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Rbf1-induced apoptosis activates a compensatory proliferation mechanism which also depends on Slipper and TRAF1, indicating that these two proteins seem to be key players of compensatory proliferation in Drosophila.
Traf4 is expressed throughout development, and is required for efficient apical constrictions of ventral furrow cells.
Expression of Reaper leads to a loss of DIAP1 (show DIAPH1 Proteins) inhibition of DTRAF1-mediated JNK (show MAPK8 Proteins) activation in Drosophila cells.
DTRAF1-null mutant showed a remarkable reduction in JNK (show MAPK8 Proteins) activity with an impaired development of imaginal discs and a defective formation of photosensory neuron arrays.
this study reveals an unexpected role for TRAF1 in negatively regulating Toll-like receptor signaling, providing a mechanistic explanation for the increased inflammation seen with a rheumatoid arthritis-associated single-nucleotide polymorphism in the TRAF1 gene
H. pylori infection significantly inhibits the cleavage of TRAF1 via a CagA (show S100A8 Proteins)-dependent mechanism, which would increase the relative amounts of full-length TRAF1 and exert an antiapoptotic effect on H. pylori-infected cells.
Alleles of rs2416804 in TRAF1 were identified as being linked and associated with carotid intima-media thickness.
Molecular basis for TANK recognition by TRAF1 revealed by the crystal structure of TRAF1/TANK complex has been reported.
Single nucleotide polymorphisms (SNP) in angiotensin II receptor, type 1 (AGTR1 (show AGTR1 Proteins)), transcription factor AP-2 beta (TFAP2B (show TFAP2B Proteins)), and tumor necrosis factor (show TNF Proteins) receptor-associated factor 1 (TRAF1) have been reported to be associated with the incidence of PDA in preterm infants.
TRAF1 plays a crucial role in the pathogenesis of autoantibodies and may serve as a serologic inflammatory marker of disease activity in rheumatoid arthritis patients.
Helicobacter pylori infection induces the overexpression of TRAF1 in gastric epithelial cells. The upregulation of TRAF1 plays an antiapoptotic role in Helicobacte pylori -infected gastric cells and may contribute to the gastric carcinogenesis.
The increased serum TRAF-1 may be a useful non-invasive indicator of Renal cell carcinoma (show MOK Proteins) (RCC (show XRCC1 Proteins)) development.
Data suggest that, during B-cell transformation by Epstein-Barr virus, LMP1 (show PDLIM7 Proteins) (EBV latent membrane protein 1) induces signaling that stimulates Lys63-polyubiquitin (show UBB Proteins) chain attachment to TRAF1 (TNF receptor-associated factor 1) in the B-lymphocytes.
This study did not replicate the association between PTPRC (show PTPRC Proteins) and the response to anti-TNF (show TNF Proteins) treatment in our Southern European population. We found that TRAF1/C5 risk RA variants potentially influence anti-TNF (show TNF Proteins) treatment response.
this study shows that Traf1 gene knock-out mice show increased susceptibility to lipopolysaccharide-induced septic shock
NFkappaB anti-apoptotic target genes TNF receptor-associated factor 1 (TRAF1), TNF receptor-associated factor 2 (TRAF2 (show TRAF2 Proteins)), cellular inhibitor of apoptosis (cIAP2 (show BIRC3 Proteins)), and Ferritin heavy chain (FTH1 (show FTH1 Proteins)) were increased following Losartan treatment
TRAF1 is a crucial early mediator of hepatic ischemia/reperfusion injury.
Increased neuronal TRAF1 leads to elevated neuronal death and enlarged ischaemic lesions.
The pathogenesis of spontaneous KRN/I-A(g7) arthritis can largely proceed by TRAF1-independent pathways.
Together, these findings define the importance of the basal phosphorylation state of the TRAF1 Serine 139 residue in coordinating signalling events downstream of 4-1BB (show TNFRSF9 Proteins) in primary T cells.
TRAF1 and LSP1 (show LSP1 Proteins) cooperate downstream of 4-1BB (show TNFRSF9 Proteins) to activate ERK (show EPHB2 Proteins) signaling and down-modulate the levels of Bim (show BCL2L11 Proteins) leading to enhanced T cell survival.
TRAF1 plays a critical role in regulating T cell activation both through restricting the costimulation independent activation of NIK (show MAP4K4 Proteins) in activated T cells and by promoting the 4-1BB (show TNFRSF9 Proteins)-induced classical NF-kappaB (show NFKB1 Proteins) pathway.
These findings identify TRAF1 as a potential biomarker of HIV-specific CD8 (show CD8A Proteins) T cell fitness during the chronic phase of disease and a target for therapy.
combined signaling from the TNF (show TNF Proteins) or IL-1 (show IL1A Proteins) receptors promotes maximal lung inflammation that may contribute to the severity of disease caused by H5N1 virus infection
The protein encoded by this gene is a member of the TNF receptor (TNFR) associated factor (TRAF) protein family. TRAF proteins associate with, and mediate the signal transduction from various receptors of the TNFR superfamily. This protein and TRAF2 form a heterodimeric complex, which is required for TNF-alpha-mediated activation of MAPK8/JNK and NF-kappaB. The protein complex formed by this protein and TRAF2 also interacts with inhibitor-of-apoptosis proteins (IAPs), and thus mediates the anti-apoptotic signals from TNF receptors. The expression of this protein can be induced by Epstein-Barr virus (EBV). EBV infection membrane protein 1 (LMP1) is found to interact with this and other TRAF proteins\; this interaction is thought to link LMP1-mediated B lymphocyte transformation to the signal transduction from TNFR family receptors. Three transcript variants encoding two different isoforms have been found for this gene.
, TNF receptor associated factor 1
, TNF-receptor-associated factor 1
, Epstein-Barr virus-induced protein 6
, TNF receptor-associated factor 1
, TNF receptor-associated factor 1-like
, Epstein-Bar virus-induced protein 6