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Data show that Toll (show TLR4 Proteins)/IL-1R domain-containing adaptor molecule (TICAM)-2 possesses two conserved acidic amino acids, D91 and E92, which regulate TICAM-2 self-activation and signaling.
Findings were SNPs in TICAM2 (P = 3.6 x 10(-6)) and IL1B (show IL1B Proteins) (P = 4.3 x 10(-5)) associated with TB.
TRAM (show TRAM1 Proteins) plays a role in TLR7 (show TLR7 Proteins) signaling through a novel signaling axis towards the activation of anti-viral immunity.
TRAM acts as a sorting adaptor not only for TLR4, but also for TLR2, to facilitate signaling to IRF7 at the endosome, which explains how TLR2 is capable of causing type I IFN induction.
A putative TRAF6 (show TRAF6 Proteins)-binding motif in TRAM (show TRAM1 Proteins) may mediate a new TRAM (show TRAM1 Proteins) function in TLR4 (show TLR4 Proteins) signaling in regulating inflammatory responses, distinct from its bridging TLR4 (show TLR4 Proteins) and TRIF (show TRIM69 Proteins). A TRAM (show TRAM1 Proteins) E183A mutation abolished this.
results suggest TLR adaptor molecules knockdown, such as MyD88 (show MYD88 Proteins) or TRAM (show TRAM1 Proteins), can decrease IL-6 (show IL6 Proteins) and IL-8 (show IL8 Proteins) mRNA and increase CXCL12 (show CXCL12 Proteins) mRNA expression in HGF (show HGF Proteins) and HPDLF.
The homotypic interaction between TICAM-2 TIR is indispensable to present a scaffold for recruiting the monomeric moiety of the TICAM-1 (show TICAM1 Proteins) TIR dimer.
induction of both IL-6 (show IL6 Proteins) and IL-8 (show IL8 Proteins) is associated with elevated TIRAP (show TIRAP Proteins) and reduced TRAM (show TRAM1 Proteins) mRNA expression
Data indicate that MyD88 works together with the IL-1/IL-18 receptors, can interact with two distinct sorting adaptors, TRAM and Mal, in a conserved manner.
viral inhibitor peptide of TLR4 (show TLR4 Proteins) possibly represents a surface domain of A46 that specifically inhibits TLR4 (show TLR4 Proteins) by masking critical binding sites on MyD88 adaptor (show MYD88 Proteins)-like and TRIF-related adaptor molecule
Distinct mechanisms downstream of TLR4 (show TLR4 Proteins) signaling mediate myelosuppression and hematopoietic stem cell exhaustion during sepsis through unique effects of MyD88 (show MYD88 Proteins) and TRIF (show RNF138 Proteins).
these data show that both Myd88 (show MYD88 Proteins) and TRIF (show RNF138 Proteins) are necessary for Th17 differentiation in the lungs in response to immunization with lipopolysaccharide
these studies reveal an additional regulatory function of TRIM8 (show TRIM8 Proteins) in innate immune responses: TRIM8 (show TRIM8 Proteins) catalyzes polyubiquitination of TRIF (show RNF138 Proteins), resulting in disruption of TRIF (show RNF138 Proteins)-TBK1 (show TBK1 Proteins) interaction
Stimulation of the TLR4 (show TLR4 Proteins)-TRIF (show RNF138 Proteins) pathway can protect against the development of allergic airway disease and that a TRIF (show RNF138 Proteins)-dependent adjuvant effect on CD4 (show CD4 Proteins)(+) ICOS (show ICOS Proteins)(+) T-cell responses may be a contributing mechanism.
Monophosphoryl lipid A stimulation of a TLR4 (show TLR4 Proteins)-TRIF (show RNF138 Proteins)-PI3K-Akt (show AKT1 Proteins) pathway prevents lipopolysaccharide-induced ERK (show EPHB2 Proteins) activation in the medullar thick ascending limb.
study reporst a key role for TNF (show TNF Proteins)/TNFR1 (show TNFRSF1A Proteins) in Yersinia-induced cell death of murine macrophages, which occurs despite the blockade of NF-kappaB (show NFKB1 Proteins) and MAPK (show MAPK1 Proteins) signaling imposed by Yersinia on infected cells
STING and TRIF (show RNF138 Proteins) Contribute to Mouse Sepsis, Depending on Severity of the Disease Model
the role of Toll (show TLR4 Proteins)-like receptor (TLR) 2, TLR4 (show TLR4 Proteins), myeloid differentiation response gene 88, and Toll (show TLR4 Proteins)-IL-1 (show IL1A Proteins) receptor domain-containing adaptor-inducing interferon-gamma (show IFNG Proteins) (TRIF (show RNF138 Proteins)), factors critically involved in the TLR signaling pathway, was studied in experimental autoimmune neuritis.
Juniperus rigida Sieb. extract inhibits macrophage inflammatory responses by attenuating TRIF (show RNF138 Proteins)-dependent signaling and inflammasome activation.
TRIF (show RNF138 Proteins)-independent pathways can be involved in the downregulation of drug metabolizing enzymes and transporters through TLR4 (show TLR4 Proteins) and 3. JNK (show MAPK8 Proteins)-dependent mechanisms likely mediate this downregulation.
TIRP is a Toll/interleukin-1 receptor (IL1R\; MIM 147810) (TIR) domain-containing adaptor protein involved in Toll receptor signaling (see TLR4\; MIM 603030).
NF-kappa-B-activating protein 502
, TIR domain-containing adapter molecule 2
, TRIF-related adaptor molecule
, cytoplasmic adaptor
, putative NF-kappa-B-activating protein 502
, toll-like receptor adaptor protein 3
, toll/interleukin-1 receptor (TIR) domain-containing adapter protein
, TRIF-related adapter molecule
, TMED7-TICAM2 readthrough
, TIR domain-containing adapter protein
, TRIF-related adapter molecule TRAM
, Toll-interleukin I receptor domain (TIR)-containing adaptor molecule (TICAM) 2
, toll/interleukin-1 receptor domain-containing protein