Transcription Factor Nrf2 Regulates Inflammation by Mediating the Effect of 15-Deoxy-Δ12,14-Prostaglandin J2

Inhibition of Prostaglandin Synthesis as a Mechanism of Action for Aspirin-like Drugs

VANE, J. R. (1971) · Nature New Biology · doi:10.1038/newbio231232a0 · Cited by 8,605 · see citing works

An Nrf2/Small Maf Heterodimer Mediates the Induction of Phase II Detoxifying Enzyme Genes through Antioxidant Response Elements

Itoh, K., Chiba, T., Takahashi, S., Ishii, T., Igarashi, K., Katoh, Y., Oyake, T., Hayashi, N., Satoh, K., Hatayama, I., et al. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.6943 · Cited by 3,999 · see citing works

Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain

Itoh, K., Wakabayashi, N., Katoh, Y., Ishii, T., Igarashi, K., Engel, J. D., & Yamamoto, M. (1999) · Genes & Development · doi:10.1101/gad.13.1.76 · Cited by 3,634 · see citing works

The peroxisome proliferator-activated receptor-γ is a negative regulator of macrophage activation

Ricote, M., Li, A. C., Willson, T. M., Kelly, C. J., & Glass, C. K. (1998) · Nature · doi:10.1038/34178 · Cited by 3,525 · see citing works

PPAR-γ agonists inhibit production of monocyte inflammatory cytokines

Jiang, C., Ting, A. T., & Seed, B. (1998) · Nature · doi:10.1038/34184 · Cited by 2,899 · see citing works

Points of control in inflammation

Nathan, C. (2002) · Nature · doi:10.1038/nature01320 · Cited by 2,738 · see citing works

Carbon monoxide has anti-inflammatory effects involving the mitogen-activated protein kinase pathway

Otterbein, L. E., Bach, F. H., Alam, J., Soares, M., Tao Lu, H., Wysk, M., Davis, R. J., Flavell, R. A., & Choi, A. M. K. (2000) · Nature Medicine · doi:10.1038/74680 · Cited by 2,153 · see citing works

Direct evidence that sulfhydryl groups of Keap1 are the sensors regulating induction of phase 2 enzymes that protect against carcinogens and oxidants

Dinkova-Kostova, A. T., Holtzclaw, W. D., Cole, R. N., Itoh, K., Wakabayashi, N., Katoh, Y., Yamamoto, M., & Talalay, P. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.172398899 · Cited by 1,947 · see citing works

Pharmacological and biochemical demonstration of the role of cyclooxygenase 2 in inflammation and pain.

Seibert, K., Zhang, Y., Leahy, K., Hauser, S. D., Masferrer, J. L., Perkins, W., Lee, L., & Isakson, P. C. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.25.12013 · Cited by 1,551 · see citing works

Nonsteroid drug selectivities for cyclo-oxygenase-1 rather than cyclo-oxygenase-2 are associated with human gastrointestinal toxicity: A full in vitro analysis

Warner, T. D., Giuliano, F., Vojnovic, I., Bukasa, A., Mitchell, J. A., & Vane, J. R. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.13.7563 · Cited by 1,521 · see citing works

Transcription Factor Nrf2 Coordinately Regulates a Group of Oxidative Stress-inducible Genes in Macrophages

Ishii, T., Itoh, K., Takahashi, S., Sato, H., Yanagawa, T., Katoh, Y., Bannai, S., & Yamamoto, M. P. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.21.16023 · Cited by 1,460 · see citing works

Studies of the mediators of the acute inflammatory response induced in rats in different sites by carrageenan and turpentine

Rosa, M. D., Giroud, J. P., & Willoughby, D. A. (1971) · The Journal of Pathology · doi:10.1002/path.1711040103 · Cited by 1,409 · see citing works

Anti-inflammatory cyclopentenone prostaglandins are direct inhibitors of IκB kinase

Rossi, A., Kapahi, P., Natoli, G., Takahashi, T., Chen, Y., Karin, M., & Santoro, M. G. (2000) · Nature · doi:10.1038/47520 · Cited by 1,310 · see citing works

Inducible cyclooxygenase may have anti-inflammatory properties

Gilroy, D. W., Colville‐Nash, P., Willis, D., Chivers, J. E., Paul‐Clark, M. J., & Willoughby, D. A. (1999) · Nature Medicine · doi:10.1038/9550 · Cited by 1,243 · see citing works

Sensitivity to carcinogenesis is increased and chemoprotective efficacy of enzyme inducers is lost in <i>nrf2</i> transcription factor-deficient mice

Ramos-Gomez, M., Kwak, M.-K., Dolan, P. M., Itoh, K., Yamamoto, M., Talalay, P., & Kensler, T. W. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.051618798 · Cited by 1,102 · see citing works

Nrf1 and Nrf2 positively and c-Fos and Fra1 negatively regulate the human antioxidant response element-mediated expression of NAD(P)H:quinone oxidoreductase 1 gene

Radjendirane, V., & Jaiswal, A. K. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.25.14960 · Cited by 1,034 · see citing works

Keap1 regulates both cytoplasmic‐nuclear shuttling and degradation of Nrf2 in response to electrophiles

Itoh, K., Wakabayashi, N., Katoh, Y., Ishii, T., O'Connor, T., & Yamamoto, M. P. (2003) · Genes to Cells · doi:10.1046/j.1365-2443.2003.00640.x · Cited by 817 · see citing works

