Health position paper and redox perspectives – Bench to bedside transition for pharmacological regulation of NRF2 in noncommunicable diseases

Disruption of Nrf2, a Key Inducer of Antioxidant Defenses, Attenuates ApoE-Mediated Atherosclerosis in Mice

Sussan, T. E., Jun, J. C., Thimmulappa, R. K., Bedja, D., Antero, M. F., Gabrielson, K. L., Polotsky, V. Y., & Biswal, S. S. (2008) · PLoS ONE · doi:10.1371/journal.pone.0003791 · Cited by 182

Binding Mode and Structure–Activity Relationships around Direct Inhibitors of the Nrf2–Keap1 Complex

Jnoff, E., Albrecht, C., Barker, J. J., Barker, O., Beaumont, E., Bromidge, S. M., Brookfield, F. A., Brooks, M., Bubert, C., Ceska, T., et al. (2014) · ChemMedChem · doi:10.1002/cmdc.201300525 · Cited by 180

Increased Alzheimer's disease–like pathology in the APP/ PS1ΔE9 mouse model lacking Nrf2 through modulation of autophagy

Gururaj Joshi, A., Gan, K. A., Johnson, D. A., & Johnson, J. A. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.09.004 · Cited by 180

Pharmacological targeting of GSK-3 and NRF2 provides neuroprotection in a preclinical model of tauopathy

Cuadrado, A., Kügler, S., & Lastres‐Becker, I. (2017) · Redox Biology · doi:10.1016/j.redox.2017.10.010 · Cited by 180

Nuclear Erythroid 2-Related Factor 2-Antioxidative Response Element Signaling Pathway in Motor Cortex and Spinal Cord in Amyotrophic Lateral Sclerosis

Sarlette, A., Krampfl, K., Grothe, C., Neuhoff, N. V., Dengler, R., & Petri, S. (2008) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e31818b4906 · Cited by 179

Nrf2 protects against pulmonary fibrosis by regulating the lung oxidant level and Th1/Th2 balance

Kikuchi, N., Ishii, Y., Morishima, Y., Yageta, Y., Haraguchi, N., Itoh, K., Yamamoto, M. P., & Hizawa, N. (2010) · Respiratory Research · doi:10.1186/1465-9921-11-31 · Cited by 176

The Role of Oxidative Stress in the Pathogenesis of Asthma

Cho, Y. S., & Moon, H. (2010) · Allergy Asthma and Immunology Research · doi:10.4168/aair.2010.2.3.183 · Cited by 175

Safety, pharmacodynamics, and potential benefit of omaveloxolone in Friedreich ataxia

Lynch, D. R., Farmer, J. M., Hauser, L. A., Blair, I. A., Wang, Q. Q., Mesaros, C., Snyder, N. W., Boesch, S., Chin, M. P., Delatycki, M. B., et al. (2018) · Annals of Clinical and Translational Neurology · doi:10.1002/acn3.660 · Cited by 173

Nrf2 expression modifies influenza A entry and replication in nasal epithelial cells

Kesic, M. J., Simmons, S. O., Bauer, R. N., & Jaspers, I. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.04.027 · Cited by 171

NRF2 Activation Promotes Aggressive Lung Cancer and Associates with Poor Clinical Outcomes

Singh, A., Daemen, A., Nickles, D., Jeon, S., Foreman, O., Sudini, K. R., Gnad, F., Lajoie, S., Gour, N., Mitzner, W., et al. (2020) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-20-1985 · Cited by 170

NF-E2–Related Factor 2 Promotes Atherosclerosis by Effects on Plasma Lipoproteins and Cholesterol Transport That Overshadow Antioxidant Protection

Barajas, B., Che, N., Yin, F., Rowshanrad, A., Orozco, L. D., Gong, K., Wang, X., Castellani, L. W., Reue, K., Lusis, A. J., et al. (2010) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.110.210906 · Cited by 169

Adipose Deficiency of Nrf2 in ob/ob Mice Results in Severe Metabolic Syndrome

Xue, P., Hou, Y., Chen, Y., Yang, B., Fu, J., Zheng, H., Yarborough, K., Woods, C. G., Liu, D., Yamamoto, M. P., et al. (2012) · Diabetes · doi:10.2337/db12-0584 · Cited by 169

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 168

Clinical and Pathological Characteristics of KEAP1 - and NFE2L2 -Mutated Non–Small Cell Lung Carcinoma (NSCLC)

Frank, R., Scheffler, M., Merkelbach‐Bruse, S., Ihle, M. A., Kron, A., Rauer, M., Ueckeroth, F., König, K., Michels, S. Y. F., Fischer, R. N., et al. (2018) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-17-3416 · Cited by 167

Immunohistochemical detection of NAD(P)H:quinone oxidoreductase in human lung and lung tumors.

Siegel, D. M., Franklin, W. A., & Ross, D. (1998) · PubMed · Cited by 165

Halofuginone enhances the chemo-sensitivity of cancer cells by suppressing NRF2 accumulation

Tsuchida, K., Tsujita, T., Hayashi, M., Ojima, A., Keleku-Lukwete, N., Katsuoka, F., Otsuki, A., Kikuchi, H., Oshima, Y., Suzuki, M., et al. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.12.041 · Cited by 165

KEAP1/NFE2L2 Mutations Predict Lung Cancer Radiation Resistance That Can Be Targeted by Glutaminase Inhibition

Binkley, M. S., Jeon, Y.-J., Nesselbush, M. C., Moding, E. J., Nabet, B. Y., Almanza, D., Kunder, C. A., Stehr, H., Yoo, C. H., Rhee, S., et al. (2020) · Cancer Discovery · doi:10.1158/2159-8290.cd-20-0282 · Cited by 165

Induction of the Phase 2 Response in Mouse and Human Skin by Sulforaphane-containing Broccoli Sprout Extracts

Dinkova‐Kostova, A. T., Fahey, J. W., Wade, K. L., Jenkins, S. N., Shapiro, T. A., Fuchs, E. J., Kerns, M. L., & Talalay, P. (2007) · Cancer Epidemiology Biomarkers & Prevention · doi:10.1158/1055-9965.epi-06-0934 · Cited by 162

NRF2 activation induces NADH-reductive stress, providing a metabolic vulnerability in lung cancer

Weiss‐Sadan, T., Ge, M., Hayashi, M., Gohar, M., Yao, C.-H., de Groot, A., Harry, S. A., Carlin, A. D., Fischer, H., Shi, L., et al. (2023) · Cell Metabolism · doi:10.1016/j.cmet.2023.01.012 · Cited by 159

Nrf2-regulated phase II enzymes are induced by chronic ambient nanoparticle exposure in young mice with age-related impairments

Zhang, H., Liu, H., Davies, K. J. A., Sioutas, C., Finch, C. E., Morgan, T. E., & Forman, H. J. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.02.042 · Cited by 155

