"In the present study, we showed that development of cardiac hypertrophy was closely associated with the up-regulation of myocardial TNFR1, ADAM-17 and TNF-α, indicating an important role of TNF–α signal system in cardiac hypertrophy."
"Using mice deficient in SP-A and MCs (SP-A −/− Kit W-sh/W-sh mice) engrafted with either TNF-α −/− or TNF receptor (TNF-R) −/− MCs, we found that augmented airway responses during M pneumoniae infection is a result of TNF-α interactions with MCs through the TNF-R and not MC-derived TNF-α."
"The Fas-Fas ligand interaction between macrophages and L929 cells increased the expression of Fas-associated death domain, and tumor necrosis factor-tumor necrosis factor receptor 1 interaction between macrophages and L929 cells increased the expression of tumor necrosis factor receptor-associated death domain in L929 cells."
"VanArsdale and Ware 1994 have demonstrated the TNF-dependent association with TNFR1 of a serine protein kinase activity in U937 cells."
No evidence text available
No evidence text available
No evidence text available
No evidence text available
No evidence text available
No evidence text available
No evidence text available
No evidence text available
No evidence text available
No evidence text available
No evidence text available
No evidence text available
No evidence text available
No evidence text available
No evidence text available
No evidence text available
No evidence text available
No evidence text available
No evidence text available
No evidence text available
No evidence text available
No evidence text available
No evidence text available
No evidence text available
No evidence text available
No evidence text available
No evidence text available
No evidence text available
No evidence text available
No evidence text available
No evidence text available
No evidence text available
No evidence text available
No evidence text available
No evidence text available
No evidence text available
No evidence text available
No evidence text available
No evidence text available
No evidence text available
No evidence text available
No evidence text available
No evidence text available
No evidence text available
No evidence text available
No evidence text available
No evidence text available
No evidence text available
No evidence text available
No evidence text available
No evidence text available
No evidence text available
No evidence text available
No evidence text available
No evidence text available
No evidence text available
No evidence text available
No evidence text available
No evidence text available
No evidence text available
No evidence text available
No evidence text available
No evidence text available
No evidence text available
No evidence text available
No evidence text available
No evidence text available
"TNF-TNFR1 binding activates the nuclear factor kappa-light-chain-enhancer of activated B cells (NF-κB), c-Jun amino-terminal kinase (JNK), the mitogen-activated protein kinases (MAPKs), and p38 [ xref ]."
"Binding of TNF to TNFR1 induces the independent recruitment of the adaptor protein TRADD and the kinase RIPK1 to the receptor 's DD via homotypic DD interactions."
"The molecular mechanism of cell cycle arrest and apoptosis induced by QdNOs were explored. xref report that MEQ inhibited cell proliferation by arresting cells at the G2/M phase of the cell cycle. xref demonstrated that OLA induced cell cycle arrest to the S phase and dose-dependent apoptotic cell death in HepG2 cells through a caspase-9 and -3 dependent mitochondrial pathway. xref found that QCT induced apoptosis in HepG2 cells via activation of caspase, interaction of TNF-α and TNFR1 and modulation of the protein levels of Bid, Bax, and Bcl-2, involving the participation of p53, p38, and JNK."
"In the network identified by GeneGo, conditions in the extracellular environment are sensed inside the cell via binding of TNF to TNF-R1, activating TNF-R1 [XREF_BIBR, XREF_BIBR]."
"TNF-α binds to its receptor TNFR-I in VSMC and EC and results in ROS production in a time and dose-dependent manner."
"TNF interacts with two receptors, TNF-R1 and -R2."
"In chronic inflammatory conditions, e.g. in IBD, interaction between TNF-alpha and TNFR1 can lead to stimulation of nuclear factor kappaB (NF-kappaB) in immune cells, which promotes transcription of genes, leading to cellular proliferation."
"It has also been proposed that p70 can facilitate the binding of TNF to p55 (Tartaglia and Goeddel, 1992a)."
"TNFalpha binds to TNFR1."
"TNF binding to TNFR1 triggers apoptosis through two pathways, by activation of the adaptor proteins TNFR1-associated death domain (TRADD) and Fas-associated death domain (FADD)."
"Moreover, since TNF-α can bind to two receptor subtypes, TNFR1 (p55-R) and TNF receptor 2 (p75-R), we next wish to examine which receptor is involved in SAH-induced apoptosis."
"In contrast, in cells exposed to both TNFalpha and AgNPs, the nanoparticles non specifically bind to TNFR1 and TNFalpha binds specifically with the same receptor, forming a TNFR1, TNFalpha, and AgNPs complex which then enters the cells by receptor mediated endocytosis."
