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PMID: 17667936,12763684
There are also a number of ligands such as lipoteichoic acid and mycobacterial lipoarabinomannan that appear to be recognized by TLR2 independent of TLR1 or TLR6
PMID: 17667936,11095740,15795223,16720699
TLR2 is known to form heterodimers with TLR1 or TLR6 while TLR4 homodimerizes in a similar fashion to dToll
indirect
PMID: 17667936,12077222
While the TLR2/TLR6 heterodimer detects diacylated lipoproteins from bacteria, the TLR2/TLR1 heterodimer senses triacylated lipoproteins.
PMID: 17667936,15690042
CD14 has also been shown to be required for signalling induced by TLR2 ligands,and it has been found recently that the scavenger receptor CD36 is involved in recognition of diacylated lipopeptides by TLR2/6 heterodimers.
PMID: 17667936,12077222
While the TLR2/TLR6 heterodimer detects diacylated lipoproteins from bacteria, the TLR2/TLR1 heterodimer senses triacylated lipoproteins.
PMID: 17667936
TLR3 detects the double-stranded RNA (dsRNA) from viruses.
PMID: 17667936
TLR5 senses flagellin, a highly conserved component of bacterial flagella.
PMID: 17667936
Both TLR7 and TLR8 recognize the single-stranded RNA (ssRNA) from viruses, while TLR9 is responsible for detecting bacterial and viral CpG DNA motifs.
PMID: 17667936
Both TLR7 and TLR8 recognize the single-stranded RNA (ssRNA) from viruses, while TLR9 is responsible for detecting bacterial and viral CpG DNA motifs.
PMID: 17667936
Both TLR7 and TLR8 recognize the single-stranded RNA (ssRNA) from viruses, while TLR9 is responsible for detecting bacterial and viral CpG DNA motifs.
PMID: 17667936,15010525,15895089
It seems that an LPS response requires the sequential interaction and transfer of LPS to LPS-binding protein, the glycosylphosphatidylinositol-anchored protein CD14 and MD-2, and the simultaneous engagement of LPS and TLR4 by MD-2
PMID: 17667936,15010525,15895089
It seems that an LPS response requires the sequential interaction and transfer of LPS to LPS-binding protein, the glycosylphosphatidylinositol-anchored protein CD14 and MD-2, and the simultaneous engagement of LPS and TLR4 by MD-2
PMID: 17667936,15010525,15895089
It seems that an LPS response requires the sequential interaction and transfer of LPS to LPS-binding protein, the glycosylphosphatidylinositol-anchored protein CD14 and MD-2, and the simultaneous engagement of LPS and TLR4 by MD-2
PMID: 17667936,15010525,15895089
It seems that an LPS response requires the sequential interaction and transfer of LPS to LPS-binding protein, the glycosylphosphatidylinositol-anchored protein CD14 and MD-2, and the simultaneous engagement of LPS and TLR4 by MD-2
PMID: 17667936
MyD88 is recruited to the cytoplasmic portion of the TLR and interacts with IRAK4 and IRAK1 via homophilic DD interactions.
PMID: 17667936
Mal recruits MyD88, which binds IRAK4 and -1.
PMID: 17667936
MyD88 is recruited to the cytoplasmic portion of the TLR and interacts with IRAK4 and IRAK1 via homophilic DD interactions.
PMID: 17667936,11518704,9430229,12538665,12885415,11960013
17362201
Activated IRAK4 phosphorylates and activates IRAK1 which subsequently interacts with TNFR-associated factor-6 (TRAF6),causing the oligomerization and activation of TRAF6.
PMID: 17667936,11518704,9430229,12538665,12885415,11960013
17362201
Activated IRAK4 phosphorylates and activates IRAK1 which subsequently interacts with TNFR-associated factor-6 (TRAF6),causing the oligomerization and activation of TRAF6.
PMID: 17667936,11518704,9430229,12538665,12885415,11960013
17362201
Activated IRAK4 phosphorylates and activates IRAK1 which subsequently interacts with TNFR-associated factor-6 (TRAF6),causing the oligomerization and activation of TRAF6.
indirect
indirect
PMID: 17667936,16056267,11057907
TRAF6 is a ubiquitin E3 ligase and functions with the ubiquitin-conjugating enzyme Ubc13 and the Ubc-like protein Uev1a to catalyze the synthesis of Lys63-linked polyubiquitin chains on target proteins including TRAF6 itself.
