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These adaptors are recruited to receptor TIR domains and initiate signaling processes through IL-1R-associated kinases (IRAKs) and the adaptor molecule TRAF-6, which leads to activation of four protein kinase cascades, culminating in the activation of NF-kappaB and the MAP kinases p38, JNK and ERK1/2.

PMID: 15585304, 12538665
MyD88s, a splice variant of MyD88, prevents IRAK-4 recruitment.</csml:comment>
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These adaptors are recruited to receptor TIR domains and initiate signaling processes through IL-1R-associated kinases (IRAKs) and the adaptor molecule TRAF-6, which leads to activation of four protein kinase cascades, culminating in the activation of NF-kappaB and the MAP kinases p38, JNK and ERK1/2.</csml:comment>
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<csml:comment type="text">PMID: 15585304, 12467243
These adaptors are recruited to receptor TIR domains and initiate signaling processes through IL-1R-associated kinases (IRAKs) and the adaptor molecule TRAF-6, which leads to activation of four protein kinase cascades, culminating in the activation of NF-kappaB and the MAP kinases p38, JNK and ERK1/2.</csml:comment>
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These adaptors are recruited to receptor TIR domains and initiate signaling processes through IL-1R-associated kinases (IRAKs) and the adaptor molecule TRAF-6, which leads to activation of four protein kinase cascades, culminating in the activation of NF-kappaB and the MAP kinases p38, JNK and ERK1/2.</csml:comment>
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These adaptors are recruited to receptor TIR domains and initiate signaling processes through IL-1R-associated kinases (IRAKs) and the adaptor molecule TRAF-6, which leads to activation of four protein kinase cascades, culminating in the activation of NF-kappaB and the MAP kinases p38, JNK and ERK1/2.</csml:comment>
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</csml:processKinetic>
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<csml:comment type="text">PMID: 15585304, 12467243
These adaptors are recruited to receptor TIR domains and initiate signaling processes through IL-1R-associated kinases (IRAKs) and the adaptor molecule TRAF-6, which leads to activation of four protein kinase cascades, culminating in the activation of NF-kappaB and the MAP kinases p38, JNK and ERK1/2.</csml:comment>
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<csml:comment type="text">PMID: 15585304
These molecules in turn promote the production of many proinflammatory proteins and enhance immune reactivity.</csml:comment>
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<csml:comment type="text">PMID: 15585304
These molecules in turn promote the production of many proinflammatory proteins and enhance immune reactivity.</csml:comment>
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<csml:comment type="text">PMID: 15585304
These molecules in turn promote the production of many proinflammatory proteins and enhance immune reactivity.</csml:comment>
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These molecules in turn promote the production of many proinflammatory proteins and enhance immune reactivity.</csml:comment>
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Although macrophages from wild-type (WT) mice produced minimal amounts of IL-6, IL-12 and Tumour necrosis factor (TNF) in response to IL-1alpha and IL-1beta, those from ST2-deficient mice produced large amounts of these cytokines under identical culture conditions.</csml:comment>
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Although macrophages from wild-type (WT) mice produced minimal amounts of IL-6, IL-12 and Tumour necrosis factor (TNF) in response to IL-1alpha and IL-1beta, those from ST2-deficient mice produced large amounts of these cytokines under identical culture conditions.</csml:comment>
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Although macrophages from wild-type (WT) mice produced minimal amounts of IL-6, IL-12 and Tumour necrosis factor (TNF) in response to IL-1alpha and IL-1beta, those from ST2-deficient mice produced large amounts of these cytokines under identical culture conditions.</csml:comment>
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Although macrophages from wild-type (WT) mice produced minimal amounts of IL-6, IL-12 and Tumour necrosis factor (TNF) in response to IL-1alpha and IL-1beta, those from ST2-deficient mice produced large amounts of these cytokines under identical culture conditions.</csml:comment>
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Although macrophages from wild-type (WT) mice produced minimal amounts of IL-6, IL-12 and Tumour necrosis factor (TNF) in response to IL-1alpha and IL-1beta, those from ST2-deficient mice produced large amounts of these cytokines under identical culture conditions.</csml:comment>
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Although macrophages from wild-type (WT) mice produced minimal amounts of IL-6, IL-12 and Tumour necrosis factor (TNF) in response to IL-1alpha and IL-1beta, those from ST2-deficient mice produced large amounts of these cytokines under identical culture conditions.</csml:comment>
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Macrophages from ST2-deficient mice also produced significantly more IL-6 and IL-12 than cells from the WT mice when stimulated with LPS, a ligand of TLR4.</csml:comment>
