PubMed:1372388 JSON TXT

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jnlpba-st-training

{"project":"jnlpba-st-training","denotations":[{"id":"T1","span":{"begin":2,"end":39},"obj":"protein"},{"id":"T2","span":{"begin":51,"end":70},"obj":"protein"},{"id":"T3","span":{"begin":101,"end":137},"obj":"DNA"},{"id":"T4","span":{"begin":172,"end":186},"obj":"cell_type"},{"id":"T5","span":{"begin":192,"end":215},"obj":"protein"},{"id":"T6","span":{"begin":235,"end":285},"obj":"protein"},{"id":"T7","span":{"begin":306,"end":309},"obj":"protein"},{"id":"T8","span":{"begin":314,"end":326},"obj":"protein"},{"id":"T9","span":{"begin":330,"end":352},"obj":"protein"},{"id":"T10","span":{"begin":372,"end":377},"obj":"protein"},{"id":"T11","span":{"begin":387,"end":400},"obj":"DNA"},{"id":"T12","span":{"begin":404,"end":414},"obj":"protein"},{"id":"T13","span":{"begin":426,"end":438},"obj":"protein"},{"id":"T14","span":{"begin":444,"end":447},"obj":"protein"},{"id":"T15","span":{"begin":455,"end":465},"obj":"protein"},{"id":"T16","span":{"begin":470,"end":482},"obj":"protein"},{"id":"T17","span":{"begin":550,"end":564},"obj":"DNA"},{"id":"T18","span":{"begin":585,"end":600},"obj":"protein"},{"id":"T19","span":{"begin":625,"end":638},"obj":"protein"},{"id":"T20","span":{"begin":640,"end":644},"obj":"protein"},{"id":"T21","span":{"begin":650,"end":679},"obj":"DNA"},{"id":"T22","span":{"begin":714,"end":717},"obj":"protein"},{"id":"T23","span":{"begin":748,"end":785},"obj":"protein"},{"id":"T24","span":{"begin":808,"end":813},"obj":"protein"},{"id":"T25","span":{"begin":822,"end":834},"obj":"protein"},{"id":"T26","span":{"begin":856,"end":886},"obj":"protein"},{"id":"T27","span":{"begin":911,"end":926},"obj":"protein"},{"id":"T28","span":{"begin":965,"end":1000},"obj":"DNA"},{"id":"T29","span":{"begin":1049,"end":1067},"obj":"DNA"},{"id":"T30","span":{"begin":1090,"end":1135},"obj":"DNA"},{"id":"T31","span":{"begin":1139,"end":1156},"obj":"cell_type"},{"id":"T32","span":{"begin":1200,"end":1214},"obj":"cell_type"},{"id":"T33","span":{"begin":1225,"end":1243},"obj":"cell_line"},{"id":"T34","span":{"begin":1275,"end":1305},"obj":"protein"},{"id":"T35","span":{"begin":1344,"end":1379},"obj":"DNA"},{"id":"T36","span":{"begin":1383,"end":1397},"obj":"cell_type"}],"text":"A lymphoid cell-specific nuclear factor containing c-Rel-like proteins preferentially interacts with interleukin-6 kappa B-related motifs whose activities are repressed in lymphoid cells.\nThe proto-oncoprotein c-Rel is a member of the nuclear factor kappa B transcription factor family, which includes the p50 and p65 subunits of nuclear factor kappa B. We show here that c-Rel binds to kappa B sites as homodimers as well as heterodimers with p50. These homodimers and heterodimers show distinct DNA-binding specificities and affinities for various kappa B motifs. In particular, the c-Rel homodimer has a high affinity for interleukin-6 (IL-6) and beta interferon kappa B sites. In spite of its association with p50 in vitro, however, we found a lymphoid cell-specific nuclear factor in vivo that contains c-Rel but not p50 epitopes; this factor, termed IL-6 kappa B binding factor II, appears to contain the c-Rel homodimer and preferentially recognizes several IL-6 kappa B-related kappa B motifs. Although it has been previously shown that the IL-6 kappa B motif functions as a potent IL-1/tumor necrosis factor-responsive element in nonlymphoid cells, its activity was found to be repressed in lymphoid cells such as a Jurkat T-cell line. We also present evidence that IL-6 kappa B binding factor II functions as a repressor specific for IL-6 kappa B-related kappa B motifs in lymphoid cells."}

pubmed-sentences-benchmark

{"project":"pubmed-sentences-benchmark","denotations":[{"id":"S1","span":{"begin":0,"end":187},"obj":"Sentence"},{"id":"S2","span":{"begin":188,"end":353},"obj":"Sentence"},{"id":"S3","span":{"begin":354,"end":448},"obj":"Sentence"},{"id":"S4","span":{"begin":449,"end":565},"obj":"Sentence"},{"id":"S5","span":{"begin":566,"end":680},"obj":"Sentence"},{"id":"S6","span":{"begin":681,"end":1001},"obj":"Sentence"},{"id":"S7","span":{"begin":1002,"end":1244},"obj":"Sentence"},{"id":"S8","span":{"begin":1245,"end":1398},"obj":"Sentence"}],"text":"A lymphoid cell-specific nuclear factor containing c-Rel-like proteins preferentially interacts with interleukin-6 kappa B-related motifs whose activities are repressed in lymphoid cells.\nThe proto-oncoprotein c-Rel is a member of the nuclear factor kappa B transcription factor family, which includes the p50 and p65 subunits of nuclear factor kappa B. We show here that c-Rel binds to kappa B sites as homodimers as well as heterodimers with p50. These homodimers and heterodimers show distinct DNA-binding specificities and affinities for various kappa B motifs. In particular, the c-Rel homodimer has a high affinity for interleukin-6 (IL-6) and beta interferon kappa B sites. In spite of its association with p50 in vitro, however, we found a lymphoid cell-specific nuclear factor in vivo that contains c-Rel but not p50 epitopes; this factor, termed IL-6 kappa B binding factor II, appears to contain the c-Rel homodimer and preferentially recognizes several IL-6 kappa B-related kappa B motifs. Although it has been previously shown that the IL-6 kappa B motif functions as a potent IL-1/tumor necrosis factor-responsive element in nonlymphoid cells, its activity was found to be repressed in lymphoid cells such as a Jurkat T-cell line. We also present evidence that IL-6 kappa B binding factor II functions as a repressor specific for IL-6 kappa B-related kappa B motifs in lymphoid cells."}

genia-medco-coref

GENIAcorpus

PubMed:1372388 JSONTXT

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jnlpba-st-training

pubmed-sentences-benchmark

genia-medco-coref

GENIAcorpus

PubMed:1372388 JSON TXT