PMID: 17667936,16056267,11057907,10882101
Ubiquitinated TRAF6 then recruits TAB2 and activates the TAB2-associated TAK1 kinase
PMID: 17667936,16056267,11057907,10882101
Ubiquitinated TRAF6 then recruits TAB2 and activates the TAB2-associated TAK1 kinase
indirect
PMID: 17667936
Activated TAK1 then activates the IKK complex which phosphorylates IkappaB resulting in its ubiquitination and subsequent proteosome-mediated degradation.
indirect
PMID: 17667936
Activated TAK1 then activates the IKK complex which phosphorylates IkappaB resulting in its ubiquitination and subsequent proteosome-mediated degradation.
PMID: 17667936,15371334,11460167
This leaves NF-kappaB free to translocate to the nucleus and initiate gene transcription
PMID: 17667936,15371334,11460167
This leaves NF-kappaB free to translocate to the nucleus and initiate gene transcription
indirect
PMID: 17667936,15371334,11460167
This leaves NF-kappaB free to translocate to the nucleus and initiate gene transcription
PMID: : 17667936,11460167
TAK1 is also responsible for the activation of MKK6 which phosphorylates and activates the kinases JNK and P38 and thereby mediates AP-1 activation
indirect
PMID: : 17667936,11460167
TAK1 is also responsible for the activation of MKK6 which phosphorylates and activates the kinases JNK and P38 and thereby mediates AP-1 activation
indirect
PMID: : 17667936,11460167
TAK1 is also responsible for the activation of MKK6 which phosphorylates and activates the kinases JNK and P38 and thereby mediates AP-1 activation
indirect
PMID: : 17667936,11460167
TAK1 is also responsible for the activation of MKK6 which phosphorylates and activates the kinases JNK and P38 and thereby mediates AP-1 activation
indirect
PMID: : 17667936,11460167
TAK1 is also responsible for the activation of MKK6 which phosphorylates and activates the kinases JNK and P38 and thereby mediates AP-1 activation
PMID: 17667936,15361868,15492225,15767370
Upon ligand binding to TLR 7, 8 or 9, IRF7 is recruited to a complex containing MyD88, TRAF6, IRAK4 and IRAK1.
PMID: 17667936,15361868,15492225,15767370
Upon ligand binding to TLR 7, 8 or 9, IRF7 is recruited to a complex containing MyD88, TRAF6, IRAK4 and IRAK1.
PMID: 17667936
Phosphorylation of IRF7 by IRAK1 in this complex was found to be essential for its transcriptional activation.
PMID: 17667936
This results in the activation of IRF7 which translocates to the nucleus to produce IFN-alpha and IFN-inducible genes.
PMID: 17667936
Figure 1
PMID: 17667936
Figure 1
indirect
PMID: 17667936
This results in the activation of IRF7 which translocates to the nucleus to produce IFN-alpha and IFN-inducible genes.
indirect
PMID: 17667936
This results in the activation of IRF7 which translocates to the nucleus to produce IFN-alpha and IFN-inducible genes.
indirect
PMID: 17667936
TRAF6 can also activate IRF5.
PMID: 17667936,15665823
It was shown that IRF5 interacts with, and is activated by MyD88 and TRAF6 causing the nuclear translocation of IRF5 and the expression of inflammatory cytokines.
indirect
indirect
PMID: 17667936,17018642
Upon TLR activation, IRF1 is activated by MyD88, causing it to translocate to the nucleus where it induces a specific gene subset including IFN-beta, inducible NO synthase and IL-12p35
indirect
PMID: 17667936,17018642
Upon TLR activation, IRF1 is activated by MyD88, causing it to translocate to the nucleus where it induces a specific gene subset including IFN-beta, inducible NO synthase and IL-12p35
indirect
PMID: 17667936,17018642
Upon TLR activation, IRF1 is activated by MyD88, causing it to translocate to the nucleus where it induces a specific gene subset including IFN-beta, inducible NO synthase and IL-12p35
indirect
PMID: 17667936,17018642
Upon TLR activation, IRF1 is activated by MyD88, causing it to translocate to the nucleus where it induces a specific gene subset including IFN-beta, inducible NO synthase and IL-12p35
PMID: 17667936
It is initiated in the case of TLR4 by the TIR domain of Mal binding the TIR domain of TLR4, which has dimerized after ligand binding.
PMID: 17667936
It is initiated in the case of TLR4 by the TIR domain of Mal binding the TIR domain of TLR4, which has dimerized after ligand binding.
