IndraLab

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Ubiquitin inhibits CYLD. 4 / 4
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"Together, these results suggest that MIB2 enhances NF-kappaB signaling in inflammation by promoting the ubiquitin dependent degradation of CYLD."
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"Our studies reveal that under physiological conditions, TNF- and RIPK1-dependent cell death is suppressed by the linear ubiquitin-dependent inhibition of CYLD."
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"It has been reported that MIB2 enhanced NF-κB signaling in inflammation via facilitating the ubiquitin-dependent degradation of CYLD ( Uematsu et al., 2019 )."
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"CYLD recognises and cleaves K63-linked ubiquitin chains to promote protein–protein interactions in the assembly of signalling molecule complex.32 CYLD can inhibit NF-κB upstream signalling molecules and regulate inflammatory response by deconjugating the K63-linked ubiquitin chains.33 Disruption of CYLD induces hepatocyte death and activates Kupffer cells, which promotes inflammation and pro-inflammatory mediators,34 suggesting that CYLD is an essential regulator of immune and inflammatory responses."
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