"An exciting recent study of Gómez et al. [ xref ] showed that SpA interacts directly with TNFR1 and mimics TNF- α proinflammatory signaling by recruitment of the adaptor molecules the TNFR-associated death domain (TRADD), receptor-interacting protein (RIP), and TNFR-associated factor (TRAF) 2 to the receptor and the activation of the mitogen-activated protein kinases (MAPKs) p38 and c-Jun NH2-terminal kinases 1 and 2 (JNK1/2), which induces translocation and activation of transcriptional factor NF- κ B and mediates IL-8 gene expression."
"The difference in the signaling of the p60 form of the TNF receptor
and Fas has been reported previously [17]."
"Upon stimulation of TNF-R1 with TNF-α, death domain-containing protein TRADD (TNF receptor-associated death domain) becomes associated with the receptor and then recruits another death domain protein via the death domain/death domain binding."
"Upon binding to TNFα, which is a trimer, TNFR1 also forms a trimer that recruits TNFR1-associated death domain protein (TRADD) and triggers the sequential formation of two distinct complexes: complex I and II, which activate NF-κB and apoptosis, respectively ( xref ) xref ."
"Upon binding to TNF, TNFR1 binds the adaptor protein TRADD which recruits caspase-8 via FADD leading to apoptosis [8] ."
"Thus, upon TNF binding, TRADD binds the DD of TNFR1 and, in turn recruits RIP1."
"A slightly higher concentration of LTa was re-
quired to inhibit 125I-TNF binding to p60:Fc (Ki ~ 650 pM)."
"Unlabeled TNF at a
concentration of ~ 150 pM inhibited 50% of the maximum 125I-TNF
binding (Ki) to p60:Fc."
"In the present study, binding activity of TNF-alpha to TNF-R1 and protein levels of IkappaB-alpha and nuclear transcription factor kappa B (NF-kappaB) p65 subunit in HeLa cells were measured using enzyme-linked immunosorbent assay (ELISA) and western-blot analysis."
"To examine the association of A20 with the p55 TNF receptor complex and its effect on the recruitment of IKK1 to the receptor and to examine the effect of NEMO on IKK1 recruitment, HEK 293T cells were seeded on 10 cm plates (2 × 10 6 /plate)."
"The possible reasons might be that the increased binding of Mt rh471 TNFalpha mainly to TNFR-p55 results in induction of apoptosis of SP cells, while Wt rhTNFalpha could bind to both TNFR-p55 and TNFR-p75 which would lead to NFkappaB activity, resulting in a discounted apoptotic effect."
"Using surface plasmon resonance, we measured single-site binding affinities for the large receptor TNFR1 binding to its ligands TNFα (K D = 1.4 ± 0.4 nM) and lymphotoxin-α (K D = 50 ± 10 nM), and also for the small receptor Fn14 binding to TWEAK (K D = 70 ± 10 nM)."
"Tumor necrosis factor receptor 1 (TNFR1) is a membrane receptor able to bind TNF-alpha or TNF-beta."
"Tumor necrosis factor-alpha (TNF-α) binds to TNFR1 and TNFR2 and the TNFRs induce TNF-α production."
"TNF interacted with TYK2 and TNFRSF1A interacted with JAK2 , SOCS2 , SOCS1 , and STAT4."
"The antitumor activity of TNF-α is associated with death receptor-mediated programmed cell death, which is initiated by the binding of TNF-α to TNFR1 ( xref )."
"The denser fractions failed to show association of TNFR1 with caveolin-1 even after TNF treatment."
"Our study shows that high sCD30, TNFalpha, IL6 and TNF-RI levels are associated with advanced disease or a worse prognostic score."
"The binding of TNFR1-Ig and TNFR2-Ig to bovine TNF-α was analyzed by enzyme-linked immunosorbent assay (ELISA)."
"For those cytokines significantly associated with ALS, the ESs associated with the results of TNF-α, TNFR1 and VEGF were large, suggesting the potential usefulness of these cytokines as practical diagnostic biomarkers for ALS in the future."
"After the binding of TNF-α to TNFR1, the activated receptor may interact with RIP1 via the death domains (DD), which may recruit cellular inhibitor of apoptosis proteins (cIAPs) (such as cIAP1 and cIAP2) and subsequently form the plasma membrane associated complex, leading to the activation of nuclear factor κB and mitogen-activated protein kinases (MAPKs)."
"Pleural effusion as diagnosed by either chest X-ray or ultrasonography was associated with up-regulation of members of the NF-κB pathway such as TNFA and TNFR1 , but also with IL1RA , MIP1A and TLR1 and was inversely related to MIF and TLR7 ."
