PMC:3333881 / 106-1359 JSON TXT

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pmc-enju-pas

bionlp-st-ge-2016-coref

{"project":"bionlp-st-ge-2016-coref","denotations":[{"id":"T356","span":{"begin":419,"end":432},"obj":"Anaphor"},{"id":"T357","span":{"begin":395,"end":400},"obj":"Antecedent"}],"relations":[{"id":"R685","pred":"boundBy","subj":"T356","obj":"T357"}],"namespaces":[{"prefix":"_base","uri":"https://bionlp.dbcls.jp/ontology/ge.owl#"}],"text":"Nuclear factor (NF)-κB is a master regulator of pro-inflammatory genes and is upregulated in human immunodeficiency virus 1 (HIV-1) infection. Mechanisms underlying the NF-κB deregulation by HIV-1 are relevant for immune dysfunction in AIDS. We report that in single round HIV-1 infection, or single-pulse PMA stimulation, the HIV-1 Tat transactivator activated NF-κB by hijacking the inhibitor IκB-α and by preventing the repressor binding to the NF-κB complex. Moreover, Tat associated with the p65 subunit of NF-κB and increased the p65 DNA-binding affinity and transcriptional activity. The arginine- and cysteine-rich domains of Tat were required for IκB-α and p65 association, respectively, and for sustaining the NF-κB activity. Among an array of NF-κB-responsive genes, Tat mostly activated the MIP-1α expression in a p65-dependent manner, and bound to the MIP-1α NF-κB enhancer thus promoting the recruitment of p65 with displacement of IκB-α; similar findings were obtained for the NF-κB-responsive genes CSF3, LTA, NFKBIA and TLR2. Our results support a novel mechanism of NF-κB activation via physical interaction of Tat with IκB-α and p65, and may contribute to further insights into the deregulation of the inflammatory response by HIV-1.\n"}

bionlp-st-ge-2016-spacy-parsed

GO-BP

{"project":"GO-BP","denotations":[{"id":"T634","span":{"begin":352,"end":367},"obj":"http://purl.obolibrary.org/obo/GO_0051092"},{"id":"T635","span":{"begin":1084,"end":1100},"obj":"http://purl.obolibrary.org/obo/GO_0051092"},{"id":"T636","span":{"begin":565,"end":580},"obj":"http://purl.obolibrary.org/obo/GO_0006351"},{"id":"T637","span":{"begin":1221,"end":1242},"obj":"http://purl.obolibrary.org/obo/GO_0006954"}],"text":"Nuclear factor (NF)-κB is a master regulator of pro-inflammatory genes and is upregulated in human immunodeficiency virus 1 (HIV-1) infection. Mechanisms underlying the NF-κB deregulation by HIV-1 are relevant for immune dysfunction in AIDS. We report that in single round HIV-1 infection, or single-pulse PMA stimulation, the HIV-1 Tat transactivator activated NF-κB by hijacking the inhibitor IκB-α and by preventing the repressor binding to the NF-κB complex. Moreover, Tat associated with the p65 subunit of NF-κB and increased the p65 DNA-binding affinity and transcriptional activity. The arginine- and cysteine-rich domains of Tat were required for IκB-α and p65 association, respectively, and for sustaining the NF-κB activity. Among an array of NF-κB-responsive genes, Tat mostly activated the MIP-1α expression in a p65-dependent manner, and bound to the MIP-1α NF-κB enhancer thus promoting the recruitment of p65 with displacement of IκB-α; similar findings were obtained for the NF-κB-responsive genes CSF3, LTA, NFKBIA and TLR2. Our results support a novel mechanism of NF-κB activation via physical interaction of Tat with IκB-α and p65, and may contribute to further insights into the deregulation of the inflammatory response by HIV-1.\n"}

