Publication for NFKB1 and TRAF3

Species Symbol Function* Entrez Gene ID* Other ID Gene
coexpression		 CoexViewer
hsa NFKB1 nuclear factor kappa B subunit 1 4790 [link]
hsa TRAF3 TNF receptor associated factor 3 7187

Pubmed ID Priority Text
31244811 0.98 TRAF3 positively regulates IFN-I production, while it inhibits the MAPK pathway and the non-canonical NF-kappaB pathway.
0.98 TRAF3 is a component of a multiprotein complex containing TRAF2 and the cellular inhibitor of apoptosis proteins cIAP1 and cIAP2, which restrict the activation of the non-canonical NF-kappaB pathway.
0.98 TRAF3 plays a critical role in Tax-mediated NF-kappaB activation.
0.98 TRAF3 Is Required for an Efficient Activation of NF-kappaB Mediated by Tax
0.98 TRAF3-KO clones were first characterized for their ability to activate an NF-kappaB promoter.
0.98 NF-kappaB promoter activity was increased 50 folds in TRAF3-KO cell lines as compared to wild type cells (WT) (Figure 1A).
0.98 NF-kappaB pathway is also activated in the absence of TRAF3, the processing of the p100 protein was analyzed.
0.98 TRAF3 is required for an efficient activation of NF-kappaB mediated by Tax.
0.98 TRAF3-KO cells transfected with phRG-TK renilla vector (control for transfection efficiency) and NF-kappaB-luciferase reporter expressing vector.
0.98 TRAF3-KO cells were transfected with phRG-TK renilla vector, NF-kappaB-luciferase reporter and p65, Tax-1, Tax-2, or TRAF3 expression plasmids.
0.98 NF-kappaB induction by Tax-1 or Tax-2 was observed in TRAF3-KO cells compared to WT cells (about 5-fold and 6-fold decrease, respectively) (Figure 1F).
0.98 TRAF3-KO cells (Supplementary Figure 1B), indicating that the NF-kappaB pathway was activated, although the resulting transcriptional activity of p65 was reduced.
0.98 NF-kappaB activation is impaired in TRAF3-KO cells, we observed that Tax-1 failed to induce endogenous p65 nuclear translocation in transfected cells (Figure 1H).
0.98 TRAF3 is involved in Tax-induced NF-kappaB hyper-activation, and it is known that HBZ and APH-2 interfere with NF-kappaB signaling, we aimed to analyze whether the antisense proteins might interfere with TRAF3 functions.
0.98 TRAF3, we first aimed at precisely comparing their ability of antagonize Tax-induced NF-kappaB activation.
0.98 NF-kappaB activation in TRAF3-KO cell lines.
0.98 TRAF3 depletion causes an accumulation of distinct subsets of NF-kappaB inhibitors, including A20.
0.97 TRAF3 enables detectable translocation of p65 into the nucleus, as well as p100 processing, suggest that both the canonical and non-canonical NF-kappaB may be partially activated.
0.97 NF-kappaB activation induced by the expression of p65 in TRAF3-KO cells, we unexpectedly measured a limited induction compared to WT cells (about 9-fold decrease).
0.97 NF-kappaB hyper-activation by Tax is strictly dependent upon TRAF3 expression.
0.97 NF-kappaB activity, we investigated the possible recruitment of HBZ and APH-2 in cytoplasmic complexes containing TRAF3.
0.97 NF-kappaB activation by associating with Tax-2 and TRAF3 complexes.
0.97 TRAF3 may be involved in the mechanisms of NF-kappaB deregulation mediated by HTLV proteins and that its expression may be altered by both HBZ and APH-2 proteins.
0.97 TRAF3 is required not only for Tax-1, but also for Tax-2 NF-kappaB activation, supporting a mechanism in which TRAF3 may be involved in the association with factors that cooperate in the canonical and non-canonical NF-kappaB pathway.
0.97 TRAF3 is required for NF-kappaB dysregulation mediated by Tax, thus representing a novel factor recruited by the viral regulatory proteins to alter cell pathways.
0.97 TRAF3 not only acts on NF-kappaB pathway, but also plays significant roles in the immunity-related signal transduction.
0.97 NF-kappaB pathway, TRAF3, in concert with TRAF2, cIAP1 and cIAP2, promotes the constitutive degradation of NIK that in turn serves as negative regulator of IFN.
0.96 TRAF3 also participates in the degradation of the alternative NF-kappaB inducing kinase NIK, acting as a negative regulator of the non-canonical NF-kappaB pathway.
0.96 NF-kappaB activation in TRAF3-KO cells, although lower when compared to WT cells (Supplementary Figure 1A).
0.96 NF-kappaB, but in the absence of TRAF3, LMP1-induced activation of JNK, p38, and NF-kappaB are impaired.
0.95 NF-kappaB mediated by p65 in the absence of TRAF3, we analyzed TNF-alpha-mediated induction of the NF-kappaB promoter in TRAF3-KO cells.
0.95 TRAF3-KO cells the basal activation of NF-kappaB may lead to the expression of NF-kappaB target genes that control p65 activity by negative feedback loops, we analyzed the expression of A20 and BCL2 genes, which are well known negative regulators of NF-kappaB. We found that both genes were significantly more expressed in TRAF3-KO cells compared to WT suggesting that limited p65-mediated induction of NF-kappaB in TRAF3-KO cells can be due to negative feedback mechanisms (Figure 1G).
0.94 TRAF3 Is Required for NF-kappaB Pathway Activation Mediated by HTLV Tax Proteins
0.94 TRAF3-KO cells transfected with phRG-TK renilla vector, NF-kappaB-luciferase reporter and increasing amount of Flag-TRAF3 expressing vector.
0.93 NF-kappaB activation is impaired in TRAF3 deficient cells obtained by CRISPR/Cas9 editing.
0.93 NF-kappaB activation and TRAF3 interaction.
0.92 NF-kappaB pathway by affecting the expression of TRAF3, as it was previously shown with p65, HEK293T cells were transfected with increasing amounts of HBZ and the expression levels of TRAF3 was evaluated.
0.87 NF-kappaB in TRAF3-KO cells was further confirmed by analyzing IkappaB protein level.
0.84 NF-kappaB pathway is constitutively although partially activated in the absence of TRAF3.
0.82 TRAF3 is a negative regulator of the NF-kappaB pathway, but it may also participate to the functional regulation between the two NF-kappaB pathways.
0.81 NF-kappaB pathway and that NIK turnover is regulated by protein complexes that contain the E3 ubiquitin ligase TRAF3.
0.80 TRAF3 on HTLV-mediated NF-kappaB activation has not yet been understood.
28295222 0.98 TRAF3 and CYLD identified in The Cancer Genome Atlas data set are correlated with the activation of nuclear factor-kappaB, define a distinct etiologic subset of head and neck cancers, and will be useful as biomarkers for predicting improved prognosis and selecting patients with human papillomavirus-positive head and neck cancer who may be successfully treated with de-escalating therapy.
