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Ubiquitin E3 ligase TRAF2 reduces BMAL1 protein level.BMAL1 interacts with the zinc finger domain in TRAF2.TRAF2 promotes BMAL1 ubiquitination and degradation.TRAF2 attenuates the BMAL1 transcriptional activity.
The authors found that tumor necrosis factor receptor-associated factor 2 (TRAF2), as well as TRAF1 and 3, directly binds to the active caspase-2 dimer.
The up-regulation of TRAF2 may play an important role in the inhibition of chondrocyte apoptosis of facet joint osteoarthritis (FJOA).
The TRAIP coiled-coil domain altered its stoichiometry between dimer and trimer in a concentration-dependent manner. Additionally, the TRAIP RING domain induced even higher-ordered assembly, which was necessary for interacting with the TRAF-N domain of TRAF2 but not TRAF1.
high levels of CASC9.5 expression promote the proliferation, metastasis and metabolism of lung adenocarcinoma cells and might serve as a prognostic indicator.
down-regulation of USP48 increases E-cadherin expression and epithelial barrier integrity through reducing TRAF2 stability
DR5-Cbl-b/c-Cbl-TRAF2 complex inhibited TRAIL-induced apoptosis by promoting TRAF2-mediated polyubiquitination of caspase-8 in gastric cancer cells.
CPNE1 overexpression can upregulate TRAF2 expression in prostate cancer DU-145 cells as determined by Western blotting and immunofluorescence assays.
TRAF2 functions as an important modulator in tumor metastasis and tumor microenvironment formation and is a novel independent prognostic factor of gastric cancer.
High expression of TRAF2 can predict poorer prognosis of GBM and was identified as an independent biomarker in GBM prognosis.
TRAF2 can influence in vitro growth of TRAIL-treated DU-145 cells at least partially via regulating SIRT1 expression.
Intestinal I/R induced the membrane translocation and phosphorylation of PKCzeta. Pretreatment with the PKCzeta activator phosphatidylcholine remarkably attenuated gut injury by suppressing apoptosis. H/R induced PKCzeta to combine with TRAF2, which was phosphorylated by PKCzeta at Ser(55), but not at Ser(11), under intestinal I/R or H/R conditions
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.
Both S1P and caspase-8 are critical for TRAF2 stabilization, polyubiquitination, subsequent activation of JNK/AP1 signaling and MMP1 expression and final promotion of cell invasion.
Results showed that high expression of TRAF2 was significantly associated with tumor stage of prostate cancer.
The addition of nanomolar concentration of TRAF2 in GUVs also seems to exert a mechanical action.
TRAF2 and OTUD7B govern a ubiquitin-dependent switch that regulates mTORC2 signalling
destabilization of TRAF2 by miR-17 reduced the ability of TRAF2 to associate with cIAP2, resulting in the downregulation of TNF-alpha-induced NF-kappaBp65, c-Jun, and STAT3 nuclear translocation and the production of IL-6, IL-8, MMP-1, and MMP-13 in human rheumatoid arthritis synovial fibroblasts.
HOXA1-mediated activation of NF-kappaB is non-transcriptional and the RBCK1 and TRAF2 influences on NF-kappaB are epistatic to HOXA1
RIPK1 collaborates with TRAF2 to inhibit murine and human hepatocarcinogenesis.
The results demonstrate that gp130-associated TRAF2 and TRAF5 inhibit the interaction between two JAK proteins in the IL-6R complex that is essential for initiating the JAK-STAT signaling pathway.
TRAF2 is essential but TRAF3 is dispensable for T cell-dependent humoral immunity and CD40-induced class switch recombination
TRAF2 modulates the maximal Per1 mRNA level of the circadian clock.
work reveals that simulated microgravity promotes the apoptotic response through a combined modulation of the Uev1A/TICAM/TRAF/NF-kappaB-regulated apoptosis and the p53/PCNA- and ATM/ATR-Chk1/2-controlled DNA-damage response pathways.
