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PMID: 16343886
Lipid-based structures are recognized by TLR2 (in combination with TLR1 or TLR6 as heterodimers) and TLR4 (as a homodimer): the most studied examples of lipid-based recognition are bacterial or mycobacterial lipopeptides, or glycerophosphatidylinositol anchors from parasites, both of which are recognized by TLR2, and bacterial lipopolysaccharide (LPS), which is recognized by TLR4.</csml:comment>
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PMID: 16343886
Lipid-based structures are recognized by TLR2 (in combination with TLR1 or TLR6 as heterodimers) and TLR4 (as a homodimer): the most studied examples of lipid-based recognition are bacterial or mycobacterial lipopeptides, or glycerophosphatidylinositol anchors from parasites, both of which are recognized by TLR2, and bacterial lipopolysaccharide (LPS), which is recognized by TLR4.</csml:comment>
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</csml:comment>
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</csml:comment>
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</csml:comment>
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PMID: 16343886, 15795223
The hypothesised model here involves the assembly of a TIR&#8211;TIR platform by the dimerization of two TLRs.</csml:comment>
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</csml:comment>
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</csml:comment>
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</csml:comment>
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PMID: 16343886
he most characterised are the recognition of double stranded RNA (dsRNA) by TLR3 and recognition of CpG motifs in DNA by TLR9.</csml:comment>
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</csml:comment>
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<csml:comment type="text">




PMID: 16343886
Lipid-based structures are recognized by TLR2 (in combination with TLR1 or TLR6 as heterodimers) and TLR4 (as a homodimer): the most studied examples of lipid-based recognition are bacterial or mycobacterial lipopeptides, or glycerophosphatidylinositol anchors from parasites, both of which are recognized by TLR2, and bacterial lipopolysaccharide (LPS), which is recognized by TLR4.</csml:comment>
</csml:comments>
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PMID: 16343886
It now appears, however, that CD14 can influence signalling by TLR4, and is required for activation of the Trif&#8211;Tram pathway by TLR4 because when CD14 is absent LPS can only engage with the MyD88 pathway.

PMID: 16343886
This is also the case with TLR4, but only when so-called &#8216;smooth&#8217; LPS, which has longer O-polysaccharide chains compared to &#8216;rough&#8217; LPS, is used as a ligand.</csml:comment>
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PMID: 16343886
It now appears, however, that CD14 can influence signalling by TLR4, and is required for activation of the Trif&#8211;Tram pathway by TLR4 because when CD14 is absent LPS can only engage with the MyD88 pathway.