0.98 TRAF3 and CYLD leading to constitutive activation of NF-kappaB have been identified in other cancers, such as multiple myeloma; however, among solid tumors, inactivating TRAF3/CYLD gene defects were most common in HPV-positive HNSCC.
0.98 TRAF3 or CYLD identify a distinct subset of HPV-positive HNSCC and that this subset has constitutive activation of NF-kappaB signaling.
0.98 TRAF3 and CYLD alterations, which are predicted to constitutively activate NF-kappaB pathways while inhibiting innate immunity, occur only in HPV-positive HNSCC.
0.97 TRAF3/CYLD were accompanied with the activation of nuclear factor kappaB signaling and maintenance of episomal HPV in tumors, suggesting that these mutations may support an alternative mechanism of HPV tumorigenesis in head and neck tumors.
0.97 tumor necrosis factor receptor-associated factor 3 (TRAF3) and cylindromatosis lysine 63 deubiquitinase (CYLD), or in other genes, lead to constitutively active nuclear factor kappaB (NF-kappaB), which supports persistence of the HPV episome; these tumors will be sensitive to DNA damage.
0.97 TRAF3/CYLD (dashed red ovals) identified in HPV-positive HNSCC result in the activation of both NF-kappaB pathways.
0.97 kappaB activation, HPV integration was associated with TRAF3/CYLD gene defects.
0.97 TRAF3 or CYLD gene defects have increased transcription of targets on the NF-kappaB pathway and are consistent with the known roles of TRAF3 and CYLD as negative regulators of NF-kappaB. Combined with data correlating the maintenance of episomal forms with TRAF3 and CYLD gene alterations, these data suggest that NF-kappaB activation may be required for episomal maintenance in HPV-positive HNSCC.
0.94 tumor necrosis factor receptor-associated factor 3 (TRAF3) and cylindromatosis lysine 63 deubiquitinase (CYLD) are associated with activated nuclear factor kappaB (NF-kappaB) in human papillomavirus (HPV)-positive head and neck squamous cell carcinoma.
0.93 TRAF3 and CYLD correlated with the activation of transcriptional factor nuclear factor kappaB, episomal HPV status of tumors, and improved patient survival.
0.90 TRAF3 or CYLD Activate NF-kappaB Signaling in HPV-Positive HNSCC
0.90 TRAF3 and CYLD lead to constitutive activation of both canonical and alternative NF-kappaB signaling, as reported in multiple myeloma.24, 25 Because of its ability to induce expression of immune response genes, NF-kappaB signaling was initially viewed as a protector against viral infection; however, it became evident that viruses co-opt NF-kappaB activity to increase viral replication, elevate expression of viral genes, promote virion assembly, and block apoptosis in infected cells, allowing completion of the viral life cycle.58, 59, 60 To assess whether the genetic alterations in TRAF3 and CYLD genes identified in HPV-positive HNSCC were associated with activation of NF-kappaB, we performed GSEA using 615 data sets focusing on transcription factor target genes and a list of genes with significantly different expression in TRAF3/CYLD-mutant compared versus wild-type tumors.
0.89 TRAF3/CYLD mutations were enriched for those that shared NF-kappaB or epidermal growth factor 1 (EGR-1) binding sites (Fig. 4A).
0.87 nuclear factor-kappaB (NF-kappaB), a potent transcription factor central to the cell's control of apoptosis, inflammation, and several aspects of the immune response.14, 15 It has long been noted that NF-kappaB signaling is activated in many HNSCCs.16, 17, 18, 19 It has been demonstrated that constitutive NF-kappaB activation is induced by carcinogens or oncogenic viruses in patients with head and neck cancer or in cell lines.20, 21 TRAF3 is unique, in that it plays a role in negatively regulating canonical and noncanonical NF-kappaB pathways while simultaneously stimulating a potent antiviral response, which is mediated through type I interferon (IFN) signaling.14, 22 Here, we report that the gene cylindromatosis lysine 63 deubiquitinase (CYLD), which, like TRAF3, inhibits NF-kappaB pathways,23 is also mutated in a subset of HPV-positive HNSCC.
0.86 TRAF3 or CYLD may rely on overactive NF-kappaB and defective innate immunity.
0.81 NF-kappaB resulting from somatic mutations in TRAF3 or CYLD may serve as a biomarker to predict an improved prognosis for patients with HPV-positive head and neck cancer.
0.80 TRAF3/CYLD mutations in HNSCC and to determine whether additional regulators of NF-kappaB, which is known to be mutated in human cancer (Fig. 6B), are genetically altered in HNSCC.
0.60 TRAF3, CYLD inhibits NF-kappaB pathways at various steps including, binding, deubiquitinating, and inhibiting the NF-kappaB essential modulator (NEMO).
28295216 0.98 TRAF3 is implicated in TLR-induced canonical and alternative NF-kappaB pathway signaling.
0.98 NF-kappaB activation and target genes in HPV+ HNSCC tumor subtypes containing episome HPV with altered TRAF3/CYLD, could open a new area of research for promising novel cancer treatment options targeting the NF-kappaB pathways or target genes.
0.98 TRAF3 alteration-mediated alternative NF-kappaB pathway could provide potential targets for therapy.
0.97 TRAF3 and CYLD are negative regulators of NF-kappaB pathway activation
0.97 TRAF3) and Cylindromatosis (CYLD; Turban Tumor Syndrome), that were previously implicated as negative regulators of NF-kappaB activation.
0.97 TRAF3 and CYLD, HPV status, and NF-kappaB gene activation were revealed by bioinformatic analyses of TCGA datasets for HPV+/- HNSCC and HPV+ cervical SCC.
0.96 TRAF3 have been linked to decreased IFN production and antiviral immunity in pediatric herpes simplex encephalitis (PSE), and alternative NF-kappaB pathway activation in multiple myeloma.
0.96 TRAF3 deletion and rescue studies in HPV+ HNSCC derived cell lines, revealed an important link between deficient TRAF3, alternative NF-kappaB pathway activation, as well as increased tumor cell migration and drug resistance in HPV+ HNSCC.
0.94 TRAF3/CYLD define distinct subsets of HPV+ HNSCC with associated activation of transcription factor NF-kappaB, episomal HPV infection of tumors, and improved survival of patients.
0.93 TRAF3 deletion and elevated downstream alternative NF-kappaB pathway activity.
0.92 TRAF3 and CYLD that Regulate NF-kappaB and Interferon Signaling define Head and Neck Cancer Subsets Harboring Human Papilloma Virus
0.92 tumor necrosis factor receptor associated factor 3 (TRAF3) and cylindomatosis (CYLD), previously implicated in regulation NF-kappaB, and anti-viral interferon signaling in response to other DNA viruses.
