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Front cover: Under unstressed condition Nrf2 is sequestered in the cytoplasm by Keap1 and rapidly degraded via the ubiquitin-proteasome system. Upon exposure to oxidants or electrophiles Keap1 is inactivated but stays in the cytoplasm. In this situation de novo synthesized Nrf2 protein can bypass the cytoplasmic Keap1-proteasome destruction gate and accumulate in the nucleus. These results support the model that electrophilic modifications of Keap1 cysteine residues provoke conformational changes of Keap1 and disrupt the Nrf2 binding to Keap1. For detail see the article by Y. Watai et al. in this issue (pp. 1163–1178).