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Macrophages from ST2-deficient mice also produced significantly more IL-6 and IL-12 than cells from the WT mice when stimulated with LPS, a ligand of TLR4.</csml:comment>
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Macrophages from ST2-deficient mice also produced significantly more IL-6 and IL-12 than cells from the WT mice when stimulated with LPS, a ligand of TLR4.</csml:comment>
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A similar effect was observed following overexpression of the TIR domain-containing adaptor Mal, which is involved in signaling from TLR4 and TLR2.</csml:comment>
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A similar elevation of proinflammatory cytokine production was observed when the cells were stimulated with BLP (bacterial lipoprotein, Pam3Cys-SK4, ligand for TLR2), and CpG (ligand for TLR9).</csml:comment>
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A similar elevation of proinflammatory cytokine production was observed when the cells were stimulated with BLP (bacterial lipoprotein, Pam3Cys-SK4, ligand for TLR2), and CpG (ligand for TLR9).</csml:comment>
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A similar elevation of proinflammatory cytokine production was observed when the cells were stimulated with BLP (bacterial lipoprotein, Pam3Cys-SK4, ligand for TLR2), and CpG (ligand for TLR9).</csml:comment>
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A similar effect was observed following overexpression of the TIR domain-containing adaptor Mal, which is involved in signaling from TLR4 and TLR2.</csml:comment>
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A similar elevation of proinflammatory cytokine production was observed when the cells were stimulated with BLP (bacterial lipoprotein, Pam3Cys-SK4, ligand for TLR2), and CpG (ligand for TLR9).</csml:comment>
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A similar elevation of proinflammatory cytokine production was observed when the cells were stimulated with BLP (bacterial lipoprotein, Pam3Cys-SK4, ligand for TLR2), and CpG (ligand for TLR9).</csml:comment>
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A similar elevation of proinflammatory cytokine production was observed when the cells were stimulated with BLP (bacterial lipoprotein, Pam3Cys-SK4, ligand for TLR2), and CpG (ligand for TLR9).</csml:comment>
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<csml:comment type="text">PMID: 15585304
A similar elevation of proinflammatory cytokine production was observed when the cells were stimulated with BLP (bacterial lipoprotein, Pam3Cys-SK4, ligand for TLR2), and CpG (ligand for TLR9).</csml:comment>
</csml:comments>
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A similar elevation of proinflammatory cytokine production was observed when the cells were stimulated with BLP (bacterial lipoprotein, Pam3Cys-SK4, ligand for TLR2), and CpG (ligand for TLR9).</csml:comment>
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A similar elevation of proinflammatory cytokine production was observed when the cells were stimulated with BLP (bacterial lipoprotein, Pam3Cys-SK4, ligand for TLR2), and CpG (ligand for TLR9).</csml:comment>
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However, when the cells were cultured with LPS, ST2 was clearly detected by 4 h and sustained for at least 48 h.</csml:comment>
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<csml:comment type="text">PMID: 15585304, 12150927
IRAK-M also interferes with IRAK function by preventing dissociation of IRAK from the signaling complex.</csml:comment>
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<csml:comment type="text">PMID: 15585304, 12467243
These adaptors are recruited to receptor TIR domains and initiate signaling processes through IL-1R-associated kinases (IRAKs) and the adaptor molecule TRAF-6, which leads to activation of four protein kinase cascades, culminating in the activation of NF-kappaB and the MAP kinases p38, JNK and ERK1/2.</csml:comment>
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ST2 appears to exert its negative regulatory function on IL-1RI and TLR4 mediated NF-kappaB activation via sequestrating TLR proximal signaling components, MyD88 and Mal.</csml:comment>
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ST2 appears to exert its negative regulatory function on IL-1RI and TLR4 mediated NF-kappaB activation via sequestrating TLR proximal signaling components, MyD88 and Mal.</csml:comment>
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ST2 appears to exert its negative regulatory function on IL-1RI and TLR4 mediated NF-kappaB activation via sequestrating TLR proximal signaling components, MyD88 and Mal.</csml:comment>
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ST2 appears to exert its negative regulatory function on IL-1RI and TLR4 mediated NF-kappaB activation via sequestrating TLR proximal signaling components, MyD88 and Mal.</csml:comment>
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<csml:comment type="text">PMID: 15585304
ST2 appears to exert its negative regulatory function on IL-1RI and TLR4 mediated NF-kappaB activation via sequestrating TLR proximal signaling components, MyD88 and Mal.</csml:comment>
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<csml:comments>
<csml:comment type="text">Indirect</csml:comment>
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<csml:comment type="text">PMID: 15585304
ST2 is able to activate MAP kinases but not NF-kappaB.</csml:comment>
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