Direct Interaction between Nrf2 and p21Cip1/WAF1 Upregulates the Nrf2-Mediated Antioxidant Response

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

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

Oxidative stress sensor Keap1 functions as an adaptor for Cul3-based E3 ligase to regulate proteasomal degradation of Nrf2

Kobayashi, A., Kang, M.-I., Okawa, H., Ohtsuji, M., Zenke, Y., Chiba, T., Igarashi, K., & Yamamoto, M. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.16.7130-7139.2004 · Cited by 2,224

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

Keap1 Is a Redox-Regulated Substrate Adaptor Protein for a Cul3-Dependent Ubiquitin Ligase Complex

Zhang, D. D., Lo, S., Cross, J. V., Templeton, D. J., & Hannink, M. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.24.10941-10953.2004 · Cited by 1,284

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

Mechanistic Studies of the Nrf2-Keap1 Signaling Pathway

Zhang, D. D. (2006) · Drug Metabolism Reviews · doi:10.1080/03602530600971974 · Cited by 1,105

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

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 1,087

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

Wakabayashi, N., Dinkova-Kostova, A. T., Holtzclaw, W. D., Kang, M.-I., Kobayashi, A., Yamamoto, M., Kensler, T. W., & Talalay, P. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0307301101 · Cited by 986

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 191

iASPP Is an Antioxidative Factor and Drives Cancer Growth and Drug Resistance by Competing with Nrf2 for Keap1 Binding

Ge, W., Zhao, K., Wang, X., Li, H., Yu, M., He, M., Xue, X., Zhu, Y., Zhang, C. L., Cheng, Y., et al. (2017) · Cancer Cell · doi:10.1016/j.ccell.2017.09.008 · Cited by 188

Oxidative stress, a trigger of hepatitis C and B virus-induced liver carcinogenesis

Ivanov, A. V., Треворович, В.-Э. В., Tyurina, D. A., Ivanova, O. N., Kochetkov, S. N., Bartosch, B., & Isaguliants, M. G. (2016) · Oncotarget · doi:10.18632/oncotarget.13904 · Cited by 193

NRF2 Activation in Cancer: From DNA to Protein

Cloer, E. W., Goldfarb, D., Schrank, T. P., Weissman, B. E., & Major, M. B. (2019) · Cancer Research · doi:10.1158/0008-5472.can-18-2723 · Cited by 182

The transcription factor NF‐E2‐related Factor 2 (Nrf2): a protooncogene?

Shelton, P. M., & Jaiswal, A. K. (2012) · The FASEB Journal · doi:10.1096/fj.12-217257 · Cited by 185

Potential Applications of NRF2 Inhibitors in Cancer Therapy

Panieri, E., & Saso, L. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/8592348 · Cited by 189

The Hallmarks of Flavonoids in Cancer

Ponte, L. G. S., Pavan, I. C. B., Mancini, M. C. S., da Silva, L. G. S., Morelli, A. P., Severino, M. B., Bezerra, R. M. N., & Simabuco, F. M. (2021) · Molecules · doi:10.3390/molecules26072029 · Cited by 188

Regulation of redox balance in cancer and T cells

Kong, H., & Chandel, N. S. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.tm117.000257 · Cited by 182

Collaborative Power of Nrf2 and PPAR γ Activators against Metabolic and Drug‐Induced Oxidative Injury

Lee, C.-H. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/1378175 · Cited by 185

Luteolin promotes apoptotic cell death via upregulation of Nrf2 expression by DNA demethylase and the interaction of Nrf2 with p53 in human colon cancer cells

Kang, K. A., Piao, M. J., Hyun, Y. J., Zhen, A. X., Cho, S. J., Ahn, M. J., Yi, J. M., & Hyun, J. W. (2019) · Experimental & Molecular Medicine · doi:10.1038/s12276-019-0238-y · Cited by 179

p53 Regulation of Metabolic PathwaysPreprint

Gottlieb, E., & Vousden, K. H. (2009) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a001040 · Cited by 189

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 174

An update of Nrf2 activators and inhibitors in cancer prevention/promotion

Pouremamali, F., Pouremamali, A., Dadashpour, M., Soozangar, N., & Jeddi, F. (2022) · Cell Communication and Signaling · doi:10.1186/s12964-022-00906-3 · Cited by 183

Monitoring Keap1–Nrf2 interactions in single live cells

Baird, L., Swift, S., Llères, D., & Dinkova‐Kostova, A. T. (2014) · Biotechnology Advances · doi:10.1016/j.biotechadv.2014.03.004 · Cited by 179

Nrf2 as regulator of innate immunity: A molecular Swiss army knife!