The Epithelial-to-Mesenchymal Transition as a Possible Therapeutic Target in Fibrotic Disorders

Gregorio, J. D., Robuffo, I., Spalletta, S., Giambuzzi, G., Iuliis, V. D., Toniato, E., Martinotti, S., Conti, P., & Flati, V. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.607483 · Cited by 155

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

Genetic dissection of systemic autoimmune disease in Nrf2-deficient mice

Li, J., Stein, T. D., & Johnson, J. A. (2004) · Physiological Genomics · doi:10.1152/physiolgenomics.00209.2003 · Cited by 154

Nrf2 antioxidant pathway suppresses Numb-mediated epithelial–mesenchymal transition during pulmonary fibrosis

Zhang, Z., Qu, J., Zheng, C., Zhang, P., Zhou, W., Cui, W., Mo, X., Li, L., Xu, L., & Gao, J. (2018) · Cell Death and Disease · doi:10.1038/s41419-017-0198-x · Cited by 154

Harnessing the E3 Ligase KEAP1 for Targeted Protein Degradation

Wei, J., Meng, F., Park, K.-S., Yim, H., Velez, J., Kumar, P., Wang, L., Xie, L., Chen, H., Shen, Y., et al. (2021) · Journal of the American Chemical Society · doi:10.1021/jacs.1c04841 · Cited by 154

Mechanisms Contributing to Adverse Cardiovascular Events in Patients with Type 2 Diabetes Mellitus and Stage 4 Chronic Kidney Disease Treated with Bardoxolone Methyl

Chin, M. P., Reisman, S. A., Bakris, G. L., O’Grady, M. L., Linde, P. G., McCullough, P. A., Packham, D., Vaziri, N. D., Ward, K. W., Warnock, D. G., et al. (2014) · American Journal of Nephrology · doi:10.1159/000362906 · Cited by 153

Bardoxolone conjugation enables targeted protein degradation of BRD4

Tong, B., Luo, M., Xie, Y., Spradlin, J. N., Tallarico, J. A., McKenna, J. M., Schirle, M., Maimone, T. J., & Nomura, D. K. (2020) · Scientific Reports · doi:10.1038/s41598-020-72491-9 · Cited by 152

CPUY192018, a potent inhibitor of the Keap1-Nrf2 protein-protein interaction, alleviates renal inflammation in mice by restricting oxidative stress and NF-κB activation

Lu, M., Zhao, J., Liu, Y.-T., Liu, T., Tao, M., You, Q., & Jiang, Z. (2019) · Redox Biology · doi:10.1016/j.redox.2019.101266 · Cited by 151

KEAP1 inhibition is neuroprotective and suppresses the development of epilepsy

Shekh‐Ahmad, T., Eckel, R., Naidu, S. D., Higgins, M., Yamamoto, M. P., Dinkova‐Kostova, A. T., Kovac, S., Abramov, A. Y., & Walker, M. C. (2018) · Brain · doi:10.1093/brain/awy071 · Cited by 150

Activation of Oxidative Stress Response in Cancer Generates a Druggable Dependency on Exogenous Non-essential Amino Acids

LeBoeuf, S. E., Wu, W. L., Karakousi, T. R., Karadal, B., Jackson, S. R., Davidson, S. M., Wong, K.-K., Koralov, S. B., Sayin, V. I., & Papagiannakopoulos, T. (2020) · Cell Metabolism · doi:10.1016/j.cmet.2019.11.012 · Cited by 150

Ursodeoxycholic acid stimulates Nrf2-mediated hepatocellular transport, detoxification, and antioxidative stress systems in mice

Okada, K., Shoda, J., Taguchi, K., Maher, J. M., Ishizaki, K., Inoue, Y., Ohtsuki, M., Goto, N., Takeda, K., Utsunomiya, H., et al. (2008) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.90321.2008 · Cited by 149

Activation of peroxisome proliferator-activated receptor gamma by a novel synthetic triterpenoid 2-cyano-3,12-dioxooleana-1,9-dien-28-oic acid induces growth arrest and apoptosis in breast cancer cells.

Lapillonne, H., Konopleva, M. Y., Tsao, T., Gold, D. L., McQueen, T. J., Sutherland, R. L., Madden, T. L., & Andreeff, M. (2003) · PubMed · Cited by 144

Triptolide suppresses IDH1-mutated malignancy via Nrf2-driven glutathione metabolism

Yu, D., Liu, Y., Zhou, Y., Ruiz‐Rodado, V., Larion, M., Xu, G., & Yang, C. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1913633117 · Cited by 142

Subcellular localization and cytoplasmic complex status of endogenous Keap1

Watai, Y., Kobayashi, A., Nagase, H., Mizukami, M., McEvoy, J. D., Singer, J. D., Itoh, K., & Yamamoto, M. P. (2007) · Genes to Cells · doi:10.1111/j.1365-2443.2007.01118.x · Cited by 141

A quantitative and multiplexed approach to uncover the fitness landscape of tumor suppression in vivo

Rogers, Z. N., McFarland, C. D., Winters, I. P., Naranjo, S., Chuang, C.-H., Petrov, D. A., & Winslow, M. M. (2017) · Nature Methods · doi:10.1038/nmeth.4297 · Cited by 141

Chemistry-First Approach for Nomination of Personalized Treatment in Lung Cancer

McMillan, E. A., Ryu, M.-J., Diep, C. H., Mendiratta, S., Clemenceau, J. R., Vaden, R. M., Kim, J.-H., Motoyaji, T., Covington, K. R., Peyton, M., et al. (2018) · Cell · doi:10.1016/j.cell.2018.03.028 · Cited by 141

Genetic reduction of Nrf2 exacerbates cognitive deficits in a mouse model of Alzheimer’s disease

Branca, C., Ferreira, E., Nguyen, T.-V., Doyle, K., Caccamo, A., & Oddo, S. (2017) · Human Molecular Genetics · doi:10.1093/hmg/ddx361 · Cited by 139

Brusatol overcomes chemoresistance through inhibition of protein translation

Harder, B. G., Tian, W., Clair, J. J. L., Tan, A. C., Ooi, A., Chapman, E., & Zhang, D. D. (2016) · Molecular Carcinogenesis · doi:10.1002/mc.22609 · Cited by 138

The effects of NRF2 modulation on the initiation and progression of chemically and genetically induced lung cancer

Tao, S., de la Vega, M. R., Chapman, E., Ooi, A., & Zhang, D. D. (2017) · Molecular Carcinogenesis · doi:10.1002/mc.22745 · Cited by 136

KEAP1, a cysteine-based sensor and a drug target for the prevention and treatment of chronic disease