Heme oxygenase: A novel target for the modulation of inflammatory response

Willis, D., Moore, A., Frederick, R., & Willoughby, D. A. (1996) · Nature Medicine · doi:10.1038/nm0196-87 · Cited by 782 · see citing works

High Sensitivity of Nrf2 Knockout Mice to Acetaminophen Hepatotoxicity Associated with Decreased Expression of ARE-Regulated Drug Metabolizing Enzymes and Antioxidant Genes

Enomoto, A. (2001) · Toxicological Sciences · doi:10.1093/toxsci/59.1.169 · Cited by 728 · see citing works

Mammalian Peroxiredoxin Isoforms Can Reduce Hydrogen Peroxide Generated in Response to Growth Factors and Tumor Necrosis Factor-α

Kang, S. W., Chae, H. Z., Seo, M. S., Kim, K., Baines, I., & Rhee, S. G. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.11.6297 · Cited by 693 · see citing works

Role of NRF2 in Protection Against Hyperoxic Lung Injury in Mice

Cho, H., Jedlicka, A., Reddy, S. P., Kensler, T. W., Yamamoto, M. P., Zhang, L.-Y., & Kleeberger, S. R. (2002) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/ajrcmb.26.2.4501 · Cited by 660 · see citing works

NRF2, a member of the NFE2 family of transcription factors, is not essential for murine erythropoiesis, growth, and development

Chan, K., Lu, R., Chang, J. C., & Kan, Y. W. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.24.13943 · Cited by 643 · see citing works

Identification of a common chemical signal regulating the induction of enzymes that protect against chemical carcinogenesis.

Talalay, P., Long, M. J., & Prochaska, H. J. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.21.8261 · Cited by 595 · see citing works

MIF regulates innate immune responses through modulation of Toll-like receptor 4

Roger, T., David, J. R., Glauser, M. P., & Calandra, T. (2001) · Nature · doi:10.1038/414920a · Cited by 584 · see citing works

Nrf2 is essential for protection against acute pulmonary injury in mice

Chan, K., & Kan, Y. W. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.22.12731 · Cited by 574 · see citing works

Nrf2 Transcription Factor, a Novel Target of Keratinocyte Growth Factor Action Which Regulates Gene Expression and Inflammation in the Healing Skin Wound

Braun, S., Hanselmann, C., Gassmann, M. G., auf dem Keller, U., Born-Berclaz, C., Chan, K., Kan, Y. W., & Werner, S. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.15.5492-5505.2002 · Cited by 410 · see citing works

15-Deoxy-Δ12,14-prostaglandin J2

Shibata, T., Kondo, M., Osawa, T., Shibata, N., Kobayashi, M., & Uchida, K. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m110314200 · Cited by 391 · see citing works

Nrf2-deficient female mice develop lupus-like autoimmune nephritis11See Editorial by Byrd and Thomas, p. 1606.

Yoh, K., Itoh, K., Enomoto, A., Hirayama, A., Yamaguchi, N., Kobayashi, M., Morito, N., Kôyama, A., Yamamoto, M. P., & Takahashi, S. (2001) · Kidney International · doi:10.1046/j.1523-1755.2001.00939.x · Cited by 345 · see citing works

Laminar Flow Induction of Antioxidant Response Element-mediated Genes in Endothelial Cells

Chen, X.-L., Varner, S. E., Rao, A. S., Grey, J. Y., Thomas, S., Cook, C. K., Wasserman, M. A., Medford, R. M., Jaiswal, A. K., & Kunsch, C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m203161200 · Cited by 333 · see citing works

Accelerated DNA adduct formation in the lung of the Nrf2 knockout mouse exposed to diesel exhaust

Aoki, Y., Sato, H., Nishimura, N., Takahashi, S., Itoh, K., & Yamamoto, M. (2001) · Toxicology and Applied Pharmacology · doi:10.1006/taap.2001.9176 · Cited by 297 · see citing works

15-Deoxy-Δ12,14-prostaglandin J2Inhibition of NF-κB-DNA Binding through Covalent Modification of the p50 Subunit

Cernuda‐Morollón, E., Pineda‐Molina, E., Cañada, F. J., & Pérez‐Sala, D. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104518200 · Cited by 292 · see citing works

The electrophile counterattack response: Protection against neoplasia and toxicity

Prestera, T., Zhang, Y., Spencer, S. R., Wilczak, C. A., & Talalay, P. (1993) · Advances in Enzyme Regulation · doi:10.1016/0065-2571(93)90024-8 · Cited by 256 · see citing works

Induction of Heme Oxygenase-1 Expression in Murine Macrophages Is Essential for the Anti-inflammatory Effect of Low Dose 15-Deoxy-Δ12,14-prostaglandin J2

Lee, T., Tsai, H.-L., & Chau, L. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300498200 · Cited by 211 · see citing works

Cloning and characterization of a 23-kDa stress-induced mouse peritoneal macrophage protein.

Ishii, T., Yamada, M., Sato, H., Matsue, M., Taketani, S., Nakayama, K., Sugita, Y., & Bannai, S. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)46676-2 · Cited by 192 · see citing works

Resolution of inflammation

Willoughby, D. A., Moore, A., Colville‐Nash, P., & Gilroy, D. W. (2000) · International Journal of Immunopharmacology · doi:10.1016/s0192-0561(00)00064-3 · Cited by 190 · see citing works

Biological activities and mechanisms of action of PGJ2 and related compounds: an update

Fukushima, M. (1992) · Prostaglandins Leukotrienes and Essential Fatty Acids · doi:10.1016/0952-3278(92)90178-l · Cited by 187 · see citing works

[18] Roles of Nrf2 in activation of antioxidant enzyme genes via antioxidant responsive elements

Ishii, T., Itoh, K., & Yamamoto, M. P. (2002) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(02)48637-5 · Cited by 161 · see citing works

Site and mechanism of growth inhibition by prostaglandins. III. Distribution and binding of prostaglandin A2 and delta 12-prostaglandin J2 in nuclei.

