PMC:3320587 / 48558-49448 JSON TXT

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2_test

{"project":"2_test","denotations":[{"id":"22496647-8253080-98010821","span":{"begin":509,"end":511},"obj":"8253080"},{"id":"22496647-19132086-98010822","span":{"begin":514,"end":516},"obj":"19132086"}],"text":"Intriguingly, both in the absence and presence of MTb co-infection, disruption of NF-κB site II consistently resulted in greater suppression of virus replication than disruption of NF-κB site I. Consistent with these findings, synthetic reporter assays have previously shown that these two sites have distinct roles in driving transcription. The downstream NF-κB site I binding site, which is directly upstream of three highly conserved Sp binding sites, appears to enhance Sp protein recruitment to the LTR [71]–[73]. Because NF-κB site I overlaps the NFAT5 binding site, it is possible that loss of NF-κB binding to this site is mitigated, at least in part, by increased NFAT5 binding to the mutated site. This hypothesis is consistent with our quantitative DNase I footprinting analysis that shows that specific disruption of NF-κB site I results in enhanced binding of NFAT5 to the LTR."}

pmc-enju-pas

bionlp-st-ge-2016-test-proteins

{"project":"bionlp-st-ge-2016-test-proteins","denotations":[{"id":"T17350","span":{"begin":873,"end":878},"obj":"Protein"},{"id":"T17349","span":{"begin":760,"end":767},"obj":"Protein"},{"id":"T17348","span":{"begin":673,"end":678},"obj":"Protein"}],"namespaces":[{"prefix":"_base","uri":"http://bionlp.dbcls.jp/ontology/ge.owl#"}],"text":"Intriguingly, both in the absence and presence of MTb co-infection, disruption of NF-κB site II consistently resulted in greater suppression of virus replication than disruption of NF-κB site I. Consistent with these findings, synthetic reporter assays have previously shown that these two sites have distinct roles in driving transcription. The downstream NF-κB site I binding site, which is directly upstream of three highly conserved Sp binding sites, appears to enhance Sp protein recruitment to the LTR [71]–[73]. Because NF-κB site I overlaps the NFAT5 binding site, it is possible that loss of NF-κB binding to this site is mitigated, at least in part, by increased NFAT5 binding to the mutated site. This hypothesis is consistent with our quantitative DNase I footprinting analysis that shows that specific disruption of NF-κB site I results in enhanced binding of NFAT5 to the LTR."}

bionlp-st-ge-2016-uniprot

{"project":"bionlp-st-ge-2016-uniprot","denotations":[{"id":"T18831","span":{"begin":873,"end":878},"obj":"http://www.uniprot.org/uniprot/O94916"},{"id":"T18830","span":{"begin":673,"end":678},"obj":"http://www.uniprot.org/uniprot/O94916"},{"id":"T18829","span":{"begin":553,"end":558},"obj":"http://www.uniprot.org/uniprot/O94916"}],"namespaces":[{"prefix":"_base","uri":"http://www.uniprot.org/uniprot/"}],"text":"Intriguingly, both in the absence and presence of MTb co-infection, disruption of NF-κB site II consistently resulted in greater suppression of virus replication than disruption of NF-κB site I. Consistent with these findings, synthetic reporter assays have previously shown that these two sites have distinct roles in driving transcription. The downstream NF-κB site I binding site, which is directly upstream of three highly conserved Sp binding sites, appears to enhance Sp protein recruitment to the LTR [71]–[73]. Because NF-κB site I overlaps the NFAT5 binding site, it is possible that loss of NF-κB binding to this site is mitigated, at least in part, by increased NFAT5 binding to the mutated site. This hypothesis is consistent with our quantitative DNase I footprinting analysis that shows that specific disruption of NF-κB site I results in enhanced binding of NFAT5 to the LTR."}

GO-BP

{"project":"GO-BP","denotations":[{"id":"T17421","span":{"begin":477,"end":496},"obj":"http://purl.obolibrary.org/obo/GO_0045184"},{"id":"T17379","span":{"begin":327,"end":340},"obj":"http://purl.obolibrary.org/obo/GO_0006351"}],"text":"Intriguingly, both in the absence and presence of MTb co-infection, disruption of NF-κB site II consistently resulted in greater suppression of virus replication than disruption of NF-κB site I. Consistent with these findings, synthetic reporter assays have previously shown that these two sites have distinct roles in driving transcription. The downstream NF-κB site I binding site, which is directly upstream of three highly conserved Sp binding sites, appears to enhance Sp protein recruitment to the LTR [71]–[73]. Because NF-κB site I overlaps the NFAT5 binding site, it is possible that loss of NF-κB binding to this site is mitigated, at least in part, by increased NFAT5 binding to the mutated site. This hypothesis is consistent with our quantitative DNase I footprinting analysis that shows that specific disruption of NF-κB site I results in enhanced binding of NFAT5 to the LTR."}