Battino, M. A., Giampieri, F., Pistollato, F., Sureda, A., de Oliveira, M. R., Pittalà, V., Fallarino, F., Nabavi, S. F., Atanasov, A. G., & Nabavi, S. M. (2017) · Biotechnology Advances · doi:10.1016/j.biotechadv.2017.12.012 · Cited by 170

Targeting NRF2 and Its Downstream Processes: Opportunities and Challenges

Torrente, L., & DeNicola, G. M. (2021) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-052220-104025 · Cited by 175

Antioxidant and Adaptative Response Mediated by Nrf2 during Physical Exercise

Vargas-Mendoza, N., Morales‐González, Á., Madrigal‐Santillán, E., Madrigal‐Bujaidar, E., Álvarez‐González, I., García-Melo, L. F., Anguiano‐Robledo, L., Fregoso-Aguilar, T. A., & Morales‐González, J. A. (2019) · Antioxidants · doi:10.3390/antiox8060196 · Cited by 170

Potential Applications of NRF2 Modulators in Cancer Therapy

Panieri, E., Djordjević, A. B., Telkoparan‐Akillilar, P., Cevik, D., Kouretas, D., Veskoukis, A. S., Skaperda, Z., Tsatsakis, A. M., Wallace, D., Süzen, S., et al. (2020) · Antioxidants · doi:10.3390/antiox9030193 · Cited by 167

From structures to functions: insights into exosomes as promising drug delivery vehicles

Ren, J., He, W., Zheng, L., & Duan, H. (2016) · Biomaterials Science · doi:10.1039/c5bm00583c · Cited by 164

Role of the Keap1–Nrf2 Pathway in Cancer

Leinonen, H. M., Kansanen, E., Pölönen, P., Heinäniemi, M., & Levonen, A. (2014) · Advances in cancer research · doi:10.1016/b978-0-12-420117-0.00008-6 · Cited by 158

A human tRNA synthetase is a potent PARP1-activating effector target for resveratrol

Sajish, M., & SCHIMMEL, P. R. (2014) · Nature · doi:10.1038/nature14028 · Cited by 153

Green tea polyphenols causes cell cycle arrest and apoptosis in prostate cancer cells by suppressing class I histone deacetylases

Thakur, V. S., Gupta, K., & Gupta, S. (2011) · Carcinogenesis · doi:10.1093/carcin/bgr277 · Cited by 152

p53 and metabolism: from mechanism to therapeutics

Simabuco, F. M., Morale, M. G., Pavan, I. C. B., Morelli, A. P., Silva, F. R., & Tamura, R. E. (2018) · Oncotarget · doi:10.18632/oncotarget.25267 · Cited by 159

The regulation of cellular metabolism by tumor suppressor p53

Liang, Y., Liu, J., & Feng, Z. (2013) · Cell & Bioscience · doi:10.1186/2045-3701-3-9 · Cited by 154

Regulation of Cellular Metabolism and Hypoxia by p53Preprint

Humpton, T. J., & Vousden, K. H. (2016) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a026146 · Cited by 154

Regulation of Nrf2 Signaling

Li, Y., Jia, Z., & Zhu, H. (2019) · doi:10.20455/ros.2019.865 · Cited by 149

Targeting Nrf2 Signaling to Combat Chemoresistance

No, J. H., Kim, Y.-B., & Song, Y. S. (2014) · Journal of Cancer Prevention · doi:10.15430/jcp.2014.19.2.111 · Cited by 146

Sustained Activation of Nuclear Erythroid 2-Related Factor 2/Antioxidant Response Element Signaling Promotes Reductive Stress in the Human Mutant Protein Aggregation Cardiomyopathy in Mice

Rajasekaran, N. S., Varadharaj, S., Khanderao, G. D., Davidson, C. J., Kannan, S., Firpo, M. A., Zweier, J. L., & Benjamin, I. J. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3587 · Cited by 141

Mutant p53 confers chemoresistance in non-small cell lung cancer by upregulating Nrf2