Naidu, S. D., & Dinkova‐Kostova, A. T. (2020) · Open Biology · doi:10.1098/rsob.200105 · Cited by 135

Nrf2 Activators Attenuate the Progression of Nonalcoholic Steatohepatitis–Related Fibrosis in a Dietary Rat Model

Shimozono, R., Asaoka, Y., Yoshizawa, Y., Aoki, T., Noda, H., Yamada, M., Kaino, M., & Mochizuki, H. (2013) · Molecular Pharmacology · doi:10.1124/mol.112.084269 · Cited by 134

Functional interference between glycogen synthase kinase-3 beta and the transcription factor Nrf2 in protection against kainate-induced hippocampal celldeath

Rojo, A. I., Rada, P., Egea, J., Rosa, A. O., López, M. G., & Cuadrado, A. (2008) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2008.06.007 · Cited by 133

Efficacy of Omaveloxolone in Friedreich's Ataxia: Delayed‐Start Analysis of the MOXIe Extension

Lynch, D. R., Chin, M. P., Boesch, S., Delatycki, M. B., Giunti, P., Goldsberry, A., Hoyle, J. C., Mariotti, C., Mathews, K. D., Nachbauer, W., et al. (2022) · Movement Disorders · doi:10.1002/mds.29286 · Cited by 131

Induction of cancer chemopreventive enzymes by coffee is mediated by transcription factor Nrf2. Evidence that the coffee-specific diterpenes cafestol and kahweol confer protection against acrolein

Higgins, L. G., Cavin, C., Itoh, K., Yamamoto, M. P., & Hayes, J. D. (2007) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2007.09.018 · Cited by 129

Cysteine dioxygenase 1 is a metabolic liability for non-small cell lung cancer

Kang, Y. P., Torrente, L., Falzone, A., Elkins, C. M., Liu, M., Asara, J. M., Dibble, C. C., & DeNicola, G. M. (2019) · eLife · doi:10.7554/elife.45572 · Cited by 129

Association of Nrf2-encoding NFE2L2 haplotypes with Parkinson's disease

von Otter, M., Landgren, S., Nilsson, S., Celojevic, D., Bergström, P., Håkansson, A. S., Nissbrandt, H., Droździk, M., Białecka, M. A., Kurzawski, M., et al. (2010) · BMC Medical Genetics · doi:10.1186/1471-2350-11-36 · Cited by 128

An effective strategy for increasing the radiosensitivity of Human lung Cancer cells by blocking Nrf2-dependent antioxidant responses

Lee, S., Lim, M., Kim, M., Yu, C., Yun, Y., Ahn, J., & Song, J. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.05.038 · Cited by 127

Ursodeoxycholic acid ameliorates apoptotic cascade in the rotenone model of Parkinson's disease: Modulation of mitochondrial perturbations

Abdelkader, N. F., Safar, M. M., & Salem, H. A. (2016) · Molecular Neurobiology · doi:10.1007/s12035-014-9043-8 · Cited by 127

Regulation of the human thioredoxin gene promoter and its key substrates: A study of functional and putative regulatory elements

Hawkes, H.-J. K., Karlenius, T., & Tonissen, K. F. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.09.013 · Cited by 126

Nrf2 Induces IL-17D to Mediate Tumor and Virus Surveillance

Saddawi-Konefka, R., Seelige, R., Gross, E. T. E., Levy, E., Searles, S. C., Washington, A., Santosa, E. K., Liu, B., O’Sullivan, T. E., Harismendy, O., et al. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.07.075 · Cited by 126

Role of KEAP1/NFE2L2 Mutations in the Chemotherapeutic Response of Patients with Non–Small Cell Lung Cancer

Jeong, Y., Hellyer, J. A., Stehr, H., Hoang, N. T., Niu, X., Das, M. S., Padda, S. K., Ramchandran, K. J., Neal, J. W., Wakelee, H. A., et al. (2019) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-19-1237 · Cited by 125

Metformin inhibits heme oxygenase-1 expression in cancer cells through inactivation of Raf-ERK-Nrf2 signaling and AMPK-independent pathways

Truong, M., Kim, H. G., Khanal, T., Choi, J. H., Kim, D. H., Jeong, T. C., & Jeong, H. G. (2013) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2013.05.010 · Cited by 124

Nrf2 Activation Protects against Solar-Simulated Ultraviolet Radiation in Mice and Humans

Knatko, E. V., Ibbotson, S. H., Zhang, Y., Higgins, M., Fahey, J. W., Talalay, P., Dawe, R. S., Ferguson, J., Huang, J. T.-J., Clarke, R. G., et al. (2015) · Cancer Prevention Research · doi:10.1158/1940-6207.capr-14-0362 · Cited by 124

Ursocholanic acid rescues mitochondrial function in common forms of familial Parkinson’s disease

Mortiboys, H., Aasly, J. O., & Bandmann, O. (2013) · Brain · doi:10.1093/brain/awt224 · Cited by 124

Chronic activation of JNK JAK/STAT and oxidative stress signalling causes the loser cell status

Kuciński, I., Dinan, M., Kolahgar, G., & Piddini, E. (2017) · Nature Communications · doi:10.1038/s41467-017-00145-y · Cited by 121

Deficiency in the transcription factor NRF2 worsens inflammatory parameters in a mouse model with combined tauopathy and amyloidopathy

Rojo, A. I., Pajares, M., García‐Yagüe, Á. J., Buendía, I., LEUVEN, F. V., Yamamoto, M. P., López, M. G., & Cuadrado, A. (2018) · Redox Biology · doi:10.1016/j.redox.2018.07.006 · Cited by 121

Quinone reductase (NQO1), a sensitive redox indicator, is increased in Alzheimer’s disease

Raina, A. K., Templeton, D. J., deak, J. C., Perry, G., & Smith, M. A. (1999) · Redox Report · doi:10.1179/135100099101534701 · Cited by 120

Glycogen synthase kinase-3 and its inhibitors: Potential target for various therapeutic conditions

Saraswati, A. P., Hussaini, S. M. A., Krishna, N. H., Babu, B. N., & Kamal, Ä. (2017) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2017.11.103 · Cited by 120

Regulation of the Expression of Heme Oxygenase-1: Signal Transduction, Gene Promoter Activation, and Beyond

Medina, M. V., Sapochnik, D., Solá, M. E. G., & Coso, O. A. (2019) · Antioxidants and Redox Signaling · doi:10.1089/ars.2019.7991 · Cited by 119

Nrf2 Regulates Angiogenesis: Effect on Endothelial Cells, Bone Marrow-Derived Proangiogenic Cells and Hind Limb Ischemia

Florczyk, U., Jaźwa, A., Maleszewska, M., Mendel, M., Szade, K., Kozakowska, M., Grochot‐Przeczek, A., Viscardi, M., Czauderna, S., Bukowska-Straková, K., et al. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5219 · Cited by 117

Nrf2 Activator PB125® as a Potential Therapeutic Agent against COVID-19

McCord, J. M., Hybertson, B. M., Cota‐Gomez, A., Geraci, K. P., & Gao, B. (2020) · Antioxidants · doi:10.3390/antiox9060518 · Cited by 117

A clinical drug library screen identifies clobetasol propionate as an NRF2 inhibitor with potential therapeutic efficacy in KEAP1 mutant lung cancer

Choi, E.-J., Jung, B.-J., Lee, S.-H., Yoo, H.-S., Shin, E.-A., Ko, H., Chang, S., Kim, S.-Y., & Jeon, S.-M. (2017) · Oncogene · doi:10.1038/onc.2017.153 · Cited by 115

STK11/LKB1 and KEAP1 mutations in non-small cell lung cancer: Prognostic rather than predictive?