GO-MF

{"project":"GO-MF","denotations":[{"id":"T17455","span":{"begin":853,"end":869},"obj":"http://purl.obolibrary.org/obo/GO_0035326"},{"id":"T17451","span":{"begin":601,"end":614},"obj":"http://purl.obolibrary.org/obo/GO_0051059"},{"id":"T17443","span":{"begin":862,"end":869},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T17442","span":{"begin":679,"end":686},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T17441","span":{"begin":607,"end":614},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T17440","span":{"begin":559,"end":566},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T17439","span":{"begin":440,"end":447},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T17438","span":{"begin":370,"end":377},"obj":"http://purl.obolibrary.org/obo/GO_0005488"}],"text":"Intriguingly, both in the absence and presence of MTb co-infection, disruption of NF-κB site II consistently resulted in greater suppression of virus replication than disruption of NF-κB site I. Consistent with these findings, synthetic reporter assays have previously shown that these two sites have distinct roles in driving transcription. The downstream NF-κB site I binding site, which is directly upstream of three highly conserved Sp binding sites, appears to enhance Sp protein recruitment to the LTR [71]–[73]. Because NF-κB site I overlaps the NFAT5 binding site, it is possible that loss of NF-κB binding to this site is mitigated, at least in part, by increased NFAT5 binding to the mutated site. This hypothesis is consistent with our quantitative DNase I footprinting analysis that shows that specific disruption of NF-κB site I results in enhanced binding of NFAT5 to the LTR."}

sentences

{"project":"sentences","denotations":[{"id":"T17223","span":{"begin":708,"end":890},"obj":"Sentence"},{"id":"T17222","span":{"begin":519,"end":707},"obj":"Sentence"},{"id":"T17221","span":{"begin":342,"end":518},"obj":"Sentence"},{"id":"T17220","span":{"begin":0,"end":341},"obj":"Sentence"},{"id":"T287","span":{"begin":0,"end":194},"obj":"Sentence"},{"id":"T288","span":{"begin":195,"end":341},"obj":"Sentence"},{"id":"T289","span":{"begin":342,"end":518},"obj":"Sentence"},{"id":"T290","span":{"begin":519,"end":707},"obj":"Sentence"},{"id":"T291","span":{"begin":708,"end":890},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Intriguingly, both in the absence and presence of MTb co-infection, disruption of NF-κB site II consistently resulted in greater suppression of virus replication than disruption of NF-κB site I. Consistent with these findings, synthetic reporter assays have previously shown that these two sites have distinct roles in driving transcription. The downstream NF-κB site I binding site, which is directly upstream of three highly conserved Sp binding sites, appears to enhance Sp protein recruitment to the LTR [71]–[73]. Because NF-κB site I overlaps the NFAT5 binding site, it is possible that loss of NF-κB binding to this site is mitigated, at least in part, by increased NFAT5 binding to the mutated site. This hypothesis is consistent with our quantitative DNase I footprinting analysis that shows that specific disruption of NF-κB site I results in enhanced binding of NFAT5 to the LTR."}

simple1

{"project":"simple1","denotations":[{"id":"T17488","span":{"begin":873,"end":878},"obj":"Protein"},{"id":"T17487","span":{"begin":760,"end":767},"obj":"Protein"},{"id":"T17486","span":{"begin":673,"end":678},"obj":"Protein"}],"text":"Intriguingly, both in the absence and presence of MTb co-infection, disruption of NF-κB site II consistently resulted in greater suppression of virus replication than disruption of NF-κB site I. Consistent with these findings, synthetic reporter assays have previously shown that these two sites have distinct roles in driving transcription. The downstream NF-κB site I binding site, which is directly upstream of three highly conserved Sp binding sites, appears to enhance Sp protein recruitment to the LTR [71]–[73]. Because NF-κB site I overlaps the NFAT5 binding site, it is possible that loss of NF-κB binding to this site is mitigated, at least in part, by increased NFAT5 binding to the mutated site. This hypothesis is consistent with our quantitative DNase I footprinting analysis that shows that specific disruption of NF-κB site I results in enhanced binding of NFAT5 to the LTR."}

