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- W2003147175 abstract "Deregulation of the transcription factor NF-κB can mediate several inflammatory diseases in addition to cancer. Therefore, several proteins, including the zinc finger protein A20, tightly control its activation. Recently, the underlying mechanism by which A20 downregulates NF-κB activation in response to the pro-inflammatory cytokine tumor necrosis factor (TNF) has been described. A20 was shown to exert two opposing activities: sequential de-ubiquitination and ubiquitination of the TNF receptor-interacting protein (RIP), thereby targeting RIP to proteasomal degradation. Deregulation of the transcription factor NF-κB can mediate several inflammatory diseases in addition to cancer. Therefore, several proteins, including the zinc finger protein A20, tightly control its activation. Recently, the underlying mechanism by which A20 downregulates NF-κB activation in response to the pro-inflammatory cytokine tumor necrosis factor (TNF) has been described. A20 was shown to exert two opposing activities: sequential de-ubiquitination and ubiquitination of the TNF receptor-interacting protein (RIP), thereby targeting RIP to proteasomal degradation." @default.
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- W2003147175 date "2005-01-01" @default.
- W2003147175 modified "2023-09-26" @default.
- W2003147175 title "A20 inhibits NF-κB activation by dual ubiquitin-editing functions" @default.
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- W2003147175 doi "https://doi.org/10.1016/j.tibs.2004.11.001" @default.
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