0.91 TRAF3 to ubiquitylate a scaffold to activate canonical IKK-NF-kappaB signaling and proinflammatory cytokines, while alternative pathway LTbetaR and CD40 receptors displace TRAF3 to stabilize NIK to activate alternative IKKalpha-mediated NF-kappaB pathway signaling.
0.82 TRAF3 and CYLD define a distinct subset of HPV+ HNSCC with associated activation of transcriptional factor NF-kappaB, episomal HPV infection of tumors, and improved survival of patients
0.56 TRAF3) and Cylindromatosis (CYLD; Turban Tumor Syndrome) that were previously implicated in NF-kappaB and anti-viral Interferon responses.
26740054 0.98 NF-kappaB inhibition was initially believed to be responsible for the anti-cancer activity of bortezomib, we detected contrasting roles of bortezomib on NF-kappaB1 and NF-kappaB2 pathways in TRAF3-/- malignant B cells.
0.97 NF-kappaB activation while moderately inhibiting non-canonical NF-kappaB activation in TRAF3-/- malignant B cells.
0.96 NF-kappaB pathways in TRAF3-/- malignant B cells.
0.93 NF-kappaB activation in most TRAF3-/- cell lines examined in this study (Fig. 2B, and Supplementary Fig. 2 and 3).
0.75 NF-kappaB pathways in TRAF3-/- malignant B cells after treatment with bortezomib.
0.75 NF-kappaB pathways prompted us to test the hypothesis that a universal NF-kappaB inhibitor may enhance the anti-tumor activity of bortezomib on TRAF3-/- malignant B cells.
0.74 TRAF3 inactivation results in constitutive activation of the non-canonical NF-kappaB (NF-kappaB2) pathway, which is pivotal for the survival of B cells.
0.67 NF-kappaB pathways in TRAF3-/- mouse B lymphoma cells.
19426221 0.98 TRAF3 to constitutively degrade NIK, with engagement of another TNFR, BAFF-R, releasing this degradation and allowing for activation of the non-canonical NFkappaB pathway.
0.97 TRAF3 to the cytoplasmic domains of CD40, with activation of the non-canonical NFkappaB pathway resulting from the subsequent accumulation of NIK as a result of TRAF2 and TRAF3 degradation following recruitment to CD40.
0.95 TRAF3 are situated at the membrane distal domain of the intracellular tail of CD40 and is demarcated by the aa sequence PxQxT. The insertion of mutations at the PxQxT domain disrupts the binding of TRAF2/3 to the CD40 cytoplasmic tail and dampens CD40 signaling by abrogating the NFkappaB, MAPK8 (Jnk), and p38 pathways during ligand engagement.
0.95 TRAF3 plays in CD40 signaling proposed that it functioned as a negative regulator of the canonical NFkappaB pathway.
0.95 TRAF3-dominant negative protein expressed in B cells leads induction of the canonical NFkappaB and Jnk signaling pathways upon CD40 engagement.
0.93 TRAF3 in non-canonical NFkappaB and Jnk signaling in epithelial cells.
0.72 TRAF3 induces canonical NFkappaB signaling during CD40 stimulation, suggesting that TRAF3 has different roles in different types of cells.
27164085 0.98 TRAF3/6-TBK1-IRF3/NF-kappaB/AP1 signals by PLPro is responsible for the antagonistic mechanism of SARS-CoV PLPro against TLR7-medaited production of type I IFNs and pro-inflammatory cytokines.
0.98 TRAF3 and TRAF6 and then inactivates their downstream molecules, such as kinases (TBK1 and p38 MAPK) and transcription factors (IRF3, NF-kappaB and AP-1).
0.97 TRAF3/6-TBK1-IRF3/NF-kappaB/AP1 signals.
0.97 TRAF3 and TRAF6, which correlated with the activation of TBK1, p38 MAPK, NF-kappaB and IRF3 in the TLR7 signaling pathway.
0.96 NF-kappaB has been demonstrated to correlate with PLPro-reduced ubiquitination of RIG-I, STING TRAF3, TBK1 and IRF3 in the TLR3 and RIG-I pathways.
0.93 TRAF3 and TRFA6 played the crucial role in the antagonistic mechanisms of TLR7-mediated type I IFN induction and NF-kappaB activation by PLPro.
0.93 TRAF3/6-TBK1-IRF3/NF-kappaB/AP1 signals in TLR7-mediated antiviral and inflammatory responses.
26471241 0.98 TRAF3-cells (Figure 5c, lane 5), suggesting that CnB-mediated NF-kappaB activation is dependent on TRAF3 rather than TRAF6.
0.98 TRAF3, is critical for IkappaB-alpha phosphorylation and the subsequent activation of nuclear factor NF-kappaB. In response to LPS, TRAF3-deficient cells overproduced pro-inflammatory cytokines due to defects in the anti-inflammatory cytokine IL-10; thus, the TRAF3-knockdown cells displayed stronger and detectable IkappaB-alpha phosphorylation.
0.98 TRAF3 was dispensable for NF-kappaB activation and the production of pro-inflammatory cytokines in the LPS-induced TLR4 signaling pathway.
0.98 TRAF3 results demonstrated a pivotal role of TRAF3 in CnB-induced NF-kappaB activation.
0.97 TRAF3 in TLR4 signaling pathway have been emerging based on TRAF3-dependent NF-kappaB activation (Figures 4c and d).
30778351 0.98 TRAF3 to induce the TBK1/IKKepsilon/IRF3 axis, or TRAF6 to induce NF-kappaB and AP-1 via late phase (slower) kinetics.
0.98 NF-kappaB family, in a mechanism that also requires TRAF3 and cIAP1/2.
0.92 NF-kappaB. Additionally, TLR 7, 8, or 9 can recruit MyD88, TRAF3, IRAK1, and IKKalpha to activate IRF7.
0.91 NF-kappaB signaling by deubiquitinating TRAF2, TRAF3, and TRAF6.
0.67 NF-kappaB stimulation by interacting with TRAF3 and NIK causing NIK is degraded preventing/reducing cleavage of p100 to p52.
30196473 0.98 TRAF3 is critical for virus-induced IRF3-IRF7 activation and controls the non-canonical NF-kappaB pathway.
0.98 TRAF3 deficiency resulted in NIK accumulation and constitutive activation of the non-canonical NF-kappaB signaling pathway.
0.98 NF-kappaB signaling regulatory strategy is represented by A20, an ubiquitin-editing enzyme, which is involved in switching from canonical to non-canonical NF-kappaB signaling upon LT-betaR stimulation by binding of cIAP1, which results in dissociation of TRAF2/TRAF3 interaction (Yamaguchi et al.).