PMID: 16343886
This is also the case with TLR4, but only when so-called &#8216;smooth&#8217; LPS, which has longer O-polysaccharide chains compared to &#8216;rough&#8217; LPS, is used as a ligand.</csml:comment>
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PMID: 16343886, 15690042
A role for other co-receptors is also emerging, with CD36 shown to be an essential co-receptor for TLR2.</csml:comment>
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PMID: 16343886, 15690042
A role for other co-receptors is also emerging, with CD36 shown to be an essential co-receptor for TLR2.</csml:comment>
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PMID: 16343886
Lipid-based structures are recognized by TLR2 (in combination with TLR1 or TLR6 as heterodimers) and TLR4 (as a homodimer): the most studied examples of lipid-based recognition are bacterial or mycobacterial lipopeptides, or glycerophosphatidylinositol anchors from parasites, both of which are recognized by TLR2, and bacterial lipopolysaccharide (LPS), which is recognized by TLR4.</csml:comment>
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PMID: 16343886
Lipid-based structures are recognized by TLR2 (in combination with TLR1 or TLR6 as heterodimers) and TLR4 (as a homodimer): the most studied examples of lipid-based recognition are bacterial or mycobacterial lipopeptides, or glycerophosphatidylinositol anchors from parasites, both of which are recognized by TLR2, and bacterial lipopolysaccharide (LPS), which is recognized by TLR4.</csml:comment>
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PMID: 16343886
Lipid-based structures are recognized by TLR2 (in combination with TLR1 or TLR6 as heterodimers) and TLR4 (as a homodimer): the most studied examples of lipid-based recognition are bacterial or mycobacterial lipopeptides, or glycerophosphatidylinositol anchors from parasites, both of which are recognized by TLR2, and bacterial lipopolysaccharide (LPS), which is recognized by TLR4.</csml:comment>
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PMID: 16343886
Lipid-based structures are recognized by TLR2 (in combination with TLR1 or TLR6 as heterodimers) and TLR4 (as a homodimer): the most studied examples of lipid-based recognition are bacterial or mycobacterial lipopeptides, or glycerophosphatidylinositol anchors from parasites, both of which are recognized by TLR2, and bacterial lipopolysaccharide (LPS), which is recognized by TLR4.</csml:comment>
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PMID: 16343886, 15860593
Finally, TLR5 and TLR11 recognize proteins from pathogens (flagellin in the case of TLR5 and profilin in the case of TLR11 [only in the mouse]).</csml:comment>
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PMID: 16343886, 15860593
Finally, TLR5 and TLR11 recognize proteins from pathogens (flagellin in the case of TLR5 and profilin in the case of TLR11 [only in the mouse]).</csml:comment>
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PMID: 16343886
he most characterised are the recognition of double stranded RNA (dsRNA) by TLR3 and recognition of CpG motifs in DNA by TLR9.</csml:comment>
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PMID: 16343886, 15795223
The hypothesised model here involves the assembly of a TIR&#8211;TIR platform by the dimerization of two TLRs.</csml:comment>
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PMID: 16343886
This platform then recruits MyD88, leading in turn to the recruitment of IRAK-4 (whose death domain interacts with the death domain of MyD88). IRAK-4 becomes activated and phosphorylates IRAK-1 (which might already be in the complex, as it also has a death domain).

PMID: 16343886, 15004556
An early demonstration of this was the observation that ST2, which is another member of the IL-1R subgroup of TIR proteins, inhibits TLR signalling in macrophages by sequestering MyD88 and Mal from signalling pathways.</csml:comment>
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PMID: 16343886
This platform then recruits MyD88, leading in turn to the recruitment of IRAK-4 (whose death domain interacts with the death domain of MyD88). IRAK-4 becomes activated and phosphorylates IRAK-1 (which might already be in the complex, as it also has a death domain).

PMID: 16343886
MyD88s lacks a region important for IRAK-4 recruitment and so IRAK-4 is not engaged, hence limiting NF-kappaB activation.</csml:comment>
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PMID: 16343886
This platform then recruits MyD88, leading in turn to the recruitment of IRAK-4 (whose death domain interacts with the death domain of MyD88). IRAK-4 becomes activated and phosphorylates IRAK-1 (which might already be in the complex, as it also has a death domain).</csml:comment>
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PMID: 16343886
This platform then recruits MyD88, leading in turn to the recruitment of IRAK-4 (whose death domain interacts with the death domain of MyD88). IRAK-4 becomes activated and phosphorylates IRAK-1 (which might already be in the complex, as it also has a death domain).</csml:comment>
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</csml:comment>
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<csml:comment type="text">