Federico, A. D., Giglio, A. D., Parisi, C., & Gelsomino, F. (2021) · European Journal of Cancer · doi:10.1016/j.ejca.2021.08.011 · Cited by 115

Cellular Responses to the Metal-Binding Properties of Metformin

Logie, L., Harthill, J. E., Patel, K., Bacon, S., Hamilton, D. L., Macrae, K., McDougall, G. J., Wang, H., Xue, L., Jiang, H., et al. (2012) · Diabetes · doi:10.2337/db11-0961 · Cited by 113

EMSY inhibits homologous recombination repair and the interferon response, promoting lung cancer immune evasion

Marzio, A., Kurz, E., Sahni, J. M., Feo, G. D., Puccini, J., Jiang, S., Hirsch, C. A., Arbini, A., Wu, W., Pass, H. I., et al. (2021) · Cell · doi:10.1016/j.cell.2021.12.005 · Cited by 113

Triterpenoid CDDO‐methylamide improves memory and decreases amyloid plaques in a transgenic mouse model of Alzheimer’s disease

Dumont, M., Wille, E. J., Calingasan, N. Y., Tampellini, D., Williams, C. R., Gouras, G. K., Liby, K. T., Sporn, M. B., Beal, M. F., & Lin, M. T. S. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.05970.x · Cited by 112

An inhibitor of the Keap1-Nrf2 protein-protein interaction protects NCM460 colonic cells and alleviates experimental colitis

Lu, M., Ji, J., Jiang, Y.-L., Chen, Z., Yuan, Z., You, Q., & Jiang, Z. (2016) · Scientific Reports · doi:10.1038/srep26585 · Cited by 112

Non-covalent Small-Molecule Kelch-like ECH-Associated Protein 1–Nuclear Factor Erythroid 2-Related Factor 2 (Keap1–Nrf2) Inhibitors and Their Potential for Targeting Central Nervous System Diseases

Pallesen, J. S., Tran, K. T., & Bach, A. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b00358 · Cited by 112

Gut commensals and their metabolites in health and disease

Krishnamurthy, H. K., Pereira, M., Bosco, J., George, J., Jayaraman, V., Krishna, K., Wang, T., Bei, K., & Rajasekaran, J. J. (2023) · Frontiers in Microbiology · doi:10.3389/fmicb.2023.1244293 · Cited by 112

Probing the structural requirements of non-electrophilic naphthalene-based Nrf2 activators

Jain, A. D., Potteti, H. R., Richardson, B. G., Kingsley, L. J., Luciano, J. P., Ryuzoji, A. F., Lee, H., Krunić, A., Mesecar, A. D., Reddy, S. P., et al. (2015) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2015.08.049 · Cited by 111

Occupational and environmental risk factors of idiopathic pulmonary fibrosis: a systematic review and meta-analyses

Park, Y., Ahn, C., & Kim, T. (2021) · Scientific Reports · doi:10.1038/s41598-021-81591-z · Cited by 111

The absence of macrophage Nrf2 promotes early atherogenesis

Ruotsalainen, A.-K., Inkala, M., Partanen, M. E., Lappalainen, J. P., Kansanen, E., Mäkinen, P. I., Heinonen, S. E., Laitinen, H. M., Heikkilä, J., Vatanen, T., et al. (2013) · Cardiovascular Research · doi:10.1093/cvr/cvt008 · Cited by 109

Succination of Keap1 and Activation of Nrf2-Dependent Antioxidant Pathways in FH-Deficient Papillary Renal Cell Carcinoma Type 2

Kinch, L. N., Grishin, N. V., & Brugarolas, J. (2011) · Cancer Cell · doi:10.1016/j.ccr.2011.10.005 · Cited by 109

Evidence of activation of the Nrf2 pathway in multiple sclerosis patients treated with delayed-release dimethyl fumarate in the Phase 3 DEFINE and CONFIRM studies

Gopal, S., Mikulskis, A., Gold, R., Fox, R. J., Dawson, K. T., & Amaravadi, L. S. (2017) · Multiple Sclerosis Journal · doi:10.1177/1352458517690617 · Cited by 109

Distinct initiating events underpin the immune and metabolic heterogeneity of KRAS-mutant lung adenocarcinoma

Best, S. A., Ding, S., Kersbergen, A., Dong, X., Song, J.-Y., Xie, Y., Reljic, B., Li, K., Vince, J. E., Rathi, V., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-12164-y · Cited by 108

Induction of Glutathione Synthesis in Macrophages by Oxidized Low-Density Lipoproteins Is Mediated by Consensus Antioxidant Response Elements

Bea, F., Hudson, F. N., Chait, A., Kavanagh, T. J., & Rosenfeld, M. E. (2003) · Circulation Research · doi:10.1161/01.res.0000059561.65545.16 · Cited by 106

A potent small-molecule inhibitor of the DCN1-UBC12 interaction that selectively blocks cullin 3 neddylation

Zhou, H., Lü, J., Liu, L., Bernard, D., Yang, C., Fernández‐Salas, E., Chinnaswamy, K., Layton, S. D., Stuckey, J. A., Yu, Q., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-01243-7 · Cited by 105

Structure–Activity and Structure–Conformation Relationships of Aryl Propionic Acid Inhibitors of the Kelch-like ECH-Associated Protein 1/Nuclear Factor Erythroid 2-Related Factor 2 (KEAP1/NRF2) Protein–Protein Interaction

Heightman, T. D., Callahan, J. F., Chiarparin, E., Coyle, J. E., Griffiths-Jones, C., Lakdawala, A. S., McMenamin, R. L., Mortenson, P. N., Norton, D., Peakman, T. M., et al. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b00279 · Cited by 104

GSK3β-mediated Keap1-independent regulation of Nrf2 antioxidant response: A molecular rheostat of acute kidney injury to chronic kidney disease transition

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Induction of glutathione transferases and NAD(P)H:quinone reductase by fumaric acid derivatives in rodent cells and tissues.

