end":1361},"obj":"protein_subunit"},{"id":"T36","span":{"begin":1385,"end":1400},"obj":"protein_molecule"},{"id":"T37","span":{"begin":1414,"end":1418},"obj":"protein_molecule"},{"id":"T38","span":{"begin":1433,"end":1437},"obj":"protein_subunit"},{"id":"T39","span":{"begin":1460,"end":1491},"obj":"protein_domain_or_region"},{"id":"T40","span":{"begin":1533,"end":1537},"obj":"protein_subunit"},{"id":"T41","span":{"begin":1565,"end":1580},"obj":"protein_molecule"},{"id":"T42","span":{"begin":1590,"end":1594},"obj":"protein_subunit"},{"id":"T43","span":{"begin":1606,"end":1610},"obj":"protein_molecule"},{"id":"T44","span":{"begin":1620,"end":1638},"obj":"other_name"},{"id":"T45","span":{"begin":1692,"end":1734},"obj":"other_name"},{"id":"T46","span":{"begin":1787,"end":1794},"obj":"protein_complex"},{"id":"T47","span":{"begin":1795,"end":1805},"obj":"protein_complex"}],"text":"Autoregulation of the NF-kappa B transactivator RelA (p65) by multiple cytoplasmic inhibitors containing ankyrin motifs.\nRelA (p65) functions as the critical transactivating component of the heterodimeric p50-p65 NF-kappa B complex and contains a high-affinity binding site for its cytoplasmic inhibitor, I kappa B alpha. After cellular activation, I kappa B alpha is rapidly degraded in concert with the induced nuclear translocation of NF-kappa B. The present study demonstrates that tumor necrosis factor alpha-induced degradation of I kappa B alpha in human T cells is preceded by its rapid phosphorylation in vivo. However, these effects on I kappa B alpha result in nuclear mobilization of only a fraction of the entire cytoplasmic pool of RelA. Subsequent studies have revealed that (i) cytoplasmic RelA is stably associated not only with I kappa B alpha but also with other ankyrin motif-rich proteins including the products of the NF-kappa B2 (p100) and NF-kappa B1 (p105) genes; (ii) in contrast to RelA-I kappa B alpha, RelA-p100 cytoplasmic complexes are not dissociated following tumor necrosis factor alpha activation; (iii) p100 functions as a potent inhibitor of RelA-mediated transcription in vivo; (iv) the interaction of RelA and p100 involves the conserved Rel homology domain of both proteins but not the nuclear localization signal of RelA, which is required for I kappa B alpha binding; (v) p100 inhibition of RelA function requires the C-terminal ankyrin motif domain, which mediates cytoplasmic retention of RelA; and (vi) as observed with I kappa B alpha, nuclear RelA stimulates p100 mRNA and protein expression. These findings thus reveal the presence of a second inducible autoregulated inhibitory pathway that helps ensure the rapid but transient action of nuclear NF-kappa B."}