Browse our anti-TRADD (TRADD) Antibodies

Human TNFRSF1A-Associated Via Death Domain (TRADD) interaction partners

1. 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.

2. Translocation of TRADD to DSBs into the nucleus contributes to cell survival in response to DNA damage through an activation of NHEJ DNA repair.

3. potential biological significance of TRADD mediated inflammatory response in the development of uterine leiomyoma, is reported.

4. 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.

5. 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.

6. These data for the first time identifies miR-485-5p/TRADD axis in hydrogen sulfide protecting against TNF-alpha-induced neuronal cell apoptosis.

7. By reducing the levels of TRADD, wild type CFTR suppresses downstream proinflammatory NFkappaB signaling.

8. NPM-RAR binding to TRADD selectively inhibits caspase activation, while allowing activation of NFkappaB and JNK

9. The release of extracellular vesicles was triggered by TNFA from BEAS-2b cells.TNFA-triggered extracellular vesicles contained TNFR1 and TRADD.

10. MicroRNA-30c-2-3p negatively regulates NF-kappaB signaling and cell cycle progression through downregulation of TRADD and CCNE1 in breast cancer.

11. domains of calmodulin mediate FADD and TRADD interaction

12. 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).

13. 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.

14. TRADD gene expression was knocked down by an antisense oligonucleotide.

15. 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

16. Data indicate that the ASK1-FoxO3a-TRADD-caspase 8 pathway is present in neural tube defects (NTDs)-affected tissues.

17. we demonstrated that the association between DR6 and TRADD was enhanced upon DQM3 stimulation and TRADD was involved in DR6-induced signaling activation

18. 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.

19. 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

20. rpS3 appears to be recruited to the death-inducing signaling complex (DISC) to induce apoptosis by interacting TRADD in response to extracellular stresses.

Mouse (Murine) TNFRSF1A-Associated Via Death Domain (TRADD) interaction partners

1. TRADD knockout blunts pressure overload-induced cardiac hypertrophy through mediating TAK1/p38 MAPK but not AKT phosphorylation

2. 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.

3. 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

4. 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.

5. 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

6. We show that TRADD is recruited to the TRAIL-receptor complex, and RIP1 recruitment is mediated by TRADD.

7. 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.

8. Tradd activates distinct mechanisms of apoptosis from the nucleus and the cytoplasm.

9. silencing TRADD expression with small-interfering RNA reduced neuronal apoptosis and subsequent microglial and astroglial activation

10. TRADD is a multifunctional protein crucial both for TNFR1 signaling and other signaling pathways relevant to immune responses.

Cow (Bovine) TNFRSF1A-Associated Via Death Domain (TRADD) interaction partners

1. 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.