Tung, M., Lin, P.-L., Wang, Y.-C., He, T.-Y., Lee, M.-C., Yeh, S.-D., Chen, C., & Lee, H. (2015) · Oncotarget · doi:10.18632/oncotarget.6150 · Cited by 140

Therapeutic Targeting of the NRF2 Signaling Pathway in Cancer

Telkoparan‐Akillilar, P., Panieri, E., Cevik, D., Süzen, S., & Saso, L. (2021) · Molecules · doi:10.3390/molecules26051417 · Cited by 148

Cancer-Derived Mutations in KEAP1 Impair NRF2 Degradation but not Ubiquitination

Hast, B. E., Cloer, E. W., Goldfarb, D., Li, H., Siesser, P. F., Yan, F., Walter, V., Zheng, N., Hayes, D. N., & Major, M. B. (2014) · Cancer Research · doi:10.1158/0008-5472.can-13-1655 · Cited by 138

The critical role of catalase in prooxidant and antioxidant function of p53

Kang, M. Y., Kim, H.-B., Piao, C., Lee, K. K., Hyun, J. W., Chang, I.-Y., & You, H. J. (2012) · Cell Death and Differentiation · doi:10.1038/cdd.2012.102 · Cited by 140

Concerted action of Nrf2-ARE pathway, MRN complex, HMGB1 and inflammatory cytokines - Implication in modification of radiation damage

Anuranjani, & Bala, M. (2014) · Redox Biology · doi:10.1016/j.redox.2014.02.008 · Cited by 138

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

Keap1-Nrf2 signaling pathway: Mechanisms of regulation and role in protection of cells against toxicity caused by xenobiotics and electrophiles

Turpaev, K. T. (2013) · Biochemistry (Moscow) · doi:10.1134/s0006297913020016 · Cited by 135

Stepping up melanocytes to the challenge of UV exposure: DNA damage response of human melanocytes to UV exposure

Abdel-Malek, Z. A., Kadekaro, A. L., & Swope, V. B. (2010) · Pigment Cell & Melanoma Research · doi:10.1111/j.1755-148x.2010.00679.x · Cited by 134

Contribution of the Nrf2 Pathway on Oxidative Damage and Mitochondrial Failure in Parkinson and Alzheimer’s Disease

Villavicencio-Tejo, F., & Quintanilla, R. A. (2021) · Antioxidants · doi:10.3390/antiox10071069 · Cited by 143

Redox Modulating NRF2: A Potential Mediator of Cancer Stem Cell Resistance

Ryoo, I.-G., Lee, S.-H., & Kwak, M.-K. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/2428153 · Cited by 135

p53 as a hub in cellular redox regulation and therapeutic target in cancer

Eriksson, S. E., Ceder, S., Bykov, V. J. N., & Wiman, K. G. (2019) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjz005 · Cited by 123

Wilms Tumor Gene on X Chromosome (WTX) Inhibits Degradation of NRF2 Protein through Competitive Binding to KEAP1 Protein

Camp, N. D., James, R. G., Dawson, D. W., Yan, F., Davison, J. M., Houck, S. A., Tang, X., Zheng, N., Major, M. B., & Moon, R. T. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.316471 · Cited by 128

Nestin regulates cellular redox homeostasis in lung cancer through the Keap1–Nrf2 feedback loop

Wang, J., Lu, Q., Cai, J., Wang, Y., Lai, X., Qiu, Y., Huang, Y., Ke, Q., Zhang, Y., Guan, Y., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-12925-9 · Cited by 130

Involvement of activating ERK1/2 through G protein coupled receptor 30 and estrogen receptor α/β in low doses of bisphenol A promoting growth of Sertoli TM4 cells

Ge, L.-C., Chen, Z.-J., Liu, H.-Y., Zhang, K.-S., Liu, H., Huang, H.-B., Zhang, G., Wong, C. K. C., Giesy, J. P., Du, J., et al. (2014) · Toxicology Letters · doi:10.1016/j.toxlet.2014.01.035 · Cited by 129

Saponin Formosanin C-Induced Ferritinophagy and Ferroptosis in Human Hepatocellular Carcinoma Cells

Lin, P.-L., Tang, H. F., Wu, S., Shaw, N.-S., & Su, C. (2020) · Antioxidants · doi:10.3390/antiox9080682 · Cited by 129

Does Nrf2 Contribute to p53-Mediated Control of Cell Survival and Death?

