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PMID: 16419614
The host defence against microorganisms mediated by TLRs relies mainly on signalling pathways induced by a common Toll-interleukin 1 receptor (TIR) domain and shows a high homology to that of the IL-1R (IL-1 receptor) family.</csml:comment>
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PMID: 16419614, 11544529, 11526399
In the process of analysing the MyD88-independent activation of the LPS-TLR4 signalling a novel adaptor protein named TIRAP or Mal was discovered (Fitzgerald et al. 2001; Horng et al., 2001).</csml:comment>
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PMID: 16419614, 11544529, 11526399
In the process of analysing the MyD88-independent activation of the LPS-TLR4 signalling a novel adaptor protein named TIRAP or Mal was discovered (Fitzgerald et al. 2001; Horng et al., 2001).</csml:comment>
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PMID: 16419614
Hence, in LPS signalling, the TLR4 recruits two types of adaptors, TIRAP and TRAM, to its cytoplasmic domain that are indirectly connected to two effec-tive adaptors, MyD88 and TRIF, respectively.</csml:comment>
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PMID: 16419614
NK cells are major players in the antiviral immune response and express TLR3 and are activated directly in response to poly(I:C).</csml:comment>
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PMID: 16419614, 11489966
Accordingly, TLR5, the receptor for flagellin, is exclusively expressed on the basolateral, but not the apical surface of the intestinal epithelial cells (Gewirtz et al., 2001).</csml:comment>
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PMID: 16419614
Renal inflammation evoked by ischaemia markedly enhanced synthesis of TLR2 and TLR4 mRNA followed by significant elevation of protein expression in the distal tubular epithelium, the thin limb of Henle&#8217;s loop and collecting ducts. This phenomenon was shown to be completely dependent on the action of IFN-gamma and TNF.

PMID: 16419614
Preincubation with TNF or IFN-gamma significantly induces endothelial TLR2 expression.</csml:comment>
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PMID: 16419614
Renal inflammation evoked by ischaemia markedly enhanced synthesis of TLR2 and TLR4 mRNA followed by significant elevation of protein expression in the distal tubular epithelium, the thin limb of Henle&#8217;s loop and collecting ducts. This phenomenon was shown to be completely dependent on the action of IFN-gamma and TNF.

PMID: 16419614
Preincubation with TNF or IFN-gamma significantly induces endothelial TLR2 expression.</csml:comment>
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PMID: 16419614
Renal inflammation evoked by ischaemia markedly enhanced synthesis of TLR2 and TLR4 mRNA followed by significant elevation of protein expression in the distal tubular epithelium, the thin limb of Henle&#8217;s loop and collecting ducts. This phenomenon was shown to be completely dependent on the action of IFN-gamma and TNF.</csml:comment>
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PMID: 16419614
Renal inflammation evoked by ischaemia markedly enhanced synthesis of TLR2 and TLR4 mRNA followed by significant elevation of protein expression in the distal tubular epithelium, the thin limb of Henle&#8217;s loop and collecting ducts. This phenomenon was shown to be completely dependent on the action of IFN-gamma and TNF.</csml:comment>
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PMID: 16419614
The host defence against microorganisms mediated by TLRs relies mainly on signalling pathways induced by a common Toll-interleukin 1 receptor (TIR) domain and shows a high homology to that of the IL-1R (IL-1 receptor) family.</csml:comment>
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PMID: 16419614
Both TLRs and IL-1R interact with the intracellular adaptor protein MyD88 (myeloid differentiation factor).</csml:comment>
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PMID: 16419614
Both TLRs and IL-1R interact with the intracellular adaptor protein MyD88 (myeloid differentiation factor).</csml:comment>
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PMID: 16419614
MyD88 afterwards recruits the serine/threonine kinase IRAK.

PMID: 16419614
Before IL-1 treatment, Tollip is present in a complex with IRAK. Following the IL-1 stimulation, the recruitment of Tollip-IRAK complexes to the activated IL-1R occurs through the association of Tollip with IL-1R.</csml:comment>
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PMID: 16419614
MyD88 afterwards recruits the serine/threonine kinase IRAK.

