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the transcription factor NFAT5 binds to a core NF-κB binding motif in the HIV-1 LTR enhancer region of subtype B, when two thymines (TT) are changed to cytosines (CC) in the proximal NF-κB binding motif (named N5-Mut) (bottom of Figure 1B), the binding of NFAT5 can be disrupted while leaving binding of NF-κB unperturbed [31]. We examined the requirement of NFAT5 for MTb-induced LTR activity by transfecting a wild-type and NFAT5 mutant LTR reporter construct into THP-1 cells, followed by stimulation with an MTb lysate. As shown in Figure 1B, in the absence of MTb lysate stimulation the activity of the NFAT5 binding site-mutant LTR was significantly reduced (p\u003c0.05) in comparison to the wild-type LTR. When the NFAT5 binding site-mutant LTR was examined in THP-1 cells stimulated with the MTb lysate, its activity was reduced to an even more significant extent (p\u003c0.01)."}
bionlp-st-ge-2016-test-proteins
{"project":"bionlp-st-ge-2016-test-proteins","denotations":[{"id":"T7328","span":{"begin":368,"end":373},"obj":"Protein"},{"id":"T7327","span":{"begin":265,"end":270},"obj":"Protein"},{"id":"T7326","span":{"begin":34,"end":39},"obj":"Protein"}],"namespaces":[{"prefix":"_base","uri":"http://bionlp.dbcls.jp/ontology/ge.owl#"}],"text":"Although the transcription factor NFAT5 binds to a core NF-κB binding motif in the HIV-1 LTR enhancer region of subtype B, when two thymines (TT) are changed to cytosines (CC) in the proximal NF-κB binding motif (named N5-Mut) (bottom of Figure 1B), the binding of NFAT5 can be disrupted while leaving binding of NF-κB unperturbed [31]. We examined the requirement of NFAT5 for MTb-induced LTR activity by transfecting a wild-type and NFAT5 mutant LTR reporter construct into THP-1 cells, followed by stimulation with an MTb lysate. As shown in Figure 1B, in the absence of MTb lysate stimulation the activity of the NFAT5 binding site-mutant LTR was significantly reduced (p\u003c0.05) in comparison to the wild-type LTR. When the NFAT5 binding site-mutant LTR was examined in THP-1 cells stimulated with the MTb lysate, its activity was reduced to an even more significant extent (p\u003c0.01)."}
bionlp-st-ge-2016-uniprot
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GO-BP
{"project":"GO-BP","denotations":[{"id":"T7334","span":{"begin":13,"end":26},"obj":"http://purl.obolibrary.org/obo/GO_0006351"}],"text":"Although the transcription factor NFAT5 binds to a core NF-κB binding motif in the HIV-1 LTR enhancer region of subtype B, when two thymines (TT) are changed to cytosines (CC) in the proximal NF-κB binding motif (named N5-Mut) (bottom of Figure 1B), the binding of NFAT5 can be disrupted while leaving binding of NF-κB unperturbed [31]. We examined the requirement of NFAT5 for MTb-induced LTR activity by transfecting a wild-type and NFAT5 mutant LTR reporter construct into THP-1 cells, followed by stimulation with an MTb lysate. As shown in Figure 1B, in the absence of MTb lysate stimulation the activity of the NFAT5 binding site-mutant LTR was significantly reduced (p\u003c0.05) in comparison to the wild-type LTR. When the NFAT5 binding site-mutant LTR was examined in THP-1 cells stimulated with the MTb lysate, its activity was reduced to an even more significant extent (p\u003c0.01)."}
GO-MF