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Activation of the Nrf2/antioxidant response pathway increases IL-8 expression

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The NRF 2 pathway as potential biomarker for dimethyl fumarate treatment in multiple sclerosis

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The KEAP1-NRF2 System in Healthy Aging and Longevity

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Sulforaphane attenuates pulmonary fibrosis by inhibiting the epithelial-mesenchymal transition

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Nrf2 inhibits epithelial-mesenchymal transition by suppressing snail expression during pulmonary fibrosis

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CAND1-Mediated Substrate Adaptor Recycling Is Required for Efficient Repression of Nrf2 by Keap1

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Protection against oxidative stress mediated by the Nrf2/Keap1 axis is impaired in Primary Biliary Cholangitis

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A PGAM5–KEAP1–Nrf2 complex is required for stress-induced mitochondrial retrograde trafficking

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C151 in KEAP1 is the main cysteine sensor for the cyanoenone class of NRF2 activators, irrespective of molecular size or shape

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Nrf2 deficiency impairs the barrier function of mouse oesophageal epithelium

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Toll-Like Receptor Signaling Induces Nrf2 Pathway Activation through p62-Triggered Keap1 Degradation

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A Small Molecule Inhibits Deregulated NRF2 Transcriptional Activity in Cancer

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Ezetimibe, an NPC1L1 inhibitor, is a potent Nrf2 activator that protects mice from diet-induced nonalcoholic steatohepatitis

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Activation of the NRF2 antioxidant program sensitizes tumors to G6PD inhibition

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NRF2 Activation Reprograms Defects in Oxidative Metabolism to Restore Macrophage Function in Chronic Obstructive Pulmonary Disease

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Protective effects of rutin on liver injury induced by biliary obstruction in rats

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Therapeutic advantage of pro-electrophilic drugs to activate the Nrf2/ARE pathway in Alzheimer’s disease models

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Nrf2 deficiency deteriorates diabetic kidney disease in Akita model mice

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Nrf2-encoding NFE2L2 haplotypes influence disease progression but not risk in Alzheimer's disease and age-related cataract

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Aging-InducedNrf2-AREPathway Disruption in the Subventricular Zone Drives Neurogenic Impairment in Parkinsonian Mice viaPI3K-Wnt/β-CateninDysregulation

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Nrf2 deficiency prevents reductive stress-induced hypertrophic cardiomyopathy

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Sulforaphane improves the bronchoprotective response in asthmatics through Nrf2-mediated gene pathways

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Guideline-based management of acute respiratory failure and acute respiratory distress syndrome

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Nrf2 reduces allergic asthma in mice through enhanced airway epithelial cytoprotective function

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Structure–Activity and Structure–Property Relationship and Exploratory in Vivo Evaluation of the Nanomolar Keap1–Nrf2 Protein–Protein Interaction Inhibitor

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Role of Nrf2 in Host Defense against Influenza Virus in Cigarette Smoke-Exposed Mice

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Nitro-fatty acids: New drug candidates for chronic inflammatory and fibrotic diseases

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The Dark Side of Nrf2 in the Heart

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Enhancer remodeling promotes tumor-initiating activity in NRF2-activated non-small cell lung cancers

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Myeloid Deletion of Nuclear Factor Erythroid 2−Related Factor 2 Increases Atherosclerosis and Liver Injury

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Nrf2 and SQSTM1/p62 jointly contribute to mesenchymal transition and invasion in glioblastoma

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Nrf2-Mediated Cardiac Maladaptive Remodeling and Dysfunction in a Setting of Autophagy Insufficiency

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An Update on the Role of Nrf2 in Respiratory Disease: Molecular Mechanisms and Therapeutic Approaches

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Role of Nrf2 in the pathogenesis of respiratory diseases

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Pirfenidone for idiopathic pulmonary fibrosis and beyond

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NAD(P)H:quinone oxidoreductase activity is increased in hippocampal pyramidal neurons of patients with alzheimer’s disease

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Therapeutic targeting of GSK3β enhances the Nrf2 antioxidant response and confers hepatic cytoprotection in hepatitis C

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Mutations in the KEAP1-NFE2L2 Pathway Define a Molecular Subset of Rapidly Progressing Lung Adenocarcinoma

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Health Benefits of Coffee Consumption for Cancer and Other Diseases and Mechanisms of Action

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The relationship between Helicobacter pylori infection and promoter polymorphism of the Nrf2 gene in chronic gastritis

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Activation of the Nrf2–ARE pathway in muscle and spinal cord during ALS-like pathology in mice expressing mutant SOD1

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Cardiovascular disease in the elderly: proceedings of the European Society of Cardiology—Cardiovascular Round Table

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Keap1 is localized in neuronal and glial cytoplasmic inclusions in various neurodegenerative diseases

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Identification of the Highly Reactive Cysteine 151 in the Chemopreventive Agent-Sensor Keap1 Protein is Method-Dependent

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Activation of NAD(P)H:Quinone Oxidoreductase 1 Prevents Arterial Restenosis by Suppressing Vascular Smooth Muscle Cell Proliferation

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Generation of a New Model Rat: Nrf2 Knockout Rats Are Sensitive to Aflatoxin B 1 Toxicity

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KEAP1 deficiency drives glucose dependency and sensitizes lung cancer cells and tumors to GLUT inhibition

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Genetic associations of Nrf2-encoding NFE2L2 variants with Parkinson’s disease – a multicenter study

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Current strategies and progress for targeting the “undruggable” transcription factors

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Oltipraz: A laboratory and clinical review

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A Double‐Blind, Randomized, Placebo‐Controlled Trial of Ursodeoxycholic Acid (UDCA) in Parkinson's Disease

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Role of ROS in ischemia-induced lung angiogenesis

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NRF2 Activation Impairs Quiescence and Bone Marrow Reconstitution Capacity of Hematopoietic Stem Cells

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Coffees rich in chlorogenic acid or N‐methylpyridinium induce chemopreventive phase II‐enzymes via the Nrf2/ARE pathway in vitro and in vivo

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Oxidative stress and Nrf2 expression in peripheral blood mononuclear cells derived from COPD patients: an observational longitudinal study

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Role of Nadph Oxidase in Atherosclerosis

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Transcription Factor Nrf2 as a Potential Therapeutic Target for Prevention of Cytokine Storm in COVID-19 Patients

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Direct inhibition of Keap1-Nrf2 Protein-Protein interaction as a potential therapeutic strategy for Alzheimer's disease

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A Polymorphism in the Promoter Region of the Selenoprotein S Gene (SEPS1) Contributes to Hashimoto's Thyroiditis Susceptibility

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Opposing effects of Nrf2 and Nrf2-activating compounds on the NLRP3 inflammasome independent of Nrf2-mediated gene expression

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Bioactivity, bioavailability, and gut microbiota transformations of dietary phenolic compounds: implications for COVID-19

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Nrf2 gene promoter polymorphism is associated with ulcerative colitis in a Japanese population.

