Protection against electrophile and oxidant stress by induction of the phase 2 response: Fate of cysteines of the Keap1 sensor modified by inducers

Manipulating the mouse embryo: A laboratory manual

Hogan, B. L. M., Costantini, F. D., & Lacy, E. (1986) · Cited by 4,460

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

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

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

Glutathione and glutathione-dependent enzymes represent a co-ordinately regulated defence against oxidative stress

Hayes, J. D., & McLellan, L. I. (1999) · Free Radical Research · doi:10.1080/10715769900300851 · Cited by 1,528

Distinct cysteine residues in Keap1 are required for Keap1-dependent ubiquitination of Nrf2 and for stabilization of Nrf2 by chemopreventive agents and oxidative stress

Zhang, D. D., & Hannink, M. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.22.8137-8151.2003 · Cited by 1,480

Regulatory Mechanisms Controlling Gene Expression Mediated by the Antioxidant Response Element

Nguyen, T., Sherratt, P. J., & Pickett, C. B. (2003) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.43.100901.140229 · Cited by 1,232

Activation of the OxyR Transcription Factor by Reversible Disulfide Bond Formation

Zheng, M., Åslund, F., & Storz, G. (1998) · Science · doi:10.1126/science.279.5357.1718 · Cited by 1,197

Keap1-dependent proteasomal degradation of transcription factor Nrf2 contributes to the negative regulation of antioxidant response element-driven gene expression

McMahon, M., Itoh, K., Yamamoto, M., & Hayes, J. D. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300931200 · Cited by 1,141

Sensitivity to carcinogenesis is increased and chemoprotective efficacy of enzyme inducers is lost in nrf2 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

Keap1 Controls Postinduction Repression of the Nrf2-Mediated Antioxidant Response by Escorting Nuclear Export of Nrf2

Sun, Z., Zhang, S., Chan, J. Y., & Zhang, D. D. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00630-07 · Cited by 332

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 336

Elucidating mechanisms of drug-induced toxicity

Liebler, D. C., & Guengerich, F. P. (2005) · Nature Reviews Drug Discovery · doi:10.1038/nrd1720 · Cited by 330

Monoacidic Inhibitors of the Kelch-like ECH-Associated Protein 1: Nuclear Factor Erythroid 2-Related Factor 2 (KEAP1:NRF2) Protein–Protein Interaction with High Cell Potency Identified by Fragment-Based Discovery

Davies, T. G., Wixted, W. E., Coyle, J. E., Griffiths-Jones, C., Hearn, K., McMenamin, R., Norton, D., Rich, S. J., Richardson, C., Saxty, G., et al. (2016) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b00228 · Cited by 322

Specific Patterns of Electrophile Adduction Trigger Keap1 Ubiquitination and Nrf2 Activation

Hong, F., Sekhar, K. R., Freeman, M. L., & Liebler, D. C. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m503346200 · Cited by 316

Oxidative and electrophilic stress induces multidrug resistance–associated protein transporters via the nuclear factor-E2–related factor-2 transcriptional pathway

Maher, J. M., Dieter, M. Z., Aleksunes, L. M., Slitt, A. L., Guo, G. L., Tanaka, Y., Scheffer, G. L., Chan, J. Y., Manautou, J. E., Chen, Y., et al. (2007) · Hepatology · doi:10.1002/hep.21831 · Cited by 319

Modification of Keap1 Cysteine Residues by Sulforaphane

Hu, C., Eggler, A. L., Mesecar, A. D., & van Breemen, R. B. (2011) · Chemical Research in Toxicology · doi:10.1021/tx100389r · Cited by 312

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 312

Oxidative Damage in Huntington's Disease Pathogenesis

Browne, S. E., & Beal, M. F. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.2061 · Cited by 313

Molecular Basis of the KEAP1-NRF2 Signaling Pathway

Suzuki, T., Takahashi, J. A., & Yamamoto, M. P. (2023) · Molecules and Cells · doi:10.14348/molcells.2023.0028 · Cited by 320

Targeting NRF2 signaling for cancer chemoprevention

Kwak, M.-K., & Kensler, T. W. (2009) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2009.08.028 · Cited by 306

miR-200a Regulates Nrf2 Activation by Targeting Keap1 mRNA in Breast Cancer Cells

