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Open AccessJournal ArticleDOI

Phosphorylation of Nrf2 at Ser-40 by protein kinase C regulates antioxidant response element-mediated transcription.

H.-C. Huang, +2 more
- 08 Nov 2002 - 
- Vol. 277, Iss: 45, pp 42769-42774
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TLDR
It is shown that phosphorylation of purified rat Nrf2 by the catalytic subunit of PKC was blocked by a synthetic peptide mimicking one of the potential PKC sites, suggesting that the PKC-catalyzed phosphorylating of NRF2 at Ser-40 is a critical signaling event leading to ARE-mediated cellular antioxidant response.
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This article is published in Journal of Biological Chemistry.The article was published on 2002-11-08 and is currently open access. It has received 952 citations till now. The article focuses on the topics: Protein kinase C & Phosphorylation.

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Citations
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Cell Survival Responses to Environmental Stresses Via the Keap1-Nrf2-ARE Pathway

TL;DR: The development of Nrf2 knockout mice has provided key insights into the toxicological importance of this pathway, and this review highlights the key elements in this adaptive response to protection against acute and chronic cell injury provoked by environmental stresses.
Journal ArticleDOI

Role of nrf2 in oxidative stress and toxicity.

TL;DR: The nuclear factor erythroid 2-related factor 2 (Nrf2) is an emerging regulator of cellular resistance to oxidants that controls the basal and induced expression of an array of antioxidant response element-dependent genes to regulate the physiological and pathophysiological outcomes of oxidant exposure.
Journal ArticleDOI

Cancer chemoprevention with dietary phytochemicals

TL;DR: Attention has recently been focused on intracellular-signalling cascades as common molecular targets for various chemopreventive phytochemicals.
Journal ArticleDOI

The Nrf2-Antioxidant Response Element Signaling Pathway and Its Activation by Oxidative Stress

TL;DR: A possible role of the Nrf2-antioxidant response element transcriptional pathway in neuroprotection and the nature of this pathway and the mechanisms by which Keap1 acts to repress NRF2 activity are the topics of discussion in this minireview.
Journal ArticleDOI

Redox Regulation of Cell Survival

TL;DR: The current understanding of how disturbance in redox homeostasis may affect cell death and contribute to the development of diseases such as cancer and degenerative disorders is reviewed and the basic knowledge on redox regulation of cell survival can be used to develop strategies for the treatment or prevention of those diseases.
References
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Journal ArticleDOI

An nrf2/small maf heterodimer mediates the induction of phase ii detoxifying enzyme genes through antioxidant response elements

TL;DR: It is demonstrated that Nrf2 is essential for the transcriptional induction of phase II enzymes and the presence of a coordinate transcriptional regulatory mechanism for phase II enzyme genes and the nrf2-deficient mice may prove to be a very useful model for the in vivo analysis of chemical carcinogenesis and resistance to anti-cancer drugs.
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Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain

TL;DR: It is postulate that Keap1 and Nrf2 constitute a crucial cellular sensor for oxidative stress, and together mediate a key step in the signaling pathway that leads to transcriptional activation by this novel NRF2 nuclear shuttling mechanism.
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Isolation of NF-E2-related factor 2 (Nrf2), a NF-E2-like basic leucine zipper transcriptional activator that binds to the tandem NF-E2/AP1 repeat of the beta-globin locus control region.

TL;DR: Although Nrf2 is expressed ubiquitously, a role of this protein in mediating enhancer activity of hypersensitive site 2 in erythroid cells cannot be excluded and NRF2 contains a powerful acidic activation domain that may participate in the transcriptional stimulation of beta-globin genes.
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Nrf2, a Cap'n'Collar transcription factor, regulates induction of the heme oxygenase-1 gene.

TL;DR: Results implicate Nrf2 in the induction of the HO-1 gene but suggest that the NRF2 partner in this function is a factor other than p18 or Jun proteins.
Journal ArticleDOI

Reversible Oxidation and Inactivation of Protein Tyrosine Phosphatases In Vivo

TL;DR: The results indicate that SHP-2 inhibits PDGFR signaling and suggest a mechanism by which autophosphorylation of the PDG FR occurs despite its association with SHp-2, which is shown to be transient oxidation of the SH2 domain containing PTP.
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