0.97 NF-kappaB receptors bind TRAF2 and TRAF3, which are subsequently degraded.
19116625 0.98 NF-kappaB activity, including TRAF2 (a negative regulator of alternative NF-kappaB but positive regulator of classical NF-kappaB), TRAF3, cIAP1/2, and CYLD (Fig. 3).
0.98 NF-kappaB signaling pathway, especially in response to BAFF and CD40L, is crucial for normal B cell survival, and TRAF3 and TRAF2 both behave as negative regulators of B cell survival downstream of BAFF-R, in part via the suppression of NF-kappaB2/p100 processing.
0.97 TRAF3 inactivation, supports the key role of NF-kappaB in MM pathogenesis.
24533079 0.98 TRAF3 or cIAP1/2 protects NIK from proteasomal degradation leading to accumulation of NIK and subsequent constitutive noncanonical NF-kappaB activation in multiple myeloma cells.
0.97 NF-kappaB pathway is activated through particular TNF receptor family members such as B cell-activating factor (BAFF) receptor, CD40 and lymphotoxin beta receptor that bind to the TNF receptor-associated factor (TRAF) 2 or TRAF3.
0.97 TRAF3-binding site, which enables constitutive noncanonical NF-kappaB signaling in MALT lymphoma.
25753787 0.98 NF-kappaB activation and TRAF3 for IRF3/7 activation.
0.97 TRAF3, removing its K63-linked ubiquitination, which prevented TRAF3 proteolysis and consequently aberrant non-canonical NF-kappaB activation.
0.96 TRAF3 and 6 - as well as the kinases TBK1 (or IKKepsilon) and IKKalpha/beta/gamma which trigger the activation of the IRF3/7- and NF-kappaB-induced signaling arm, respectively.
31311877 0.98 NF-kappaB activation is associated with TRAF3 degradation and concomitant accumulation of NIK.
0.94 TRAF3 to activate the alternative NF-kappaB pathway, and this alternative activation is dependent on the TRAF-binding site in CTAR1.
0.89 NF-kappaB activation pathway, whereas TRAF2 and TRAF3 are involved in nonredundant negative regulatory roles in the alternative NF-kappaB activation pathway.
22792062 0.98 TRAF3-mediated RLH type I IFN response: (1) Sec16A and p115 are found in immunocomplexes containing TRAF3, but not TRAF2 or TRAF6; (2) inactivation of TRAF3 by deletion of its N-terminal RING finger domain and the C-terminal TRAF domain displaces TRAF3 from the ER-Golgi transport compartments; (3) in non-treated cells, TRAF3 colocalizes and tightly associates with p115, Sec16A, ERGIC53 and GM130, markers of the ER-to-Golgi vesicular compartment; (4) activation of the RLH pathway leads to reorganization of the Golgi apparatus into punctate structures containing TRAF3 and GM130; (5) an increased association between TRAF3, Sec16A, p115 and TBK1 is observed in virally-infected, dsRNA- and dsDNA-transfected cells; (6) mild overexpression of both proteins enhances SeV-, TBK1- and MAVS-stimulated IFNbeta, ISG56 and NF-kappaB promoter induction; (7) knocking down the expression level of p115 or Sec16A affects the cellular distribution of TRAF3, impairs its capacity to associate with MAVS and diminishes the type I IFN response following poly I:C or polydA:dT transfection and SeV infection; and (8) enforced retention of TRAF3 at the ER-to-Golgi compartment by the addition of a COPI and COP II sorting signal peptide impairs TRAF3 recruitment to the cis-Golgi and diminishes the type I IFN response.
0.92 NF-kappaB signalling on one hand and TRAF3- and TANK-mediated IRF-3 signalling on the other.
26569329 0.98 NF-kappaB signaling is normally suppressed because of constitutive proteasomal degradation of NIK, mediated by a complex consisting of TRAF2, TRAF3 and cIAPs.
0.97 TRAF3-TRAF2-cIAP E3 complex results in stabilization of NIK, which subsequently phosphorylates IKKalpha and the NF-kappaB precursor p100.
26579219 0.98 TRAF3-TRAF2-cIAP complex controls the steady state function of NIK and noncanonical NF-kappaB signaling.
0.77 TRAF3-dependent uibuiqination mechanism, and induction of noncanonical NF-kappaB signaling involves stabilization and accumulation of NIK as a result of TRAF3 degradation.
27070702 0.98 TRAF3 complex to the receptor, causing cIAP1/2 to instead target TRAF2 and TRAF3 for destruction, thereby stabilizing NIK and activating NF-kappaB. Deletion of both cIAP1 and cIAP2 in mouse B cells results in expansion of the peripheral B cell pool, apparently due to constitutive activation of the alternative NF-kappaB pathway.
0.89 TRAF3 occurs in ~15% of ABC DLBCL tumors and contributes to alternative NF-kappaB activation in these cases.
30845975 0.98 NF-kappaB pathway, their predominant action is to promote ubiquitination/degradation of TRAF3 (TNF receptor-associated factor 3), required for NIK ubiquitination/degradation.
0.97 TRAF3, downregulated TRAF2, and diminished p52 processing and BCL-XL expression, consistent with disruption of the non-canonical NF-kappaB pathway.
30948493 0.98 TRAF3, cIAP1, and cIAP2 lead to increased stability of NIK and subsequent aberrant activation of the non-canonical and canonical NF-kappaB pathways.
0.98 NF-kappaB negative regulators that, together with TRAF3, form a molecular bridge that couples NIK to the NIK K48-ubiquitin ligase cIAP1/2.
16191192 0.98 TRAF3 has inhibitory functions to those of TRAF 2/6 in TNF induced NF-kappaB activation.
20818435 0.98 TRAF3 degradation and that NIK is required for RP3-induced NF-kappaB activation.
21135871 0.98 TRAF3, NIK is stabilized, leading to the activation of IKKalpha, which phosphorylates the NF-kappaB precursor p100.
22924041 0.98 TRAF3 also binds to TBK1, linking upstream signaling responses of RIG-I/Mda5-MAVS-STING to the TBK1-directed activation of IRF3 and NF-kappaB and transcription from IFNbeta and IFN response element (ISRE) containing promoters (Figure 1).
23717208 0.98 TRAF3, TRAF6 and NEMO which all function at junctions for the immune stimulating signals from different PRR and type I IFNR to activate NF-kappaB- and IRF-mediated immune responses.
27597804 0.98 TRAF3 with K63 poly-Ub, which consequently recruits the TBK1 (TRAF family member-associated NF-kappaB activator-binding kinase)/IKKepsilon kinase complex.
22709905 0.97 TRAF3 is a molecular switch that inhibits the LTBR-dependent activation of NF-kappaB1, and has been reported to be capable of suppressing canonical NF-kappaB activation and downstream gene expression both in vitro and in vivo.