PMID: 16419614
Before IL-1 treatment, Tollip is present in a complex with IRAK. Following the IL-1 stimulation, the recruitment of Tollip-IRAK complexes to the activated IL-1R occurs through the association of Tollip with IL-1R.</csml:comment>
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PMID: 16419614
This, similarly to MyD88, contains DD and upon recruitment to MyD88 via DD-domain interactions is phosphorylated and subsequently associated with TRAF-6.</csml:comment>
</csml:comments>
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PMID: 16419614
This, similarly to MyD88, contains DD and upon recruitment to MyD88 via DD-domain interactions is phosphorylated and subsequently associated with TRAF-6.</csml:comment>
</csml:comments>
</csml:process>
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PMID: 16419614
This, similarly to MyD88, contains DD and upon recruitment to MyD88 via DD-domain interactions is phosphorylated and subsequently associated with TRAF-6.

PMID: 16419614, 10854325
Co-recruited MyD88 then triggers IRAK autophosphorylation, which in turn leads to rapid dissociation of IRAK from Tollip (Burns et al., 2000).</csml:comment>
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<csml:comment type="text">
PMID: 16419614
This, similarly to MyD88, contains DD and upon recruitment to MyD88 via DD-domain interactions is phosphorylated and subsequently associated with TRAF-6.