Eades, G. L., Yang, M., Yao, Y., Zhang, Y., & Zhou, Q. Y. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.275495 · Cited by 305

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

Glutathione, Stress Responses, and Redox Signaling in Lung Inflammation

Rahman, I., Biswas, S. K., Jimenez, L. A., Torrès, M., & Forman, H. J. (2004) · Antioxidants and Redox Signaling · doi:10.1089/ars.2005.7.42 · Cited by 295

Characterization of the cancer chemopreventive NRF2-dependent gene battery in human keratinocytes: demonstration that the KEAP1–NRF2 pathway, and not the BACH1–NRF2 pathway, controls cytoprotection against electrophiles as well as redox-cycling compounds

MacLeod, A. K., McMahon, M. J., Plummer, S. M., Higgins, L. G., Penning, T. M., Igarashi, K., & Hayes, J. D. (2009) · Carcinogenesis · doi:10.1093/carcin/bgp176 · Cited by 305

Characterizations of Three Major Cysteine Sensors of Keap1 in Stress Response

Saito, R., Suzuki, T., Hiramoto, K., Asami, S., Naganuma, E., Suda, H., Iso, T., Yamamoto, H., Morita, M., Baird, L., et al. (2016) · Molecular and Cellular Biology · doi:10.1128/mcb.00868-15 · Cited by 294

The Nrf2/HO‐1 Axis in Cancer Cell Growth and Chemoresistance

Furfaro, A. L., Traverso, N., Domenicotti, C., Piras, S., Moretta, L., Marinari, U. M., Pronzato, M. A., & Nitti, M. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/1958174 · Cited by 303

Nrf2-ARE stress response mechanism: A control point in oxidative stress-mediated dysfunctions and chronic inflammatory diseases

Singh, S., Vrishni, S., Singh, B. K., Rahman, I., & Kakkar, P. (2010) · Free Radical Research · doi:10.3109/10715762.2010.507670 · Cited by 305

The Role of Nrf2 in Cardiovascular Function and Disease

Satta, S., Mahmoud, A. M., Wilkinson, F. L., Alexander, M. Y., & White, S. J. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/9237263 · Cited by 306

NRF2 Blockade Suppresses Colon Tumor Angiogenesis by Inhibiting Hypoxia-Induced Activation of HIF-1α

Kim, T., Hur, E.-G., Kang, S., Kim, J., Thapa, D., Lee, Y. M., Ku, S., Jung, Y., & Kwak, M. (2011) · Cancer Research · doi:10.1158/0008-5472.can-10-3007 · Cited by 292

The Nrf2–ARE cytoprotective pathway in astrocytes

Vargas, M. R., & Johnson, J. A. (2009) · Expert Reviews in Molecular Medicine · doi:10.1017/s1462399409001094 · Cited by 295

Redox homeostasis: the linchpin in stem cell self-renewal and differentiation

Wang, K., Zhang, T., Dong, Q. G., Nice, E. C., Huang, C., & Wei, Y. (2013) · Cell Death and Disease · doi:10.1038/cddis.2013.50 · Cited by 298

Molecular Mechanism of Cellular Oxidative Stress Sensing by Keap1

Suzuki, T., Muramatsu, A., Saito, R., Iso, T., Shibata, T., Kuwata, K., Kawaguchi, S.-I., Iwawaki, T., Adachi, S., Suda, H., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.06.047 · Cited by 297

The emerging family of CULLIN3-RING ubiquitin ligases (CRL3s): cellular functions and disease implications

Genschik, P., Sumara, I., & Lechner, E. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.173 · Cited by 278

Emerging Role of Nrf2 in Protecting Against Hepatic and Gastrointestinal Disease

Aleksunes, L. M., & Manautou, J. E. (2007) · Toxicologic Pathology · doi:10.1080/01926230701311344 · Cited by 288

Chemoprevention by isothiocyanates and their underlying molecular signaling mechanisms

Keum, Y., Jeong, W., & Kong, A. (2004) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2004.05.024 · Cited by 285

MiR-28 regulates Nrf2 expression through a Keap1-independent mechanism

Yang, M., Yao, Y., Eades, G. L., Zhang, Y., & Zhou, Q. Y. (2011) · Breast Cancer Research and Treatment · doi:10.1007/s10549-011-1604-1 · Cited by 280