0.97 TRAF3 is an important suppressor of inflammatory responses through negative regulation of the canonical and noncanonical NF-kappaB pathways.
0.96 TRAF3 and TRAF6 have both positive and negative regulatory functions in activation of the canonical nuclear factor kappa B (NF-kappaB) pathway.
0.96 TRAF3 causes specific accumulation of a particular subset of NF-kappaB regulators, including key components of NF-kappaB2, such as p100, RelB, and NIK.
0.95 TRAF3-deficient cells display only a partial reduction in IFN production after RNA virus infection and NF-kappaB activation.
0.93 TRAF3 results in activation of both the canonical and non-canonical NF-kappaB activation pathways.
0.73 TRAF3 has been shown to bind constitutively to NIK (an essential activator of the alternative NFkappaB pathway) in unstimulated cells, and to block the activation of the non-canonical NF-kappaB pathway.
0.64 TRAF3 protein levels are reduced in HIV-1 Tat C treated and miR-32-transfected cells, the repressive function of TRAF3 is removed, leading to activation of the non-canonical NF-kappaB pathway.
31311932 0.97 TRAF3/CYLD have been implicated in the activation of NF-kappaB signaling in HPV-positive head and neck squamous cell carcinoma (HNSCC) and EBV-positive NPC, suggesting that TRAF3 and CYLD genetic alterations may also participate in EBV-mediated tumorigenesis in pulmonary LELC.
0.97 TRAF3 expression with short hairpin RNAs (shRNAs) up-regulated key components of NF-kappaB signaling pathway including p52 and IKbetaalpha (Fig. 4c) and led to markedly increased cell growth, cell migration, and colony formation (Fig. 4d-f).
0.96 TRAF3 functions as a negative regulator of the non-canonical NF-kappaB pathway.
0.94 NF-kappaB pathway including TRAF3, CYLD, NFKBIA, and NLRC5 were frequently deleted in pulmonary LELC.
0.93 NF-kappaB pathway (TRAF3 [14q32.3, 80%], NFKBIA [14q13, 52%], NLRC5 [16q13, 52%], and CYLD [16q12.1, 48%]).
0.82 NF-kappaB pathway (TRAF3), one epigenetic modifier (KMT2C), and one laminin subunit essential for basement membrane (LAMA4).
0.72 TRAF3 loss accounts for the core element of NF-kappaB dysregulation and plays important role in tumorigenesis of pulmonary LELC.
0.64 TRAF3 served as a tumor suppressor gene and negatively regulated NF-kappaB pathway.
19893624 0.97 NF-kappaB and IFNbeta gene transcription but readily inhibited TRIF-mediated activation (Figure 5D,E), thus indicating the specificity of the TIM domain of Triad3A for TRAF3.
0.96 NF-kappaB promoter activity by targeting TRAF3 for degradation.
0.95 NF-kappaB and IRF pathways by targeting the TRAF3 adapter for degradation via Lys48-linked ubiquitinination.
0.94 TRAF3 degradation would enhance NF-kappaB promoter activity, the observed decrease in NF-kappaB activity suggests that Triad3A may disrupt other TRAF family members such as TRAF2 and TRAF6, prevent their association with MAVS, and thus disrupt NF-kappaB activation.
0.87 TRAF3/TANK/FADD/RIP1, and leads to activation of IRF-3 and NF-kappaB. Furthermore, the effect of Triad3A on NF-kappaB activation was shown to be independent of RIP1 proteolytic degradation, thus strengthening the possibility that another TRAF family member associates with the TIM domain of Triad3A.
0.72 TRAF3 negatively regulates noncanonical p100/p52 NF-kappaB activation through degradation of the NF-kappaB inducing kinase NIK.
0.55 NF-kappaB activator (TANK) adapter and the viral oncogene LMP1 of the Epstein Barr Virus also bind to the same structural crevice of TRAF3.
28098136 0.97 NF-kappaB pathway, including CYLD, TRAF3, NFKBIA and NLRC5, in a total of 41% of cases.
0.97 TRAF3, a key negative regulator of the non-canonical NF-kappaB pathway in NPC, was found to be mutated in 8.6% cases (9/105 cases), a rate higher than previously reported in NPC (1/33 cases; 3.0%) (refs).
0.97 NF-kappaB pathway, such as NFKBIA (14q13), TRAF3 (14q32.3), CYLD (16q12.1) and NLRC5 (16q13).
0.97 NF-kappaB pathway aberrations dominated by CYLD, TRAF3, NFKBI and NLRC5 events (Fig. 6; Supplementary Fig. 13).
0.95 TRAF3 mutations were located in the RING finger and the MATH/TRAF domains (Fig. 3a), regions known to be essential for the suppression of NIK-activating NF-kappaB signalling.
0.92 TRAF3, but not the patient-derived mutants inhibited the non-canonical NF-kappaB pathway in NPC cells (Supplementary Fig. 9).
0.89 TRAF3 and NFKBIA are important negative regulators of NF-kappaB activity.
24391645 0.97 TRAF3, promote constitutive ubiquitination and proteasomal degradation of NF-kappaB inducing kinase (NIK) - a kinase with critical role in the activation of non-canonical NF-kappaB signaling.
0.97 TRAF3, and c-IAP proteins at the receptor complex would not permit efficient induction of non-canonical NF-kappaB signaling.
0.97 TRAF3 from the soluble cytoplasmic compartment eliminates the physical link between c-IAPs and NIK and enables activation of the non-canonical NF-kappaB signaling.
0.97 NF-kappaB signaling in non-enzymatic fashion by disrupting interaction between c-IAP1 and TRAF2/TRAF3, thereby breaking the link between E3 ligase c-IAP1 and its substrate NIK.
0.97 TRAF3 in the OTUD7B knockouts allows faster activation of non-canonical NF-kappaB and results in B cell hyper-responsiveness to antigens.
0.75 NF-kappaB pathway and TWEAK/FN14 and most of the related TRAF3-binding TNFR family members depend on ubiquitination for effective activation of signaling.
20064526 0.97 NF-kappaB pathway, takes place constitutively in TRAF2 KO, TRAF2/5 DKO and TRAF3 KO cells, due to the accumulation of NIK in these cells.
0.97 NF-kappaB pathway requires the accumulation of NIK, which is otherwise constitutively targeted by TRAF2 and TRAF3 in unstimulated cells.
0.92 TRAF3 must be structurally intact for its inhibition of the noncanonical NF-kappaB pathway.
0.58 TRAF3 have nonredundant and complementary functions in targeting NIK for ubiquitination-dependent degradation, as the noncanonical NF-kappaB pathway is constitutively activated in both TRAF2-deficient and TRAF3-deficient cells.