BioNLP16_DUT

{"project":"BioNLP16_DUT","denotations":[{"id":"T20735","span":{"begin":853,"end":861},"obj":"Positive_regulation"},{"id":"T20734","span":{"begin":862,"end":869},"obj":"Binding"},{"id":"T20733","span":{"begin":679,"end":686},"obj":"Binding"},{"id":"T20732","span":{"begin":663,"end":672},"obj":"Positive_regulation"},{"id":"T20697","span":{"begin":873,"end":878},"obj":"Protein"},{"id":"T20696","span":{"begin":760,"end":767},"obj":"Protein"},{"id":"T20695","span":{"begin":673,"end":678},"obj":"Protein"}],"relations":[{"id":"R15385","pred":"themeOf","subj":"T20695","obj":"T20732"},{"id":"R15386","pred":"themeOf","subj":"T20695","obj":"T20733"},{"id":"R15387","pred":"themeOf","subj":"T20697","obj":"T20734"},{"id":"R15416","pred":"themeOf","subj":"T20734","obj":"T20735"}],"text":"Intriguingly, both in the absence and presence of MTb co-infection, disruption of NF-κB site II consistently resulted in greater suppression of virus replication than disruption of NF-κB site I. Consistent with these findings, synthetic reporter assays have previously shown that these two sites have distinct roles in driving transcription. The downstream NF-κB site I binding site, which is directly upstream of three highly conserved Sp binding sites, appears to enhance Sp protein recruitment to the LTR [71]–[73]. Because NF-κB site I overlaps the NFAT5 binding site, it is possible that loss of NF-κB binding to this site is mitigated, at least in part, by increased NFAT5 binding to the mutated site. This hypothesis is consistent with our quantitative DNase I footprinting analysis that shows that specific disruption of NF-κB site I results in enhanced binding of NFAT5 to the LTR."}

BioNLP16_Messiy

{"project":"BioNLP16_Messiy","denotations":[{"id":"T19029","span":{"begin":873,"end":878},"obj":"Protein"},{"id":"T19028","span":{"begin":760,"end":767},"obj":"Protein"},{"id":"T19027","span":{"begin":673,"end":678},"obj":"Protein"},{"id":"T19067","span":{"begin":853,"end":861},"obj":"Positive_regulation"},{"id":"T19066","span":{"begin":862,"end":869},"obj":"Binding"},{"id":"T19065","span":{"begin":663,"end":672},"obj":"Positive_regulation"},{"id":"T19064","span":{"begin":679,"end":686},"obj":"Binding"}],"relations":[{"id":"R13909","pred":"themeOf","subj":"T19027","obj":"T19064"},{"id":"R13910","pred":"themeOf","subj":"T19029","obj":"T19066"},{"id":"R13930","pred":"themeOf","subj":"T19064","obj":"T19065"},{"id":"R13931","pred":"themeOf","subj":"T19066","obj":"T19067"}],"text":"Intriguingly, both in the absence and presence of MTb co-infection, disruption of NF-κB site II consistently resulted in greater suppression of virus replication than disruption of NF-κB site I. Consistent with these findings, synthetic reporter assays have previously shown that these two sites have distinct roles in driving transcription. The downstream NF-κB site I binding site, which is directly upstream of three highly conserved Sp binding sites, appears to enhance Sp protein recruitment to the LTR [71]–[73]. Because NF-κB site I overlaps the NFAT5 binding site, it is possible that loss of NF-κB binding to this site is mitigated, at least in part, by increased NFAT5 binding to the mutated site. This hypothesis is consistent with our quantitative DNase I footprinting analysis that shows that specific disruption of NF-κB site I results in enhanced binding of NFAT5 to the LTR."}