{"project":"GO-MF","denotations":[{"id":"T7342","span":{"begin":302,"end":318},"obj":"http://purl.obolibrary.org/obo/GO_0051059"},{"id":"T7341","span":{"begin":733,"end":740},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T7340","span":{"begin":623,"end":630},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T7339","span":{"begin":302,"end":309},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T7338","span":{"begin":254,"end":261},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T7337","span":{"begin":198,"end":205},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T7336","span":{"begin":62,"end":69},"obj":"http://purl.obolibrary.org/obo/GO_0005488"}],"text":"Although the transcription factor NFAT5 binds to a core NF-κB binding motif in the HIV-1 LTR enhancer region of subtype B, when two thymines (TT) are changed to cytosines (CC) in the proximal NF-κB binding motif (named N5-Mut) (bottom of Figure 1B), the binding of NFAT5 can be disrupted while leaving binding of NF-κB unperturbed [31]. We examined the requirement of NFAT5 for MTb-induced LTR activity by transfecting a wild-type and NFAT5 mutant LTR reporter construct into THP-1 cells, followed by stimulation with an MTb lysate. As shown in Figure 1B, in the absence of MTb lysate stimulation the activity of the NFAT5 binding site-mutant LTR was significantly reduced (p\u003c0.05) in comparison to the wild-type LTR. When the NFAT5 binding site-mutant LTR was examined in THP-1 cells stimulated with the MTb lysate, its activity was reduced to an even more significant extent (p\u003c0.01)."}
GO-CC
{"project":"GO-CC","denotations":[{"id":"T7348","span":{"begin":51,"end":55},"obj":"http://purl.obolibrary.org/obo/GO_0019013"},{"id":"T7345","span":{"begin":779,"end":784},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T7344","span":{"begin":482,"end":487},"obj":"http://purl.obolibrary.org/obo/GO_0005623"}],"text":"Although the transcription factor NFAT5 binds to a core NF-κB binding motif in the HIV-1 LTR enhancer region of subtype B, when two thymines (TT) are changed to cytosines (CC) in the proximal NF-κB binding motif (named N5-Mut) (bottom of Figure 1B), the binding of NFAT5 can be disrupted while leaving binding of NF-κB unperturbed [31]. We examined the requirement of NFAT5 for MTb-induced LTR activity by transfecting a wild-type and NFAT5 mutant LTR reporter construct into THP-1 cells, followed by stimulation with an MTb lysate. As shown in Figure 1B, in the absence of MTb lysate stimulation the activity of the NFAT5 binding site-mutant LTR was significantly reduced (p\u003c0.05) in comparison to the wild-type LTR. When the NFAT5 binding site-mutant LTR was examined in THP-1 cells stimulated with the MTb lysate, its activity was reduced to an even more significant extent (p\u003c0.01)."}
sentences
{"project":"sentences","denotations":[{"id":"T7303","span":{"begin":718,"end":886},"obj":"Sentence"},{"id":"T7302","span":{"begin":533,"end":717},"obj":"Sentence"},{"id":"T7301","span":{"begin":337,"end":532},"obj":"Sentence"},{"id":"T7300","span":{"begin":0,"end":336},"obj":"Sentence"},{"id":"T126","span":{"begin":0,"end":336},"obj":"Sentence"},{"id":"T127","span":{"begin":337,"end":532},"obj":"Sentence"},{"id":"T128","span":{"begin":533,"end":717},"obj":"Sentence"},{"id":"T129","span":{"begin":718,"end":886},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Although the transcription factor NFAT5 binds to a core NF-κB binding motif in the HIV-1 LTR enhancer region of subtype B, when two thymines (TT) are changed to cytosines (CC) in the proximal NF-κB binding motif (named N5-Mut) (bottom of Figure 1B), the binding of NFAT5 can be disrupted while leaving binding of NF-κB unperturbed [31]. We examined the requirement of NFAT5 for MTb-induced LTR activity by transfecting a wild-type and NFAT5 mutant LTR reporter construct into THP-1 cells, followed by stimulation with an MTb lysate. As shown in Figure 1B, in the absence of MTb lysate stimulation the activity of the NFAT5 binding site-mutant LTR was significantly reduced (p\u003c0.05) in comparison to the wild-type LTR. When the NFAT5 binding site-mutant LTR was examined in THP-1 cells stimulated with the MTb lysate, its activity was reduced to an even more significant extent (p\u003c0.01)."}
simple1