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Fortunellin protects against high fructose-induced diabetic heart injury in mice by suppressing inflammation and oxidative stress via AMPK/Nrf-2 pathway regulation

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Tricyclic Compounds Containing Nonenolizable Cyano Enones. A Novel Class of Highly Potent Anti-Inflammatory and Cytoprotective Agents

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Nonalcoholic steatohepatitis and mechanisms by which it is ameliorated by activation of the CNC-bZIP transcription factor Nrf2

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BACH1 Is a Specific Repressor of HMOX1 That Is Inactivated by Arsenite

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In-silico drug repurposing study predicts the combination of pirfenidone and melatonin as a promising candidate therapy to reduce SARS-CoV-2 infection progression and respiratory distress caused by cytokine storm

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Overlooked and valuable facts to know in the NRF2/KEAP1 field

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S[+] Apomorphine is a CNS penetrating activator of the Nrf2-ARE pathway with activity in mouse and patient fibroblast models of amyotrophic lateral sclerosis

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Redox biology and the interface between bioenergetics, autophagy and circadian control of metabolism

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Deconstructing Noncovalent Kelch-like ECH-Associated Protein 1 (Keap1) Inhibitors into Fragments to Reconstruct New Potent Compounds

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Biomarker Exploration in Human Peripheral Blood Mononuclear Cells for Monitoring Sulforaphane Treatment Responses in Autism Spectrum Disorder

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Synthesis, Chemical Reactivity as Michael Acceptors, and Biological Potency of Monocyclic Cyanoenones, Novel and Highly Potent Anti-inflammatory and Cytoprotective Agents

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Erioflorin Stabilizes the Tumor Suppressor Pdcd4 by Inhibiting Its Interaction with the E3-ligase β-TrCP1

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Dihydroquercetin (DHQ) ameliorated concanavalin A-induced mouse experimental fulminant hepatitis and enhanced HO-1 expression through MAPK/Nrf2 antioxidant pathway in RAW cells

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Ursodeoxycholic acid suppresses mitochondria-dependent programmed cell death induced by sodium nitroprusside in SH-SY5Y cells

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Nuclear factor-E2-related factor 2 is a major determinant of bile acid homeostasis in the liver and intestine

Weerachayaphorn, J., Mennone, A., Soroka, C. J., Harry, K., Hagey, L. R., Kensler, T. W., & Boyer, J. L. (2012) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00263.2011 · Cited by 62

The Nrf2 inhibitor brusatol is a potent antitumour agent in an orthotopic mouse model of colorectal cancer

Evans, J. P., Winiarski, B. K., Sutton, P. A., Jones, R. P., Ressel, L., Duckworth, C. A., Pritchard, D. M., Lin, Z., Fretwell, V. L., Tweedle, E. M., et al. (2018) · Oncotarget · doi:10.18632/oncotarget.25497 · Cited by 62

Novel semisynthetic analogues of betulinic acid with diverse cytoprotective, antiproliferative, and proapoptotic activities

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Nrf2 enhances myocardial clearance of toxic ubiquitinated proteins

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Enhanced Hepatic Nrf2 Activation After Ursodeoxycholic Acid Treatment in Patients with Primary Biliary Cirrhosis

Kawata, K., Kobayashi, Y., Souda, K., Kawamura, K., Sumiyoshi, S., Takahashi, Y., Noritake, H., Watanabe, S., Suehiro, T., & Nakamura, H. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2903 · Cited by 60

Microenvironmental Activation of Nrf2 Restricts the Progression of Nrf2-Activated Malignant Tumors

Hayashi, M., Kuga, A., Suzuki, M., Panda, H., Kitamura, H., Motohashi, H., & Yamamoto, M. P. (2020) · Cancer Research · doi:10.1158/0008-5472.can-19-2888 · Cited by 60

Diffusion dynamics of the Keap1–Cullin3 interaction in single live cells

Baird, L., & Dinkova‐Kostova, A. T. (2013) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2013.02.065 · Cited by 59

Phosphorylation of serine 349 of p62 in Alzheimer’s disease brain

Tanji, K., Miki, Y., Ozaki, T., Maruyama, A., Yoshida, H., Mimura, J., Matsumiya, T., Mori, F., Imaizumi, T., Itoh, K., et al. (2014) · Acta Neuropathologica Communications · doi:10.1186/2051-5960-2-50 · Cited by 59

GSK-3β-dependent Nrf2 antioxidant response modulates ferroptosis of lens epithelial cells in age-related cataract

Ma, D.-Y., Liu, J., Wang, L., Zhi, X.-Y., Luo, L., Zhao, J., & Yu, Q. (2023) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2023.04.022 · Cited by 59

Association between the NF-E2 Related Factor 2 Gene Polymorphism and Oxidative Stress, Anti-Oxidative Status, and Newly-Diagnosed Type 2 Diabetes Mellitus in a Chinese Population

Wang, X., Chen, H., Liu, J., Ouyang, Y., Wang, D., Bao, W., & Liu, L. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms160716483 · Cited by 58

Ferroptosis in the colon epithelial cells as a therapeutic target for ulcerative colitis

Yokote, A., Imazu, N., Umeno, J., Kawasaki, K., Fujioka, S., Fuyuno, Y., Matsuno, Y., Moriyama, T., Miyawaki, K., Akashi, K., et al. (2023) · Journal of Gastroenterology · doi:10.1007/s00535-023-02016-4 · Cited by 58

Replacement of a Naphthalene Scaffold in Kelch-like ECH-Associated Protein 1 (KEAP1)/Nuclear Factor (Erythroid-derived 2)-like 2 (NRF2) Inhibitors

Richardson, B. G., Jain, A. D., Potteti, H. R., Lazzara, P. R., David, B. P., Tamatam, C. R., Choma, E., Skowron, K. J., Dye, K., Siddiqui, Z., et al. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b01133 · Cited by 57

Keap1-Knockdown Decreases Fasting-Induced Fatty Liver via Altered Lipid Metabolism and Decreased Fatty Acid Mobilization from Adipose Tissue

Xu, J., Donepudi, A. C., Moscovitz, J. E., & Slitt, A. L. (2013) · PLoS ONE · doi:10.1371/journal.pone.0079841 · Cited by 56

Sulforaphane prevents bleomycin-induced pulmonary fibrosis in mice by inhibiting oxidative stress via nuclear factor erythroid 2-related factor-2 activation

Yan, B., Ma, Z., Shi, S., Hu, Y., Ma, T., Gao, R., & Yang, J. (2017) · Molecular Medicine Reports · doi:10.3892/mmr.2017.6546 · Cited by 56