PMID: 16419614, 10854325
Co-recruited MyD88 then triggers IRAK autophosphorylation, which in turn leads to rapid dissociation of IRAK from Tollip (Burns et al., 2000).</csml:comment>
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Indirect</csml:comment>
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<csml:comments>
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</csml:comment>
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<csml:priority value="0"/>
<csml:firing firingStyle="csml-firingStyle:and" firingOnce="false" type="csml-variable:Boolean" value="true"/>
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<csml:processKinetic calcStyle="csml-calcStyle:speed" kineticStyle="csml-kineticStyle:mass" fast="false">
<csml:parameter key="coefficient1" value="0.1"/>
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</csml:processKinetic>
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<csml:comment type="text">
PMID: 16419614, 9374458
Its activation in turn leads to initiation of two distinct downstream pathways resulting in activation of NF-kappaB and AP-1 transcription factors (Muzio et al., 1997; 1998).</csml:comment>
</csml:comments>
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Indirect</csml:comment>
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PMID: 16419614, 9374458
Its activation in turn leads to initiation of two distinct downstream pathways resulting in activation of NF-kappaB and AP-1 transcription factors (Muzio et al., 1997; 1998).</csml:comment>
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PMID: 16419614
Hence, in LPS signalling, the TLR4 recruits two types of adaptors, TIRAP and TRAM, to its cytoplasmic domain that are indirectly connected to two effec-tive adaptors, MyD88 and TRIF, respectively.</csml:comment>
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PMID: 16419614
Hence, in LPS signalling, the TLR4 recruits two types of adaptors, TIRAP and TRAM, to its cytoplasmic domain that are indirectly connected to two effec-tive adaptors, MyD88 and TRIF, respectively.</csml:comment>
</csml:comments>
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PMID: 16419614, 10854325
Co-recruited MyD88 then triggers IRAK autophosphorylation, which in turn leads to rapid dissociation of IRAK from Tollip (Burns et al., 2000).</csml:comment>
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PMID: 16419614, 10854325
Co-recruited MyD88 then triggers IRAK autophosphorylation, which in turn leads to rapid dissociation of IRAK from Tollip (Burns et al., 2000).</csml:comment>
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PMID: 16419614
The inhibition of NF-kappaB activation in response to IL-1, as well as TLR2 and TLR4 ligands (Fig. 1), is mediated through the ability of Tollip to suppress the activity of IRAK.</csml:comment>
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PMID: 16419614, 10854325
Co-recruited MyD88 then triggers IRAK autophosphorylation, which in turn leads to rapid dissociation of IRAK from Tollip (Burns et al., 2000).</csml:comment>
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PMID: 16419614, 10854325
Co-recruited MyD88 then triggers IRAK autophosphorylation, which in turn leads to rapid dissociation of IRAK from Tollip (Burns et al., 2000).</csml:comment>
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PMID: 16419614
This, similarly to MyD88, contains DD and upon recruitment to MyD88 via DD-domain interactions is phosphorylated and subsequently associated with TRAF-6</csml:comment>
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PMID: 16419614
TIRAP/Mal forms dimers with MyD88 followed by association with IRAK and activation of NF-kappaB (Fig. 1).</csml:comment>
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TIRAP/Mal forms dimers with MyD88 followed by association with IRAK and activation of NF-kappaB (Fig. 1).</csml:comment>
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PMID: 16419614
TIRAP/Mal forms dimers with MyD88 followed by association with IRAK and activation of NF-kappaB (Fig. 1).</csml:comment>
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PMID: 16419614
TIRAP/Mal forms dimers with MyD88 followed by association with IRAK and activation of NF-kappaB (Fig. 1).</csml:comment>
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PMID: 16419614, 12447441
Further data suggest that TIRAP/Mal is not specific to TLR4 signalling and that it takes part in the TLR2 signalling as well; however, it does not participate in the MyD88- independent pathway (Yamamoto et al., 2002). </csml:comment>
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PMID: 16419614, 12447441
Further data suggest that TIRAP/Mal is not specific to TLR4 signalling and that it takes part in the TLR2 signalling as well; however, it does not participate in the MyD88- independent pathway (Yamamoto et al., 2002). </csml:comment>
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Indirect</csml:comment>
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PMID: 16419614, 12447441
Further data suggest that TIRAP/Mal is not specific to TLR4 signalling and that it takes part in the TLR2 signalling as well; however, it does not parti</csml:comment>
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PMID: 16419614
The inhibition of NF-kappaB activation in response to IL-1, as well as TLR2 and TLR4 ligands (Fig. 1), is mediated through the ability of Tollip to suppress the activity of IRAK.</csml:comment>
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PMID: 16419614, 10854325
Co-recruited MyD88 then triggers IRAK autophosphorylation, which in turn leads to rapid dissociation of IRAK from Tollip (Burns et al., 2000).</csml:comment>
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PMID: 16419614, 10854325
Co-recruited MyD88 then triggers IRAK autophosphorylation, which in turn leads to rapid dissociation of IRAK from Tollip (Burns et al., 2000).</csml:comment>
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PMID: 16419614
This, similarly to MyD88, contains DD and upon recruitment to MyD88 via DD-domain interactions is phosphorylated and subsequently associated with TRAF-6.</csml:comment>
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Indirect</csml:comment>
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PMID: 16419614
The inhibition of NF-kappaB activation in response to IL-1, as well as TLR2 and TLR4 ligands (Fig. 1), is mediated through the ability of Tollip to suppress the activity of IRAK.</csml:comment>
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PMID: 16419614, 11607032
Similarly to LPS, the dsRNA stimulation of TLR3 in the MyD88- deficient cells induced activation of NF-kappaB, but no production of inflammatory cytokines (Alexopoulou et al.,2001).</csml:comment>
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PMID: 16419614, 12539043, 14519765
Thus, dsRNA-TLR3-dependent production of IFN-beta is mediated mainly by TRIF/TICAM-1.</csml:comment>
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PMID: 16419614
TRIF physically associates with TLR3 and IRF-3 in response to poly(I:C).</csml:comment>
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PMID: 16419614
TRIF physically associates with TLR3 and IRF-3 in response to poly(I:C).</csml:comment>
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PMID: 16419614
In these experiments, TRIF was found to recruit TRAF-6 to TLR3 through its TRAF6-binding site.</csml:comment>
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PMID: 16419614, 14982987
Furthermore, mutation of the TRAF6-binding site of TRIF only abolished its ability to activate NF-kappaB but not IRF3, suggesting that TLR3-mediated activation of NF-kappaB and IRF3 might bifurcate at TRIF (Jiang et al., 2004).</csml:comment>
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PMID: 16419614
Recently, two IKK-related kinases, inducible IkappaB kinase (IKK-i) and TANK-binding kinase 1 (TBK1), were suggested to act as IRF-3 kinases and to be involved in IFN-beta production in TLR signalling and viral infection (Fig. 1, Fig. 2b).