Chen, W., Jiang, T., Wang, H., Tao, S., Lau, A., Fang, D., & Zhang, D. D. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4674 · Cited by 126

Modulation of NRF2 signaling pathway by nuclear receptors: Implications for cancer

Namani, A., Li, Y., Wang, X. J., & Tang, X. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.05.003 · Cited by 128

Discovery and Development of Kelch-like ECH-Associated Protein 1. Nuclear Factor Erythroid 2-Related Factor 2 (KEAP1:NRF2) Protein–Protein Interaction Inhibitors: Achievements, Challenges, and Future Directions

Jiang, Z., Lu, M., & You, Q. (2016) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b00586 · Cited by 128

Chlorogenic acid promotes the Nrf2/HO-1 anti-oxidative pathway by activating p21Waf1/Cip1 to resist dexamethasone-induced apoptosis in osteoblastic cells

Han, D., Gu, X., Gao, J., Wang, Z., Liu, G., Barkema, H. W., & Han, B. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2019.04.014 · Cited by 126

Natural compounds against doxorubicin‐induced cardiotoxicity: A review on the involvement of Nrf2/ ARE signaling pathway

Yarmohammadi, F., Rezaee, R., & Karimi, G. (2020) · Phytotherapy Research · doi:10.1002/ptr.6882 · Cited by 126

Hydrogen peroxide-induced oxidative stress activates NF-κB and Nrf2/Keap1 signals and triggers autophagy in piglets

Yin, J., Duan, J., Cui, Z., Ren, W., Li, Y., & Yin, Y. (2015) · RSC Advances · doi:10.1039/c4ra13557a · Cited by 126

Asah2 Represses the p53–Hmox1 Axis to Protect Myeloid-Derived Suppressor Cells from Ferroptosis

Zhu, H., Klement, J. D., Lu, C., Redd, P. S., Yang, D., Smith, A. D., Poschel, D. B., Zou, J., Liu, D., Wang, P. G., et al. (2021) · The Journal of Immunology · doi:10.4049/jimmunol.2000500 · Cited by 126

Role of NRF2 in Lung Cancer

Sánchez-Ortega, M., Carrera, A. C., & Garrido, A. (2021) · Cells · doi:10.3390/cells10081879 · Cited by 130

USP15 Negatively Regulates Nrf2 through Deubiquitination of Keap1

Villeneuve, N. F., Tian, W., Wu, T., Sun, Z., Lau, A., Chapman, E., Fang, D., & Zhang, D. D. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.04.022 · Cited by 120

Mutant p53 tunes the NRF2-dependent antioxidant response to support survival of cancer cells

Lisek, K., Campaner, E., Ciani, Y., Walerych, D., & Sal, G. D. (2018) · Oncotarget · doi:10.18632/oncotarget.24974 · Cited by 119

Breast cancer susceptibility protein 1 (BRCA1) rescues neurons from cerebral ischemia/reperfusion injury through NRF2-mediated antioxidant pathway

Xu, P., Liu, Q., Xie, Y., Shi, X., Li, Y., Peng, M., Guo, H., Sun, R., Li, J., Hong, Y., et al. (2018) · Redox Biology · doi:10.1016/j.redox.2018.06.012 · Cited by 100

Keap1 as the redox sensor of the antioxidant response

Sihvola, V., & Levonen, A. (2016) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2016.10.010 · Cited by 120

Nrf2 is a potential therapeutic target in radioresistance in human cancer

Zhou, S., Ye, W., Shao, Q., Zhang, M., & Liang, J. (2013) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2013.09.001 · Cited by 115

Micromanaging aerobic respiration and glycolysis in cancer cells

Orang, A., Petersen, J., McKinnon, R. A., & Michael, M. (2019) · Molecular Metabolism · doi:10.1016/j.molmet.2019.01.014 · Cited by 117

Human Alveolar Epithelial Cell Injury Induced by Cigarette Smoke

Kośmider, B., Messier, E. M., Chu, H. W., & Mason, R. J. (2011) · PLoS ONE · doi:10.1371/journal.pone.0026059 · Cited by 114

Role of Oxidative Stress and Inflammation in Doxorubicin-Induced Cardiotoxicity: A Brief Account

