Sites of alkylation of human Keap1 by natural chemoprevention agents
Author:
Affiliation:
1. Department of Medicinal Chemistry and Pharmacognosy, University of Illinois College of Pharmacy, 833 S. Wood Street, 60612, Chicago, IL, USA
Publisher
American Chemical Society (ACS)
Subject
Spectroscopy,Structural Biology
Link
https://pubs.acs.org/doi/pdf/10.1016/j.jasms.2007.09.015
Reference36 articles.
1. Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain
2. Direct evidence that sulfhydryl groups of Keap1 are the sensors regulating induction of phase 2 enzymes that protect against carcinogens and oxidants
3. Distinct Cysteine Residues in Keap1 Are Required for Keap1-Dependent Ubiquitination of Nrf2 and for Stabilization of Nrf2 by Chemopreventive Agents and Oxidative Stress
4. Chemoprotection against cancer by Phase 2 enzyme induction
5. The Keap1-BTB Protein Is an Adaptor That Bridges Nrf2 to a Cul3-Based E3 Ligase: Oxidative Stress Sensing by a Cul3-Keap1 Ligase
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