Novel n-3 Fatty Acid Oxidation Products Activate Nrf2 by Destabilizing the Association between Keap1 and Cullin3

Gao, L., Wang, J., Sekhar, K. R., Yin, H., Yared, N. F., Schneider, S. N., Sasi, S., Dalton, T. P., Anderson, M. E., Chan, J. Y., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m607622200 · Cited by 289

Validation of the multiple sensor mechanism of the Keap1-Nrf2 system

Takaya, K., Suzuki, T., Motohashi, H., Onodera, K., Satomi, S., Kensler, T. W., & Yamamoto, M. P. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.06.023 · Cited by 284

Dietary Sulforaphane-Rich Broccoli Sprouts Reduce Colonization and Attenuate Gastritis in Helicobacter pylori –Infected Mice and Humans

Yanaka, A., Fahey, J. W., Fukumoto, A., Nakayama, M., Inoue, S., Zhang, S., Tauchi, M., Suzuki, H., Hyodo, I., & Yamamoto, M. P. (2009) · Cancer Prevention Research · doi:10.1158/1940-6207.capr-08-0192 · Cited by 276

Induction of the Nrf2-driven Antioxidant Response Confers Neuroprotection during Mitochondrial Stress in Vivo

Shih, A. Y., Imbeault, S., Barakauskas, V., Erb, H., Jiang, L., Li, P., & Murphy, T. H. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414635200 · Cited by 273

Protein S-guanylation by the biological signal 8-nitroguanosine 3′,5′-cyclic monophosphate

Sawa, T., Zaki, M. H., Okamoto, T., Akuta, T., Tokutomi, Y., Kim‐Mitsuyama, S., Ihara, H., Kobayashi, A., Yamamoto, M. P., Fujii, S., et al. (2007) · Nature Chemical Biology · doi:10.1038/nchembio.2007.33 · Cited by 274

Discovery of Vinyl Sulfones as a Novel Class of Neuroprotective Agents toward Parkinson’s Disease Therapy

Woo, S. Y., Kim, J. H., Moon, M. K., Han, S. H., Yeon, S. K., Choi, J., Jang, B. K., Song, H. J., Kang, Y. G., Kim, J. W., et al. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm401788m · Cited by 270

Molecular Mechanisms of 4-Hydroxy-2-nonenal and Acrolein Toxicity: Nucleophilic Targets and Adduct Formation

LoPachin, R. M., Gavin, T., Petersen, D. R., & Barber, D. S. (2009) · Chemical Research in Toxicology · doi:10.1021/tx900147g · Cited by 266

Mitochondrial Quality Control as a Therapeutic Target

Suliman, H. B., & Piantadosi, C. A. (2015) · Pharmacological Reviews · doi:10.1124/pr.115.011502 · Cited by 267

Beyond repression of Nrf2: An update on Keap1

Kopacz, A., Klóska, D., Forman, H. J., Józkowicz, A., & Grochot‐Przeczek, A. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.03.023 · Cited by 269

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 265

Structure of the BTB Domain of Keap1 and Its Interaction with the Triterpenoid Antagonist CDDO

Cleasby, A., Yon, J. R., Day, P. J., Richardson, C. J., Tickle, I. J., Williams, P. A., Callahan, J. F., Carr, R. A. E., Concha, N. O., Kerns, J. K., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0098896 · Cited by 271

Mechanism of action of isothiocyanates: the induction of ARE-regulated genes is associated with activation of ERK and JNK and the phosphorylation and nuclear translocation of Nrf2

Xu, C., Yuan, X., Pan, Z., Shen, G., Kim, J. H., Yu, S., Khor, T. O., Li, W., Ma, J., & Kong, A. T. (2006) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-05-0497 · Cited by 265

Hypermethylation of the Keap1 gene in human lung cancer cell lines and lung cancer tissues

Wang, R., An, J., Ji, F., Jiao, H., Sun, H., & Zhou, D. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.06.004 · Cited by 265

Induction of detoxifying enzymes by garlic organosulfur compounds through transcription factor Nrf2: effect of chemical structure and stress signals