24497610 0.97 TRAF3, TRAF2, and cIAP1 in wild-type MEFs and in cells lacking NEMO or p65, suggesting that defective classical NF-kappaB signaling does not prevent the basal NIK regulatory complex from forming in these cells.
0.95 TRAF3 plays no role in the IKKalpha-driven degradation of active NIK and imply that a previously uncharacterized regulatory mechanism is responsible for this phase of deactivation of non-canonical NF-kappaB signaling.
0.86 TRAF3, cIAP1, and cIAP2 were similar or increased in p65KO MEFs compared to those in wild-type cells (Fig. 6E), consistent with a potential role for non-canonical NF-kappaB signaling in regulating the abundance of TRAF3.
0.73 TRAF3 proteins were similar, if not increased, among the cell lines that we studied (fig. S9B), and TRAF3 stability was unaffected by loss of classical NF-kappaB activity (fig. S9C).
26036313 0.97 TRAF3 mutations leading to hyperactivation of the NF-kappaB pathway and more dependency on the canonical pathway.
0.96 NF-kappaB pathway leading to uncontrolled NF-kappaB activation, loss of functional TRAF3 being the most common gene deleted/mutated.
0.93 TRAF3 and a hyperactivated NF-kappaB signature e.g. high expression of genes that are involved in NF-kappaB signaling, are associated to initial good response to proteasome inhibitors.
0.59 NF-kappaB pathway, cIAP1/2, TRAF2 and TRAF3 have repressive roles by promoting the ubiquitination and degradation of NIK.
22301546 0.97 TRAF3 interactions are insufficient to mediate inhibition of NF-kappaB by the MC159 protein.
0.96 TRAF3 are dispensable for NF-kappaB inhibitory function
0.90 TRAF3 stabilizes MC159-TRAF2 interactions to aid in the inhibition of NF-kappaB, then we hypothesized that MC159 proteins that do not bind to TRAF3 would not inhibit NF-kappaB. Accordingly, two mutant MC159 proteins (MC159 DM and MC159 Delta) that are deficient in TRAF3 binding were assessed by a luciferase reporter assay for their ability to inhibit TNF-induced NF-kappaB activation (Fig. 3, graph).
22685329 0.97 NF-kappaB pathway, by reducing its association with the degradative complex containing TRAF2, TRAF3 and cIAP1.
0.96 NF-kappaB signaling depends on the levels of NIK which under resting conditions are very low, due to constant degradation by an ubiquitination-dependent mechanism involving cIAP E3 ligases complexed to TRAF2 and TRAF3.
22963717 0.97 NFkappaB. NFkappaB-inducing kinase (NIK) activates the noncanonical pathway of NFkappaB. In resting cells, NIK is ubiquitinated by a ubiquitin-ligase complex, composed of TRAF3-TRAF2-cIAP1 and/or cIAP2, and is proteasomally degraded.
0.97 NFkappaB and TNFR2, leads to recruitment of the TRAF3-TRAF2-cIAP complex to the receptor.
26861016 0.97 NF-kappaB through a TLR-related signaling pathway independent of TRAF3.
0.97 NF-kappaB responses through TLR-related TRAF3-independent signaling cascades.
28626800 0.97 TRAF3, and involved in TRAF-mediated NF-kappaB signaling pathways.
0.97 TRAF3 association with TBK1 and IKKepsilon, which promotes phosphorylation and activation of Interferon Regulatory Factor 3 (IRF3)/IRF7 as well as NF-kappaB signaling.
30038267 0.97 TRAF3 binding for regulating NF-kappaB activation by USP17.
0.51 TRAF3 binding for enhancing inflammatory responses by USP17 in IL-1beta-stimulated HEK293 cells and LLC cells using an NF-kappaB-driven luciferase-reporter assay.
30081579 0.97 NF-kappaB signaling pathway, and TRAF2, TRAF3, TRAF5, and TRAF6 act as E3 ubiquitin ligases.
0.95 TRAF3 and TRAF6; the transmissible gastroenteritis virus (TGEV) PLP1 binds and deubiquitinates RIG-I; and PRRSV NSP2, which contains the ovarian tumor (OTU) domain DUB and has been characterized as PLP2, interferes with the polyubiquitination process of IkappaBalpha to inhibit the activation of NF-kappaB. The PLP2 of equine arterivirus (EAV) adopts a compact OTU domain DUB fold with a unique integral zinc finger, which plays a central role in binding and positioning the distal Ub molecule on the protease surface.
31349873 0.97 TRAF3 and Effects on NF-kappaB signaling pathway.
0.95 TRAF3 and activates the NF-kappaB signaling pathway.
21042276 0.97 NF-kappaB family members NFKB1(encoding p105/p50) and NFKB2 (encoding p100/p52) as well as genes whose protein products regulate the IKK complex such as CIAP1, CIAP2, CYLD, NIK, and TRAF3 are associated with the pathogenesis of multiple myeloma.
25873381 0.97 NFkB1 and NFkB2, CD40, NIK, TRAF3, GSK-3beta, and beta-catenin, all of which are known to be affected by LMP-CTAR1.
30524423 0.97 TRAF3 (and often also of TRAF2), releasing NIK and allowing p100 processing to the active p52 NF-kappaB subunit [reviewed in ].
23329887 0.96 TRAF3 function was provided in that TRAF3 is constitutively bound to NF-kappaB inducing kinase (NIK), an essential activator of the alternative NF-kappaB pathway in unstimulated B cells for regulation of homeostasis.
0.96 TRAF3 in recruitment to NF-kappaB, CD40 or LMP1 pathways via homotypic multimers or heterotypic multimers, sparking our interest in the combined analysis of TRAF3 and TRAF5.
0.94 TRAF3 and TRAF5 are found to be involved in different signaling pathways, including NF-kappaB, MAPK, TLRs and IL-1R families.
0.89 TRAF3 plays negative regulatory roles in CD40-stimulated classical NF-kappaB signaling and TNFR-induced MAPK activation.
0.73 TRAF3 and TRAF5 are all involved in NF-kappaB activation, it seems that TRAF5 participates in the regulation of canonical and non-canonical NF-kappaB pathways, whereas TRAF3 is mainly involved in the control of non-canonical NF-kappaB signaling and has not been reported to contribute to the canonical pathway.
18718859 0.96 Traf3-/- B cells show a normal proliferative response to CD40 ligand which is generally thought to require NF-kappaB, and overexpression of wt TRAF3 fails to induce NF-kappaB in reporter gene assays.
0.69 TRAF3 in normal CD40-based activation of NF-kappaB signaling is unclear.
0.59 TRAF3, overexpression of all TRAF3 variants, except for the variant lacking the entire zinc-finger domain, can activate an NF-kappaB-dependent luciferase reporter in A293 cells, and three of the eight are able to induce NF-kappaB in BJAB human B-lymphoma cells.
