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Article

A mutation of Keap1 found in breast cancer impairs its ability to repress Nrf2 activity.

Biochemical and biophysical research communications - 3 Nov 2007

Nioi Paul, Nguyen Truyen

Abstract excerpt

Keap1 is the substrate recognition module of a Cullin 3-based E3 ubiquitin ligase. Its primary role is to catalyze the ubiquitylation of the Nrf2 transcription factor. Oxidative stress blocks the E3 ligase activity of Keap1 which stabilizes Nrf2 allowing it to drive the expression of certain anti...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Kelch-Like ECH-Associated Protein 1

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Source

Identifiers

PMID: 17822677
DOI: 10.1016/j.bbrc.2007.08.051

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-17822677-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

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A mutation of Keap1 found in breast cancer impairs its ability to repress Nrf2 activity.PMID 17822677Read ↗

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BTB protein Keap1 targets antioxidant transcription factor Nrf2 for ubiquitination by the Cullin 3-Roc1 ligase.Semantic proximity Read ↗

Structural and biochemical characterization establishes a detailed understanding of KEAP1-CUL3 complex assemblySemantic proximity Read ↗

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