Narumiya, S., Ohno, K., Fukushima, M., & Fujiwara, M. (1987) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1016/s0022-3565(25)39070-1 · Cited by 138 · see citing works

Activation of the Mouse Heme Oxygenase-1 Gene by 15-Deoxy-Δ 12,14 -Prostaglandin J 2 Is Mediated by the Stress Response Elements and Transcription Factor Nrf2

Gong, P., Stewart, D., Hu, B., Li, N., Cook, J. L., Nel, A. E., & Alam, J. (2002) · Antioxidants and Redox Signaling · doi:10.1089/152308602753666307 · Cited by 137 · see citing works

Induction of Cellular Antioxidative Stress Genes through Heterodimeric Transcription Factor Nrf2/Small Maf by Antirheumatic Gold(I) Compounds

Kataoka, K., Handa, H., & Nishizawa, M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105383200 · Cited by 125 · see citing works

The Cyclopentenone Prostaglandin 15-Deoxy-Δ12,14-Prostaglandin J2Attenuates the Development of Acute and Chronic Inflammation

Cuzzocrea, S., Wayman, N. S., Mazzon, E., Dugo, L., Paola, R. D., Serraino, I., Britti, D., Chatterjee, P. K., Caputi, A. P., & Thiemermann, C. (2002) · Molecular Pharmacology · doi:10.1124/mol.61.5.997 · Cited by 122 · see citing works

Antioxidant-Inducible Genes

Primiano, T., Sutter, T. R., & Kensler, T. W. (1996) · Advances in pharmacology · doi:10.1016/s1054-3589(08)60989-8 · Cited by 112 · see citing works

Regulation of Macrophage Migration Inhibitory Factor and Thiol-specific Antioxidant Protein PAG by Direct Interaction

Jung, H., Kim, T., Chae, H. Z., Kim, K., & Ha, H. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m009620200 · Cited by 99 · see citing works

Role of Macrophage Migration Inhibitory Factor in the Regulation of the Immune Response

Metz, C. N., & Bucala, R. (1997) · Advances in immunology · doi:10.1016/s0065-2776(08)60598-2 · Cited by 91 · see citing works

Cyclopentenone prostaglandins—new allies in the war on inflammation

Willoughby, D. A., Moore, A., & Colville‐Nash, P. (2000) · Nature Medicine · doi:10.1038/72224 · Cited by 48 · see citing works

Biological actions of δ12-prostaglandin J2

Negishi, M., Koizumi, T., & Ichikawa, A. (1995) · Journal of Lipid Mediators and Cell Signalling · doi:10.1016/0929-7855(95)00029-p · Cited by 38 · see citing works

GLUTATHIONE TRANSFERASES

Hayes, J. D., Flanagan, J. U., & Jowsey, I. R. (2004) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.45.120403.095857 · Cited by 3,565 · see citing works

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

Kensler, T. W., Wakabayashi, N., & Biswal, S. (2007) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.46.120604.141046 · Cited by 3,630 · see citing works

The KEAP1-NRF2 system: a thiol-based sensor-effector apparatus for maintaining redox homeostasis

Yamamoto, M., Kensler, T. W., & Motohashi, H. (2018) · Physiological Reviews · doi:10.1152/physrev.00023.2017 · Cited by 1,968 · see citing works

Nrf2 suppresses macrophage inflammatory response by blocking proinflammatory cytokine transcription

Kobayashi, E. H., Suzuki, T., Funayama, R., Nagashima, T., Hayashi, M., Sekine, H., Tanaka, N., Moriguchi, T., Motohashi, H., Nakayama, K., et al. (2016) · Nature Communications · doi:10.1038/ncomms11624 · Cited by 1,878 · see citing works

Nrf2 signaling pathway: pivotal roles in inflammation

Ahmed, S. M. U., Luo, L., Namani, A., Wang, X. J., & Tang, X. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2016.11.005 · Cited by 1,794 · see citing works

Nrf2–Keap1 defines a physiologically important stress response mechanism

Motohashi, H., & Yamamoto, M. (2004) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2004.09.003 · Cited by 1,725 · see citing works

NRF2 and the Hallmarks of Cancer

Rojo de la Vega, M., Chapman, E., & Zhang, D. D. (2018) · Cancer Cell · doi:10.1016/j.ccell.2018.03.022 · Cited by 1,672 · see citing works

An Overview of Nrf2 Signaling Pathway and Its Role in Inflammation

Saha, S., Buttari, B., Panieri, E., Profumo, E., & Saso, L. (2020) · Molecules · doi:10.3390/molecules25225474 · Cited by 1,419 · see citing works

Nrf2 and Oxidative Stress: A General Overview of Mechanisms and Implications in Human Disease

Ngo, V., & Duennwald, M. L. (2022) · Antioxidants · doi:10.3390/antiox11122345 · Cited by 1,130 · see citing works

Molecular Mechanisms Activating the Nrf2-Keap1 Pathway of Antioxidant Gene Regulation

Kobayashi, M., & Yamamoto, M. P. (2005) · Antioxidants and Redox Signaling · doi:10.1089/ars.2005.7.385 · Cited by 1,075 · see citing works