0.55 TRAF3 splice variants can induce NF-kappaB, it will be of interest to determine whether expression of these variants is a product of aberrant splicing machinery in lymphomas, many of which have high constitutive levels of NF-kappaB activity, or is a regulated cellular or developmental event.
19479062 0.96 TRAF3-dependent pathway has been genetically confirmed by experiments showing that Traf3 -/- MEF cells show impaired production of type I IFNs but normal activation of NF-kappaB in response to viral infection.
0.91 TRAF3-dependent IRF activation pathway and the TRAF6-dependent NF-kappaB activation pathway.
0.80 NF-kappaB activation requires TRAF6 (Figure 3B and 3C), whereas TRAF3 deficiency does not affect the activation of NF-kappaB or expression of NF-kappaB target genes, such as IkappaBalpha .
23301098 0.96 NF-kappaB activation pathway, in absence of a stimulus, NIK associates with the TRAF3/TRAF2/cIAP1/cIAP2 complex that targets it for degradation.
0.96 NF-kappaB pathway in PDAC, downregulation of TRAF2 is preferred to downregulation of TRAF3 or cIAPs instead.
0.56 TRAF3 and cIAP1/2 have been identified in patients, leading to NIK-induced activation of both the canonical and alternative NF-kappaB pathways to regulate cell growth and survival.
30294322 0.96 TRAF3 inhibits H. pylori infection-induced NF-kappaB activation and Cdx2 expression, and is required to resist the infection by acting in the NOD1-RIP2-TRAF3 pathway in gastric epithelial cells.
0.87 NF-kappaB by inhibiting the expression of miR-3178, which directly targets TRAF3 mRNA for downregulation, in gastric epithelial cells.
0.58 NF-kappaB-IL-13 in the survival of Hodgkin-Reed-Sternberg (H-RS) cells of HL and a similar CD30v-TRAF2/TRAF5-NIK-NF-kappaB pathway in acute myeloid leukemia (AML) and ALL; (2) LIGHT-LTbetaR-TRAF3/TRAF5-ROS-ASK1-Caspase 3 in the apoptosis of human colon cancer and hepatoma cells; (3) upregulated TRAF5-NF-kappaB in the migration and invasion of glioma cells, in which TRAF5 is directly targeted for degradation by the tumor suppressor Numbl; (4) TRAF5/TRAF6-NF-kappaB-Vimentin/TWIST1/SNAIL2/MMP13/IL-11 in the EMT and metastasis of prostate cancer cells, in which TRAF5 is directly targeted for downregulation by the tumor suppressive miR-141-3p; and (5) TRAF5-MEK1/2-ERK1/2-Bcl2 in the survival and proliferation of melanoma cells, in which TRAF5 is directly targeted for downregulation by tumor suppressive MiR-26b.
20501935 0.96 NF-kappaB signaling, because knockdown of TRAF3 by RNA interference or knockout of TRAF3 leads to the accumulation of NIK and the processing of p100.
0.95 TRAF3, TRAF2, cIAP1, or cIAP2 are associated with aberrant activation of noncanonical NF-kappaB signaling and B cell malignancies.
22158412 0.96 TRAF3 and TRAF6 : which mediate the ubiquitylation of signalling proteins such as receptor-interacting protein 1 (RIP1) and TRAF3, downstream pathways leading to nuclear factor-kappaB (NF-kappaB) activation and type I interferon (IFN) induction are activated.
0.90 NF-kappaB activation), by contrast, does not require TRAF3 degradation.
23612498 0.96 NF-kappaB -mediated expression of cIAP1, cIAP2, TRAF2 and TRAF3 plays a negative role in non-canonical signaling by degrading NIK.
0.85 NF-kappaB activation requires TRAF2- and cellular inhibitors of apoptosis 1 and 2 (cIAP1/2)-dependent ubiquitination and degradation of TRAF3 and the subsequent accumulation of NF-kappaB-inducing kinase (NIK), which is habitually targeted for degradation by the TRAF2/TRAF3/cIAP1/2 E3 ligase complex in unstimulated cells.
19281271 0.96 TRAF3 (TNF receptor-associated factor 3), a key negative regulator of the non-canonical NF-kappaB pathway.
20161788 0.95 TRAF3 has been shown to not be required for NF-kappaB activation.
0.92 TRAF3 and TRAF5 are both important for IRF3/7 activation and type I interferon production, TRAF5 also plays a role in NF-kappaB activation and proinflammatory cytokine induction.
0.84 TRAF3 and TRAF5 each have at least some nonredundant functions in IRF3 activation while TRAF5 has an additional role in NF-kappaB activation.
0.83 NF-kappaB. However, TRAF3-deficient cells display only a partial reduction in interferon production in response to RNA virus infection and are not defective in NF-kappaB activation.
0.78 TRAF3 and TRAF5-dependent manner to activate IRF3/7 and in a TRAF5-dependent manner to activate NF-kappaB. NEMO may be recruited to the MAVS signaling complex by ubiquitinated TRAF3 and TRAF5, and may lead to IRF3 phosphorylation through the recruitment of TANK and TBK1.
0.71 TRAF3 mediates IRF3 activation, we find that TRAF5 is important for the activation of NF-kappaB as well as IRF3.
0.63 TRAF3, TRAF5 is necessary for full IRF3/7 activation and IFNbeta induction in response to RLR signaling, whereas TRAF5 is also required for NF-kappaB activation.
0.61 NF-kappaB activation, it is likely that there exists a downstream target for the MAVS CARD other than TRAF3.
0.60 TRAF3 and TRAF5 may act coordinately to recruit NEMO and TANK to activate IRF3, TRAF5 alone may recruit NEMO and IKK kinase subunits to activate NF-kappaB (Figure 7).
0.58 TRAF3 knockout cells were found to display a partial defect in type I interferon production in response to RNA virus infection, but an enhanced activation of NF-kappaB activation and production of inflammatory cytokines as a result of NIK stabilization.
26881431 0.95 TRAF3 leading to non-canonical NF-kappaB activation.
0.90 TRAF3 represent an important step in the activation of the non-canonical NF-kappaB signaling pathway.
27208423 0.94 TRAF3 negatively regulates TLR-mediated activation of classical NF-kappaB and MAPKs, as well as TNFR family-mediated stimulation of the alternative NF-kappaB pathway.
0.91 NF-kappaB. Here, the structure of TRAF3-LTbetaR (PDB ID: 1RF3) is shown as an example of TNFR activation.
0.90 TRAF3 leads to constitutive activation of the non-canonical NF-kappaB, since NIK cannot bind to this mutant form of TRAF3 and be degraded, suggesting that this residue is likely to be in the interface.
0.88 TRAF3 inhibits the canonical NF-kappaB through TRAF6 in the TLR pathway, and the non-canonical NF-kappaB through NIK in the TNFR pathway.