PMID: 16419614
Thus, viral infection or dsRNA stimulation via TLR3 as well as LPS stimulation via TLR4 induces phosphorylation and subsequent activation of IRF-3 and its translocation to the nucleus, thereby leading to the IFN-beta gene expression.</csml:comment>
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PMID: 16419614
Restricted to the TLR4 pathway, TRAM activates IRF-3, IRF-7, and NF-kappaB-dependent signalling pathways in MyD88-independent manner (Figs. 1, 2a).

PMID: 16419614
Recently, two IKK-related kinases, inducible IkappaB kinase (IKK-i) and TANK-binding kinase 1 (TBK1), were suggested to act as IRF-3 kinases and to be involved in IFN-beta production in TLR signalling and viral infection (Fig. 1, Fig. 2b).

PMID: 16419614
Thus, viral infection or dsRNA stimulation via TLR3 as well as LPS stimulation via TLR4 induces phosphorylation and subsequent activation of IRF-3 and its translocation to the nucleus, thereby leading to the IFN-beta gene expression.</csml:comment>
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PMID: 16419614
Restricted to the TLR4 pathway, TRAM activates IRF-3, IRF-7, and NF-kappaB-dependent signalling pathways in MyD88-independent manner (Figs. 1, 2a).</csml:comment>
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PMID: 16419614
Restricted to the TLR4 pathway, TRAM activates IRF-3, IRF-7, and NF-kappaB-dependent signalling pathways in MyD88-independent manner (Figs. 1, 2a).</csml:comment>
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PMID: 16419614
Thus, viral infection or dsRNA stimulation via TLR3 as well as LPS stimulation via TLR4 induces phosphorylation and subsequent activation of IRF-3 and its translocation to the nucleus, thereby leading to the IFN-beta gene expression.</csml:comment>
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PMID: 16419614
Thus, viral infection or dsRNA stimulation via TLR3 as well as LPS stimulation via TLR4 induces phosphorylation and subsequent activation of IRF-3 and its translocation to the nucleus, thereby leading to the IFN-beta gene expression.

PMID: 16419614
Activated by TLR3 and TLR4, IRF-3 binds the interferon-sensitive response element (ISRE) in DNA and induces expression of the IFN-beta gene.</csml:comment>
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PMID: 16419614
Activated by TLR3 and TLR4, IRF-3 binds the interferon-sensitive response element (ISRE) in DNA and induces expression of the IFN-beta gene.</csml:comment>
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PMID: 16419614, 11790540, 15800576
IRF-7 is also induced by viral infection and is critically involved in the system of IFN-alpha/beta gene induction (Taniguchi et al., 2002, Honda et al., 2005).</csml:comment>
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PMID: 16419614, 11790540, 15800576
IRF-7 is also induced by viral infection and is critically involved in the system of IFN-alpha/beta gene induction (Taniguchi et al., 2002, Honda et al., 2005).</csml:comment>
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PMID: 16419614
In the TLR2-mediated signalling, stimulation of human monocytes by S. aureus induces a fast and transient activation of the Rho GTPases Rac1 and Cdc42 followed by the recruitment of active Rac1 and phosphatidylinositol-3 kinase (PI3K) to the TLR2 cytosolic domain.</csml:comment>
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PMID: 16419614, 11101877
This in turn activates Akt kinase that induces activation and translocation of the p65 subunit of NF-kappaB into the cell nucleus in a process that is independent of IkappaB degradation.</csml:comment>
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PMID: 16419614, 11101877
This in turn activates Akt kinase that induces activation and translocation of the p65 subunit of NF-kappaB into the cell nucleus in a process that is independent of IkappaB degradation.</csml:comment>
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PMID: 16419614, 11101877
This in turn activates Akt kinase that induces activation and translocation of the p65 subunit of NF-kappaB into the cell nucleus in a process that is independent of IkappaB degradation.</csml:comment>
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</csml:comment>
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PMID: 16419614
NK cells also seem to be able to respond directly to other viral TLR stimuli, such as CpG DNA.</csml:comment>
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PMID: 16419614
However, all these effects are MyD88-dependent.</csml:comment>
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Indirect</csml:comment>
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</csml:comment>
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<csml:comment type="text">
PMID: 16419614
Similar to the LPS response, TLR9 signalling can also induce expression of IFN-beta and IFN-inducible genes, and upregulation of CD40.</csml:comment>
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Indirect</csml:comment>
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</csml:comment>
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<csml:comment type="text">
PMID: 16419614
Similar to the LPS response, TLR9 signalling can also induce expression of IFN-beta and IFN-inducible genes, and upregulation of CD40.</csml:comment>
</csml:comments>
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PMID: 16419614
Similar to the LPS response, TLR9 signalling can also induce expression of IFN-beta and IFN-inducible genes, and upregulation of CD40.</csml:comment>
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PMID: 16419614, 9374458
Its activation in turn leads to initiation of two distinct downstream pathways resulting in activation of NF-kappaB and AP-1 transcription factors (Muzio et al., 1997; 1998).

