Keap1 is a forked-stem dimer structure with two large spheres enclosing the intervening, double glycine repeat, and C-terminal domains
Author:
Publisher
Proceedings of the National Academy of Sciences
Subject
Multidisciplinary
Reference42 articles.
1. An Nrf2/Small Maf Heterodimer Mediates the Induction of Phase II Detoxifying Enzyme Genes through Antioxidant Response Elements
2. Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain
3. Nrf2–Keap1 regulation of cellular defense mechanisms against electrophiles and reactive oxygen species
4. Keap1-null mutation leads to postnatal lethality due to constitutive Nrf2 activation
5. Hepatocyte-specific deletion of the keap1 gene activates Nrf2 and confers potent resistance against acute drug toxicity
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