PMC:3062687 / 4044-5021 JSON TXT

Annnotations TAB JSON ListView MergeView

bionlp-st-ge-2016-uniprot

{"project":"bionlp-st-ge-2016-uniprot","denotations":[{"id":"T2807","span":{"begin":0,"end":4},"obj":"P23396"},{"id":"T2808","span":{"begin":9,"end":13},"obj":"O14920"},{"id":"T2809","span":{"begin":155,"end":159},"obj":"O14920"},{"id":"T2810","span":{"begin":278,"end":282},"obj":"P23396"},{"id":"T2811","span":{"begin":315,"end":318},"obj":"P21579"},{"id":"T2812","span":{"begin":315,"end":318},"obj":"Q04206"},{"id":"T2813","span":{"begin":319,"end":322},"obj":"P19838"},{"id":"T2814","span":{"begin":323,"end":327},"obj":"P25963"},{"id":"T2815","span":{"begin":397,"end":401},"obj":"O14920"},{"id":"T2816","span":{"begin":439,"end":443},"obj":"P23396"},{"id":"T2817","span":{"begin":488,"end":492},"obj":"O14920"},{"id":"T2818","span":{"begin":497,"end":501},"obj":"P23396"},{"id":"T2819","span":{"begin":595,"end":599},"obj":"O14920"},{"id":"T2820","span":{"begin":600,"end":604},"obj":"P23396"},{"id":"T2821","span":{"begin":731,"end":735},"obj":"P23396"},{"id":"T2822","span":{"begin":736,"end":740},"obj":"O14920"},{"id":"T2823","span":{"begin":780,"end":783},"obj":"P01375"},{"id":"T2824","span":{"begin":857,"end":861},"obj":"P23396"},{"id":"T2825","span":{"begin":953,"end":957},"obj":"P23396"}],"namespaces":[{"prefix":"_base","uri":"http://www.uniprot.org/uniprot/"}],"text":"RPS3 and IKKβ interaction\nThe activation of the inhibitor of κB kinase (IKK), consisting of a regulatory subunit IKKγ and two catalytic subunits, IKKα and IKKβ, is critical for the phosphorylation and dispatch of the inhibitory IκBs and the liberation of NF-κB20-22. Given that RPS3 can be found in the cytoplasmic p65-p50-IκBα inhibitory complex in resting cells6, we hypothesized that activated IKKβ might also bind to and phosphorylate RPS3. First, we found that ectopically expressed IKKβ and RPS3 interacted (Fig. 1c). We next examined resting Jurkat cells and detected a modest endogenous IKKβ-RPS3 interaction (Fig. 1d), potentially accounting for the basal NF-κB transcription required for cell proliferation and survival. RPS3-IKKβ association was clearly augmented upon TNF stimulation, peaking at 10 min. (Fig. 1d), following similar kinetics to RPS3 serine phosphorylation (Fig. 1b). By contrast, there was no detectable interaction between RPS3 and IKKα (Fig. 1d)."}

2_test

{"project":"2_test","denotations":[{"id":"21399639-17072322-74765153","span":{"begin":260,"end":262},"obj":"17072322"},{"id":"21399639-17072322-74765153","span":{"begin":260,"end":262},"obj":"17072322"},{"id":"21399639-10602462-74765153","span":{"begin":260,"end":262},"obj":"10602462"},{"id":"21399639-10602462-74765153","span":{"begin":260,"end":262},"obj":"10602462"},{"id":"21399639-10740266-74765153","span":{"begin":260,"end":262},"obj":"10740266"},{"id":"21399639-10740266-74765153","span":{"begin":260,"end":262},"obj":"10740266"},{"id":"21399639-18045535-74765154","span":{"begin":363,"end":364},"obj":"18045535"},{"id":"21399639-18045535-74765154","span":{"begin":363,"end":364},"obj":"18045535"}],"text":"RPS3 and IKKβ interaction\nThe activation of the inhibitor of κB kinase (IKK), consisting of a regulatory subunit IKKγ and two catalytic subunits, IKKα and IKKβ, is critical for the phosphorylation and dispatch of the inhibitory IκBs and the liberation of NF-κB20-22. Given that RPS3 can be found in the cytoplasmic p65-p50-IκBα inhibitory complex in resting cells6, we hypothesized that activated IKKβ might also bind to and phosphorylate RPS3. First, we found that ectopically expressed IKKβ and RPS3 interacted (Fig. 1c). We next examined resting Jurkat cells and detected a modest endogenous IKKβ-RPS3 interaction (Fig. 1d), potentially accounting for the basal NF-κB transcription required for cell proliferation and survival. RPS3-IKKβ association was clearly augmented upon TNF stimulation, peaking at 10 min. (Fig. 1d), following similar kinetics to RPS3 serine phosphorylation (Fig. 1b). By contrast, there was no detectable interaction between RPS3 and IKKα (Fig. 1d)."}

