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PMID: 14609719 TRAF6 activates MAPK kinases.

PMID: 14609719 TRAF6 activates MAPK kinases,which can lead to AP-1 activation through MAPK.

PMID: 14609719 TRAF6 activates the inhibitors of ¦ÊB (I¦ÊB) kinase (IKK) complex.

PMID: 14609719 The IKK complex is composed of 2 catalytic subunits IKK¦Á and IKK¦Â and one regulatory subunit IKK¦Ã and induces phosphorylation of I¦ÊB.

PMID: 14609719 The phosphorylation of the I¦ÊBs results in their polyubiquitination, which in turn leads to their 26S proteasome-mediated degradation.

PMID: 14609719 The phosphorylation of the I¦ÊBs results in their polyubiquitination, which in turn leads to their 26S proteasome-mediated degradation.

PMID: 14609719 NF-¦ÊB translocates into the nucleus.

PMID: 14609719 NF-¦ÊappaB translocate into the nucleus and activate the transcription of many ¦ÊB-dependent genes, including TNF-¦Á and I¦ÊB¦Á.

PMID: 14609719 NF-¦ÊappaB translocate into the nucleus and activate the transcription of many ¦ÊB-dependent genes, including TNF-¦Á and I¦ÊB¦Á.

PMID: 14609719 TIRAP/Mal binds directly to TLR4. PMID: 14609719,12447441 TIRAP-deficient mice have similar LPS-responsive phenotypes to MyD88-deficient mice with regard to the MyD88-independent pathway.

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PMID: 14609719 Activation of TLR4 by LPS also induces the phosphorylation and nuclear translocation of IRF3.

PMID: 14609719 Activation of TLR4 by LPS also induces the phosphorylation and nuclear translocation of IRF3.

PMID: 14609719 Activation of TLR4 by LPS induces the phosphorylation and nuclear translocation of IRF3, which causes up-regulation of a set of genes, including IFN-¦Â.

PMID: 14609719 Phosphorylated IRAK-1 first binds TRAF6, resulting in the activation of NF-¦ÊB. The phosphorylated IRAK-1 is then degraded in an ubiquitination-dependent pathway.

PMID: 14609719 Phosphorylated IRAK-1 first binds TRAF6, resulting in the activation of NF-¦ÊB. The phosphorylated IRAK-1 is then degraded in an ubiquitination-dependent pathway.

PMID: 14609719 LBP transfers LPS to membrane CD14, and the intercalated LPS is released in lipid membrane; subsequently,the intercalated LPS binds to a complex of receptors composed of chemokine receptor 4, growth differentiation factor 5, and heat shock proteins 70 and 90 in lipid rafts.

PMID: 14609719, 12791997 Nod1 specifically detects a diaminopimelate-containing N-acetylglucosamine-N-acetylmuramic acid tripeptide motif of peptidoglycan found in Gram-negative bacteria.

PMID: 14609719,11894097 Nod1 activates NF-¦ÊB through its association with the receptor-interacting protein 2 (Rip2), a CARD-containing serine/threonine kinase that directly interacts with IKK¦Ã, the regulatory subunit of the IKK complex.

PMID: 14609719 MD-2, a small protein that lacks a transmembrane domain, is identified to associate with the extracellular domain of TLR4.

PMID: 14609719 Dimers of MyD88 bind IRAK-1and IRAK-4 bringing the respective domains in close association,resulting in the phosphorylation of IRAK-1 by IRAK-4, which may induce the kinase activity of IRAK-1 leading to its autophosphorylation.

PMID: 14609719 Dimers of MyD88 bind IRAK-1and IRAK-4 bringing the respective domains in close association,resulting in the phosphorylation of IRAK-1 by IRAK-4, which may induce the kinase activity of IRAK-1 leading to its autophosphorylation.

PMID: 14609719 Dimers of MyD88 bind IRAK-1and IRAK-4 bringing the respective domains in close association,resulting in the phosphorylation of IRAK-1 by IRAK-4, which may induce the kinase activity of IRAK-1 leading to its autophosphorylation.

PMID: 14609719 CD14 concentrates LPS and presents it to TLR4-MD-2. TLR4, MD-2 and CD11b/CD18 are recruited to the rafts, thereby triggering multiple signaling cascades (i.e., activation of NF-¦ÊB and MAPK).

PMID: 14609719 The TIR domain of MyD88 associates with the TIR domain of TLR and IL-1 receptor.

PMID: 1469719 The IKK complex is composed of 2 catalytic subunits IKKa and IKKb and one regulatory subunit IKKg and induces phosphorylation of IkappaB. PMID: 1469719,11894097 Nod1 activates NF-kB through its association with the receptor-interacting protein 2 (Rip2), a CARD-containing serine/threonine kinase that directly interacts with IKKg, the regulatory subunit of the IKK complex. Studies using Rip2-deficient cells have demonstrated that Rip2 is essential for the activation of NF-kB by Nod1 and Nod2.

PMID: 1469719,11894097 Nod1 activates NF-kB through its association with the receptor-interacting protein 2 (Rip2), a CARD-containing serine/threonine kinase that directly interacts with IKKg, the regulatory subunit of the IKK complex. Studies using Rip2-deficient cells have demonstrated that Rip2 is essential for the activation of NF-kB by Nod1 and Nod2.

PMID: 14609719 IRAKs are subsequently phosphorylated and are dissociated from the receptor complex. IRAKs associate receptor complex transiently.(Fig3)

PMID: 14609719, 9625770, 8599092 IRAKs are subsequently phosphorylated and are dissociated from the receptor complex and interact with another adaptor molecule, TRAF6.