DLUT931

{"project":"DLUT931","denotations":[{"id":"T18990","span":{"begin":853,"end":861},"obj":"Positive_regulation"},{"id":"T18989","span":{"begin":842,"end":849},"obj":"Positive_regulation"},{"id":"T18988","span":{"begin":862,"end":869},"obj":"Binding"},{"id":"T18987","span":{"begin":663,"end":672},"obj":"Positive_regulation"},{"id":"T18986","span":{"begin":631,"end":640},"obj":"Positive_regulation"},{"id":"T18985","span":{"begin":679,"end":686},"obj":"Binding"},{"id":"T18949","span":{"begin":873,"end":878},"obj":"Protein"},{"id":"T18948","span":{"begin":760,"end":767},"obj":"Protein"},{"id":"T18947","span":{"begin":673,"end":678},"obj":"Protein"}],"relations":[{"id":"R13873","pred":"themeOf","subj":"T18949","obj":"T18988"},{"id":"R13892","pred":"themeOf","subj":"T18985","obj":"T18986"},{"id":"R13893","pred":"themeOf","subj":"T18985","obj":"T18987"},{"id":"R13894","pred":"themeOf","subj":"T18988","obj":"T18989"},{"id":"R13895","pred":"themeOf","subj":"T18988","obj":"T18990"},{"id":"R13872","pred":"themeOf","subj":"T18947","obj":"T18985"}],"text":"Intriguingly, both in the absence and presence of MTb co-infection, disruption of NF-κB site II consistently resulted in greater suppression of virus replication than disruption of NF-κB site I. Consistent with these findings, synthetic reporter assays have previously shown that these two sites have distinct roles in driving transcription. The downstream NF-κB site I binding site, which is directly upstream of three highly conserved Sp binding sites, appears to enhance Sp protein recruitment to the LTR [71]–[73]. Because NF-κB site I overlaps the NFAT5 binding site, it is possible that loss of NF-κB binding to this site is mitigated, at least in part, by increased NFAT5 binding to the mutated site. This hypothesis is consistent with our quantitative DNase I footprinting analysis that shows that specific disruption of NF-κB site I results in enhanced binding of NFAT5 to the LTR."}

bionlp-st-ge-2016-test-ihmc

{"project":"bionlp-st-ge-2016-test-ihmc","denotations":[{"id":"T20945","span":{"begin":477,"end":517},"obj":"Binding"},{"id":"T20944","span":{"begin":342,"end":382},"obj":"Binding"},{"id":"T20941","span":{"begin":463,"end":517},"obj":"Positive_regulation"},{"id":"T20939","span":{"begin":440,"end":454},"obj":"Binding"},{"id":"T20928","span":{"begin":850,"end":889},"obj":"Positive_regulation"},{"id":"T20927","span":{"begin":738,"end":834},"obj":"Negative_regulation"},{"id":"T20894","span":{"begin":870,"end":878},"obj":"Protein"},{"id":"T20893","span":{"begin":527,"end":532},"obj":"Protein"},{"id":"T20891","span":{"begin":687,"end":706},"obj":"Entity"},{"id":"T20890","span":{"begin":549,"end":558},"obj":"Protein"},{"id":"T20886","span":{"begin":181,"end":186},"obj":"Protein"},{"id":"T20867","span":{"begin":747,"end":767},"obj":"Protein"},{"id":"T20866","span":{"begin":527,"end":539},"obj":"Entity"},{"id":"T20863","span":{"begin":50,"end":53},"obj":"Protein"},{"id":"T20858","span":{"begin":82,"end":87},"obj":"Protein"},{"id":"T20853","span":{"begin":663,"end":678},"obj":"Protein"},{"id":"T20846","span":{"begin":342,"end":382},"obj":"Entity"},{"id":"T20833","span":{"begin":477,"end":484},"obj":"Protein"},{"id":"T20823","span":{"begin":79,"end":95},"obj":"Entity"},{"id":"T20817","span":{"begin":835,"end":841},"obj":"Entity"},{"id":"T20815","span":{"begin":280,"end":295},"obj":"Entity"},{"id":"T20810","span":{"begin":342,"end":382},"obj":"Entity"},{"id":"T20792","span":{"begin":342,"end":382},"obj":"Protein"},{"id":"T20783","span":{"begin":826,"end":834},"obj":"Protein"},{"id":"T20782","span":{"begin":440,"end":454},"obj":"Entity"},{"id":"T20778","span":{"begin":567,"end":571},"obj":"Entity"},{"id":"T20772","span":{"begin":79,"end":95},"obj":"Entity"},{"id":"T20769","span":{"begin":178,"end":225},"obj":"Entity"},{"id":"T20764","span":{"begin":618,"end":627},"obj":"Entity"},{"id":"T20922","span":{"begin":47,"end":66},"obj":"Regulation"},{"id":"T20916","span":{"begin":850,"end":889},"obj":"Binding"}],"relations":[{"id":"R15402","pred":"themeOf","subj":"T20782","obj":"T20939"},{"id":"R15410","pred":"themeOf","subj":"T20783","obj":"T20927"},{"id":"R15425","pred":"themeOf","subj":"T20833","obj":"T20945"},{"id":"R15432","pred":"themeOf","subj":"T20945","obj":"T20941"},{"id":"R15433","pred":"themeOf","subj":"T20846","obj":"T20944"},{"id":"R15439","pred":"themeOf","subj":"T20863","obj":"T20922"},{"id":"R15442","pred":"causeOf","subj":"T20867","obj":"T20927"},{"id":"R15449","pred":"themeOf","subj":"T20894","obj":"T20916"},{"id":"R15453","pred":"themeOf","subj":"T20916","obj":"T20928"}],"text":"Intriguingly, both in the absence and presence of MTb co-infection, disruption of NF-κB site II consistently resulted in greater suppression of virus replication than disruption of NF-κB site I. Consistent with these findings, synthetic reporter assays have previously shown that these two sites have distinct roles in driving transcription. The downstream NF-κB site I binding site, which is directly upstream of three highly conserved Sp binding sites, appears to enhance Sp protein recruitment to the LTR [71]–[73]. Because NF-κB site I overlaps the NFAT5 binding site, it is possible that loss of NF-κB binding to this site is mitigated, at least in part, by increased NFAT5 binding to the mutated site. This hypothesis is consistent with our quantitative DNase I footprinting analysis that shows that specific disruption of NF-κB site I results in enhanced binding of NFAT5 to the LTR."}