Vitale, R., Marzocco, S., & Popolo, A. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25137477 · Cited by 122

p62/ SQSTM 1—Dr. Jekyll and Mr. Hyde that prevents oxidative stress but promotes liver cancer

Taniguchi, K., Yamachika, S., He, F., & Karin, M. (2016) · FEBS Letters · doi:10.1002/1873-3468.12301 · Cited by 117

Comparative study on the response of rat primary astrocytes and microglia to methylmercury toxicity

Ni, M., Li, X., Yin, Z., Sidoryk‐Wȩgrzynowicz, M., Jiang, H., Farina, M., da Rocha, J. B. T., Syversen, T. L. M., & Aschner, M. (2011) · Glia · doi:10.1002/glia.21153 · Cited by 116

Copper( ii ) thiosemicarbazone complexes induce marked ROS accumulation and promote nrf2-mediated antioxidant response in highly resistant breast cancer cells

Sîrbu, A., Palamarciuc, O. V., Babak, M. V., Lim, J. M., Ohui, K. A., Enyedy, É. A., Shova, S. G., Darvasiová, D., Rapta, P., Ang, W. H., et al. (2017) · Dalton Transactions · doi:10.1039/c7dt00283a · Cited by 114

HACE1 reduces oxidative stress and mutant Huntingtin toxicity by promoting the NRF2 response

Rotblat, B., Southwell, A. L., Ehrnhoefer, D. E., Skotte, N. H., Metzler, M., Franciosi, S., Leprivier, G., Somasekharan, S. P., Barokas, A., Deng, Y., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1314421111 · Cited by 111

NRF2 and p53: Januses in cancer?

Rotblat, B., Melino, G., & Knight, R. A. (2012) · Oncotarget · doi:10.18632/oncotarget.754 · Cited by 114

Current mechanistic insights into the CCCP-induced cell survival response

Kane, M. S., Paris, A., Codron, P., Cassereau, J., Procaccio, V., Lenaers, G., Reynier, P., & Chevrollier, A. (2017) · Biochemical Pharmacology · doi:10.1016/j.bcp.2017.12.018 · Cited by 115

ROS/Autophagy/Nrf2 Pathway Mediated Low-Dose Radiation Induced Radio-Resistance in Human Lung Adenocarcinoma A549 Cell

Chen, N., Wu, L., Yuan, H., & Wang, J. (2015) · International Journal of Biological Sciences · doi:10.7150/ijbs.10564 · Cited by 107

Epigenetic Mechanisms in Cerebral Ischemia

Schweizer, S., Meisel, A., & Märschenz, S. (2013) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.2013.93 · Cited by 104

The Hallmarks of Cancer from a Redox Perspective

Hornsveld, M., & Dansen, T. B. (2016) · Antioxidants and Redox Signaling · doi:10.1089/ars.2015.6580 · Cited by 105

Role of Nrf2 and Autophagy in Acute Lung Injury

de la Vega, M. R., Dodson, M. B., Groß, C., Mansour, H. M., Lantz, R. C., Chapman, E., Wang, T., Black, S. M., Garcia, J. G. N., & Zhang, D. D. (2016) · Current Pharmacology Reports · doi:10.1007/s40495-016-0053-2 · Cited by 104

A p21-ZEB1 Complex Inhibits Epithelial-Mesenchymal Transition through the MicroRNA 183-96-182 Cluster

Li, X. L., Hara, T., Choi, Y., Subramanian, M., Francis, P., Bilke, S., Walker, R. L., Pineda, M. A., Zhu, Y. J., Yang, Y.-A., et al. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.01043-13 · Cited by 103

Dietary Phytochemicals and Cancer Chemoprevention: A Perspective on Oxidative Stress, Inflammation, and Epigenetics

Li, W., Guo, Y., Zhang, C., Wu, R., Yang, Y., Gaspar, J. M., & Kong, A. T. (2016) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.6b00413 · Cited by 101

NRF2 preserves genomic integrity by facilitating ATR activation and G2 cell cycle arrest

Sun, X., Wang, Y., Ji, K., Liu, Y., Kong, Y., Nie, S., Li, N., Hao, J., Xie, Y., Xu, C., et al. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa631 · Cited by 103

NRF2, a Key Regulator of Antioxidants with Two Faces towards Cancer

Kim, J., & Keum, Y. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/2746457 · Cited by 101

Role of Nrf2 in cell senescence regulation

Yuan, H., Xu, Y., Luo, Y., Wang, N.-X., & Xiao, J. (2020) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-020-03901-9 · Cited by 104

The intricacies of NRF2 regulation in cancer

Schmidlin, C. J., Shakya, A., Dodson, M. B., Chapman, E., & Zhang, D. D. (2021) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2021.05.016 · Cited by 103

Effect of local intra-arterial asymmetric dimethylarginine (ADMA) on the forearm arteriolar bed of healthy volunteers.