Inflammation, a Key Event in Cancer Development

Lu, H., Ouyang, W., & Huang, C. (2006) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-05-0261 · Cited by 1,031 · see citing works

Oxidative stress in health and disease: The therapeutic potential of Nrf2 activation

Hybertson, B. M., Gao, B., Bose, S. K., & McCord, J. M. (2011) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2011.10.006 · Cited by 1,029 · see citing works

Oxidative and Electrophilic Stresses Activate Nrf2 through Inhibition of Ubiquitination Activity of Keap1

Kobayashi, A., Kang, M.-I., Watai, Y., Tong, K. I., Shibata, T., Uchida, K., & Yamamoto, M. P. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.26.1.221-229.2006 · Cited by 933 · see citing works

Bardoxolone Methyl and Kidney Function in CKD with Type 2 Diabetes

Pergola, P. E., Raskin, P., Toto, R. D., Meyer, C. J., Huff, J. W., Grossman, E. B., Krauth, M., Ruiz, S., Audhya, P., Christ-Schmidt, H., et al. (2011) · New England Journal of Medicine · doi:10.1056/nejmoa1105351 · Cited by 890 · see citing works

Nrf2–Keap1 regulation of cellular defense mechanisms against electrophiles and reactive oxygen species

Kobayashi, M., & Yamamoto, M. P. (2006) · Advances in Enzyme Regulation · doi:10.1016/j.advenzreg.2006.01.007 · Cited by 855 · see citing works

Mechanisms of activation of the transcription factor Nrf2 by redox stressors, nutrient cues, and energy status and the pathways through which it attenuates degenerative disease

Tebay, L. E., Robertson, H., Durant, S. T., Vitale, S. R., Penning, T. M., Dinkova-Kostova, A. T., & Hayes, J. D. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.06.021 · Cited by 837 · see citing works

The Antioxidant Defense System Keap1-Nrf2 Comprises a Multiple Sensing Mechanism for Responding to a Wide Range of Chemical Compounds

Kobayashi, M., Li, L., Iwamoto, N., Nakajima‐Takagi, Y., Kaneko, H., Nakayama, Y., Eguchi, M., Wada, Y., Kumagai, Y., & Yamamoto, M. P. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01080-08 · Cited by 641 · see citing works

When NRF2 Talks, Who's Listening?

Wakabayashi, N., Slocum, S. L., Skoko, J. J., Shin, S., & Kensler, T. W. (2010) · Antioxidants &amp; Redox Signaling · doi:10.1089/ars.2010.3216 · Cited by 595 · see citing works

Basic Principles and Emerging Concepts in the Redox Control of Transcription Factors

Brigelius-Flohé, R., & Flohé, L. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3534 · Cited by 577 · see citing works

Extremely potent triterpenoid inducers of the phase 2 response: Correlations of protection against oxidant and inflammatory stress

Dinkova‐Kostova, A. T., Liby, K. T., Stephenson, K. K., Holtzclaw, W. D., Gao, X., Suh, N., Williams, C. R., Risingsong, R., Honda, T., Gribble, G. W., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0500815102 · Cited by 575 · see citing works

Coordination of ER and oxidative stress signaling: The PERK/Nrf2 signaling pathway

Cullinan, S. B., & Diehl, J. A. (2006) · The International Journal of Biochemistry &amp; Cell Biology · doi:10.1016/j.biocel.2005.09.018 · Cited by 554 · see citing works

Nrf2 signaling: An adaptive response pathway for protection against environmental toxic insults

Osburn, W. O., & Kensler, T. W. (2007) · Mutation Research/Reviews in Mutation Research · doi:10.1016/j.mrrev.2007.11.006 · Cited by 549 · see citing works

Discovery of the Negative Regulator of Nrf2, Keap1: A Historical Overview

Itoh, K., Mimura, J., & Yamamoto, M. P. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3222 · Cited by 513 · see citing works

Modulation of Nrf2-mediated antioxidant and detoxifying enzyme induction by the green tea polyphenol EGCG

Na, H., & Surh, Y. (2007) · Food and Chemical Toxicology · doi:10.1016/j.fct.2007.10.006 · Cited by 486 · see citing works

Modifying specific cysteines of the electrophile-sensing human Keap1 protein is insufficient to disrupt binding to the Nrf2 domain Neh2

Eggler, A. L., Liu, G., Pezzuto, J. M., van Breemen, R. B., & Mesecar, A. D. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0502402102 · Cited by 459 · see citing works

Curcumin upregulates transcription factor Nrf2, HO-1 expression and protects rat brains against focal ischemia

Yang, C., Zhang, X., Fan, H., & Liu, Y. (2009) · Brain Research · doi:10.1016/j.brainres.2009.05.009 · Cited by 444 · see citing works

The Crosstalk Between Nrf2 and AMPK Signal Pathways Is Important for the Anti-Inflammatory Effect of Berberine in LPS-Stimulated Macrophages and Endotoxin-Shocked Mice

Mo, C., Wang, L., Zhang, J., Numazawa, S., Tang, H. W., Tang, X., Han, X., Li, J., Yang, M., Wang, Z., et al. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.5116 · Cited by 442 · see citing works

A Small-Molecule-Inducible Nrf2-Mediated Antioxidant Response Provides Effective Prophylaxis against Cerebral Ischemia<i>In Vivo</i>

Shih, A. Y., Li, P., & Murphy, T. H. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.4014-05.2005 · Cited by 413 · see citing works

Stress-sensing mechanisms and the physiological roles of the Keap1–Nrf2 system during cellular stress