Traf2 mediates the pro-survival pathway in the heart by suppressing necroptotic signaling.
Targeting TRAF2 may be useful as a therapeutic approach for immunosuppression-free islet allograft survival that avoids the thromboembolic complications associated with the use of anti-CD40L antibodies.
Celastrol promotes Nur77 migration from the nucleus to mitochondria, where it is ubiquitinated by TRAF2. Ubiquitinated Nur77 then interacts with p62/SQSTM1, leading to autophagy of dysfunctional mitochondria and alleviation of inflammation.
this study shows that TRAF2 and TRAF5 work as important regulators of the IL-6R signaling needed for Th17 development
Keratinocyte-specific deletion of Traf2, but not Sphk1 deficiency, disrupted TNF mediated NF-kappaB and MAP kinase signalling and caused epidermal hyperplasia and psoriatic skin inflammation.
TRAF2 functions as a key activator of MST1 in oxidative stress-induced intracellular signaling processes.
Proinflammatory TLR signalling is regulated by a TRAF2-dependent proteolysis mechanism in macrophages.
NFkappaB anti-apoptotic target genes TNF receptor-associated factor 1 (TRAF1), TNF receptor-associated factor 2 (TRAF2), cellular inhibitor of apoptosis (cIAP2), and Ferritin heavy chain (FTH1) were increased following Losartan treatment
These studies demonstrate a critical role for TRAF2 in the maintenance of peripheral CD8(+) CD44(hi) CD122(+) T-cell and NKT-cell homeostasis by modulating sensitivity to T-cell intrinsic growth factors such as IL-15.
HGK/MAP4K4 deficiency has a role in inducing TRAF2 stabilization and Th17 differentiation leading to insulin resistance
identifying the CYLD-TRAF2-p38MAPK pathway as a novel important regulator of HSC function restricting HSC cycling and promoting dormancy.
Data indicate that caspase-8 activity is lost upon deletion of c-FLIPL, and p43FLIP rescues caspase-8 activity through Raf1, TRAF2, and RIPK1 association, augmenting ERK and NF-kappaB pathways
IpaH0722 dampens the acute inflammatory response by preferentially inhibiting the PKC-mediated activation of NF-kappaB by ubiquitinating TRAF2, a molecule downstream of PKC, and by promoting its proteasome-dependent degradation.
Data indicate that deletion of Tnfr1 gene more efficiently decreased the percentages of IL-10-secreting neutrophils in PB and BM cells from tumor necrosis factor (TNF) receptor-associated factor (Traf)2(-/-) mice.
The protein encoded by this gene is a member of the TNF receptor associated factor (TRAF) protein family. TRAF proteins associate with, and mediate the signal transduction from members of the TNF receptor superfamily. This protein directly interacts with TNF receptors, and forms a heterodimeric complex with TRAF1. This protein is required for TNF-alpha-mediated activation of MAPK8/JNK and NF-kappaB. The protein complex formed by this protein and TRAF1 interacts with the inhibitor-of-apoptosis proteins (IAPs), and functions as a mediator of the anti-apoptotic signals from TNF receptors. The interaction of this protein with TRADD, a TNF receptor associated apoptotic signal transducer, ensures the recruitment of IAPs for the direct inhibition of caspase activation. BIRC2/c-IAP1, an apoptosis inhibitor possessing ubiquitin ligase activity, can unbiquitinate and induce the degradation of this protein, and thus potentiate TNF-induced apoptosis. Multiple alternatively spliced transcript variants have been found for this gene, but the biological validity of only one transcript has been determined.
, conjugal transfer protein TraF
, E3 ubiquitin-protein ligase TRAF2
, tumor necrosis factor type 2 receptor associated protein 3
, tumor necrosis factor type 2 receptor-associated protein 3
, TRAF family member-associated NFKB activator
, TNF receptor-associated factor 2