</csml:comment>
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PMID: 16343886
Phosphorylated IRAK-1 is active, and then somehow activates Traf-6.</csml:comment>
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PMID: 16343886
Phosphorylated IRAK-1 is active, and then somehow activates Traf-6.</csml:comment>
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PMID: 16343886
Phosphorylated IRAK-1 is active, and then somehow activates Traf-6.</csml:comment>
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PMID: 16343886
A series of ubiquitinylation reactions then occur on Traf-6 itself and on the protein kinase TAK-1, which is a candidate kinase for the activation of the inhibitor of NF-kappaB kinase (IKK) complex, leading to NF-kappaB activation, and activation of upstream kinases for p38 and JNK.</csml:comment>
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PMID: 16343886
A series of ubiquitinylation reactions then occur on Traf-6 itself and on the protein kinase TAK-1, which is a candidate kinase for the activation of the inhibitor of NF-kappaB kinase (IKK) complex, leading to NF-kappaB activation, and activation of upstream kinases for p38 and JNK.</csml:comment>
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PMID: 16343886
A series of ubiquitinylation reactions then occur on Traf-6 itself and on the protein kinase TAK-1, which is a candidate kinase for the activation of the inhibitor of NF-kappaB kinase (IKK) complex, leading to NF-kappaB activation, and activation of upstream kinases for p38 and JNK.</csml:comment>
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PMID: 16343886
A series of ubiquitinylation reactions then occur on Traf-6 itself and on the protein kinase TAK-1, which is a candidate kinase for the activation of the inhibitor of NF-kappaB kinase (IKK) complex, leading to NF-kappaB activation, and activation of upstream kinases for p38 and JNK.</csml:comment>
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PMID: 16343886
A series of ubiquitinylation reactions then occur on Traf-6 itself and on the protein kinase TAK-1, which is a candidate kinase for the activation of the inhibitor of NF-kappaB kinase (IKK) complex, leading to NF-kappaB activation, and activation of upstream kinases for p38 and JNK.</csml:comment>
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Indirect</csml:comment>
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PMID: 16343886
A series of ubiquitinylation reactions then occur on Traf-6 itself and on the protein kinase TAK-1, which is a candidate kinase for the activation of the inhibitor of NF-kappaB kinase (IKK) complex, leading to NF-kappaB activation, and activation of upstream kinases for p38 and JNK.</csml:comment>
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PMID: 16343886
A series of ubiquitinylation reactions then occur on Traf-6 itself and on the protein kinase TAK-1, which is a candidate kinase for the activation of the inhibitor of NF-kappaB kinase (IKK) complex, leading to NF-kappaB activation, and activation of upstream kinases for p38 and JNK.</csml:comment>
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PMID: 16343886, 11544529, 11526399
The discovery of the second TIR domain-containing adaptor, MyD88 adaptor-like (Mal), also known as TIRAP, indicated that there might be specificity in the signalling pathways, particularly when Mal was shown to have a role in TLR4, but not IL-1, signalling to NF-kappaB.

PMID: 16343886, 15004556
An early demonstration of this was the observation that ST2, which is another member of the IL-1R subgroup of TIR proteins, inhibits TLR signalling in macrophages by sequestering MyD88 and Mal from signalling pathways.</csml:comment>
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PMID: 16343886, 15849357
MyD88 homodimerization has been shown to involve another region of the TIR domain called Box 3.</csml:comment>
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PMID: 16343886, 12471095, 12692549
A third adaptor was then described, termed TIR-related adaptor protein inducing interferon (Trif), which is recruited by both TLR4 and TLR3, and is responsible for activation of IRF3 [10, 11 and 12], acting via an IKK-like kinase termed TBK-1.

PMID: 16343886, 14517278, 14519765, 14556004
The fourth adaptor to be described was named Trif-related adaptor molecule (Tram), and interestingly acts only in TLR4 signalling, where it interacts with Trif.</csml:comment>
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PMID: 16343886, 12471095, 12692549
A third adaptor was then described, termed TIR-related adaptor protein inducing interferon (Trif), which is recruited by both TLR4 and TLR3, and is responsible for activation of IRF3 [10, 11 and 12], acting via an IKK-like kinase termed TBK-1.</csml:comment>
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PMID: 16343886
The discovery of Trif provided the first molecular basis for why TLR3 and TLR4, but not TLR2, are able to induce IFN-beta &#8212; both TLR3 and TLR4 can signal via Trif to the IKK family kinase TBK-1, which phosphorylates IRF3.</csml:comment>
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PMID: 16343886
The discovery of Trif provided the first molecular basis for why TLR3 and TLR4, but not TLR2, are able to induce IFN-beta &#8212; both TLR3 and TLR4 can signal via Trif to the IKK family kinase TBK-1, which phosphorylates IRF3.</csml:comment>
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Indirect</csml:comment>
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PMID: 16343886
The discovery of Trif provided the first molecular basis for why TLR3 and TLR4, but not TLR2, are able to induce IFN-beta &#8212; both TLR3 and TLR4 can signal via Trif to the IKK family kinase TBK-1, which phosphorylates IRF3.