{"project":"simple1","denotations":[{"id":"T7360","span":{"begin":368,"end":373},"obj":"Protein"},{"id":"T7359","span":{"begin":265,"end":270},"obj":"Protein"},{"id":"T7358","span":{"begin":34,"end":39},"obj":"Protein"}],"text":"Although the transcription factor NFAT5 binds to a core NF-κB binding motif in the HIV-1 LTR enhancer region of subtype B, when two thymines (TT) are changed to cytosines (CC) in the proximal NF-κB binding motif (named N5-Mut) (bottom of Figure 1B), the binding of NFAT5 can be disrupted while leaving binding of NF-κB unperturbed [31]. We examined the requirement of NFAT5 for MTb-induced LTR activity by transfecting a wild-type and NFAT5 mutant LTR reporter construct into THP-1 cells, followed by stimulation with an MTb lysate. As shown in Figure 1B, in the absence of MTb lysate stimulation the activity of the NFAT5 binding site-mutant LTR was significantly reduced (p\u003c0.05) in comparison to the wild-type LTR. When the NFAT5 binding site-mutant LTR was examined in THP-1 cells stimulated with the MTb lysate, its activity was reduced to an even more significant extent (p\u003c0.01)."}
BioNLP16_DUT
{"project":"BioNLP16_DUT","denotations":[{"id":"T8034","span":{"begin":353,"end":364},"obj":"Positive_regulation"},{"id":"T8033","span":{"begin":40,"end":45},"obj":"Binding"},{"id":"T8032","span":{"begin":254,"end":261},"obj":"Binding"},{"id":"T8025","span":{"begin":368,"end":373},"obj":"Protein"},{"id":"T8024","span":{"begin":265,"end":270},"obj":"Protein"},{"id":"T8023","span":{"begin":34,"end":39},"obj":"Protein"}],"relations":[{"id":"R6458","pred":"themeOf","subj":"T8023","obj":"T8033"},{"id":"R6459","pred":"themeOf","subj":"T8024","obj":"T8032"},{"id":"R6460","pred":"themeOf","subj":"T8025","obj":"T8034"}],"text":"Although the transcription factor NFAT5 binds to a core NF-κB binding motif in the HIV-1 LTR enhancer region of subtype B, when two thymines (TT) are changed to cytosines (CC) in the proximal NF-κB binding motif (named N5-Mut) (bottom of Figure 1B), the binding of NFAT5 can be disrupted while leaving binding of NF-κB unperturbed [31]. We examined the requirement of NFAT5 for MTb-induced LTR activity by transfecting a wild-type and NFAT5 mutant LTR reporter construct into THP-1 cells, followed by stimulation with an MTb lysate. As shown in Figure 1B, in the absence of MTb lysate stimulation the activity of the NFAT5 binding site-mutant LTR was significantly reduced (p\u003c0.05) in comparison to the wild-type LTR. When the NFAT5 binding site-mutant LTR was examined in THP-1 cells stimulated with the MTb lysate, its activity was reduced to an even more significant extent (p\u003c0.01)."}
BioNLP16_Messiy
{"project":"BioNLP16_Messiy","denotations":[{"id":"T7682","span":{"begin":353,"end":364},"obj":"Positive_regulation"},{"id":"T7681","span":{"begin":40,"end":45},"obj":"Binding"},{"id":"T7680","span":{"begin":254,"end":261},"obj":"Binding"},{"id":"T7679","span":{"begin":278,"end":287},"obj":"Negative_regulation"},{"id":"T7672","span":{"begin":368,"end":373},"obj":"Protein"},{"id":"T7671","span":{"begin":265,"end":270},"obj":"Protein"},{"id":"T7670","span":{"begin":34,"end":39},"obj":"Protein"}],"relations":[{"id":"R6148","pred":"themeOf","subj":"T7670","obj":"T7681"},{"id":"R6149","pred":"themeOf","subj":"T7671","obj":"T7680"},{"id":"R6150","pred":"themeOf","subj":"T7672","obj":"T7682"},{"id":"R6155","pred":"themeOf","subj":"T7680","obj":"T7679"}],"text":"Although the transcription factor NFAT5 binds to a core NF-κB binding motif in the HIV-1 LTR enhancer region of subtype B, when two thymines (TT) are changed to cytosines (CC) in the proximal NF-κB binding motif (named N5-Mut) (bottom of Figure 1B), the binding of NFAT5 can be disrupted while leaving binding of NF-κB unperturbed [31]. We examined the requirement of NFAT5 for MTb-induced LTR activity by transfecting a wild-type and NFAT5 mutant LTR reporter construct into THP-1 cells, followed by stimulation with an MTb lysate. As shown in Figure 1B, in the absence of MTb lysate stimulation the activity of the NFAT5 binding site-mutant LTR was significantly reduced (p\u003c0.05) in comparison to the wild-type LTR. When the NFAT5 binding site-mutant LTR was examined in THP-1 cells stimulated with the MTb lysate, its activity was reduced to an even more significant extent (p\u003c0.01)."}
