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Study presents the characterization of the peptide binding preferences of TRAFs 2, 3, and 5 using deep mutational scanning. The three TRAF (show TRAF1 ELISA Kits) proteins demonstrated different preferences for binding to members of the CD40 (show CD40 ELISA Kits) library, and three peptides from that library individually showed striking differences in affinity for the three TRAFs.
These findings indicate that miR (show MLXIP ELISA Kits)-26b might influence TRAF5-MAPK (show MAPK1 ELISA Kits) signaling pathways to facilitate the malignant progression of melanoma cells.
findings reveal a direct link between TRAF5-mediated ubiquitination and RORgammat protein regulation
RIG-I (show DDX58 ELISA Kits)-like receptor mediated antiviral innate immune responses in the lower respiratory tract involves TRAF3 (show TRAF3 ELISA Kits) and TRAF5 signaling.
This study provides evidence that TRAF5 and TRAF3IP2 (show TRAF3IP2 ELISA Kits) genes are involved in the development of Behcet's disease (BD) and Vogt-Koyanagi-Harada (VKH) syndrome.
Data indicate that TNF receptor-associated factor 5 (TRAF5) gene is involved in the development of acute anterior uveitis (AAU) and pediatric uveitis.
Data indicate that in monocyte- derived macrophages (MDMs) acutely infected with HIV-1 and treated with HCV rCore and HIV-1 rNef, the HIV-1 replication depends on an upstream signal mediated through TRAF2 (show TRAF2 ELISA Kits), TRAF5 and TRAF6 (show TRAF6 ELISA Kits).
TRAF3 (show TRAF3 ELISA Kits) and TRAF5 are overexpressed in inflammatory bowel disease
Numbl (show NUMBL ELISA Kits) interacted with tumor necrosis factor (show TNF ELISA Kits) receptor-associated factor 5, which signals upstream and is required for the activation of NF-kappaB (show NFKB1 ELISA Kits), and committed it to proteasomal degradation by promoting K48-linked polyubiquitination of TRAF5
Resutls indicate that TRAF5 may be a key molecule in the innate response against viral infection.
this study shows that TRAF2 (show TRAF2 ELISA Kits) and TRAF5 work as important regulators of the IL-6R signaling needed for Th17 development
The results indicated that TRAF5 deficiency significantly aggravated DSS (show PMP22 ELISA Kits)-induced colitis, most likely by regulating Th cell-mediated inflammation.
In conclusion, our results suggest that as an intrinsic cardioprotective factor, TRAF5 plays a crucial role in the development of cardiac hypertrophy through the negative regulation of the MEK (show MDK ELISA Kits)-ERK1/2 (show MAPK1/3 ELISA Kits) pathway
TRAF5 negatively regulates TLR signaling in B lymphocytes.
These results provide the first demonstration that TRAF5 is a critical mediator of brain ischemia/reperfusion in an experimental stroke model.
In vitro and cellular experiments showed that forms of TRAF5 with mutation of the corresponding residues to those of TRAF3 (show TRAF3 ELISA Kits) had TRAF3 (show TRAF3 ELISA Kits)-like antiviral activity.
Treatment with IL-17 (show IL17A ELISA Kits) prolongs the half-life of chemokine (show CCL1 ELISA Kits) CXCL1 (show CXCL1 ELISA Kits) mRNA via the adaptor TRAF5 and the splicing-regulatory factor SF2 (ASF (show SRSF1 ELISA Kits)).
TNF receptor-associated factor 5 (TRAF5) deficiency accelerates atherogenesis in mice by increasing inflammatory cell recruitment and foam cell formation.
Study is the first report showing a major requirement for TRAF5 in signaling by a specific receptor both in vitro and in vivo, as well as playing an important role in biological function in B lymphocytes.
role in both RANKL (show TNFSF11 ELISA Kits)- and TNFalpha (show TNF ELISA Kits)-induced osteoclastogenesis
The scaffold protein encoded by this gene is a member of the tumor necrosis factor receptor-associated factor (TRAF) protein family and contains a meprin and TRAF homology (MATH) domain, a RING-type zinc finger, and two TRAF-type zinc fingers. TRAF proteins are associated with, and mediate signal transduction from members of the TNF receptor superfamily. This protein is one of the components of a multiple protein complex which binds to tumor necrosis factor (TNF) receptor cytoplasmic domains and mediates TNF-induced activation. Alternate transcriptional splice variants have been characterized.
TNF receptor-associated factor 5
, RING finger protein 84