PMID: 16343886
TLR3 activates IRF3 homodimers which then bind the interferon sensitive response element (ISRE) on target genes, such as IFN-beta.</csml:comment>
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Indirect</csml:comment>
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PMID: 16343886
The discovery of Trif provided the first molecular basis for why TLR3 and TLR4, but not TLR2, are able to induce IFN-beta &#8212; both TLR3 and TLR4 can signal via Trif to the IKK family kinase TBK-1, which phosphorylates IRF3.

PMID: 16343886, 1455726
For TLR4, a complex of p65 and IRF3 is activated.</csml:comment>
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Indirect</csml:comment>
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PMID: 16343886
The discovery of Trif provided the first molecular basis for why TLR3 and TLR4, but not TLR2, are able to induce IFN-beta &#8212; both TLR3 and TLR4 can signal via Trif to the IKK family kinase TBK-1, which phosphorylates IRF3.

PMID: 16343886
This limits the induction of IFN-beta by TLR3 during infection and might contribute to the persistence of the virus.</csml:comment>
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PMID: 16343886, 15849357
A recent study has, however, identified three other amino acids in the BB loop of MyD88 (Asp195, Arg196 and Asp197) as important for interaction with the IL-1 receptor accessory protein (IL-1AcP, which also has a TIR domain and is required for IL-1 signalling in complex with IL-1RI.</csml:comment>
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PMID: 16343886, 15849357
A recent study has, however, identified three other amino acids in the BB loop of MyD88 (Asp195, Arg196 and Asp197) as important for interaction with the IL-1 receptor accessory protein (IL-1AcP, which also has a TIR domain and is required for IL-1 signalling in complex with IL-1RI.</csml:comment>
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PMID: 16343886, 15849357
A recent study has, however, identified three other amino acids in the BB loop of MyD88 (Asp195, Arg196 and Asp197) as important for interaction with the IL-1 receptor accessory protein (IL-1AcP, which also has a TIR domain and is required for IL-1 signalling in complex with IL-1RI.</csml:comment>
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Indirect</csml:comment>
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Indirect</csml:comment>
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</csml:comment>
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<csml:comment type="text">




PMID: 16343886
It appears that activation of Trif by LPS leads to the rapid production of TNF, which is dependent on IRF3.</csml:comment>
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Indirect</csml:comment>
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</csml:comment>
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PMID: 16343886
Perhaps TNF induction requires an interplay between NF-kappaB, activated by MyD88, and IRF3, activated by Trif, whereas IFN-beta only requires IRF3.</csml:comment>
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PMID: 16343886
TLR9, similar to IL-1, apparently only requires MyD88 for signalling, and yet, unlike IL-1, is a strong inducer of IFN-alpha, but only in plasmacytoid dendritic cells.</csml:comment>
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Indirect</csml:comment>
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PMID: 16343886
TLR9, similar to IL-1, apparently only requires MyD88 for signalling, and yet, unlike IL-1, is a strong inducer of IFN-alpha, but only in plasmacytoid dendritic cells.</csml:comment>
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</csml:comment>
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PMID: 16343886, 15815647, 15800576, 15767370
Honda and colleagues now provide an explanation for this: IFN-alpha production requires the transcription factor IRF7, and this protein has been shown to associate with MyD88.In plasmacytoid dendritic cells, the IFN-alpha-inducing TLR9 ligand CpG-A is retained for long periods in endosomal vesicles together with the MyD88&#8211;IRF7 complex.</csml:comment>
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PMID: 16343886
MyD88s lacks a region important for IRAK-4 recruitment and so IRAK-4 is not engaged, hence limiting NF-kappaB activation.</csml:comment>
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Indirect</csml:comment>
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PMID: 16343886, 15623538
TGF-beta blocks TLR signalling by causing the ubiquitinylation and proteasomal degradation of MyD88 [36]. This may be a key aspect of the anti-inflammatory effects of TGF-beta.