PMID: 16419614, 7622446
The activation of the AP-1 is induced through phosphorylation by the MAP kinases such as JNK and ERK, respectively, that are activated by means of TLR or IL-1R engagement (Karin, 1995).</csml:comment>
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PMID: 16419614, 10626894
Not just a bacterial, but also a viral infection or dsRNA induce JNK kinase, leading to stimulation of AP-1 (Chu et al., 1999).</csml:comment>
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Indirect</csml:comment>
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PMID: 16419614, 1744583, 10318814
TLR4 ligand LPS and various TLR2 ligands rapidly activated JNK kinases, which was followed by activation of the AP-1 transcription factor (Mackman et al., 1991; Gupta et al., 1999).</csml:comment>
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PMID: 16419614, 7622446
The activation of the AP-1 is induced through phosphorylation by the MAP kinases such as JNK and ERK, respectively, that are activated by means of TLR or IL-1R engagement (Karin, 1995).</csml:comment>
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PMID: 16419614, 7622446
The activation of the AP-1 is induced through phosphorylation by the MAP kinases such as JNK and ERK, respectively, that are activated by means of TLR or IL-1R engagement (Karin, 1995).</csml:comment>
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PMID: 16419614, 7622446
The activation of the AP-1 is induced through phosphorylation by the MAP kinases such as JNK and ERK, respectively, that are activated by means of TLR or IL-1R engagement (Karin, 1995).</csml:comment>
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PMID: 16419614, 7622446
The activation of the AP-1 is induced through phosphorylation by the MAP kinases such as JNK and ERK, respectively, that are activated by means of TLR or IL-1R engagement (Karin, 1995).</csml:comment>
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PMID: 16419614, 12829592
The agonists of all TLRs expressed in neutrophils triggered cytokine release, superoxide generation, L-selectin  shedding and increased phagocytosis of opsonised latex beads (Hayashi et al., 2003).</csml:comment>
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PMID: 16419614, 12829592
The agonists of all TLRs expressed in neutrophils triggered cytokine release, superoxide generation, L-selectin  shedding and increased phagocytosis of opsonised latex beads (Hayashi et al., 2003).</csml:comment>
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PMID: 16419614, 15995707
Indeed, recently it was found that agonists of TLR3 and TLR4 had acted in synergy with agonists of TLR8 in inducing IL-12, IL-23 and Delta-4 in amounts that were 50- to 100-fold higher than those induced by optimal concentrations of single agonists leading to enhanced and sustained TH1- polarizing capacity (Napolitani et al., 2005).</csml:comment>
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PMID: 16419614, 15995707
Indeed, recently it was found that agonists of TLR3 and TLR4 had acted in synergy with agonists of TLR8 in inducing IL-12, IL-23 and Delta-4 in amounts that were 50- to 100-fold higher than those induced by optimal concentrations of single agonists leading to enhanced and sustained TH1- polarizing capacity (Napolitani et al., 2005).</csml:comment>
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PMID: 16419614, 15995707
Indeed, recently it was found that agonists of TLR3 and TLR4 had acted in synergy with agonists of TLR8 in inducing IL-12, IL-23 and Delta-4 in amounts that were 50- to 100-fold higher than those induced by optimal concentrations of single agonists leading to enhanced and sustained TH1- polarizing capacity (Napolitani et al., 2005).</csml:comment>
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PMID: 16419614
Initially, NF-kappaB (nuclear factorkappa B) was found to be essential for the transcription of immunoglobulin light chain genes in B cells.</csml:comment>
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PMID: 16419614
NF-IL6 (nuclear factor-IL6) specifically binds to an IL-1-responsive element in the IL-6 gene.</csml:comment>
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PMID: 16419614, 2112087
Interestingly, NF-IL6 was shown to bind to regulatory regions of various acute-phase protein and several other cytokine genes such as TNF, IL-8 and G-CSF, implying that NF-IL6 has a role in the regulation ot only of the IL-6 gene, but also of several other genes involved in acute-phase reaction, inflammation and haematopoiesis (Akira et al., 1990).</csml:comment>
