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anti-Human TRADD Antikörper:
anti-Mouse (Murine) TRADD Antikörper:
anti-Rat (Rattus) TRADD Antikörper:
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Human Monoclonal TRADD Primary Antibody für FACS, WB - ABIN4899051
Kolliputi, Waxman: IL-6 cytoprotection in hyperoxic acute lung injury occurs via suppressor of cytokine signaling-1-induced apoptosis signal-regulating kinase-1 degradation. in American journal of respiratory cell and molecular biology 2009
Human Polyclonal TRADD Primary Antibody für IHC (fro), IP - ABIN549593
Chen, Texada, Duggan, Liang, Reden, Kooragayala, Langford: Surface calreticulin mediates muramyl dipeptide-induced apoptosis in RK13 cells. in The Journal of biological chemistry 2005
Human Polyclonal TRADD Primary Antibody für IF (p), IHC (p) - ABIN673314
Chen, Zhang, Zhang, Li, Sun: Hydrogen sulfide protects against TNF-α induced neuronal cell apoptosis through miR-485-5p/TRADD signaling. in Biochemical and biophysical research communications 2016
The TRADD C-terminal death domain comprises two super-secondary structures, an all-helix Greek key motif and a beta-hairpin motif flanked by two alpha helices, which make it unique among all known C-terminal death domain structures.
Translocation of TRADD to DSBs into the nucleus contributes to cell survival in response to DNA damage through an activation of NHEJ DNA repair.
potential biological significance of TRADD mediated inflammatory response in the development of uterine leiomyoma, is reported.
we found that ORF3 protein downregulates TLR3-mediated NF-kappaB signaling via TRADD and RIP1. Our findings provide a new perspective on the cellular response in HEV infection and expand our understanding of the molecular mechanisms of Hepatitis E virus (HEV) pathogenesis in innate immunity.
In conclusion, for the first time, we report that TRADD, TRAF2, RIP1 and TAK1 play a role in the regulating TNF-alpha signalling in human myometrium. These findings are of significance given the central role of TNF-alpha in the processes of human labour and delivery.
These data for the first time identifies miR-485-5p/TRADD axis in hydrogen sulfide protecting against TNF-alpha-induced neuronal cell apoptosis.
By reducing the levels of TRADD, wild type CFTR suppresses downstream proinflammatory NFkappaB signaling.
NPM-RAR binding to TRADD selectively inhibits caspase activation, while allowing activation of NFkappaB and JNK
The release of extracellular vesicles was triggered by TNFA from BEAS-2b cells.TNFA-triggered extracellular vesicles contained TNFR1 and TRADD.
MicroRNA-30c-2-3p negatively regulates NF-kappaB signaling and cell cycle progression through downregulation of TRADD and CCNE1 in breast cancer.
domains of calmodulin mediate FADD and TRADD interaction
PA induced the apoptosis of HUVECs by initiating the death pathway (TNF-R1/TRADD/caspases 8 pathway), whereas AA enhanced cell survival to protect vascular endothelial cells by activating the survival pathway (TNF-R1/RIP/NF-kappaB 50/NF-kappaB 65).
Biologic assessment found that NPM-RAR expression impaired TNF-induced signaling through TRADD, blunting TNF-mediated activation of caspase-3 (CASP3) and caspase-8 (CASP8), to ultimately block apoptosis.
TRADD gene expression was knocked down by an antisense oligonucleotide.
structure-based mutations of TNFR-1 (P367A and P368A), TRADD (F266A), and RIP1 (M637A and R638A) disrupted formation of the death domain (DD) complex and prevented stable interactions among those DDs
Data indicate that the ASK1-FoxO3a-TRADD-caspase 8 pathway is present in neural tube defects (NTDs)-affected tissues.
we demonstrated that the association between DR6 and TRADD was enhanced upon DQM3 stimulation and TRADD was involved in DR6-induced signaling activation
Data indicate that silencing tumor necrosis factor receptor 1 (TNFR1)-associated death domain protein (TRADD) in glioma cells results in decreased NF-kappaB activity, decreased proliferation of cells, and increased sensitivity to temozolomide.
death domains in several proteins, including TRADD, FADD, RIPK1 and TNFR1, were directly inactivated by NleB, an enteropathogenic Escherichia coli (EPEC) type III secretion system effector known to inhibit host nuclear factor-kappaB (NF-kappaB) signalling
rpS3 appears to be recruited to the death-inducing signaling complex (DISC) to induce apoptosis by interacting TRADD in response to extracellular stresses.
TRADD knockout blunts pressure overload-induced cardiac hypertrophy through mediating TAK1/p38 MAPK but not AKT phosphorylation
Data indicate that ASK1 activation stimulated the activity of the transcription factor FoxO3a, which increased the abundance of the apoptosis-promoting adaptor protein TRADD, leading to activation of caspase 8.
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 activation.
TRADD is required for recruitment of receptor interacting protein 1 and TNFR-associated factor 2 to the DR3 signaling complex and for the ubiquitination of receptor interacting protein 1
We show that TRADD is recruited to the TRAIL-receptor complex, and RIP1 recruitment is mediated by TRADD.
TRADD may be involved in IFN-gamma signaling by forming a complex with STAT1-alpha within the nucleus and regulating IFN-gamma-mediated STAT1-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 signaling and other signaling pathways relevant to immune responses.
TNF binding induces release of AIP1 (DAB2IP) from TNFR1, resulting in cytoplasmic translocation and concomitant formation of an intracellular signaling complex comprised of TRADD, RIP1, TRAF2, 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