IndraLab

Statements

TNFAIP3 inhibits Ubiquitin. 5 / 5
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"Ubiquitin-editing enzyme TNFAIP3 is able to abolish NF-κB activation by removing ubiquitin chains from key components of TNFR signaling pathway (such as RIP1 and NEMO) that leads to their proteasomal degradation; notably, SNPs in TNFAIP3 are associated with CD [49]."
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"TNFAIP3 inhibits NF-kappaB activation by exerting dual ubiquitin editing functions [XREF_BIBR]."
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"Numerous negative modulators of the NF-κB pathway, such as the deubiquitinase TNFAIP3/A20 , ubiquitin ligase SOCS-1 , a group of miRNAs and a few lncRNAs , etc., have been identified as potent anti-inflammatory molecules."
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"CYLD and TNFAIP3 and A20 negatively regulate the NFkappaB pathway by removing ubiquitin chains from multiple signaling molecules including TRAFs and RIP."
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"TNFaIP3 prevents the NFκB-dependent upregulation of NLRP3 and conversion of pro-IL1β to mature IL1β through the binding of its A20-like zinc finger domain to ubiquitin chains [52]."
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