GO-MF

{"project":"GO-MF","denotations":[{"id":"T640","span":{"begin":433,"end":440},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T641","span":{"begin":544,"end":551},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T642","span":{"begin":433,"end":453},"obj":"http://purl.obolibrary.org/obo/GO_0051059"},{"id":"T643","span":{"begin":540,"end":551},"obj":"http://purl.obolibrary.org/obo/GO_0003677"}],"text":"Nuclear factor (NF)-κB is a master regulator of pro-inflammatory genes and is upregulated in human immunodeficiency virus 1 (HIV-1) infection. Mechanisms underlying the NF-κB deregulation by HIV-1 are relevant for immune dysfunction in AIDS. We report that in single round HIV-1 infection, or single-pulse PMA stimulation, the HIV-1 Tat transactivator activated NF-κB by hijacking the inhibitor IκB-α and by preventing the repressor binding to the NF-κB complex. Moreover, Tat associated with the p65 subunit of NF-κB and increased the p65 DNA-binding affinity and transcriptional activity. The arginine- and cysteine-rich domains of Tat were required for IκB-α and p65 association, respectively, and for sustaining the NF-κB activity. Among an array of NF-κB-responsive genes, Tat mostly activated the MIP-1α expression in a p65-dependent manner, and bound to the MIP-1α NF-κB enhancer thus promoting the recruitment of p65 with displacement of IκB-α; similar findings were obtained for the NF-κB-responsive genes CSF3, LTA, NFKBIA and TLR2. Our results support a novel mechanism of NF-κB activation via physical interaction of Tat with IκB-α and p65, and may contribute to further insights into the deregulation of the inflammatory response by HIV-1.\n"}

GO-CC

{"project":"GO-CC","denotations":[{"id":"T644","span":{"begin":448,"end":461},"obj":"http://purl.obolibrary.org/obo/GO_0071159"}],"text":"Nuclear factor (NF)-κB is a master regulator of pro-inflammatory genes and is upregulated in human immunodeficiency virus 1 (HIV-1) infection. Mechanisms underlying the NF-κB deregulation by HIV-1 are relevant for immune dysfunction in AIDS. We report that in single round HIV-1 infection, or single-pulse PMA stimulation, the HIV-1 Tat transactivator activated NF-κB by hijacking the inhibitor IκB-α and by preventing the repressor binding to the NF-κB complex. Moreover, Tat associated with the p65 subunit of NF-κB and increased the p65 DNA-binding affinity and transcriptional activity. The arginine- and cysteine-rich domains of Tat were required for IκB-α and p65 association, respectively, and for sustaining the NF-κB activity. Among an array of NF-κB-responsive genes, Tat mostly activated the MIP-1α expression in a p65-dependent manner, and bound to the MIP-1α NF-κB enhancer thus promoting the recruitment of p65 with displacement of IκB-α; similar findings were obtained for the NF-κB-responsive genes CSF3, LTA, NFKBIA and TLR2. Our results support a novel mechanism of NF-κB activation via physical interaction of Tat with IκB-α and p65, and may contribute to further insights into the deregulation of the inflammatory response by HIV-1.\n"}