</csml:comment>
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PMID: 16343886, 15623538
TGF-beta blocks TLR signalling by causing the ubiquitinylation and proteasomal degradation of MyD88 [36]. This may be a key aspect of the anti-inflammatory effects of TGF-beta.</csml:comment>
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Indirect</csml:comment>
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</csml:comment>
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PMID: 16343886, 15710891
Also of interest is the observation that the hepatitis C virus protein NS3/4A can cleave and inactivate Trif.</csml:comment>
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Indirect</csml:comment>
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PMID: 16343886, 15800576, 15767370, 15361868
IRF7 is a key transcription factor for induction of type I interferons, and its activation occurs by both MyD88-dependent pathways (activated by TLR9) and Trif pathways (activated via TBK-1).</csml:comment>
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Indirect</csml:comment>
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</csml:comment>
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<csml:comment type="text">



PMID: 16343886, 15800576, 15767370, 15361868
IRF7 is a key transcription factor for induction of type I interferons, and its activation occurs by both MyD88-dependent pathways (activated by TLR9) and Trif pathways (activated via TBK-1).</csml:comment>
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</csml:comment>
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<csml:parameter key="coefficient1" value="0.1"/>
<csml:parameter key="coefficient2" value="1.0"/>
</csml:processKinetic>
</csml:processSimulationProperty>
<csml:viewProperty>
<csml:position positionID="default" position="auto" x="642.0" y="353.0"/>
<csml:shape shapeID="default" visible="true">
<csml:image width="23.0" height="23.0" filePath="" fileType="resourceFile" fileFormat="svg" resourceID="10005" outlineColor="0 0 0 0"></csml:image>
<csml:toolSpecificGraphics/>
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<csml:comments>
<csml:comment type="text">


PMID: 16343886
IRF7 associates directly with both IRAK-4 and IRAK-1.</csml:comment>
</csml:comments>
</csml:process>
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</csml:comment>
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</csml:comment>
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</csml:comment>
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</csml:processKinetic>
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<csml:comment type="text">


PMID: 16343886
IRF5 is essential for the induction of a range of pro-inflammatory genes, including IL-6, IL-12 and TNF, but not IFN-alpha, and is found in a trimeric complex with MyD88 and Traf6.</csml:comment>
</csml:comments>
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<csml:comments>
<csml:comment type="text">


Indirect</csml:comment>
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</csml:comment>
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<csml:comments>
<csml:comment type="text">


PMID: 16343886
IRF5 is essential for the induction of a range of pro-inflammatory genes, including IL-6, IL-12 and TNF, but not IFN-alpha, and is found in a trimeric complex with MyD88 and Traf6.</csml:comment>
</csml:comments>
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<csml:comments>
<csml:comment type="text">


Indirect</csml:comment>
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</csml:comment>
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<csml:comments>
<csml:comment type="text">


PMID: 16343886
IRF5 is essential for the induction of a range of pro-inflammatory genes, including IL-6, IL-12 and TNF, but not IFN-alpha, and is found in a trimeric complex with MyD88 and Traf6.</csml:comment>
</csml:comments>
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</csml:viewProperty>
<csml:comments>
<csml:comment type="text">


Indirect</csml:comment>
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</csml:connectorSimulationProperty>
<csml:viewProperty>
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</csml:comment>
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PMID: 16343886
IRF5 is essential for the induction of a range of pro-inflammatory genes, including IL-6, IL-12 and TNF, but not IFN-alpha, and is found in a trimeric complex with MyD88 and Traf6.</csml:comment>
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Indirect</csml:comment>
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</csml:comment>
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PMID: 16343886
The discovery of Trif provided the first molecular basis for why TLR3 and TLR4, but not TLR2, are able to induce IFN-beta &#8212; both TLR3 and TLR4 can signal via Trif to the IKK family kinase TBK-1, which phosphorylates IRF3.

PMID: 16343886
This limits the induction of IFN-b
by TLR3 during infection and might contribute to the
persistence of the virus.</csml:comment>
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<csml:comment type="text"></csml:comment>
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<csml:comment type="text">
PMID: 16343886
A notable example of a gene activated by this pathway is IL-6, which is regulated by IkappaB-zeta in a complex with p50.</csml:comment>
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</csml:processSimulationProperty>
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<csml:comments>
<csml:comment type="text">PMID: 16343886, 15665823
Another IRF, IRF5, is found downstream of MyD88, and
so is activated by multiple TLRs</csml:comment>
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<csml:comments>
<csml:comment type="text">




</csml:comment>
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