PMID: 17667936
Figure 1
PMID: 17667936,14679297,14530355
TRIF mediates IRF3 activation via TRAF family member-associated NF-kappaB activator (TANK)-binding kinase 1 (TBK1), which associates with the N terminus of TRIF
PMID: 17667936
Figure 1
PMID: 17667936,14679297,14530355
TRIF mediates IRF3 activation via TRAF family member-associated NF-kappaB activator (TANK)-binding kinase 1 (TBK1), which associates with the N terminus of TRIF
indirect
PMID: 17667936
Figure 1
PMID: 17667936
Figure 1
indirect
PMID: 17667936
Figure 1
indirect
indirect
PMID: 17667936,16306937,16306936,15611223
Recently, both TRAF3 and NAK-associated protein 1 (NAP1) have been implicated in mediating the activation of TBK1 by TRIF by acting as a bridge between the two proteins
PMID: 17667936,15064760
TRIF also associates with receptor-interacting protein 1 (RIP1) via its C-terminal RIP homotypic interaction motif (RHIM), and in the absence of RIP1, TLR3-mediated NF-kappaB activation was abolished, suggesting that RIP1 mediates the TRIF-induced NF-kappaB activation
indirect
PMID: 17667936
Alternatively RIP1 is activated by TRIF and this feeds into the MyD88 pathway by activating TRAF6.
indirect
PMID: 17667936
Figure 1
PMID: 17667936,14517278
It functions as a bridging adaptor for the MyD88-independent signalling pathway, serving to recruit TRIF to TLR4
PMID: 17667936,14517278
It functions as a bridging adaptor for the MyD88-independent signalling pathway, serving to recruit TRIF to TLR4
PMID: 17667936
Figure 1
indirect
PMID: 17667936
Figure 1
indirect
PMID: 17667936
Alternatively RIP1 is activated by TRIF and this feeds into the MyD88 pathway by activating TRAF6.
indirect
PMID: 17667936
Figure 1
indirect
PMID: 17667936
Figure 1
indirect
PMID: 17667936
Figure 1
indirect
PMID: 17667936
It was found that TRAM was phosphorylated on serine-16 by PKCalt epsilon upon LPS stimulation
PMID: 17667936
Figure 2
PMID: 17667936
The TIR domain of TRIF was involved in the interaction with the TRAF-C domain of TRAF1, and inhibition most likely occurs through sequestration of the TIR domain.
PMID: 17667936
SARM associates with TRIF and blocks TRIF-induced NF-kappaB activation.
indirect
PMID: 17667936
SARM associates with TRIF and blocks TRIF-induced NF-kappaB activation.
indirect
PMID: 17667936
SARM associates with TRIF and blocks TRIF-induced NF-kappaB activation.
PMID: 17667936
It was found that the membrane bound form of ST2, which contains a TIR domain, specifically inhibited NF-kappaB activation downstream of IL-1R, TLR2, TLR4 and TLR9 but not TLR3.
PMID: 17667936
SARM associates with TRIF and blocks TRIF-induced NF-kappaB activation.
PMID: 17667936
Transforming growth factor-beta (TGF-beta) partly exerts its anti-inflammatory effects by causing direct ubiquitination of MyD88, thereby augmenting its degradation by the proteasome.
PMID: 17667936
Transforming growth factor-beta (TGF-beta) partly exerts its anti-inflammatory effects by causing direct ubiquitination of MyD88, thereby augmenting its degradation by the proteasome.
indirect
PMID: 17667936
It was found that the membrane bound form of ST2, which contains a TIR domain, specifically inhibited NF-kappaB activation downstream of IL-1R, TLR2, TLR4 and TLR9 but not TLR3.
indirect
PMID: 17667936
It was found that the membrane bound form of ST2, which contains a TIR domain, specifically inhibited NF-kappaB activation downstream of IL-1R, TLR2, TLR4 and TLR9 but not TLR3.
indirect
PMID: 17667936
It was found that the membrane bound form of ST2, which contains a TIR domain, specifically inhibited NF-kappaB activation downstream of IL-1R, TLR2, TLR4 and TLR9 but not TLR3.
PMID: 17667936
Indeed, Mal could associate with TRAF6 in a co-immunoprecipitation assay.
indirect
PMID: 17667936
It was also shown that Mal is phosphorylated by Bruton's tyrosine kinase (Btk) on tyrosine residues at positions 86 and 187, and this event is necessary for efficient TLR4 signalling.PMID: 17667936
A prerequisite for Mal degradation is tyrosine phosphorylation of Mal by Btk as this may allow SOCS1 to associate with Mal through its SH2 domain.PMID: 17667936
Here it was shown that SOCS1 mediates polyubiquitination of Mal on two N-terminal lysine residues, thereby mediating Mal degradation via the 26S proteasome.PMID: 17667936
Here it was shown that SOCS1 mediates polyubiquitination of Mal on two N-terminal lysine residues, thereby mediating Mal degradation via the 26S proteasome.indirectPMID: 17667936
It was also recently found that Mal is cleaved by caspase-1.PMID: 17667936,17161867
In addition, Mal was shown to interact via its TIR domain with protein kinase C-delta (PKCdelta)