sentences

{"project":"sentences","denotations":[{"id":"T90","span":{"begin":0,"end":142},"obj":"Sentence"},{"id":"T91","span":{"begin":143,"end":241},"obj":"Sentence"},{"id":"T92","span":{"begin":242,"end":462},"obj":"Sentence"},{"id":"T93","span":{"begin":463,"end":590},"obj":"Sentence"},{"id":"T94","span":{"begin":591,"end":735},"obj":"Sentence"},{"id":"T95","span":{"begin":736,"end":1042},"obj":"Sentence"},{"id":"T96","span":{"begin":1043,"end":1252},"obj":"Sentence"},{"id":"T3","span":{"begin":0,"end":142},"obj":"Sentence"},{"id":"T4","span":{"begin":143,"end":241},"obj":"Sentence"},{"id":"T5","span":{"begin":242,"end":462},"obj":"Sentence"},{"id":"T6","span":{"begin":463,"end":590},"obj":"Sentence"},{"id":"T7","span":{"begin":591,"end":735},"obj":"Sentence"},{"id":"T8","span":{"begin":736,"end":1042},"obj":"Sentence"},{"id":"T9","span":{"begin":1043,"end":1252},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Nuclear factor (NF)-κB is a master regulator of pro-inflammatory genes and is upregulated in human immunodeficiency virus 1 (HIV-1) infection. Mechanisms underlying the NF-κB deregulation by HIV-1 are relevant for immune dysfunction in AIDS. We report that in single round HIV-1 infection, or single-pulse PMA stimulation, the HIV-1 Tat transactivator activated NF-κB by hijacking the inhibitor IκB-α and by preventing the repressor binding to the NF-κB complex. Moreover, Tat associated with the p65 subunit of NF-κB and increased the p65 DNA-binding affinity and transcriptional activity. The arginine- and cysteine-rich domains of Tat were required for IκB-α and p65 association, respectively, and for sustaining the NF-κB activity. Among an array of NF-κB-responsive genes, Tat mostly activated the MIP-1α expression in a p65-dependent manner, and bound to the MIP-1α NF-κB enhancer thus promoting the recruitment of p65 with displacement of IκB-α; similar findings were obtained for the NF-κB-responsive genes CSF3, LTA, NFKBIA and TLR2. Our results support a novel mechanism of NF-κB activation via physical interaction of Tat with IκB-α and p65, and may contribute to further insights into the deregulation of the inflammatory response by HIV-1.\n"}

ICD10

{"project":"ICD10","denotations":[{"id":"T639","span":{"begin":99,"end":115},"obj":"http://purl.bioontology.org/ontology/ICD10/D84.9"}],"text":"Nuclear factor (NF)-κB is a master regulator of pro-inflammatory genes and is upregulated in human immunodeficiency virus 1 (HIV-1) infection. Mechanisms underlying the NF-κB deregulation by HIV-1 are relevant for immune dysfunction in AIDS. We report that in single round HIV-1 infection, or single-pulse PMA stimulation, the HIV-1 Tat transactivator activated NF-κB by hijacking the inhibitor IκB-α and by preventing the repressor binding to the NF-κB complex. Moreover, Tat associated with the p65 subunit of NF-κB and increased the p65 DNA-binding affinity and transcriptional activity. The arginine- and cysteine-rich domains of Tat were required for IκB-α and p65 association, respectively, and for sustaining the NF-κB activity. Among an array of NF-κB-responsive genes, Tat mostly activated the MIP-1α expression in a p65-dependent manner, and bound to the MIP-1α NF-κB enhancer thus promoting the recruitment of p65 with displacement of IκB-α; similar findings were obtained for the NF-κB-responsive genes CSF3, LTA, NFKBIA and TLR2. Our results support a novel mechanism of NF-κB activation via physical interaction of Tat with IκB-α and p65, and may contribute to further insights into the deregulation of the inflammatory response by HIV-1.\n"}

