A20 Regulation of Nuclear Factor–κB
نویسندگان
چکیده
منابع مشابه
Regulation of A20 and other OTU deubiquitinases by reversible oxidation
Protein ubiquitination is a highly versatile post-translational modification that regulates as diverse processes as protein degradation and kinase activation. Deubiquitinases hydrolyse ubiquitin modifications from proteins and are hence key regulators of the ubiquitin system. Ovarian tumour deubiquitinases comprise a family of fourteen human enzymes, many of which regulate cellular signalling p...
متن کاملIdentification of a Novel A20-binding Inhibitor of Nuclear Factor- B Activation Termed ABIN-2*
The nuclear factor B (NFB) plays a central role in the regulation of genes implicated in immune responses, inflammatory processes, and apoptotic cell death. The zinc finger protein A20 is a cellular inhibitor of NFB activation by various stimuli and plays a critical role in terminating NFB responses. The underlying mechanism for NFB inhibition by A20 is still unknown. A20 has been shown to inte...
متن کاملExpression of the nuclear factor-κB inhibitor A20 is altered in the cystic fibrosis epithelium.
A20 is a lipopolysaccharide (LPS)-inducible, cytoplasmic zinc finger protein, which inhibits Toll-like receptor-activated nuclear factor (NF)-κB signalling by deubiquitinating tumour necrosis factor receptor-associated factor (TRAF)-6. The action of A20 is facilitated by complex formation with ring finger protein (RNF)-11, Itch and TAX-1 binding protein-1 (TAX1BP1). This study investigated whet...
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Imiquimod, a nucleoside analogue of the imidazoquinoline family, is being used to treat various cutaneous cancers including squamous cell carcinoma (SCC). Imiquimod activates anti-tumor immunity via Toll-like receptor 7 (TLR7) in macrophage and other immune cells. Imiquimod can also affect tumor cells directly, regardless of its impact on immune system. In this study, we demonstrated that imiqu...
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ژورنال
عنوان ژورنال: American Journal of Respiratory Cell and Molecular Biology
سال: 2011
ISSN: 1044-1549,1535-4989
DOI: 10.1165/rcmb.2010-0339tr