bionlp-st-ge-2016-spacy-parsed

bionlp-st-ge-2016-test-tees

{"project":"bionlp-st-ge-2016-test-tees","denotations":[{"id":"T19158","span":{"begin":853,"end":861},"obj":"Positive_regulation"},{"id":"T19157","span":{"begin":862,"end":869},"obj":"Binding"},{"id":"T19156","span":{"begin":815,"end":825},"obj":"Positive_regulation"},{"id":"T19155","span":{"begin":873,"end":878},"obj":"Protein"},{"id":"T19154","span":{"begin":829,"end":841},"obj":"Protein"},{"id":"T19153","span":{"begin":760,"end":767},"obj":"Protein"},{"id":"T19152","span":{"begin":663,"end":672},"obj":"Positive_regulation"},{"id":"T19151","span":{"begin":593,"end":597},"obj":"Negative_regulation"},{"id":"T19150","span":{"begin":679,"end":686},"obj":"Binding"},{"id":"T19149","span":{"begin":607,"end":614},"obj":"Binding"},{"id":"T19148","span":{"begin":673,"end":678},"obj":"Protein"},{"id":"T19147","span":{"begin":601,"end":606},"obj":"Protein"},{"id":"T19146","span":{"begin":553,"end":571},"obj":"Protein"},{"id":"T19145","span":{"begin":527,"end":539},"obj":"Protein"},{"id":"T19144","span":{"begin":466,"end":473},"obj":"Positive_regulation"},{"id":"T19143","span":{"begin":485,"end":496},"obj":"Binding"},{"id":"T19142","span":{"begin":474,"end":484},"obj":"Protein"},{"id":"T19141","span":{"begin":437,"end":453},"obj":"Protein"},{"id":"T19140","span":{"begin":357,"end":382},"obj":"Protein"},{"id":"T19139","span":{"begin":181,"end":193},"obj":"Protein"},{"id":"T19138","span":{"begin":82,"end":95},"obj":"Protein"}],"relations":[{"id":"R13957","pred":"causeOf","subj":"T19140","obj":"T19144"},{"id":"R13958","pred":"themeOf","subj":"T19142","obj":"T19143"},{"id":"R13959","pred":"themeOf","subj":"T19143","obj":"T19144"},{"id":"R13960","pred":"themeOf","subj":"T19147","obj":"T19149"},{"id":"R13961","pred":"themeOf","subj":"T19148","obj":"T19150"},{"id":"R13962","pred":"themeOf","subj":"T19149","obj":"T19151"},{"id":"R13963","pred":"themeOf","subj":"T19150","obj":"T19152"},{"id":"R13964","pred":"themeOf","subj":"T19154","obj":"T19156"},{"id":"R13965","pred":"themeOf","subj":"T19155","obj":"T19157"},{"id":"R13966","pred":"themeOf","subj":"T19157","obj":"T19158"}],"text":"Intriguingly, both in the absence and presence of MTb co-infection, disruption of NF-κB site II consistently resulted in greater suppression of virus replication than disruption of NF-κB site I. Consistent with these findings, synthetic reporter assays have previously shown that these two sites have distinct roles in driving transcription. The downstream NF-κB site I binding site, which is directly upstream of three highly conserved Sp binding sites, appears to enhance Sp protein recruitment to the LTR [71]–[73]. Because NF-κB site I overlaps the NFAT5 binding site, it is possible that loss of NF-κB binding to this site is mitigated, at least in part, by increased NFAT5 binding to the mutated site. This hypothesis is consistent with our quantitative DNase I footprinting analysis that shows that specific disruption of NF-κB site I results in enhanced binding of NFAT5 to the LTR."}

