ArticleCurrent opinion in toxicology2016
Dissecting the Keap1/Nrf2 pathway through proteomics.
Article in Current opinion in toxicology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
3 citing papers in PubMed.
- ATDC binds to KEAP1 to drive NRF2-mediated tumorigenesis and chemoresistance in pancreatic cancer.Genes & development · 2021Article
- Gain-of-function genetic screen of the kinome reveals BRSK2 as an inhibitor of the NRF2 transcription factor.Journal of cell science · 2020Article
- Keap1-MCM3 interaction is a potential coordinator of molecular machineries of antioxidant response and genomic DNA replication in metazoa.Scientific reports · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
Mass spectrometry-based proteomic technologies continue to illuminate the mechanism(s) and physiological importance of the KEAP1/NRF2 antioxidant signaling pathway. Proteomic analysis of the KEAP1 and NRF2 protein complex has revealed associated proteins and post-translational modifications, which together support new modes of regulation and therapeutic intervention opportunities for prevention and treatment. Emerging proteomic data depict a highly interconnected signaling network containing numerous co-complexed proteins and post-translational modifications, the majority of which are of unknown functional significance. In this review, we have compiled the literature and public domain to produce protein interaction networks for KEAP1 and NRF2. Selected interacting proteins and their possible functional implications are covered. We also curated available proteomic datasets to create a comprehensive map of various post-translational modifications on KEAP1 and NRF2. Together, this evaluation illustrates the power of mass spectrometry-based protein sequencing to understand the signaling components and dynamics of the KEAP1-NRF2 pathway. Current challenges and future directions for mass spectrometry in antioxidant signaling are discussed.
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