Chen, C., Pung, D., Leong, V., Hebbar, V., Shen, G., Nair, S., Li, W., & Kong, A.-N. T. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.07.021 · Cited by 260

Human prx1 Gene Is a Target of Nrf2 and Is Up-regulated by Hypoxia/Reoxygenation: Implication to Tumor Biology

Kim, Y.-J., Ahn, J., Liang, P., Ip, C. C. Y., Zhang, Y., & Park, Y.-M. (2007) · Cancer Research · doi:10.1158/0008-5472.can-06-2401 · Cited by 257

Review of Molecular Mechanisms Involved in the Activation of the Nrf2-ARE Signaling Pathway by Chemopreventive Agents

Giudice, A., Arra, C., & Turco, M. C. (2010) · Methods in molecular biology · doi:10.1007/978-1-60761-738-9_3 · Cited by 254

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

Dietary phytochemicals and cancer prevention: Nrf2 signaling, epigenetics, and cell death mechanisms in blocking cancer initiation and progression

Lee, J. H., Khor, T. O., Shu, L., Su, Z., Fuentes, F., & Kong, A. T. (2012) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2012.09.008 · Cited by 254

The Nrf2-ARE Pathway: A Valuable Therapeutic Target for the Treatment of Neurodegenerative Diseases

Gururaj Joshi, A., & Johnson, J. A. (2012) · Recent Patents on CNS Drug Discovery · doi:10.2174/157488912803252023 · Cited by 246

Nrf2: a dark horse in Alzheimer's disease treatment

Osama, A., Zhang, J., Yao, J., Yao, X., & Fang, J. (2020) · Ageing Research Reviews · doi:10.1016/j.arr.2020.101206 · Cited by 264

Increased proteasome subunit protein expression and proteasome activity in colon cancer relate to an enhanced activation of nuclear factor E2-related factor 2 (Nrf2)

Arlt, A., Bauer, I., Schafmayer, C., Tepel, J., Müerköster, S. S., Brosch, M., Röder, C., Kalthoff, H., Hampe, J., Moyer, M. P., et al. (2009) · Oncogene · doi:10.1038/onc.2009.264 · Cited by 249

Thiol Chemistry in Peroxidase Catalysis and Redox Signaling

Bindoli, A., Fukuto, J. M., & Forman, H. J. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2063 · Cited by 247

Biomechanical Forces in Atherosclerosis-Resistant Vascular Regions Regulate Endothelial Redox Balance via Phosphoinositol 3-Kinase/Akt-Dependent Activation of Nrf2

Dai, G., Vaughn, S., Zhang, Y., Wang, E. T., García‐Cardeña, G., & Gimbrone, M. A. (2007) · Circulation Research · doi:10.1161/circresaha.107.152942 · Cited by 244

Nrf2 affects the efficiency of mitochondrial fatty acid oxidation

Ludtmann, M. H. R., Angelova, P. R., Zhang, Y., Abramov, A. Y., & Dinkova‐Kostova, A. T. (2013) · Biochemical Journal · doi:10.1042/bj20130863 · Cited by 241

Protein Damage by Reactive Electrophiles: Targets and Consequences

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

Nitric oxide as a modulator of apoptosis

Li, C., & Wogan, G. N. (2004) · Cancer Letters · doi:10.1016/j.canlet.2004.10.021 · Cited by 239

Crystal Structure of Quinone Reductase 2 in Complex with Resveratrol ,

Buryanovskyy, L., Fu, Y., Boyd, M., Ma, Y., Hsieh, T., WU, J. M., & Zhang, Z. (2004) · Biochemistry · doi:10.1021/bi049162o · Cited by 242

Dietary antioxidants and cardiovascular disease

Blomhoff, R. (2005) · Current Opinion in Lipidology · doi:10.1097/00041433-200502000-00009 · Cited by 235

Activation of the Nrf2–ARE signaling pathway: a promising strategy in cancer prevention

Giudice, A., & Montella, M. (2006) · BioEssays · doi:10.1002/bies.20359 · Cited by 232

Keap1 is a forked-stem dimer structure with two large spheres enclosing the intervening, double glycine repeat, and C-terminal domains

Ogura, T., Tong, K. I., Mio, K., Maruyama, Y., Kurokawa, H., Sato, C., & Yamamoto, M. P. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0914036107 · Cited by 232

