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USP18 inhibits NFkappaB. 22 / 26
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"USP18 inhibits NF-kappaB signaling at the level of the IKK complex."
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"USP18 deficiency or knockdown of USP20 resulted in enhanced K48 linked ubiquitination and accelerated degradation of STING, and impaired activation of IRF3 and NF-kappaB as well as induction of downstream genes after infection with DNA virus HSV-1 or transfection of various DNA ligands."
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"USP18 mediated NF-kappaB inhibition may be of importance not only for T cell adaptive immunity but also for liver inflammation."
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"In addition, we found that NF-kappaB activation through RIG-I (N), MAVS, or TBK1, which do not signal through TAK1, could also be inhibited by USP18 (XREF_SUPPLEMENTARY)."
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"The LPS-mediated TLR4 activation in human macrophages upregulates USP18 , which in turn inhibits NF-kappaB activation , and thus the secretion of pro-inflammatory cytokines ( TNF-alpha , IL-6 , and IL-1beta ) via interacting with TAK1-TAB1 and IKKalpha / beta-NEMO complexes ( Table 2 ) [ 193 ] ."
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"More importantly, USP18 only inhibited NF-kappaB activation in WT NEMO or NEMO (K285/309R) construct, but had no effect on NEMO (K325/326R) construct (XREF_FIG)."
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"Another way that USP18 inhibited NF-kappaB activation is by deubiquitinating K63-Ub of TAK1 and NEMO [ 42 ] ."
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"Another way that USP18 inhibited NF-kappaB activation is by deubiquitinating K63-Ub of TAK1 and NEMO [XREF_BIBR]."
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"Here, we found that ectopic expression of USP18 suppressed nuclear accumulation of p65 as well as NF-kappaB activation by LPS treatment."
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"These results suggest that USP18 inhibits NF-kappaB signaling upstream of p65, at the level of the IKK complex."
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"More importantly, results presented in XREF_FIG suggest that USP18 may directly interact with the IKK complex to inhibit NF-kappaB activation."
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"Consistent with these results, we found that knockdown of USP18 enhanced NF-kappaB-luc activity induced by TNF-alpha, LPS, MyD88, TRAF6, TAK1-TAB1, IKKbeta, but not p65 (XREF_FIG)."
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"USP18 was upregulated by various TLR ligands in THP-1 (a human monocyte cell line) cells and inhibited IkappaB degradation as well as NF-kappaB activation to form a negative feedback loop."
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"USP18 negatively regulates NF-kappaB signaling by targeting TAK1 and NEMO for deubiquitination through distinct mechanisms."
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"XREF_BIBR This study showed that USP18 or USP20 deficiency significantly inhibited HSV-I or cytosolic DNA activation of both NF-kappaB and IRF3, and type-I IFN and proinflammatory cytokine expression."
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"The LPS mediated TLR4 activation in human macrophages upregulates USP18, which in turn inhibits NF-kappaB activation, and thus the secretion of proinflammatory cytokines (TNF-alpha, IL-6, and IL-1beta) via interacting with TAK1-TAB1 and IKKalpha and beta-NEMO complexes [193]."
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"While upregulation of interferon-responsive genes suggests some form of long-lasting intrinsic inflammation response, ISG15 and USP18 in fact act to limit inflammation by controlling the NF-kB pathway[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"The LPS-mediated TLR4 activation in human macrophages upregulates USP18 , which in turn inhibits NF-kappaB activation , and thus the secretion of proinflammatory cytokines ( TNF-alpha , IL-6 , and IL-1beta ) via interacting with TAK1-TAB1 and IKKalpha / beta-NEMO complexes ( Table 2 ) [ 193 ] ."
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"Based on our experimental data, we propose a working model to explain how USP18 negatively regulates NF-kappaB signaling by targeting TAK1 and NEMO."
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"To determine whether specific knockdown of endogenous USP18 would enhance NF-kappaB activation under physiological conditions, we selected three USP18 specific small interfering RNAs (siRNA) to knock down USP18 expression."
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"A recent study showed that USP18 attenuated NF-kappaB activation by targeting TAK1-TAB1 for deubiquitination."
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"Hence, knockdown of USP18 enhances NF-kappaB activity, thus increasing NF-kappaB-dependent proinflammatory cytokine responses in human monocytes and macrophages."
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