DLUT931
{"project":"DLUT931","denotations":[{"id":"T7652","span":{"begin":353,"end":364},"obj":"Positive_regulation"},{"id":"T7651","span":{"begin":278,"end":287},"obj":"Negative_regulation"},{"id":"T7650","span":{"begin":254,"end":261},"obj":"Binding"},{"id":"T7649","span":{"begin":40,"end":45},"obj":"Binding"},{"id":"T7642","span":{"begin":368,"end":373},"obj":"Protein"},{"id":"T7641","span":{"begin":265,"end":270},"obj":"Protein"},{"id":"T7640","span":{"begin":34,"end":39},"obj":"Protein"}],"relations":[{"id":"R6132","pred":"themeOf","subj":"T7640","obj":"T7649"},{"id":"R6133","pred":"themeOf","subj":"T7641","obj":"T7650"},{"id":"R6134","pred":"themeOf","subj":"T7642","obj":"T7652"},{"id":"R6139","pred":"themeOf","subj":"T7649","obj":"T7651"},{"id":"R6140","pred":"themeOf","subj":"T7650","obj":"T7651"}],"text":"Although the transcription factor NFAT5 binds to a core NF-κB binding motif in the HIV-1 LTR enhancer region of subtype B, when two thymines (TT) are changed to cytosines (CC) in the proximal NF-κB binding motif (named N5-Mut) (bottom of Figure 1B), the binding of NFAT5 can be disrupted while leaving binding of NF-κB unperturbed [31]. We examined the requirement of NFAT5 for MTb-induced LTR activity by transfecting a wild-type and NFAT5 mutant LTR reporter construct into THP-1 cells, followed by stimulation with an MTb lysate. As shown in Figure 1B, in the absence of MTb lysate stimulation the activity of the NFAT5 binding site-mutant LTR was significantly reduced (p\u003c0.05) in comparison to the wild-type LTR. When the NFAT5 binding site-mutant LTR was examined in THP-1 cells stimulated with the MTb lysate, its activity was reduced to an even more significant extent (p\u003c0.01)."}
bionlp-st-ge-2016-test-ihmc
{"project":"bionlp-st-ge-2016-test-ihmc","denotations":[{"id":"T8080","span":{"begin":610,"end":642},"obj":"Binding"},{"id":"T8078","span":{"begin":723,"end":745},"obj":"Binding"},{"id":"T8076","span":{"begin":250,"end":270},"obj":"Binding"},{"id":"T8075","span":{"begin":302,"end":335},"obj":"Binding"},{"id":"T8072","span":{"begin":674,"end":676},"obj":"Entity"},{"id":"T8068","span":{"begin":219,"end":225},"obj":"Protein"},{"id":"T8067","span":{"begin":128,"end":145},"obj":"Entity"},{"id":"T8066","span":{"begin":9,"end":39},"obj":"Protein"},{"id":"T8065","span":{"begin":262,"end":270},"obj":"Protein"},{"id":"T8064","span":{"begin":610,"end":642},"obj":"Entity"},{"id":"T8062","span":{"begin":378,"end":381},"obj":"Protein"},{"id":"T8061","span":{"begin":172,"end":174},"obj":"Entity"},{"id":"T8060","span":{"begin":179,"end":197},"obj":"Protein"},{"id":"T8058","span":{"begin":727,"end":732},"obj":"Protein"},{"id":"T8057","span":{"begin":13,"end":33},"obj":"Protein"},{"id":"T8054","span":{"begin":161,"end":175},"obj":"Entity"},{"id":"T8052","span":{"begin":521,"end":524},"obj":"Protein"},{"id":"T8051","span":{"begin":723,"end":745},"obj":"Entity"},{"id":"T8050","span":{"begin":310,"end":330},"obj":"Protein"},{"id":"T8048","span":{"begin":574,"end":577},"obj":"Protein"},{"id":"T8047","span":{"begin":219,"end":225},"obj":"Entity"},{"id":"T8046","span":{"begin":368,"end":381},"obj":"Protein"},{"id":"T8043","span":{"begin":773,"end":815},"obj":"Entity"},{"id":"T8042","span":{"begin":435,"end":440},"obj":"Protein"},{"id":"T8041","span":{"begin":51,"end":55},"obj":"Entity"},{"id":"T8040","span":{"begin":805,"end":808},"obj":"Protein"}],"relations":[{"id":"R6466","pred":"themeOf","subj":"T8050","obj":"T8075"},{"id":"R6467","pred":"themeOf","subj":"T8051","obj":"T8078"},{"id":"R6468","pred":"themeOf","subj":"T8064","obj":"T8080"},{"id":"R6469","pred":"themeOf","subj":"T8065","obj":"T8076"}],"text":"Although