David M. Rothwarf

TL;DR: IKK turns out to be the long-sought-after protein kinase that mediates the critical regulatory step in NF-κB activation, and phosphorylates IκBs on the sites that trigger their degradation.

TL;DR: The molecular cloning and characterization of IKKbeta, a second subunit of the IKK complex, is described, which is 50% identical to IKKalpha and like it contains a kinase domain, a leucine zipper, and a helix-loop-helix.

TL;DR: In this paper, a large, cytokine-responsive IkappaB kinase (IKK) complex has been purified and the genes encoding two of its subunits have been cloned.

TL;DR: Exposure of cells to various extracellular stimuli leads to the rapid phosphorylation, ubiquitinylation, and ultimately proteolytic degradation of IκB, which frees NF-κB to translocate to the nucleus, where it regulates gene transcription.

TL;DR: Two transcription factors, NF-κB and AP-1, have emerged in recent years as major targets for signaling pathways that are activated by a variety of proinflammatory stimuli and their regulation by oxidative stress and pro-oxidants will be addressed.