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Human TIRAP Protein expressed in Escherichia coli (E. coli) - ABIN1098368
Nagpal, Plantinga, Wong, Monks, Gay, Netea, Fitzgerald, Golenbock: A TIR domain variant of MyD88 adapter-like (Mal)/TIRAP results in loss of MyD88 binding and reduced TLR2/TLR4 signaling. in The Journal of biological chemistry 2009
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Zebrafish Tirap adaptor lacks the phosphatidylinositol 4,5-bisphosphate binding motif, which could partially explain zebrafish insensitivity to lipopolysaccharide, hence its resulting inability to activate downstream Toll (show TLR4 Proteins)-like receptor signaling.
TIRAP polymorphisms are associated with progression and survival of patients with symptomatic myeloma.
This present meta-analysis suggests TIRAP C539T polymorphism is significantly correlated with reduced risk of TB infection, with stronger effect in European.
The TIRAP S180L and TLR9 (show TLR9 Proteins) -1486 T>C polymorphism showed no association with systemic lupus erythematosus (SLE) risk, but they influenced SLE phenotype.
Evaluated the possible association between TIRAP rs1893352 and rs8177374 (S180L) gene polymorphisms and pulmonary tuberculosis in a sample of Iranian population.
TIRAP rs81777374 is associated with resistance to pulmonary tuberculosis.
Data indicate that TcpB (NP_540591) may mimic the function of TIRAP through their similar TIR domain structures.
PSP (show MSMB Proteins) has an immunoregulatory effect through regulation of the TLR4 (show TLR4 Proteins)-TIRAP/MAL-MyD88 (show MYD88 Proteins) signaling pathway.
the results of our study suggest that there is a defect of TIRAP and MyD88 (show MYD88 Proteins) proteins in B-CLL lymphocytes.
TIRAP S180L polymorphism is not increased in Behcet's disease patients in Italian or Turkish populations.
In our study, a TLR pathway adapter variant (TIRAP (rs8177374)) protected against preterm birht<32 weeks, supporting our hypothesis that genetic variation in the innate immune signaling pathway contributes to altered risk of PTB (show PTBP1 Proteins).
TIRAP plays a functional role in transducing LPS (show IRF6 Proteins) signaling from TLR-4 (show TLR4 Proteins) to downstream effector molecules involved in NF-kappaB (show NFKB1 Proteins) activation, and TIRAP promotes apoptotic signaling
genetic polymorphism is associated with interferon-gamma (show IFNG Proteins) signaling and susceptibility to infections
TIRAP/Mal deficiency significantly inhibited the activity of titanium particles with adherent bacterial debris to stimulate in vivo osteolysis and in vitro cytokine mRNAs and secretion.
A critical role for the TLR signaling adapter Mal in alveolar macrophage-mediated protection against Bordetella pertussis.
The D-helix peptide, 2R9, also potently inhibited TLR4 (show TLR4 Proteins), TLR7 (show TLR7 Proteins), and TLR9 (show TLR9 Proteins), but not TLR3 (show TLR3 Proteins) or TNF-alpha (show TNF Proteins) signaling. Cell imaging, co-immunoprecipitation, and in vitro studies demonstrated that 2R9 preferentially targets TIRAP.
MyD88 adaptor-like (Mal) functions in the epithelial barrier and contributes to intestinal integrity via protein kinase C.
our data reveal a differential, but inflammation-independent, requirement for Mal and MyD88 during TLR2-promoted gastric tumourigenesis.
Mal is essential for the maintenance of intestinal homeostasis and expression of Mal in nonhematopoietic cells prevents chronic intestinal inflammation that may predispose to colon neoplasia.
Study reports that, in response to natural activators of innate immunity, the sorting adaptor TIRAP regulates TLR signaling from the plasma membrane and endosomes.
TIRAP plays a central role in regulating the effects of lipopolysaccharides or lipoteichoic acid on chlorpromazine-induced hepatotoxicity.
PIP5Kalpha promotes TLR4 (show TLR4 Proteins)-associated microglial inflammation by mediating PIP(2)-dependent recruitment of TIRAP to the plasma membrane
The innate immune system recognizes microbial pathogens through Toll-like receptors (TLRs), which identify pathogen-associated molecular patterns. Different TLRs recognize different pathogen-associated molecular patterns and all TLRs have a Toll-interleukin 1 receptor (TIR) domain, which is responsible for signal transduction. The protein encoded by this gene is a TIR adaptor protein involved in the TLR4 signaling pathway of the immune system. It activates NF-kappa-B, MAPK1, MAPK3 and JNK, which then results in cytokine secretion and the inflammatory response. Alternative splicing of this gene results in several transcript variants\; however, not all variants have been fully described.
MyD88 adapter-like protein
, Toll-interleukin 1 receptor domain-containing adaptor protein
, toll/interleukin-1 receptor domain-containing adapter protein
, TIR domain-containing adaptor protein
, Toll-like receptor adaptor protein
, adapter protein wyatt
, adaptor protein Wyatt
, toll-interleukin 1 receptor domain-containing adaptor protein
, TIR domain-containing adapter protein
, Toll-like receptor 4 adaptor protein
, myD88 adapter-like protein