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Article

Structure of the BTB domain of Keap1 and its interaction with the triterpenoid antagonist CDDO.

PloS one - 1 Jan 2014

Cleasby Anne, Yon Jeff, Day Philip J, Richardson Caroline, Tickle Ian J, Williams Pamela A, Callahan James F, Carr Robin, Concha Nestor, Kerns Jeffrey K, Qi Hongwei, Sweitzer Thomas, Ward Paris, Davies Thomas G

Abstract excerpt

The protein Keap1 is central to the regulation of the Nrf2-mediated cytoprotective response, and is increasingly recognized as an important target for therapeutic intervention in a range of diseases involving excessive oxidative stress and inflammation. The BTB domain of Keap1 plays key roles in sensing environmental electrophiles and in mediating interactions with the Cul3/Rbx1 E3 ubiquitin ligase system, and is...

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Identifiers

PMID: 24896564
DOI: 10.1371/journal.pone.0098896
PMCID: PMC4045772

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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