"RIPK1 rapidly associates with the TNF-activated TNFR1 signaling complex, and undergoes polyubiquitination with multiple linkages. xref , xref RIPK1 K63 polyubiquitination is critical for scaffolding the TAK/TAB kinase complex that phosphorylates IKKβ. xref Linear, methionine1-linked polyubiquitination of RIPK1 (effected by LUBAC) augments recruitment of IKKγ complexed to IKKα and IKKβ, which is then phosphorylated and thereby activated by transforming growth factor-β-activated kinase 1. xref Thus, deubiquitination of RIPK1 diminishes downstream NFκB activation."
"Among the pathways in which KEGG is top-ranked and associated with diseases such as diabetes and inflammatory complication, the target proteins involved in metabolic pathways were adenosine deaminase (ADA), adenosine kinase (ADK), pancreatic alpha-amylase (AMY2A), fatty acid synthase (FASN), fructose-1,6-bisphosphatase 1 (FBP1), folate hydrolase 1 (FOLH1), leukotriene A-4 hydrolase (LTA4H), prostaglandin G/H synthase 2 (PTGS2), and sorbitol dehydrogenase (SORD); the target proteins involved in cancer-related pathways included GSK3 beta, inhibitor of nuclear factor kappa-B kinase subunit beta (IKBKB), IL6, peroxisome proliferators-activated receptors (PPAR), PTGS2, transforming growth factor beta-1 (TGFB1), cellular tumor antigen p53 (TP53), and vascular endothelial growth factor A (VEGFA); target proteins involved in the PI3K-Akt signaling pathway consisted of GSK3 beta, IKBKB, IL6, IRS1, spleen tyrosine kinase (SYK), toll-like receptor (TLR4), TP53, and VEGFA; the NF-kappa B signaling pathway interacted with proteins such as IKBK beta, interleukin-1 receptor-associated kinase 4 (IRAK-4), PTGS2, SYK, TLR4, TNF, and TNFRSF1A; mitogen-activated protein kinase (MAPK), IKBK beta, transforming growth factor beta-1 (TGFB1), TNF, TNFRSF1A, and TP53 interacted with the target protein involved in the MAPK signaling pathway; IKBKB and IL6 are involved in the Toll-like receptor signaling pathway, IRAK4, TLR4, and TNF; and the target proteins involved in the TNF signaling pathway included IL6, PTGS2, TNF, and TNFRSF1A.
Previous studies have identified target proteins that were active in the mulberry leaves and involved in specific pathways."
"Extracellular TNF-α binds and activates two main receptors, TNFR1 (p55) and TNFR2 (p75) that are responsible for mediating the intracellular cytokine activity."
"Tumor necrosis factor binds to TNFR1 and TNR2."
"Interaction of TNF with TNFR2, but not TNFR1, is directly co-stimulatory to TCR-mediated T cell activation, as demonstrated by the effects of agonistic monoclonal antibodies to TNFR2 on human CD4 cells [ xref ]."
"Binding of TNF-α to its specific receptors TNFR1 and TNFR2, activation of different downstream mediators including NF-kB, c-jun N-terminal kinase (JNK), caspase cascade, phosphatidylinositide 3-kinase (PI3K)/Akt and reactive oxygen species (ROS) lead cells to inflammation and cell survival as well as cell death ( xref , xref )."
"Both TNFα (sTNF and tmTNF) can bind to both TNFR1 and TNFR2; sTNFα shows greater affinity for TNFR1 than TNFR2 causing inflammatory responses, leading to apoptosis, while tmTNFα acts mainly on TNFR2 leading to activation and cell survival."
"TNFα binds to two cognate receptors, TNFR1 and TNFR2 [ xref , xref ]."
"Although BCG induction of TNF can interact with both TNFR1 and TNFR2, it may induce TNF production at low levels, thereby possibly boosting the expansion of Tregs ( xref ), which can provide benefits for the treatment of autoimmune diseases."
"The soluble TNF-α can bind to TNFR1 and TNFR2 [28] , hence the expression pattern of both TNFR1 and TNFR2 in SH-SY5Y was analyzed in the presence/absence of TNF-α using real time PCR."
"The binding of TNFα and LTα to TNFR2 and TNFR1 have been well characterized structurally ( xref , xref )."
"We evaluated the inhibitory activity of compound 1 on the binding of TNFα to its receptors TNFRI and TNFRII using an ELISA assay."
"TNFα binds to two receptors, TNFR1 and TNFR2, which can form multimeric complexes upon ligand binding."
"TNF interacts with two plasma membrane receptors, TNF-R1 and TNF-R2."
"RIP3 can also execute cell death in a RIP1-independent manner following interaction of TNFα with TNFR1 via c-Jun N-terminal kinases (JNK) activation and ROS overproduction."