Enzastaurin: A lesson in drug development

Bourhill, T., Narendran, A., & Johnston, R. N. (2017) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2017.02.003 · Cited by 55

Involvement of the Nrf2/HO‐1/CO axis and therapeutic intervention with the CO‐releasing molecule CORM‐A1, in a murine model of autoimmune hepatitis

Mangano, K., Cavalli, E., Mammana, S., Basile, M. S., Caltabiano, R., Pesce, A., Puleo, S., Atanasov, A. G., Magro, G. G., Nicoletti, F., et al. (2017) · Journal of Cellular Physiology · doi:10.1002/jcp.26223 · Cited by 55

Isoquinoline Kelch-like ECH-Associated Protein 1-Nuclear Factor (Erythroid-Derived 2)-like 2 (KEAP1-NRF2) Inhibitors with High Metabolic Stability

Lazzara, P. R., David, B. P., Ankireddy, A., Richardson, B. G., Dye, K., Ratia, K. M., Reddy, S. P., & Moore, T. W. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b01074 · Cited by 55

The Challenges of Designing and Implementing Clinical Trials With Broccoli Sprouts… and Turning Evidence Into Public Health Action

Fahey, J. W., & Kensler, T. W. (2021) · Frontiers in Nutrition · doi:10.3389/fnut.2021.648788 · Cited by 55

The Role of KEAP1-NRF2 System in Atopic Dermatitis and Psoriasis

Ogawa, T., & Ishitsuka, Y. (2022) · Antioxidants · doi:10.3390/antiox11071397 · Cited by 55

Development of Noncovalent Small-Molecule Keap1-Nrf2 Inhibitors by Fragment-Based Drug Discovery

Narayanan, D., Tran, K. T., Pallesen, J. S., Solbak, S. M. Ø., Qin, Y., Mukminova, E., Luchini, M., Vasilyeva, K. O., Chichón, D. G., Goutsiou, G., et al. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c00830 · Cited by 55

Selective disruption of NRF2-KEAP1 interaction leads to NASH resolution and reduction of liver fibrosis in mice

Seedorf, K., Weber, C., Vinson, C., Berger, S., Vuillard, L.-M., Kiss, A., Creusot, S., Broux, O., Géant, A., Ilic, C., et al. (2022) · JHEP Reports · doi:10.1016/j.jhepr.2022.100651 · Cited by 54

Comprehensive Metabolic Tracing Reveals the Origin and Catabolism of Cysteine in Mammalian Tissues and Tumors

Yoon, S. J., Combs, J. A., Falzone, A., Prieto-Farigua, N., Caldwell, S., Ackerman, H. D., Flores, E. R., & DeNicola, G. M. (2023) · Cancer Research · doi:10.1158/0008-5472.can-22-3000 · Cited by 54

A potent phosphodiester Keap1-Nrf2 protein-protein interaction inhibitor as the efficient treatment of Alzheimer's disease

Sun, Y., Xu, L., Zheng, D., Wang, J., Liu, G., Mo, Z., Liu, C., Zhang, W., Yu, J., Xing, C., et al. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102793 · Cited by 54

MASH clinical trials and drugs pipeline: An impending tsunami

Noureddin, M. (2024) · Hepatology · doi:10.1097/hep.0000000000000860 · Cited by 54

Association of Nrf2 with airway pathogenesis: lessons learned from genetic mouse models

Cho, H., & Kleeberger, S. R. (2015) · Archives of Toxicology · doi:10.1007/s00204-015-1557-y · Cited by 53

Oxidative Stress, Environmental Pollution, and Lifestyle as Determinants of Asthma in Children

Vincenzo, S. D., Ferrante, G., Ferraro, M., Cascio, C., Malizia, V., Licari, A., Grutta, S. L., & Pace, E. (2023) · Biology · doi:10.3390/biology12010133 · Cited by 53

Nrf2 deficiency in myeloid cells is not sufficient to protect mice from high-fat diet-induced adipose tissue inflammation and insulin resistance

Meher, A. K., Sharma, P. R., Lira, V. A., Yamamoto, M. P., Kensler, T. W., Yan, Z., & Leitinger, N. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.02.022 · Cited by 51

Design, synthesis and identification of novel, orally bioavailable non-covalent Nrf2 activators

Ma, B., Lucas, B. S., Capacci, A. G., Lin, E. Y.-S., Jones, J. H., Dechantsreiter, M. A., Enyedy, I. J., Marcotte, D. J., Xiao, G., Li, B., et al. (2019) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2019.126852 · Cited by 51

A pan-cancer analysis shows immunoevasive characteristics in NRF2 hyperactive squamous malignancies

Härkönen, J., Pölönen, P., Deen, A. J., Selvarajan, I., Teppo, H., Dimova, E. Y., Kietzmann, T., Ahtiainen, M., Väyrynen, J. P., Väyrynen, S. A., et al. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102644 · Cited by 51

Omaveloxolone (SkyclarysTM) for patients with Friedreich’s ataxia

Naidu, S. D., & Dinkova‐Kostova, A. T. (2023) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2023.03.005 · Cited by 51

Mining Natural Products for Macrocycles to Drug Difficult Targets

Begnini, F., Poongavanam, V., Over, B., Castaldo, M., Geschwindner, S., Johansson, P., Tyagi, M., Tyrchan, C., Wissler, L., Sjö, P., et al. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c01569 · Cited by 50

Role of pirfenidone in TGF-β pathways and other inflammatory pathways in acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection: a theoretical perspective

Hamidi, S. H., Kadamboor Veethil, S., & Hamidi, S. H. (2021) · Pharmacological Reports · doi:10.1007/s43440-021-00255-x · Cited by 50

Importance of Binding Site Hydration and Flexibility Revealed When Optimizing a Macrocyclic Inhibitor of the Keap1–Nrf2 Protein–Protein Interaction

Begnini, F., Geschwindner, S., Johansson, P., Wissler, L., Lewis, R. J., Danelius, E., Luttens, A., Matricon, P. G., Carlsson, J., Lenders, S., et al. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c01975 · Cited by 50

Inhibition of the Keap1-Nrf2 protein-protein interaction protects retinal cells and ameliorates retinal ischemia-reperfusion injury

Hui, Q., Karlstetter, M., Xu, Z., Yang, J., Zhou, L., Eilken, H. M., Terjung, C., Cho, H., Gong, J., Lai, M. J., et al. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2019.10.414 · Cited by 49

Deep phenotyping of peripheral tissue facilitates mechanistic disease stratification in sporadic Parkinson’s disease

Carling, P. J., Mortiboys, H., Green, C., Mihaylov, S. R., Sandor, C., Schwartzentruber, A., Taylor, R. N., Wei, W., Hastings, C., Wong, S. L., et al. (2020) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2020.101772 · Cited by 49

