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By reducing the levels of TRADD, wild type CFTR suppresses downstream proinflammatory NFkappaB signaling.
NPM (show NPM1 Proteins)-RAR (show RARA Proteins) binding to TRADD selectively inhibits caspase (show CASP3 Proteins) activation, while allowing activation of NFkappaB (show NFKB1 Proteins) and JNK (show MAPK8 Proteins)
The release of extracellular vesicles was triggered by TNFA (show TNF Proteins) from BEAS-2b cells.TNFA-triggered extracellular vesicles contained TNFR1 (show TNFRSF1A Proteins) and TRADD.
MicroRNA-30c-2-3p negatively regulates NF-kappaB (show NFKB1 Proteins) signaling and cell cycle progression through downregulation of TRADD and CCNE1 (show CCNE1 Proteins) in breast cancer.
domains of calmodulin (show CALM1 Proteins) mediate FADD (show FADD Proteins) and TRADD interaction
PA induced the apoptosis of HUVECs by initiating the death pathway (TNF-R1 (show TNFRSF1A Proteins)/TRADD/caspases 8 pathway), whereas AA enhanced cell survival to protect vascular endothelial cells by activating the survival pathway (TNF-R1 (show TNFRSF1A Proteins)/RIP (show HRB Proteins)/NF-kappaB (show NFKB1 Proteins) 50/NF-kappaB (show NFKB1 Proteins) 65).
Biologic assessment found that NPM (show NPM1 Proteins)-RAR (show RARA Proteins) expression impaired TNF (show TNF Proteins)-induced signaling through TRADD, blunting TNF (show TNF Proteins)-mediated activation of caspase-3 (CASP3 (show CASP3 Proteins)) and caspase-8 (CASP8 (show CASP8 Proteins)), to ultimately block apoptosis.
TRADD gene expression was knocked down by an antisense oligonucleotide.
structure-based mutations of TNFR-1 (show TNFRSF1A Proteins) (P367A and P368A), TRADD (F266A), and RIP1 (show UQCRFS1 Proteins) (M637A and R638A) disrupted formation of the death domain (DD) complex and prevented stable interactions among those DDs
Data indicate that the (show MAP3K5 Proteins)ASK1-FoxO3a-TRADD-caspase 8 pathway is present in neural tube defects (show FOXO3 Proteins)(NTDs)-affected tissues.
Data indicate that ASK1 (show MAP3K5 Proteins) activation stimulated the activity of the transcription factor FoxO3a (show FOXO3 Proteins), which increased the abundance of the apoptosis-promoting adaptor protein TRADD, leading to activation of caspase 8 (show CASP8 Proteins).
data indicate that TRADD shuttles dynamically from the cytoplasm into the nucleus to modulate the interaction between p19(Arf) and its E3 ubiquitin ligase ULF, thereby promoting p19(Arf) protein stability and tumour suppression
Data suggest that deficiency of TRADD sensitizes cells to TRAIL-induced apoptosis, and that enhanced cell death in TRADD(-/-) MEFs is associated with defective NF-kappaB (show NFKB1 Proteins) activation.
TRADD is required for recruitment of receptor interacting protein 1 (show RIPK1 Proteins) and TNFR (show TNFRSF1A Proteins)-associated factor 2 to the DR3 (show TNFRSF25 Proteins) signaling complex and for the ubiquitination of receptor interacting protein 1 (show RIPK1 Proteins)
We show that TRADD is recruited to the TRAIL-receptor complex, and RIP1 (show RALBP1 Proteins) recruitment is mediated by TRADD.
TRADD may be involved in IFN-gamma (show IFNG Proteins) signaling by forming a complex with STAT1 (show STAT1 Proteins)-alpha within the nucleus and regulating IFN-gamma (show IFNG Proteins)-mediated STAT1 (show STAT1 Proteins)-alpha activation.
Tradd activates distinct mechanisms of apoptosis from the nucleus and the cytoplasm.
silencing TRADD expression with small-interfering RNA reduced neuronal apoptosis and subsequent microglial and astroglial activation
TRADD is a multifunctional protein crucial both for TNFR1 (show TNFRSF1A Proteins) signaling and other signaling pathways relevant to immune responses.
TNF (show TNF Proteins) binding induces release of AIP1 (DAB2IP (show DAB2IP Proteins)) from TNFR1 (show TNFRSF1A Proteins), resulting in cytoplasmic translocation and concomitant formation of an intracellular signaling complex comprised of TRADD, RIP1 (show RALBP1 Proteins), TRAF2 (show TRAF2 Proteins), and AIPl.
The protein encoded by this gene is a death domain containing adaptor molecule that interacts with TNFRSF1A/TNFR1 and mediates programmed cell death signaling and NF-kappaB activation. This protein binds adaptor protein TRAF2, reduces the recruitment of inhibitor-of-apoptosis proteins (IAPs) by TRAF2, and thus suppresses TRAF2 mediated apoptosis. This protein can also interact with receptor TNFRSF6/FAS and adaptor protein FADD/MORT1, and is involved in the Fas-induced cell death pathway.
TNFRSF1A-associated via death domain
, conjugal transfer protein D
, TNFR1-associated death domain protein
, tumor necrosis factor receptor type 1 associated death domain protein
, tumor necrosis factor receptor type 1-associated DEATH domain protein
, tumor necrosis factor receptor-1-associated protein
, TNF receptor 1 associated signal transducer
, TNFR1-associated DEATH domain protein
, Tumor necrosis factor receptor type 1-associated DEATH domain protein
, TNFRSF1A-associated via death domain protein