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- W4297590147 abstract "Upon interleukin 1 (IL-1) stimulation, the IL-1-receptor (IL-1R)-associated kinase (IRAK) is rapidly recruited to the IL-1R complex and undergoes phosphorylation. Here we demonstrate that recombinant wild-type IRAK (IRAK-WT), but not a kinase-defective mutant with Asp340 replaced by an asparagine residue (IRAK-Asp340Asn), is highly phosphorylated and is capable of auto-phosphorylation in vitro. Overexpression of both IRAK-WT and IRAK-Asp340Asn caused activation of nuclear factor κB, suggesting that the kinase activity of IRAK is not required outside of the IL-1R complex." @default.
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- W4297590147 date "1999-04-08" @default.
- W4297590147 modified "2023-09-30" @default.
- W4297590147 title "Overexpression of an enzymically inactive interleukin-1-receptor-associated kinase activates nuclear factor-κB" @default.
- W4297590147 doi "https://doi.org/10.1042/bj3390227" @default.
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