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- W87601345 abstract "Abstract The molecular events involved in NF-kB signal transduction from the cell surface to the nucleus have been extensively studied over the last two decades. However, the mechanism of recruitment of NF-kB to target genes and NF-kB-induced transcriptional events after recruitment remains enigmatic. The p65-p50 heterodimer is the most abundant form of active NF-kB. The crystal structure of the p65-p50 heterodimer bound to DNA revealed that p65 binds to the 3′ half of kB sites where most of the kB sequence variation occurs, while p50 binds to the relatively invariant 5′ half. In an effort to identify novel regulatory factors of NF-B, we used p65 as bait protein and performed tandem affinity purification combined with mass spectrometry on mammalian cell extracts. Through this approach, we identified a novel regulatory protein that specifically interacts with p65. RNA interference experiments revealed that knockdown of such protein specifically inhibited p65-mediated transcription of various target genes. This finding may shed light on the mechanism of p65 regulation and provide a new insight into NF-kB specificity." @default.
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- W87601345 date "2007-04-01" @default.
- W87601345 modified "2023-09-26" @default.
- W87601345 title "Identification a novel NF-kB regulator by tandem affinity purification combined with mass spectrometry (35.44)" @default.
- W87601345 doi "https://doi.org/10.4049/jimmunol.178.supp.35.44" @default.
- W87601345 hasPublicationYear "2007" @default.
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