Applying Mechanisms of Chemical Toxicity to Predict Drug Safety

Guengerich, F. P., & MacDonald, J. S. (2007) · Chemical Research in Toxicology · doi:10.1021/tx600260a · Cited by 234

Structural assembly of cullin-RING ubiquitin ligase complexes

Zimmerman, E. S., Schulman, B. A., & Zheng, N. (2010) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2010.08.010 · Cited by 227

Mechanism of the Nrf2/Keap1/ARE signaling system

Tkachev, V., Брониславовна, М. Е., & Зенков, Н. К. (2011) · Biochemistry (Moscow) · doi:10.1134/s0006297911040031 · Cited by 229

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 225

Dietary Regulation of Keap1/Nrf2/ARE Pathway: Focus on Plant-Derived Compounds and Trace Minerals

Stefanson, A. L., & Bakovic, M. (2014) · Nutrients · doi:10.3390/nu6093777 · Cited by 232

Protein Oxidative Modifications: Beneficial Roles in Disease and Health.

Cai, Z., & Yan, L. (2013) · PubMed · Cited by 227

Nrf2 regulates an adaptive response protecting against oxidative damage following diquat-mediated formation of superoxide anion

Osburn, W. O., Wakabayashi, N., Misra, V., Nilles, T. L., Biswal, S. S., Trush, M. A., & Kensler, T. W. (2006) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2006.08.005 · Cited by 225

Regulation of Notch1 Signaling by Nrf2: Implications for Tissue Regeneration

Wakabayashi, N., Shin, S., Slocum, S. L., Agoston, E. S., Wakabayashi, J., Kwak, M.-K., Misra, V., Biswal, S. S., Yamamoto, M. P., & Kensler, T. W. (2010) · Science Signaling · doi:10.1126/scisignal.2000762 · Cited by 224

Nrf2-induced antiapoptotic Bcl-xL protein enhances cell survival and drug resistance

Niture, S. K., & Jaiswal, A. K. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.12.014 · Cited by 220

Keap1, the Sensor for Electrophiles and Oxidants that Regulates the Phase 2 Response, Is a Zinc Metalloprotein

Dinkova‐Kostova, A. T., Holtzclaw, W. D., & Wakabayashi, N. (2005) · Biochemistry · doi:10.1021/bi047434h · Cited by 220

Somatic mutations of the KEAP1 gene in common solid cancers

Yoo, N. J., Kim, H. R., Kim, Y. R., An, C. H., & Lee, S. H. (2012) · Histopathology · doi:10.1111/j.1365-2559.2012.04178.x · Cited by 216

Transcription Factor Nrf2 Is Essential for Induction of NAD(P)H:Quinone Oxidoreductase 1, Glutathione S-Transferases, and Glutamate Cysteine Ligase by Broccoli Seeds and Isothiocyanates

McWalter, G. K., Higgins, L. G., McLellan, L. I., Henderson, C. J., Hayes, J. D., Song, L., Thornalley, P. J., Itoh, K., & Yamamoto, M. P. (2004) · Journal of Nutrition · doi:10.1093/jn/134.12.3499s · Cited by 214

Induction of phase 2 genes by sulforaphane protects retinal pigment epithelial cells against photooxidative damage

Gao, X., & Talalay, P. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0403886101 · Cited by 215

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

Nioi, P., & Nguyen, T. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.08.051 · Cited by 212

Evolutionary conserved N-terminal domain of Nrf2 is essential for the Keap1-mediated degradation of the protein by proteasome

Katoh, Y., Iida, K., Kang, M.-I., Kobayashi, A., Mizukami, M., Tong, K. I., McMahon, M. J., Hayes, J. D., Itoh, K., & Yamamoto, M. P. (2004) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2004.10.012 · Cited by 217

Transcription factor Nrf2 hyperactivation in early-phase renal ischemia-reperfusion injury prevents tubular damage progression

Nezu, M., Souma, T., Yu, L., Suzuki, T., Saigusa, D., Ito, S., Suzuki, N., & Yamamoto, M. P. (2016) · Kidney International · doi:10.1016/j.kint.2016.08.023 · Cited by 211