Design, Synthesis, and Structure–Activity Relationships of Indoline-Based Kelch-like ECH-Associated Protein 1-Nuclear Factor (Erythroid-Derived 2)-Like 2 (Keap1-Nrf2) Protein–Protein Interaction Inhibitors

Zhou, H.-S., Hu, L.-B., Zhang, H., Shan, W.-X., Wang, Y., Li, X., Liu, T., Zhao, J., You, Q., & Jiang, Z. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c01116 · Cited by 49

Distinct Nrf2 Signaling Thresholds Mediate Lung Tumor Initiation and Progression

DeBlasi, J. M., Falzone, A., Caldwell, S., Prieto-Farigua, N., Prigge, J. R., Schmidt, E. E., Chio, I. I. C., Karreth, F. A., & DeNicola, G. M. (2023) · Cancer Research · doi:10.1158/0008-5472.can-22-3848 · Cited by 49 · cited 1×

Deleterious effect of oltipraz on extrahepatic cholestasis in bile duct-ligated mice

Weerachayaphorn, J., Luo, Y., Mennone, A., Soroka, C. J., Harry, K., & Boyer, J. L. (2013) · Journal of Hepatology · doi:10.1016/j.jhep.2013.08.015 · Cited by 47

Association of Nuclear Factor‐Erythroid 2‐Related Factor 2, Thioredoxin Interacting Protein, and Heme Oxygenase‐1 Gene Polymorphisms with Diabetes and Obesity in Mexican Patients

Jiménez‐Osorio, A. S., González-Reyes, S., García‐Niño, W. R., Moreno-Macías, H., Rodríguez-Arellano, M. E., Vargas‐Alarcón, G., Zúñiga, J., Barquera, R., & Pedraza‐Chaverrí, J. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/7367641 · Cited by 47

Stigmasterol sensitizes endometrial cancer cells to chemotherapy by repressing Nrf2 signal pathway

Liao, H., Zhu, D., Bai, M., Chen, H., Yan, S., Yu, J. Q., Zhu, H., Zheng, W., & Fan, G. (2020) · Cancer Cell International · doi:10.1186/s12935-020-01470-x · Cited by 47

Association of NFE2L2 and KEAP1 haplotypes with amyotrophic lateral sclerosis

Bergström, P., von Otter, M., Nilsson, S., Nilsson, A.-C., Nilsson, M., Andersen, P. M., Hammarsten, O., & Zetterberg, H. (2013) · Amyotrophic Lateral Sclerosis and Frontotemporal Degeneration · doi:10.3109/21678421.2013.839708 · Cited by 46

A Novel Nrf2 Pathway Inhibitor Sensitizes Keap1-Mutant Lung Cancer Cells to Chemotherapy

Zhang, D., Hou, Z., Aldrich, K. E., Lockwood, L. R., Odom, A. L., & Liby, K. T. (2021) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-21-0210 · Cited by 46

Nuclear factor E2-related factor 2 deficiency impairs atherosclerotic lesion development but promotes features of plaque instability in hypercholesterolaemic mice

Ruotsalainen, A., Lappalainen, J. P., Heiskanen, E., Merentie, M., Sihvola, V., Näpänkangas, J. P., Lottonen‐Raikaslehto, L., Kansanen, E., Adinolfi, S., Kaarniranta, K., et al. (2018) · Cardiovascular Research · doi:10.1093/cvr/cvy143 · Cited by 45

Regulation of the Nrf2 Pathway by Glycogen Synthase Kinase-3β in MPP+-Induced Cell Damage

Armağan, G., Sevgili, E., Gürkan, F. T., Köse, F. A., Bilgiç, T., Dağcı, T., & Saso, L. (2019) · Molecules · doi:10.3390/molecules24071377 · Cited by 45

Redox Imbalance in Inflammation: The Interplay of Oxidative and Reductive Stress

Bellanti, F., Coda, A. R. D., Trecca, M. I., Buglio, A. L., Serviddio, G., & Vendemiale, G. (2025) · Antioxidants · doi:10.3390/antiox14060656 · Cited by 222

Sulforaphane and Brain Health: From Pathways of Action to Effects on Specific Disorders

Fahey, J. W., Liu, H., Batt, H., Panjwani, A. A., & Tsuji, P. A. (2025) · Nutrients · doi:10.3390/nu17081353 · Cited by 22

NRF2 as a guardian of health: from an ancient survival pathway to a modern therapeutic target

Tenreiro, S., Falcão, A. S., Bender, N., Bernátová, I., Berry, A., Cuadrado, A., Eppenberger, P., Giona, L., Grochot‐Przeczek, A., Heiß, E. H., et al. (2026) · Redox Biology · doi:10.1016/j.redox.2026.104217 · Cited by 8

Lithium Augmentation in Treatment‐Resistant Depression: A Qualitative Review of the Literature

González, Á. R. A., Guzmán, Y., Proaños, N. J., Bustos, R., Aconcha, M., Guerrero, I. M., Calderon, L. A. M., Berk, M., & Dodd, S. (2025) · Pharmacotherapy The Journal of Human Pharmacology and Drug Therapy · doi:10.1002/phar.70063 · Cited by 5

Interplay between NRF2 post-translational modifications and protein-protein interactions: Perspectives from emerging structural and functional evidence

Ozleyen, A., Kulabas, S. S., Novak, M. J., Cichoń, M., Heras, C. M. D. L., Honda, T., Doveston, R. G., Dinkova‐Kostova, A. T., Grochot‐Przeczek, A., & Tumer, T. B. (2026) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2026.110847 · Cited by 5

Advances and challenges in therapeutic targeting of NRF2

Dinkova‐Kostova, A. T., & Copple, I. M. (2023) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2022.12.003 · Cited by 277

NRF2: Master regulator of cellular homeostasis and therapeutic vulnerability in cancer

Chen, W.-T., McKee, N. W., Kuhnell, D., & Dodson, M. B. (2026) · Redox Biology · doi:10.1016/j.redox.2026.104050 · Cited by 29

Modulating NRF2 in Disease: Timing Is Everything

Dodson, M. B., de la Vega, M. R., Cholanians, A. B., Schmidlin, C. J., Chapman, E., & Zhang, D. D. (2018) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010818-021856 · Cited by 540

Perspectives on the Clinical Development of NRF2-Targeting Drugs

Lastra, D., Fernández-Ginés, R., Manda, G., & Cuadrado, A. (2020) · Handbook of experimental pharmacology · doi:10.1007/164_2020_381 · Cited by 29

Introduction to Special Issue on “Bench to bedside transition for pharmacological regulation of NRF2 in noncommunicable diseases”

Cuadrado, A., Dinkova‐Kostova, A. T., & Mann, G. E. (2022) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2022.12.100