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Indirect</csml:comment>
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PMID: 16419614
The NF-IL6 mRNA was induced by the stimulation with LPS, IL-1 or IL-6.</csml:comment>
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PMID: 16419614
The NF-IL6 mRNA was induced by the stimulation with LPS, IL-1 or IL-6.</csml:comment>
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PMID: 16419614
The NF-IL6 mRNA was induced by the stimulation with LPS, IL-1 or IL-6.</csml:comment>
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PMID: 16419614, 2112087
Interestingly, NF-IL6 was shown to bind to regulatory regions of various acute-phase protein and several other cytokine genes such as TNF, IL-8 and G-CSF, implying that NF-IL6 has a role in the regulation ot only of the IL-6 gene, but also of several other genes involved in acute-phase reaction, inflammation and haematopoiesis (Akira et al., 1990).</csml:comment>
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PMID: 16419614, 2112087
Interestingly, NF-IL6 was shown to bind to regulatory regions of various acute-phase protein and several other cytokine genes such as TNF, IL-8 and G-CSF, implying that NF-IL6 has a role in the regulation ot only of the IL-6 gene, but also of several other genes involved in acute-phase reaction, inflammation and haematopoiesis (Akira et al., 1990).</csml:comment>
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PMID: 16419614, 8336793
LPS or inflammatory cytokine stimulation of macrophages and hepatocytes activated MAP kinases that in turn phosphorylated NF-IL6, enhancing its transcriptional efficacy (Trautwein et al., 1993).</csml:comment>
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PMID: 16419614, 8336793
LPS or inflammatory cytokine stimulation of macrophages and hepatocytes activated MAP kinases that in turn phosphorylated NF-IL6, enhancing its transcriptional efficacy (Trautwein et al., 1993).</csml:comment>
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PMID: 16419614, 7530603
The NF-IL6 deficient mice were highly susceptible to infection with Listeria monocytogenes; moreover NF-IL6 was essential for the induction of G-CSF in macrophages.</csml:comment>
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PMID: 16419614, 12023384
NF-IL6-deficient murine macrophages in stimulation with LPS displayed impaired expression of membrane-bound glutathione-dependent PGE2 synthase or Cox-2.</csml:comment>
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PMID: 16419614, 12023384
NF-IL6-deficient murine macrophages in stimulation with LPS displayed impaired expression of membrane-bound glutathione-dependent PGE2 synthase or Cox-2.</csml:comment>
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PMID: 16419614, 14557267
The results therefore indicate that IRF-3-mediated activation of the ISRE by TLR4 requires the p65 subunit of NF-kappaB.</csml:comment>
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PMID: 16419614
IL-1 and LPS stimulation induce activation of the STAT family of transcription factors, which consists of seven members.</csml:comment>
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PMID: 16419614, 9649436
Bacterial infection of macrophages or treatment with LPS resulted in rapid STAT1 serine phosphorylation, independent of concomitant tyrosine phosphorylation.

PMID: 16419614, 9794412
Other studies proved that LPS stimulation of macrophages using the MyD88-independent pathway and IRF-3-induced expression of IFN-beta, which then induced expression of IFN-regulated genes through activation of STAT1.</csml:comment>
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PMID: 16419614, 12356687
LPS-induced expression of IRF-1, iNOS and IFN-inducible genes such as IP-10 was severely impaired in STAT1-deficient murine macrophages, suggesting that STAT1 may play a role in the response to LPS.</csml:comment>
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PMID: 16419614, 12356687
LPS-induced expression of IRF-1, iNOS and IFN-inducible genes such as IP-10 was severely impaired in STAT1-deficient murine macrophages, suggesting that STAT1 may play a role in the response to LPS.</csml:comment>
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PMID: 16419614, 12356687
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