Suzuki, T., & Yamamoto, M. P. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.r117.800169 · Cited by 402 · see citing works

Activation of NRF2 by Nitrosative Agents and H2O2 Involves KEAP1 Disulfide Formation

Fourquet, S., Guérois, R., Biard, D. S. F., & Tolédano, M. B. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.051714 · Cited by 378 · see citing works

The Role of Keap1 in Cellular Protective Responses

Dinkova‐Kostova, A. T., Holtzclaw, W. D., & Kensler, T. W. (2005) · Chemical Research in Toxicology · doi:10.1021/tx050217c · Cited by 378 · see citing works

Small Maf proteins serve as transcriptional cofactors for keratinocyte differentiation in the Keap1–Nrf2 regulatory pathway

Motohashi, H., Katsuoka, F., Engel, J. D., & Yamamoto, M. P. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0305902101 · Cited by 363 · see citing works

Environmental pollutants and the immune response

Suzuki, T., Hidaka, T., Kumagai, Y., & Yamamoto, M. P. (2020) · Nature Immunology · doi:10.1038/s41590-020-0802-6 · Cited by 356 · see citing works

Activation of the Keap1/Nrf2 pathway for neuroprotection by electrophillic phase II inducers

Satoh, T., Okamoto, S.-I., Cui, J., Watanabe, Y., Furuta, K., Suzuki, M., Tohyama, K., & Lipton, S. A. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0505723102 · Cited by 342 · see citing works

Nrf2‐deficient mice are highly susceptible to cigarette smoke‐induced emphysema

Iizuka, T., Ishii, Y., Itoh, K., Kiwamoto, T., Kimura, T., Matsuno, Y., Morishima, Y., Hegab, A. E., Homma, S., Nomura, A., et al. (2005) · Genes to Cells · doi:10.1111/j.1365-2443.2005.00905.x · Cited by 336 · see citing works

The Nrf2–Keap1 defence pathway: Role in protection against drug-induced toxicity

Copple, I. M., Goldring, C. E., Kitteringham, N. R., & Park, B. K. (2007) · Toxicology · doi:10.1016/j.tox.2007.10.029 · Cited by 328 · see citing works

Plasma Medicine: A Field of Applied Redox Biology

von Woedtke, T., Schmidt, A., Bekeschus, S., Wende, K., & Weltmann, K. (2019) · In Vivo · doi:10.21873/invivo.11570 · Cited by 321 · see citing works

Free Radicals, Mitochondria, and Oxidized Lipids

Gutiérrez, J., Ballinger, S. W., Darley-Usmar, V. M., & Landar, A. L. (2006) · Circulation Research · doi:10.1161/01.res.0000248212.86638.e9 · Cited by 319 · see citing works

Molecular Basis of Electrophilic and Oxidative Defense: Promises and Perils of Nrf2

Ma, Q., & He, X. (2012) · Pharmacological Reviews · doi:10.1124/pr.110.004333 · Cited by 317 · see citing works

Chemoprevention through the Keap1–Nrf2 signaling pathway by phase 2 enzyme inducers

Kwak, M.-K., Wakabayashi, N., & Kensler, T. W. (2004) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2004.06.041 · Cited by 311 · see citing works

Formation and signaling actions of electrophilic lipids

Schopfer, F. J., Cipollina, C., & Freeman, B. A. (2011) · Chemical Reviews · doi:10.1021/cr200131e · Cited by 299 · see citing works

Down-Regulated NF-E2–Related Factor 2 in Pulmonary Macrophages of Aged Smokers and Patients with Chronic Obstructive Pulmonary Disease

Suzuki, M., Betsuyaku, T., Ito, Y., Nagai, K., Nasuhara, Y., Kaga, K., Kondo, S., & Nishimura, M. (2008) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2007-0424oc · Cited by 286 · see citing works

Dietary cancer-chemopreventive compounds: from signaling and gene expression to pharmacological effects

Chen, C., & Kong, A. T. (2005) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2005.04.004 · Cited by 269 · see citing works

Heme Oxygenase-1 and the Vascular Bed: From Molecular Mechanisms to Therapeutic Opportunities

Łoboda, A., Jaźwa, A., Grochot‐Przeczek, A., Rutkowski, A. J., Cisowski, J., Agarwal, A., Józkowicz, A., & Dulak, J. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2043 · Cited by 263 · see citing works

TrxR1 as a Potent Regulator of the Nrf2-Keap1 Response System

Cebula, M., Schmidt, E. E., & Arnér, E. S. J. (2015) · Antioxidants and Redox Signaling · doi:10.1089/ars.2015.6378 · Cited by 251 · see citing works

Thirty years of NRF2: advances and therapeutic challenges.