the transcription factor NFAT5 binds to a core NF-κB binding motif in the HIV-1 LTR enhancer region of subtype B, when two thymines (TT) are changed to cytosines (CC) in the proximal NF-κB binding motif (named N5-Mut) (bottom of Figure 1B), the binding of NFAT5 can be disrupted while leaving binding of NF-κB unperturbed [31]. We examined the requirement of NFAT5 for MTb-induced LTR activity by transfecting a wild-type and NFAT5 mutant LTR reporter construct into THP-1 cells, followed by stimulation with an MTb lysate. As shown in Figure 1B, in the absence of MTb lysate stimulation the activity of the NFAT5 binding site-mutant LTR was significantly reduced (p\u003c0.05) in comparison to the wild-type LTR. When the NFAT5 binding site-mutant LTR was examined in THP-1 cells stimulated with the MTb lysate, its activity was reduced to an even more significant extent (p\u003c0.01)."}
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the transcription factor NFAT5 binds to a core NF-κB binding motif in the HIV-1 LTR enhancer region of subtype B, when two thymines (TT) are changed to cytosines (CC) in the proximal NF-κB binding motif (named N5-Mut) (bottom of Figure 1B), the binding of NFAT5 can be disrupted while leaving binding of NF-κB unperturbed [31]. We examined the requirement of NFAT5 for MTb-induced LTR activity by transfecting a wild-type and NFAT5 mutant LTR reporter construct into THP-1 cells, followed by stimulation with an MTb lysate. As shown in Figure 1B, in the absence of MTb lysate stimulation the activity of the NFAT5 binding site-mutant LTR was significantly reduced (p\u003c0.05) in comparison to the wild-type LTR. When the NFAT5 binding site-mutant LTR was examined in THP-1 cells stimulated with the MTb lysate, its activity was reduced to an even more significant extent (p\u003c0.01)."}
bionlp-st-ge-2016-test-tees
{"project":"bionlp-st-ge-2016-test-tees","denotations":[{"id":"T7707","span":{"begin":727,"end":756},"obj":"Protein"},{"id":"T7706","span":{"begin":665,"end":672},"obj":"Negative_regulation"},{"id":"T7705","span":{"begin":617,"end":646},"obj":"Protein"},{"id":"T7704","span":{"begin":353,"end":364},"obj":"Positive_regulation"},{"id":"T7703","span":{"begin":435,"end":451},"obj":"Protein"},{"id":"T7702","span":{"begin":378,"end":381},"obj":"Protein"},{"id":"T7701","span":{"begin":368,"end":373},"obj":"Protein"},{"id":"T7700","span":{"begin":302,"end":309},"obj":"Binding"},{"id":"T7699","span":{"begin":254,"end":261},"obj":"Binding"},{"id":"T7698","span":{"begin":40,"end":45},"obj":"Binding"},{"id":"T7697","span":{"begin":40,"end":45},"obj":"Binding"},{"id":"T7696","span":{"begin":313,"end":318},"obj":"Protein"},{"id":"T7695","span":{"begin":265,"end":270},"obj":"Protein"},{"id":"T7694","span":{"begin":222,"end":225},"obj":"Protein"},{"id":"T7693","span":{"begin":219,"end":221},"obj":"Protein"},{"id":"T7691","span":{"begin":56,"end":75},"obj":"Protein"},{"id":"T7690","span":{"begin":34,"end":39},"obj":"Protein"},{"id":"T7692","span":{"begin":192,"end":211},"obj":"Protein"}],"relations":[{"id":"R6159","pred":"themeOf","subj":"T7690","obj":"T7697"},{"id":"R6160","pred":"themeOf","subj":"T7690","obj":"T7698"},{"id":"R6161","pred":"themeOf","subj":"T7691","obj":"T7698"},{"id":"R6162","pred":"themeOf","subj":"T7695","obj":"T7699"},{"id":"R6163","pred":"themeOf","subj":"T7696","obj":"T7700"},{"id":"R6164","pred":"themeOf","subj":"T7701","obj":"T7704"},{"id":"R6165","pred":"themeOf","subj":"T7705","obj":"T7706"}],"text":"Although the transcription factor NFAT5 binds to a core NF-κB binding motif in the HIV-1 LTR enhancer region of subtype B, when two thymines (TT) are changed to cytosines (CC) in the proximal NF-κB binding motif (named N5-Mut) (bottom of Figure 1B), the binding of NFAT5 can be disrupted while leaving binding of NF-κB unperturbed [31]. We examined the requirement of NFAT5 for MTb-induced LTR activity by transfecting a wild-type and NFAT5 mutant LTR reporter construct into THP-1 cells, followed by stimulation with an MTb lysate. As shown in Figure 1B, in the absence of MTb lysate stimulation the activity of the NFAT5 binding site-mutant LTR was significantly reduced (p\u003c0.05) in comparison to the wild-type LTR. When the NFAT5 binding site-mutant LTR was examined in THP-1 cells stimulated with the MTb lysate, its activity was reduced to an even more significant extent (p\u003c0.01)."}
testone
{"project":"testone","denotations":[{"id":"T7276","span":{"begin":665,"end":672},"obj":"Negative_regulation"},{"id":"T7275","span":{"begin":563,"end":570},"obj":"Negative_regulation"},{"id":"T7274","span":{"begin":302,"end":309},"obj":"Binding"},{"id":"T7273","span":{"begin":278,"end":287},"obj":"Negative_regulation"},{"id":"T7272","span":{"begin":254,"end":261},"obj":"Binding"},{"id":"T7271","span":{"begin":40,"end":45},"obj":"Binding"},{"id":"T7266","span":{"begin":368,"end":373},"obj":"Protein"},{"id":"T7265","span":{"begin":265,"end":270},"obj":"Protein"},{"id":"T7264","span":{"begin":34,"end":39},"obj":"Protein"}],"relations":[{"id":"R5842","pred":"themeOf","subj":"T7264","obj":"T7271"},{"id":"R5843","pred":"themeOf","subj":"T7265","obj":"T7272"},{"id":"R5845","pred":"themeOf","subj":"T7272","obj":"T7273"}],"text":"Although the transcription factor NFAT5 binds to a core NF-κB binding motif in the HIV-1 LTR enhancer region of subtype B, when two thymines (TT) are changed to cytosines (CC) in the proximal NF-κB binding motif (named N5-Mut) (bottom of Figure 1B), the binding of NFAT5 can be disrupted while leaving binding of NF-κB unperturbed [31]. We examined the requirement of NFAT5 for MTb-induced LTR activity by transfecting a wild-type and NFAT5 mutant LTR reporter construct into THP-1 cells, followed by stimulation with an MTb lysate. As shown in Figure 1B, in the absence of MTb lysate stimulation the activity of the NFAT5 binding site-mutant LTR was significantly reduced (p\u003c0.05) in comparison to the wild-type LTR. When the NFAT5 binding site-mutant LTR was examined in THP-1 cells stimulated with the MTb lysate, its activity was reduced to an even more significant extent (p\u003c0.01)."}
test3
{"project":"test3","denotations":[{"id":"T7292","span":{"begin":368,"end":373},"obj":"Protein"},{"id":"T7291","span":{"begin":265,"end":270},"obj":"Protein"},{"id":"T7290","span":{"begin":40,"end":45},"obj":"Binding"},{"id":"T7289","span":{"begin":34,"end":39},"obj":"Protein"},{"id":"T7283","span":{"begin":368,"end":373},"obj":"Protein"},{"id":"T7282","span":{"begin":265,"end":270},"obj":"Protein"},{"id":"T7281","span":{"begin":34,"end":39},"obj":"Protein"}],"relations":[{"id":"R5847","pred":"themeOf","subj":"T7289","obj":"T7290"}],"text":"Although the transcription factor NFAT5 binds to a core NF-κB binding motif in the HIV-1 LTR enhancer region of subtype B, when two thymines (TT) are changed to cytosines (CC) in the proximal NF-κB binding motif (named N5-Mut) (bottom of Figure 1B), the binding of NFAT5 can be disrupted while leaving binding of NF-κB unperturbed [31]. We examined the requirement of NFAT5 for MTb-induced LTR activity by transfecting a wild-type and NFAT5 mutant LTR reporter construct into THP-1 cells, followed by stimulation with an MTb lysate. As shown in Figure 1B, in the absence of MTb lysate stimulation the activity of the NFAT5 binding site-mutant LTR was significantly reduced (p\u003c0.05) in comparison to the wild-type LTR. When the NFAT5 binding site-mutant LTR was examined in THP-1 cells stimulated with the MTb lysate, its activity was reduced to an even more significant extent (p\u003c0.01)."}