events-check-again

bionlp-st-ge-2016-reference-tees

test2

bionlp-st-ge-2016-reference

bionlp-st-ge-2016-uniprot

{"project":"bionlp-st-ge-2016-uniprot","denotations":[{"id":"T364","span":{"begin":333,"end":336},"obj":"P04605"},{"id":"T365","span":{"begin":333,"end":336},"obj":"P04610"},{"id":"T366","span":{"begin":333,"end":336},"obj":"P04608"},{"id":"T367","span":{"begin":333,"end":336},"obj":"Q8UMQ1"},{"id":"T368","span":{"begin":473,"end":476},"obj":"P04610"},{"id":"T369","span":{"begin":473,"end":476},"obj":"P04608"},{"id":"T370","span":{"begin":473,"end":476},"obj":"P04605"},{"id":"T371","span":{"begin":473,"end":476},"obj":"Q8UMQ1"},{"id":"T372","span":{"begin":497,"end":500},"obj":"Q04206"},{"id":"T373","span":{"begin":497,"end":500},"obj":"P21579"},{"id":"T374","span":{"begin":536,"end":539},"obj":"Q04206"},{"id":"T375","span":{"begin":536,"end":539},"obj":"P21579"},{"id":"T376","span":{"begin":634,"end":637},"obj":"P04610"},{"id":"T377","span":{"begin":634,"end":637},"obj":"Q8UMQ1"},{"id":"T378","span":{"begin":634,"end":637},"obj":"P04605"},{"id":"T379","span":{"begin":634,"end":637},"obj":"P04608"},{"id":"T380","span":{"begin":666,"end":669},"obj":"P21579"},{"id":"T381","span":{"begin":666,"end":669},"obj":"Q04206"},{"id":"T382","span":{"begin":778,"end":781},"obj":"P04608"},{"id":"T383","span":{"begin":778,"end":781},"obj":"P04610"},{"id":"T384","span":{"begin":778,"end":781},"obj":"Q8UMQ1"},{"id":"T385","span":{"begin":778,"end":781},"obj":"P04605"},{"id":"T386","span":{"begin":803,"end":809},"obj":"P10147"},{"id":"T387","span":{"begin":826,"end":829},"obj":"P21579"},{"id":"T388","span":{"begin":826,"end":829},"obj":"Q04206"},{"id":"T389","span":{"begin":865,"end":871},"obj":"P10147"},{"id":"T390","span":{"begin":921,"end":924},"obj":"P21579"},{"id":"T391","span":{"begin":921,"end":924},"obj":"Q04206"},{"id":"T392","span":{"begin":1015,"end":1019},"obj":"P09919"},{"id":"T393","span":{"begin":1021,"end":1024},"obj":"P01374"},{"id":"T394","span":{"begin":1026,"end":1032},"obj":"P25963"},{"id":"T395","span":{"begin":1037,"end":1041},"obj":"O60603"},{"id":"T396","span":{"begin":1129,"end":1132},"obj":"Q8UMQ1"},{"id":"T397","span":{"begin":1129,"end":1132},"obj":"P04608"},{"id":"T398","span":{"begin":1129,"end":1132},"obj":"P04610"},{"id":"T399","span":{"begin":1129,"end":1132},"obj":"P04605"},{"id":"T400","span":{"begin":1148,"end":1151},"obj":"Q04206"},{"id":"T401","span":{"begin":1148,"end":1151},"obj":"P21579"}],"namespaces":[{"prefix":"_base","uri":"http://www.uniprot.org/uniprot/"}],"text":"Nuclear factor (NF)-κB is a master regulator of pro-inflammatory genes and is upregulated in human immunodeficiency virus 1 (HIV-1) infection. Mechanisms underlying the NF-κB deregulation by HIV-1 are relevant for immune dysfunction in AIDS. We report that in single round HIV-1 infection, or single-pulse PMA stimulation, the HIV-1 Tat transactivator activated NF-κB by hijacking the inhibitor IκB-α and by preventing the repressor binding to the NF-κB complex. Moreover, Tat associated with the p65 subunit of NF-κB and increased the p65 DNA-binding affinity and transcriptional activity. The arginine- and cysteine-rich domains of Tat were required for IκB-α and p65 association, respectively, and for sustaining the NF-κB activity. Among an array of NF-κB-responsive genes, Tat mostly activated the MIP-1α expression in a p65-dependent manner, and bound to the MIP-1α NF-κB enhancer thus promoting the recruitment of p65 with displacement of IκB-α; similar findings were obtained for the NF-κB-responsive genes CSF3, LTA, NFKBIA and TLR2. Our results support a novel mechanism of NF-κB activation via physical interaction of Tat with IκB-α and p65, and may contribute to further insights into the deregulation of the inflammatory response by HIV-1.\n"}

PMC:3333881 / 106-1359 JSONTXT

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PMC:3333881 / 106-1359 JSON TXT