Zhang, D. D. (2025) · Nature Reviews Drug Discovery · doi:10.1038/s41573-025-01145-0 · Cited by 282 · see citing works

Transcription factor Nrf2 plays a pivotal role in protection against elastase-induced pulmonary inflammation and emphysema

Ishii, Y., Itoh, K., Morishima, Y., Kimura, T., Kiwamoto, T., IIzuka, T., Hegab, A. E., Hosoya, T., Nomura, A., Sakamoto, T., et al. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.175.10.6968 · Cited by 248 · see citing works

Tricarboxylic Acid (TCA) Cycle Intermediates: Regulators of Immune Responses

Choi, I., Son, H., & Baek, J.-H. (2021) · Life · doi:10.3390/life11010069 · Cited by 244 · see citing works

Protein Damage by Reactive Electrophiles: Targets and Consequences

Liebler, D. C. (2007) · Chemical Research in Toxicology · doi:10.1021/tx700235t · Cited by 235 · see citing works

The Flavanol (−)-Epicatechin Prevents Stroke Damage through the Nrf2/HO1 Pathway

Shah, Z. A., Li, R.-C., Ahmad, A. S., Kensler, T. W., Yamamoto, M. P., Biswal, S. S., & Doré, S. (2010) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.2010.53 · Cited by 236 · see citing works

Redox regulation of antioxidants, autophagy, and the response to stress: Implications for electrophile therapeutics

Levonen, A., Hill, B. G., Kansanen, E., Zhang, J., & Darley-Usmar, V. M. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.03.025 · Cited by 232 · see citing works

Transcription factor Nrf2 regulates SHP and lipogenic gene expression in hepatic lipid metabolism

Huang, J., Tabbi‐Anneni, I., Gunda, V., & Wang, L. (2010) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00322.2010 · Cited by 228 · see citing works

Differential Responses of the Nrf2-Keap1 System to Laminar and Oscillatory Shear Stresses in Endothelial Cells

Hosoya, T., Maruyama, A., Kang, M.-I., Kawatani, Y., Shibata, T., Uchida, K., Itoh, K., & Yamamoto, M. P. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m502551200 · Cited by 227 · see citing works

Nrf2 regulates ferroportin 1-mediated iron efflux and counteracts lipopolysaccharide-induced ferroportin 1 mRNA suppression in macrophages

Harada, N., Kanayama, M., Maruyama, A., Yoshida, A., Tazumi, K., Hosoya, T., Mimura, J., Toki, T., Maher, J. M., Yamamoto, M. P., et al. (2011) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2011.02.001 · Cited by 231 · see citing works

Small molecule modulators of antioxidant response pathway

Hur, W., & Gray, N. S. (2010) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2010.12.009 · Cited by 213 · see citing works

30 some years of heme oxygenase: from a "molecular wrecking ball" to a "mesmerizing" trigger of cellular events.

Maines, M. D., & Gibbs, P. (2005) · Biochemical and Biophysical Research Communications - BBRC · doi:10.1016/j.bbrc.2005.08.121 · Cited by 233 · see citing works

The Absence of the Pro-antioxidant Transcription Factor Nrf2 Exacerbates Experimental Autoimmune Encephalomyelitis

Johnson, D. A., Amirahmadi, S., Ward, C., Fabry, Z., & Johnson, J. A. (2009) · Toxicological Sciences · doi:10.1093/toxsci/kfp274 · Cited by 205 · see citing works

Transduction of Redox Signaling by Electrophile-Protein Reactions

Rudolph, T. K., & Freeman, B. Α. (2009) · Science Signaling · doi:10.1126/scisignal.290re7 · Cited by 200 · see citing works

Nutritional strategies to modulate inflammation and oxidative stress pathways via activation of the master antioxidant switch Nrf2

Cardozo, L., Pedruzzi, L. M., Stenvinkel, P., Stockler‐Pinto, M. B., Daleprane, J. B., Leite, M., & Mafra, D. (2013) · Biochimie · doi:10.1016/j.biochi.2013.04.012 · Cited by 201 · see citing works

Nrf2 as a target for cancer chemoprevention

Yu, X. Y., & Kensler, T. W. (2005) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2005.04.017 · Cited by 199 · see citing works

Nrf2: Molecular and epigenetic regulation during aging

Silva‐Palacios, A., Ostolga-Chavarría, M., Zazueta, C., & Königsberg, M. (2018) · Ageing Research Reviews · doi:10.1016/j.arr.2018.06.003 · Cited by 195 · see citing works

Increased colonic inflammatory injury and formation of aberrant crypt foci in Nrf2‐deficient mice upon dextran sulfate treatment

Osburn, W. O., Karim, B. O., Dolan, P. M., Liu, G., Yamamoto, M. P., Huso, D. L., & Kensler, T. W. (2007) · International Journal of Cancer · doi:10.1002/ijc.22943 · Cited by 197 · see citing works

Effects of 4-hydroxynonenal on vascular endothelial and smooth muscle cell redox signaling and function in health and disease

Chapple, S., Cheng, X.-H., & Mann, G. (2013) · Redox Biology · doi:10.1016/j.redox.2013.04.001 · Cited by 183 · see citing works

Crosstalk of toll-like receptors signaling and Nrf2 pathway for regulation of inflammation

Mohan, S. V., & Gupta, D. (2018) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2018.10.019 · Cited by 217 · see citing works

Lipoxins: nature's way to resolve inflammation

Sharma-Walia, N., & Chandrasekharan, J. A. (2015) · Journal of Inflammation Research · doi:10.2147/jir.s90380 · Cited by 234 · see citing works

Multiple regulations of Keap1/Nrf2 system by dietary phytochemicals

Qin, S., & Hou, D. (2016) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201501017 · Cited by 190 · see citing works

The Redox Activity of Hemoglobins: From Physiologic Functions to Pathologic Mechanisms

Reeder, B. J. (2010) · Antioxidants &amp; Redox Signaling · doi:10.1089/ars.2009.2974 · Cited by 189 · see citing works

Nrf2 Gene Transfer Induces Antioxidant Enzymes and Suppresses Smooth Muscle Cell Growth In Vitro and Reduces Oxidative Stress in Rabbit Aorta In Vivo