testone

{"project":"testone","denotations":[{"id":"T17086","span":{"begin":862,"end":869},"obj":"Binding"},{"id":"T17085","span":{"begin":815,"end":825},"obj":"Negative_regulation"},{"id":"T17084","span":{"begin":679,"end":686},"obj":"Binding"},{"id":"T17083","span":{"begin":663,"end":672},"obj":"Positive_regulation"},{"id":"T17082","span":{"begin":607,"end":614},"obj":"Binding"},{"id":"T17081","span":{"begin":593,"end":597},"obj":"Negative_regulation"},{"id":"T17080","span":{"begin":466,"end":473},"obj":"Positive_regulation"},{"id":"T17079","span":{"begin":167,"end":177},"obj":"Negative_regulation"},{"id":"T17042","span":{"begin":873,"end":878},"obj":"Protein"},{"id":"T17041","span":{"begin":760,"end":767},"obj":"Protein"},{"id":"T17040","span":{"begin":673,"end":678},"obj":"Protein"}],"relations":[{"id":"R12471","pred":"themeOf","subj":"T17040","obj":"T17084"},{"id":"R12472","pred":"themeOf","subj":"T17042","obj":"T17086"},{"id":"R12485","pred":"themeOf","subj":"T17082","obj":"T17081"},{"id":"R12486","pred":"themeOf","subj":"T17084","obj":"T17083"}],"text":"Intriguingly, both in the absence and presence of MTb co-infection, disruption of NF-κB site II consistently resulted in greater suppression of virus replication than disruption of NF-κB site I. Consistent with these findings, synthetic reporter assays have previously shown that these two sites have distinct roles in driving transcription. The downstream NF-κB site I binding site, which is directly upstream of three highly conserved Sp binding sites, appears to enhance Sp protein recruitment to the LTR [71]–[73]. Because NF-κB site I overlaps the NFAT5 binding site, it is possible that loss of NF-κB binding to this site is mitigated, at least in part, by increased NFAT5 binding to the mutated site. This hypothesis is consistent with our quantitative DNase I footprinting analysis that shows that specific disruption of NF-κB site I results in enhanced binding of NFAT5 to the LTR."}

test3

{"project":"test3","denotations":[{"id":"T17173","span":{"begin":873,"end":878},"obj":"Protein"},{"id":"T17172","span":{"begin":862,"end":869},"obj":"Binding"},{"id":"T17171","span":{"begin":760,"end":767},"obj":"Protein"},{"id":"T17170","span":{"begin":679,"end":686},"obj":"Binding"},{"id":"T17169","span":{"begin":673,"end":678},"obj":"Protein"},{"id":"T17119","span":{"begin":873,"end":878},"obj":"Protein"},{"id":"T17118","span":{"begin":760,"end":767},"obj":"Protein"},{"id":"T17117","span":{"begin":673,"end":678},"obj":"Protein"}],"relations":[{"id":"R12499","pred":"themeOf","subj":"T17169","obj":"T17170"},{"id":"R12500","pred":"themeOf","subj":"T17173","obj":"T17172"}],"text":"Intriguingly, both in the absence and presence of MTb co-infection, disruption of NF-κB site II consistently resulted in greater suppression of virus replication than disruption of NF-κB site I. Consistent with these findings, synthetic reporter assays have previously shown that these two sites have distinct roles in driving transcription. The downstream NF-κB site I binding site, which is directly upstream of three highly conserved Sp binding sites, appears to enhance Sp protein recruitment to the LTR [71]–[73]. Because NF-κB site I overlaps the NFAT5 binding site, it is possible that loss of NF-κB binding to this site is mitigated, at least in part, by increased NFAT5 binding to the mutated site. This hypothesis is consistent with our quantitative DNase I footprinting analysis that shows that specific disruption of NF-κB site I results in enhanced binding of NFAT5 to the LTR."}

PMC:3320587 / 48558-49448 JSONTXT

Annnotations TAB JSON ListView MergeView

PMC:3320587 / 48558-49448 JSON TXT