PubMed:8565075 JSONTXT

{"project":"AIMed","denotations":[{"id":"T1","span":{"begin":0,"end":5},"obj":"protein"},{"id":"T2","span":{"begin":6,"end":11},"obj":"protein"},{"id":"T3","span":{"begin":16,"end":21},"obj":"protein"},{"id":"T4","span":{"begin":22,"end":26},"obj":"protein"},{"id":"T5","span":{"begin":60,"end":74},"obj":"protein"},{"id":"T6","span":{"begin":167,"end":177},"obj":"protein"},{"id":"T7","span":{"begin":220,"end":234},"obj":"protein"},{"id":"T8","span":{"begin":236,"end":241},"obj":"protein"},{"id":"T9","span":{"begin":244,"end":249},"obj":"protein"},{"id":"T10","span":{"begin":255,"end":260},"obj":"protein"},{"id":"T11","span":{"begin":354,"end":359},"obj":"protein"},{"id":"T12","span":{"begin":384,"end":389},"obj":"protein"},{"id":"T13","span":{"begin":394,"end":398},"obj":"protein"},{"id":"T14","span":{"begin":433,"end":443},"obj":"protein"},{"id":"T15","span":{"begin":482,"end":487},"obj":"protein"},{"id":"T16","span":{"begin":586,"end":596},"obj":"protein"},{"id":"T17","span":{"begin":666,"end":670},"obj":"protein"},{"id":"T18","span":{"begin":796,"end":806},"obj":"protein"},{"id":"T19","span":{"begin":835,"end":840},"obj":"protein"},{"id":"T20","span":{"begin":841,"end":846},"obj":"protein"},{"id":"T21","span":{"begin":889,"end":894},"obj":"protein"}],"text":"TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 signal transduction pathways.\nTumor necrosis factor (TNF) can induce apoptosis and activate NF-kappa B through signaling cascades emanating from TNF receptor 1 (TNFR1). TRADD is a TNFR1-associated signal transducer that is involved in activating both pathways. Here we show that TRADD directly interacts with TRAF2 and FADD, signal transducers that activate NF-kappa B and induce apoptosis, respectively. A TRAF2 mutant lacking its N-terminal RING finger domain is a dominant-negative inhibitor of TNF-mediated NF-kappa B activation, but does not affect TNF-induced apoptosis. Conversely, a FADD mutant lacking its N-terminal 79 amino acids is a dominant-negative inhibitor of TNF-induced apoptosis, but does not inhibit NF-kappa B activation. Thus, these two TNFR1-TRADD signaling cascades appear to bifurcate at TRADD."}

{"project":"HP-phenotype","denotations":[{"id":"T1","span":{"begin":105,"end":110},"obj":"Phenotype"}],"attributes":[{"id":"A1","pred":"hp_id","subj":"T1","obj":"HP:0002664"}],"namespaces":[{"prefix":"HP","uri":"http://purl.obolibrary.org/obo/HP_"}],"text":"TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 signal transduction pathways.\nTumor necrosis factor (TNF) can induce apoptosis and activate NF-kappa B through signaling cascades emanating from TNF receptor 1 (TNFR1). TRADD is a TNFR1-associated signal transducer that is involved in activating both pathways. Here we show that TRADD directly interacts with TRAF2 and FADD, signal transducers that activate NF-kappa B and induce apoptosis, respectively. A TRAF2 mutant lacking its N-terminal RING finger domain is a dominant-negative inhibitor of TNF-mediated NF-kappa B activation, but does not affect TNF-induced apoptosis. Conversely, a FADD mutant lacking its N-terminal 79 amino acids is a dominant-negative inhibitor of TNF-induced apoptosis, but does not inhibit NF-kappa B activation. Thus, these two TNFR1-TRADD signaling cascades appear to bifurcate at TRADD."}

{"project":"mondo_disease","denotations":[{"id":"T1","span":{"begin":105,"end":110},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0005070"}],"text":"TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 signal transduction pathways.\nTumor necrosis factor (TNF) can induce apoptosis and activate NF-kappa B through signaling cascades emanating from TNF receptor 1 (TNFR1). TRADD is a TNFR1-associated signal transducer that is involved in activating both pathways. Here we show that TRADD directly interacts with TRAF2 and FADD, signal transducers that activate NF-kappa B and induce apoptosis, respectively. A TRAF2 mutant lacking its N-terminal RING finger domain is a dominant-negative inhibitor of TNF-mediated NF-kappa B activation, but does not affect TNF-induced apoptosis. Conversely, a FADD mutant lacking its N-terminal 79 amino acids is a dominant-negative inhibitor of TNF-induced apoptosis, but does not inhibit NF-kappa B activation. Thus, these two TNFR1-TRADD signaling cascades appear to bifurcate at TRADD."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":518,"end":529},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0003624"}],"text":"TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 signal transduction pathways.\nTumor necrosis factor (TNF) can induce apoptosis and activate NF-kappa B through signaling cascades emanating from TNF receptor 1 (TNFR1). TRADD is a TNFR1-associated signal transducer that is involved in activating both pathways. Here we show that TRADD directly interacts with TRAF2 and FADD, signal transducers that activate NF-kappa B and induce apoptosis, respectively. A TRAF2 mutant lacking its N-terminal RING finger domain is a dominant-negative inhibitor of TNF-mediated NF-kappa B activation, but does not affect TNF-induced apoptosis. Conversely, a FADD mutant lacking its N-terminal 79 amino acids is a dominant-negative inhibitor of TNF-induced apoptosis, but does not inhibit NF-kappa B activation. Thus, these two TNFR1-TRADD signaling cascades appear to bifurcate at TRADD."}