0.87 TRAF3 was proposed not to play a role in the classical NF-kappaB, we have shown that it may restrict the activation of classical NF-kappaB by competing with TRAF6 to bind to MyD88.
0.85 TRAF3 regulates the activation of canonical and non-canonical NF-kappaB and the generation of anti-viral responses.
0.68 TRAF3 interactions revealed how TRAF3 inhibits both the canonical and non-canonical NF-kappaB pathways.
0.65 TRAF3 is a critical control switch that negatively regulates the activation of the canonical and non-canonical NF-kappaB pathways; it is also a key protein in antiviral immunity.
0.63 NF-kappaB to ensure their survival by binding to TRAF2 and TRAF3.
0.61 TRAF3 negatively regulates the activation of the canonical and non-canonical NF-kappaB pathways and is one of the key proteins in antiviral immunity.
21113390 0.94 TRAF3 degradation links CD40 signaling to noncanonical NF-kappaB activation
0.91 TRAF3 results in constitutive activation of noncanonical NF-kappaB. Notably, in cIAP1 or cIAP2 single-knockout cells, the noncanonical NF-kappaB pathway is normal and not constitutively activated, whereas in cells in which both cIAPs are depleted by application of an siRNA or IAP antagonists it is constitutively activated.
0.80 NF-kappaB activation in response to CD40 ligation, it appears that CD40 engagement induces the assembly of a complex:through TRAF3-mediated recruitment of NIK and TRAF2-mediated recruitment of cIAP1/2:to the receptor.
0.73 TRAF3 must be structurally intact to inhibit noncanonical NF-kappaB in resting cells.
29907126 0.94 NF-kappaB. NIK is downregulated by the expression of TRAF2 and TRAF3, which are negative regulators of non-canonical NF-kappaB signaling that interact with BIRC2 and BIRC3.
0.92 NF-kappaB pathway is inactive, NIK is constantly degraded via ubiquitination by TRAF3.
0.87 TRAF3 triggers non-canonical NF-kappaB signaling.
0.58 TRAF3, which are negative regulators of non-canonical NF-kappaB signaling that interact with BIRC2 and BIRC3.
27416764 0.94 TRAF3 via regulation of the serine/threonine kinase NF-kappaB inducing kinase (NIK, MAP3K14).
0.92 NF-kappaB signaling nodes TRAF2, TRAF3, IKKalpha, NIK, and NF-kappaB2/p100.
31404116 0.94 NF-kappaB and IRF3/7 signaling by positive regulation of TRAF6 and TRAF3 function.
0.82 TRAF3 ubiquitination and served as a specific ubiquitination substrate of TRAF6, leading to transcription factor NF-kappaB, IRF3 and IRF7 translocation from the cytoplasm to the nucleus.
11304555 0.94 TRAF3 may antagonize TRAF2's effects in promoting NF-kappaB activation and CD40-mediated IgM secretion 18 20.
23028875 0.94 TRAF3, which occurs within 30 minutes of CD40 or BAFFR stimulation and which is necessary for NIK accumulation, additionally permits increased p65/p50 nuclear import and transcription of NF-kappaB target genes after TNF-alpha stimulation.
19798431 0.93 TRAF3 and TRAF6 activate IRF-3, NF-kappaB, and p38 in MEF, induction of the late phase of type I IFN may require these signaling adaptor molecules to activate the four components (IRF-3, IRF-7, NF-kappaB and ATF-2/c-Jun) of the enhanceosome.
20671747 0.93 NF-kappaB phosphorylation levels, 3-Cl-AHPC-mediated NIK stabilization and binding of TRAF3 with NIK in the NF-kappaB noncanonical pathway.
29933636 0.92 NF-kappaB defects (e.g. CYLD, TRAF3 aberrations) and the immune system defects (including MHC loss) lead to tumor formation, or immune evasion (e.g., via dysregulation of innate and adaptive immune responses)?
0.91 NF-kappaB pathways, which include: CYLD (18.6%), TRAF3 (17.5%), NFKBIA (6.7%) and NLRC5 (4.8%).
0.89 NF-kappaB, namely TRAF3 (TNF receptor associated factor 3), was also found to be aberrant in as high as 17.5% of microdissected EBV(+) NPC tumors.
0.86 TRAF3 aberrations, an EBV oncoprotein, the latent-membrane protein 1 (LMP1) is also known to be a potent activator for NF-kappaB signaling.
0.81 NF-kappaB pathway, CYLD and TRAF3 mutations appear to occur at a similar high rate in both cancers (8-11% rates), followed by the same rate of mutations of NLRC5 (6% rates) (Table 3).
29874793 0.89 TRAF3 mutations, and therefore hyperactive noncanonical NF-kappaB, are resistant to dexamethasone treatment.
0.62 TRAF3, cIAP1, cIAP2, CYLD, NFKB1/p105, and NFKB2/p100 have been observed, with TRAF3 inactivation being the most frequent alteration.
29734366 0.72 TRAF3 and promote virus-triggered activation of NF-kappaB and IRF3.
0.66 TRAF3/TRAF6 signalosome either interacts with a complex containing TBK1 and IKK to activate the transcription factor IRF3 and subsequent type I IFNs production, or interacts with IKKalpha/beta/gamma complex to activate NF-kappaB and produce downstream proinflammatory cytokines.
29772694 0.69 NF-kappaB-activating mutations, which affected most frequently CYLD and TRAF3.
23793113 0.68 TRAF3, cIAP1 and cIAP2 target the kinase MAP3K14 (also called NF-kappaB inducible kinase, or NIK) for degradation and thereby suppress the non-canonical NF-kappaB pathway.
0.63 TRAF3, and cIAP function downstream of LMP1 TES1 is complicated by high-level non-canonical NF-kappaB activity that results upon TRAF2 or TRAF3 depletion, even in the absence of stimulus.
0.56 TRAF3 recruitment, and markedly reduces LMP1-mediated NF-kappaB activation.
28561798 0.67 TRAF3, cooperates in the same protein complex to negatively regulate NIK, the central activator of non-canonical NF-kappaB signaling.
0.63 NF-kappaB pathway in approximately 20% of MM patients (inactivation of TRAF2, TRAF3, CYLD, cIAP1/cIAP2, and activation of NFKB1, NFKB2, CD40, LTBR, TACI, and NIK).
25754842 0.62 NF-kappaB. However, the relationship between RIP-1 and the TRIF/TRAF1, TRAF2, and TRAF3 pathways to produce cytokines after viral infection is unknown.
20890394 0.51 NFKB1, TACI), and one mainly the alternative pathway (NFKB2), but most activate the alternative and to a lesser extent the classical pathway (cIAP1/2, NIK, TRAF2, TRAF3, CD40) (Fig.2B).



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