Covalent Modification at Cys151 Dissociates the Electrophile Sensor Keap1 from the Ubiquitin Ligase CUL3

Rachakonda, G., Xiong, Y., Sekhar, K. R., Stamer, S. L., Liebler, D. C., & Freeman, M. L. (2008) · Chemical Research in Toxicology · doi:10.1021/tx700302s · Cited by 210

Persulfidation (S-sulfhydration) and H2S

Filipović, M. R. (2015) · Handbook of experimental pharmacology · doi:10.1007/978-3-319-18144-8_2 · Cited by 210

Detoxification and Transcriptome Response in Arabidopsis Seedlings Exposed to the Allelochemical Benzoxazolin-2(3H)-one

Baerson, S. R., Sánchez‐Moreiras, A. M., Pedrol, N., Schulz, M., Kagan, I. A., Agarwal, A. K., Reigosa, M. J., & Duke, S. O. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500694200 · Cited by 208

Activation of stress signaling pathways by electrophilic oxidized and nitrated lipids

Kansanen, E., Jyrkkänen, H.-K., & Levonen, A. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.11.038 · Cited by 210

Transcriptional regulation of thioredoxin reductase 1 expression by cadmium in vascular endothelial cells: Role of NF‐E2‐related factor‐2

Sakurai, A., Nishimoto, M., Himeno, S., Imura, N., Tsujimoto, M., Kunimoto, M., & Hara, S. (2004) · Journal of Cellular Physiology · doi:10.1002/jcp.20246 · Cited by 210

Xanthohumol Isolated from Humulus lupulus Inhibits Menadione-Induced DNA Damage through Induction of Quinone Reductase

Dietz, B. M., Kang, Y., Liu, G., Eggler, A. L., Yao, P., Chadwick, L. R., Pauli, G. F., Farnsworth, N. R., Mesecar, A. D., van Breemen, R. B., et al. (2005) · Chemical Research in Toxicology · doi:10.1021/tx050058x · Cited by 207

Electrophilic nitro-fatty acids activate NRF2 by a KEAP1 cysteine 151-independent mechanism

Kansanen, E., Bonacci, G., Schopfer, F. J., Kuosmanen, S. M., Tong, K. I., Leinonen, H., Woodcock, S. R., Yamamoto, M., Carlberg, C., Ylä-Herttuala, S., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.190710 · Cited by 208

An Auto-regulatory Loop between Stress Sensors INrf2 and Nrf2 Controls Their Cellular Abundance

Lee, O.-H., Jain, A. K., Papusha, V. Z., & Jaiswal, A. K. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m706517200 · Cited by 205

Skin Sensitizers Induce Antioxidant Response Element Dependent Genes: Application to the In Vitro Testing of the Sensitization Potential of Chemicals

Natsch, A., & Emter, R. (2007) · Toxicological Sciences · doi:10.1093/toxsci/kfm259 · Cited by 204

Advanced lipoxidation end-products

Pamplona, R. (2011) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2011.01.007 · Cited by 200

PGAM5, a Bcl-XL-interacting protein, is a novel substrate for the redox-regulated Keap1-dependent ubiquitin ligase complex

Lo, S.-C., & Hannink, M. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m606539200 · Cited by 199

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

Multiple Nuclear Localization Signals Function in the Nuclear Import of the Transcription Factor Nrf2

Theodore, M., Kawai, Y., Yang, J., Kleshchenko, Y. Y., Reddy, S. P., Villalta, F., & Arinze, I. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m709040200 · Cited by 202

Lipidomics of Human Brain Aging and Alzheimer's Disease Pathology

Naudí, A., Cabré, R., Jové, M., Ayala, V., Gonzalo‐Benito, H., Portero‐Otín, M., Ferrer, I., & Pamplona, R. (2015) · International review of neurobiology · doi:10.1016/bs.irn.2015.05.008 · Cited by 214

A genomic screen for activators of the antioxidant response element

Liu, Y., Kern, J. T., Walker, J. R., Johnson, J. A., Schultz, P. G., & Luesch, H. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0700898104 · Cited by 196

Nitric Oxide in Cell Survival: A Janus Molecule

Calabrese, V., Cornelius, C., Rizzarelli, E., Owen, J. B., Dinkova‐Kostova, A. T., & Butterfield, D. A. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2721 · Cited by 198