Levonen, A., Inkala, M., Heikura, T., Jauhiainen, S., Jyrkkänen, H.-K., Kansanen, E., Määttä, K. M., Romppanen, E., Turunen, P., Rutanen, J., et al. (2007) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000258868.80079.4d · Cited by 189 · see citing works

Celastrol suppresses colorectal cancer via covalent targeting peroxiredoxin 1

Xu, H., Zhao, H., Ding, C., Jiang, D., Zhao, Z., Li, Y., Ding, X., Gao, J., Zhou, H., Luo, C., et al. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01231-4 · Cited by 190 · see citing works

The Keap1–Nrf2 system as an in vivo sensor for electrophiles

Uruno, A., & Motohashi, H. (2011) · Nitric Oxide · doi:10.1016/j.niox.2011.02.007 · Cited by 187 · see citing works

Roles of Nrf2 in Protecting the Kidney from Oxidative Damage

Nezu, M., & Suzuki, N. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21082951 · Cited by 180 · see citing works

Cul3-mediated Nrf2 ubiquitination and antioxidant response element (ARE) activation are dependent on the partial molar volume at position 151 of Keap1

Eggler, A. L., Small, E., Hannink, M., & Mesecar, A. D. (2009) · Biochemical Journal · doi:10.1042/bj20090471 · Cited by 178 · see citing works

Transcription factor Nrf2 mediates an adaptive response to sulforaphane that protects fibroblasts in vitro against the cytotoxic effects of electrophiles, peroxides and redox-cycling agents

Higgins, L. G., Kelleher, M., Eggleston, I. M., Itoh, K., Yamamoto, M. P., & Hayes, J. D. (2009) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2009.03.005 · Cited by 177 · see citing works

Nrf2-Keap1 Signaling as a Potential Target for Chemoprevention of Inflammation-Associated Carcinogenesis

Kundu, J. K., & Surh, Y. (2010) · Pharmaceutical Research · doi:10.1007/s11095-010-0096-8 · Cited by 173 · see citing works

The Keap1–Nrf2 Cell Defense Pathway – A Promising Therapeutic Target?

Copple, I. M. (2012) · Advances in pharmacology · doi:10.1016/b978-0-12-398339-8.00002-1 · Cited by 172 · see citing works

Targeting the Nrf2 pathway against cardiovascular disease

Li, J., Ichikawa, T., Janicki, J. S., & Cui, T. (2009) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728220903025762 · Cited by 168 · see citing works

Redox Regulation of Human Thioredoxin Network

Kondo, N., Nakamura, H., Masutani, H., & Yodoi, J. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.1881 · Cited by 166 · see citing works

CXCL1 and CXCL2 Regulate NLRP3 Inflammasome Activation via G-Protein–Coupled Receptor CXCR2

Boro, M., & Balaji, K. N. (2017) · The Journal of Immunology · doi:10.4049/jimmunol.1700129 · Cited by 165 · see citing works

Nrf2 Suppresses Oxidative Stress and Inflammation in App Knock-In Alzheimer’s Disease Model Mice

Uruno, A., Matsumaru, D., Ryoke, R., Saito, R., Kadoguchi, S., Saigusa, D., Saito, T., Saido, T. C., Kawashima, R., & Yamamoto, M. P. (2020) · Molecular and Cellular Biology · doi:10.1128/mcb.00467-19 · Cited by 166 · see citing works

Nrf2-dependent and -independent Responses to Nitro-fatty Acids in Human Endothelial Cells

Kansanen, E., Jyrkkänen, H.-K., Volger, O. L., Leinonen, H., Kivelä, A. M., Häkkinen, S.-K., Woodcock, S. R., Schopfer, F. J., Horrevoets, A. J., Ylä-Herttuala, S., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.064873 · Cited by 165 · see citing works

Genetic or Pharmacologic Amplification of Nrf2 Signaling Inhibits Acute Inflammatory Liver Injury in Mice

Osburn, W. O., Yates, M. S., Dolan, P. D., Chen, S., Liby, K. T., Sporn, M. B., Taguchi, K., Yamamoto, M. P., & Kensler, T. W. (2008) · Toxicological Sciences · doi:10.1093/toxsci/kfn079 · Cited by 158 · see citing works

Cold atmospheric plasma delivery for biomedical applications

Chen, Z., Chen, G., Obenchain, R. A., Zhang, R., Bai, F., Fang, T., Wang, H., Lu, Y., Wirz, R. E., & Gu, Z. (2022) · Materials Today · doi:10.1016/j.mattod.2022.03.001 · Cited by 159 · see citing works

Small Maf Proteins in Mammalian Gene Control: Mere Dimerization Partners or Dynamic Transcriptional Regulators?

Blank, V. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.11.074 · Cited by 154 · see citing works

Redox regulation of neuronal survival mediated by electrophilic compounds

Satoh, T., & Lipton, S. A. (2006) · Trends in Neurosciences · doi:10.1016/j.tins.2006.11.004 · Cited by 154 · see citing works

Regulation of Nrf2-dependent gene expression by 15-deoxy-Δ12,14-prostaglandin J2

Kansanen, E., Kivelä, A. M., & Levonen, A. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.06.030 · Cited by 150 · see citing works

Oxidized LDL induces mitochondrially associated reactive oxygen/nitrogen species formation in endothelial cells

Żmijewski, J. W., Moellering, D. R., Goffe, C. L., Landar, A. L., Ramachandran, A., & Darley-Usmar, V. M. (2005) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00015.2005 · Cited by 148 · see citing works

Caffeic acid phenethyl ester-mediated Nrf2 activation and IκB kinase inhibition are involved in NFκB inhibitory effect: Structural analysis for NFκB inhibition