pmc-enju-pas

bionlp-st-ge-2016-spacy-parsed

GO-BP

{"project":"GO-BP","denotations":[{"id":"T3039","span":{"begin":30,"end":63},"obj":"http://purl.obolibrary.org/obo/GO_1903721"},{"id":"T3040","span":{"begin":72,"end":75},"obj":"http://purl.obolibrary.org/obo/GO_0008384"},{"id":"T3041","span":{"begin":181,"end":196},"obj":"http://purl.obolibrary.org/obo/GO_0016310"},{"id":"T3042","span":{"begin":869,"end":884},"obj":"http://purl.obolibrary.org/obo/GO_0016310"},{"id":"T3043","span":{"begin":671,"end":684},"obj":"http://purl.obolibrary.org/obo/GO_0006351"},{"id":"T3044","span":{"begin":698,"end":716},"obj":"http://purl.obolibrary.org/obo/GO_0008283"}],"text":"RPS3 and IKKβ interaction\nThe activation of the inhibitor of κB kinase (IKK), consisting of a regulatory subunit IKKγ and two catalytic subunits, IKKα and IKKβ, is critical for the phosphorylation and dispatch of the inhibitory IκBs and the liberation of NF-κB20-22. Given that RPS3 can be found in the cytoplasmic p65-p50-IκBα inhibitory complex in resting cells6, we hypothesized that activated IKKβ might also bind to and phosphorylate RPS3. First, we found that ectopically expressed IKKβ and RPS3 interacted (Fig. 1c). We next examined resting Jurkat cells and detected a modest endogenous IKKβ-RPS3 interaction (Fig. 1d), potentially accounting for the basal NF-κB transcription required for cell proliferation and survival. RPS3-IKKβ association was clearly augmented upon TNF stimulation, peaking at 10 min. (Fig. 1d), following similar kinetics to RPS3 serine phosphorylation (Fig. 1b). By contrast, there was no detectable interaction between RPS3 and IKKα (Fig. 1d)."}

GO-MF

{"project":"GO-MF","denotations":[{"id":"T3045","span":{"begin":72,"end":75},"obj":"http://purl.obolibrary.org/obo/GO_0008384"}],"text":"RPS3 and IKKβ interaction\nThe activation of the inhibitor of κB kinase (IKK), consisting of a regulatory subunit IKKγ and two catalytic subunits, IKKα and IKKβ, is critical for the phosphorylation and dispatch of the inhibitory IκBs and the liberation of NF-κB20-22. Given that RPS3 can be found in the cytoplasmic p65-p50-IκBα inhibitory complex in resting cells6, we hypothesized that activated IKKβ might also bind to and phosphorylate RPS3. First, we found that ectopically expressed IKKβ and RPS3 interacted (Fig. 1c). We next examined resting Jurkat cells and detected a modest endogenous IKKβ-RPS3 interaction (Fig. 1d), potentially accounting for the basal NF-κB transcription required for cell proliferation and survival. RPS3-IKKβ association was clearly augmented upon TNF stimulation, peaking at 10 min. (Fig. 1d), following similar kinetics to RPS3 serine phosphorylation (Fig. 1b). By contrast, there was no detectable interaction between RPS3 and IKKα (Fig. 1d)."}