Signaling pathways activated by the phytochemical nordihydroguaiaretic acid contribute to a Keap1-independent regulation of Nrf2 stability: Role of glycogen synthase kinase-3

Rojo, A. I., Medina‐Campos, O. N., Rada, P., Zúñiga-Toalá, A., López-Gazcón, A., Espada, S., Pedraza‐Chaverrí, J., & Cuadrado, A. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.11.003 · Cited by 198

Nuclear Receptors and Drug Disposition Gene Regulation

Tirona, R. G., & Kim, R. B. (2005) · Journal of Pharmaceutical Sciences · doi:10.1002/jps.20324 · Cited by 194

Hydrogen sulfide (H2S) signaling in plant development and stress responses

Liu, H., Wang, J., Liu, J., Liu, T., & Xue, S. (2021) · aBIOTECH · doi:10.1007/s42994-021-00035-4 · Cited by 195

Sites of alkylation of human Keap1 by natural chemoprevention agents

Luo, Y., Eggler, A. L., Liu, D., Liu, G., Mesecar, A. D., & van Breemen, R. B. (2007) · Journal of the American Society for Mass Spectrometry · doi:10.1016/j.jasms.2007.09.015 · Cited by 191

Principles in Redox Signaling: From Chemistry to Functional Significance

Bindoli, A., & Rigobello, M. P. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4655 · Cited by 194

Methylation of the KEAP1 gene promoter region in human colorectal cancer

Hanada, N., Takahata, T., Zhou, Q., Ye, X., Sun, R., Itoh, J., Ishiguro, A., Kijima, H., Mimura, J., Itoh, K., et al. (2012) · BMC Cancer · doi:10.1186/1471-2407-12-66 · Cited by 189

Targeting the KEAP1-NRF2 system to prevent kidney disease progression

Nezu, M., Suzuki, N., & Yamamoto, M. (2017) · American Journal of Nephrology · doi:10.1159/000475890 · Cited by 3,447

Utility and limitations of a peptide reactivity assay to predict fragrance allergens in vitro

Natsch, A., Gfeller, H., Rothaupt, M., & Ellis, G. (2007) · Toxicology in Vitro · doi:10.1016/j.tiv.2007.03.016 · Cited by 189

Butein, a Tetrahydroxychalcone, Inhibits Nuclear Factor (NF)-κB and NF-κB-regulated Gene Expression through Direct Inhibition of IκBα Kinase β on Cysteine 179 Residue

Pandey, M. K., Sandur, S. K., Sung, B., Sethi, G., Kunnumakkara, A. B., & Aggarwal, B. B. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m700890200 · Cited by 193

NRF2: KEAPing Tumors Protected

Pillai, R., Hayashi, M., Zavitsanou, A.-M., & Papagiannakopoulos, T. Y. (2022) · Cancer Discovery · doi:10.1158/2159-8290.cd-21-0922 · Cited by 196

Regulation of NF-E2-Related Factor 2 Signaling for Cancer Chemoprevention: Antioxidant Coupled with Antiinflammatory

Hu, R., Saw, C. L. L., Yu, R., & Kong, A. T. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3276 · Cited by 190

Protection against electrophile and oxidative stress by induction of phase 2 genes: the quest for the elusive sensor that responds to inducers

Holtzclaw, W. D., Dinkova‐Kostova, A. T., & Talalay, P. (2004) · Advances in Enzyme Regulation · doi:10.1016/j.advenzreg.2003.11.013 · Cited by 145

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 476

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

Importance of phase 2 gene regulation in protection against electrophile and reactive oxygen toxicity and carcinogenesis

Talalay, P., Dinkova‐Kostova, A. T., & Holtzclaw, W. D. (2003) · Advances in Enzyme Regulation · doi:10.1016/s0065-2571(02)00038-9 · Cited by 289

NRF2 Cysteine Residues Are Critical for Oxidant/Electrophile-Sensing, Kelch-Like ECH-Associated Protein-1-Dependent Ubiquitination-Proteasomal Degradation, and Transcription Activation

He, X., & Ma, Q. (2009) · Molecular Pharmacology · doi:10.1124/mol.109.058453 · Cited by 153