Lee, Y., Shin, D., Kim, J., Hong, S., Choi, D., Kim, Y.-J., Kwak, M., & Jung, Y. (2010) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2010.06.016 · Cited by 147 · see citing works

Non-thermal Plasma Activates Human Keratinocytes by Stimulation of Antioxidant and Phase II Pathways

Schmidt, A., Dietrich, S., Steuer, A., Weltmann, K., von Woedtke, T., Masur, K., & Wende, K. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.603555 · Cited by 146 · see citing works

15-Deoxy-Δ12,14-prostaglandin J2 as a potential endogenous regulator of redox-sensitive transcription factors

Kim, E. H., & Surh, Y. (2006) · Biochemical Pharmacology · doi:10.1016/j.bcp.2006.07.030 · Cited by 145 · see citing works

Nitro-linoleic acid inhibits vascular smooth muscle cell proliferation via the Keap1/Nrf2 signaling pathway

Villacorta, L., Zhang, J., Garcia-Barrio, M. T., Chen, X.-L., Freeman, B. A., Chen, Y. E., & Cui, T. (2007) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00261.2007 · Cited by 144 · see citing works

Interaction of electrophilic lipid oxidation products with mitochondria in endothelial cells and formation of reactive oxygen species

Landar, A. L., Żmijewski, J. W., Dickinson, D. A., Goffe, C. L., Johnson, M. S., Milne, G. L., Zanoni, G., Vidari, G., Morrow, J. D., & Darley-Usmar, V. M. (2005) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.01087.2005 · Cited by 139 · see citing works

15-Deoxy-Δ12,14-prostaglandin J2: An Electrophilic Trigger of Cellular Responses

Uchida, K., & Shibata, T. (2007) · Chemical Research in Toxicology · doi:10.1021/tx700177j · Cited by 139 · see citing works

Identification of polymorphisms in the promoter region of the human NRF2 gene

Yamamoto, T., Yoh, K., Kobayashi, A., Ishii, Y., Kure, S., Kôyama, A., Sakamoto, T., Sekizawa, K., Motohashi, H., & Yamamoto, M. P. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.06.112 · Cited by 137 · see citing works

Regulation of innate immunity by NADPH oxidase

Segal, B. H., Grimm, M. J., Khan, A. N. H., Han, W., & Blackwell, T. S. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.04.022 · Cited by 139 · see citing works

Oxidative Modification of Proteins: An Emerging Mechanism of Cell Signaling

Wall, S. B., Oh, J., Diers, A. R., & Landar, A. L. (2012) · Frontiers in Physiology · doi:10.3389/fphys.2012.00369 · Cited by 136 · see citing works

Cardiovascular targets for estrogens and phytoestrogens: Transcriptional regulation of nitric oxide synthase and antioxidant defense genes

Siow, R. C. M., Li, F. Y. L., Rowlands, D. J., de Winter, P., & Mann, G. E. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.01.004 · Cited by 135 · see citing works

Absolute Amounts and Status of the Nrf2-Keap1-Cul3 Complex within Cells

Iso, T., Suzuki, T., Baird, L., & Yamamoto, M. P. (2016) · Molecular and Cellular Biology · doi:10.1128/mcb.00389-16 · Cited by 130 · see citing works

15-Deoxy-Δ12,14-prostaglandin J2, an electrophilic lipid mediator of anti-inflammatory and pro-resolving signaling

Surh, Y., Na, H., Park, J., Lee, H., Kim, W., Yoon, I., & Kim, D. (2011) · Biochemical Pharmacology · doi:10.1016/j.bcp.2011.07.100 · Cited by 126 · see citing works

Pleiotropic effects of oxidized phospholipids

Bochkov, V. N., Gesslbauer, B., Mauerhofer, C., Philippova, M., Erné, P., & Oskolkova, O. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.12.034 · Cited by 125 · see citing works

Self-defense of macrophages against oxidative injury: Fighting for their own survival

Virág, L., Jaén, R. I., Regdon, Z., Boscá, L., & Prieto, P. (2019) · Redox Biology · doi:10.1016/j.redox.2019.101261 · Cited by 121 · see citing works

Abstract 2572: Pro-resolving effects of 15-deoxy-α12,14-prostaglandin J2 through activation of Nrf2-mediated CD36 expression in murine macrophages

Kim, W.-K., Lee, H., & Surh, Y. (2012) · Cancer Research · doi:10.1158/1538-7445.am2012-2572

Biological actions of δ12-prostaglandin J2

Negishi, M., Koizumi, T., & Ichikawa, A. (1995) · Journal of Lipid Mediators and Cell Signalling · doi:10.1016/0929-7855(95)00029-p · Cited by 38 · see citing works

Nrf2 is essential for the expression of lipocalin–prostaglandin D synthase induced by prostaglandin D2

Kim, K. H., Sadikot, R. T., Xiao, L., Christman, J. W., Freeman, M. L., Chan, J. Y., Oh, Y., Blackwell, T. S., & Joo, M. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.08.192 · Cited by 18 · see citing works

Close teamwork between Nrf2 and peroxiredoxins 1 and 6 for the regulation of prostaglandin D2 and E2 production in macrophages in acute inflammation

Ishii, T. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.04.034 · Cited by 50 · see citing works

Regulation of Nrf2-dependent gene expression by 15-deoxy-Δ12,14-prostaglandin J2

Kansanen, E., Kivelä, A. M., & Levonen, A. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.06.030 · Cited by 150 · see citing works