GO-CC

{"project":"GO-CC","denotations":[{"id":"T3046","span":{"begin":556,"end":561},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T3047","span":{"begin":698,"end":702},"obj":"http://purl.obolibrary.org/obo/GO_0005623"}],"text":"RPS3 and IKKβ interaction\nThe activation of the inhibitor of κB kinase (IKK), consisting of a regulatory subunit IKKγ and two catalytic subunits, IKKα and IKKβ, is critical for the phosphorylation and dispatch of the inhibitory IκBs and the liberation of NF-κB20-22. Given that RPS3 can be found in the cytoplasmic p65-p50-IκBα inhibitory complex in resting cells6, we hypothesized that activated IKKβ might also bind to and phosphorylate RPS3. First, we found that ectopically expressed IKKβ and RPS3 interacted (Fig. 1c). We next examined resting Jurkat cells and detected a modest endogenous IKKβ-RPS3 interaction (Fig. 1d), potentially accounting for the basal NF-κB transcription required for cell proliferation and survival. RPS3-IKKβ association was clearly augmented upon TNF stimulation, peaking at 10 min. (Fig. 1d), following similar kinetics to RPS3 serine phosphorylation (Fig. 1b). By contrast, there was no detectable interaction between RPS3 and IKKα (Fig. 1d)."}

sentences

{"project":"sentences","denotations":[{"id":"T2634","span":{"begin":0,"end":25},"obj":"Sentence"},{"id":"T2635","span":{"begin":26,"end":266},"obj":"Sentence"},{"id":"T2636","span":{"begin":267,"end":444},"obj":"Sentence"},{"id":"T2637","span":{"begin":445,"end":523},"obj":"Sentence"},{"id":"T2638","span":{"begin":524,"end":730},"obj":"Sentence"},{"id":"T2639","span":{"begin":731,"end":895},"obj":"Sentence"},{"id":"T2640","span":{"begin":896,"end":977},"obj":"Sentence"},{"id":"T31","span":{"begin":0,"end":25},"obj":"Sentence"},{"id":"T32","span":{"begin":26,"end":266},"obj":"Sentence"},{"id":"T33","span":{"begin":267,"end":444},"obj":"Sentence"},{"id":"T34","span":{"begin":445,"end":523},"obj":"Sentence"},{"id":"T35","span":{"begin":524,"end":730},"obj":"Sentence"},{"id":"T36","span":{"begin":731,"end":895},"obj":"Sentence"},{"id":"T37","span":{"begin":896,"end":977},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"RPS3 and IKKβ interaction\nThe activation of the inhibitor of κB kinase (IKK), consisting of a regulatory subunit IKKγ and two catalytic subunits, IKKα and IKKβ, is critical for the phosphorylation and dispatch of the inhibitory IκBs and the liberation of NF-κB20-22. Given that RPS3 can be found in the cytoplasmic p65-p50-IκBα inhibitory complex in resting cells6, we hypothesized that activated IKKβ might also bind to and phosphorylate RPS3. First, we found that ectopically expressed IKKβ and RPS3 interacted (Fig. 1c). We next examined resting Jurkat cells and detected a modest endogenous IKKβ-RPS3 interaction (Fig. 1d), potentially accounting for the basal NF-κB transcription required for cell proliferation and survival. RPS3-IKKβ association was clearly augmented upon TNF stimulation, peaking at 10 min. (Fig. 1d), following similar kinetics to RPS3 serine phosphorylation (Fig. 1b). By contrast, there was no detectable interaction between RPS3 and IKKα (Fig. 1d)."}

events-check-again

bionlp-st-ge-2016-reference-tees

bionlp-st-ge-2016-reference

test2

PMC:3062687 / 4044-5021 JSONTXT

Annnotations TAB JSON ListView MergeView

PMC:3062687 / 4044-5021 JSON TXT