Calver, A., Collier, J., Leone, A., Moncada, S., & Vallance, P. J. (1993) · PubMed · Cited by 100

Activation of KEAP1/NRF2/P62 signaling alleviates high phosphate-induced calcification of vascular smooth muscle cells by suppressing reactive oxygen species production

Wei, R., Enaka, M., & Muragaki, Y. (2019) · Scientific Reports · doi:10.1038/s41598-019-46824-2 · Cited by 100

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

Lee, D. H., Han, D. H., Nam, K. T., Park, J. S., Kim, S. H., Lee, M., Kim, G., Min, B. S., Soo, B., Lee, Y. S., et al. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.09.009 · Cited by 98

Dysregulation of NRF2 in Cancer: from Molecular Mechanisms to Therapeutic Opportunities

Jung, B.-J., Yoo, H.-S., Shin, S., Park, Y., & Jeon, S. (2017) · Biomolecules & Therapeutics · doi:10.4062/biomolther.2017.195 · Cited by 104

FoxO1 is involved in the antineoplastic effect of calorie restriction

Yamaza, H., Komatsu, T., Wakita, S., Kijogi, C., Park, S., Hayashi, H., Chiba, T., Mori, R., Furuyama, T., Mori, N., et al. (2010) · Aging Cell · doi:10.1111/j.1474-9726.2010.00563.x · Cited by 93

Nuclear Factor Erythroid 2-Related Factor 2 in Regulating Cancer Metabolism

Smolková, K., Mikó, E., Kovàcs, T., Leguina‐Ruzzi, A., Sipos, A., & Bai, P. (2020) · Antioxidants and Redox Signaling · doi:10.1089/ars.2020.8024 · Cited by 101

The Interplay Between Tumor Suppressor p53 and Hypoxia Signaling Pathways in Cancer

Zhang, C., Liu, J., Wang, J., Zhang, T., Xu, D., Hu, W., & Feng, Z. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.648808 · Cited by 100

Toward improved human health: Nrf2 plays a critical role in regulating ferroptosis

Lu, J., Zhao, Y., Liu, M., Lu, J., & Guan, S. (2021) · Food & Function · doi:10.1039/d1fo01036k · Cited by 97

Negative Regulation of the Keap1-Nrf2 Pathway by a p62/Sqstm1 Splicing Variant

Kageyama, S., Saito, T., Obata, M., Koide, R.-H., Ichimura, Y., & Komatsu, M. (2018) · Molecular and Cellular Biology · doi:10.1128/mcb.00642-17 · Cited by 95

Development of Neh2-Luciferase Reporter and Its Application for High Throughput Screening and Real-Time Monitoring of Nrf2 Activators

Smirnova, N. A., Haskew-Layton, R. E., Basso, M., Hushpulian, D. M., Payappilly, J. B., Speer, R. E., Ahn, Y., Rakhman, I., Cole, P. A., Pinto, J. T., et al. (2011) · Chemistry & Biology · doi:10.1016/j.chembiol.2011.03.013 · Cited by 96

P-TEFb Activation by RBM7 Shapes a Pro-survival Transcriptional Response to Genotoxic Stress

Bugai, A., Quaresma, A. J. C., Friedel, C. C., Lenasi, T., Düster, R., Sibley, C. R., Fujinaga, K., Kukanja, P., Hennig, T., Blasius, M., et al. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.01.033 · Cited by 92

Dual roles and therapeutic potential of Keap1-Nrf2 pathway in pancreatic cancer: a systematic review

Qin, J., Cheng, X., Zhang, J., & Zhang, W. (2019) · Cell Communication and Signaling · doi:10.1186/s12964-019-0435-2 · Cited by 94

Regulating Nrf2 activity: ubiquitin ligases and signaling molecules in redox homeostasis

Hayes, J. D., Naidu, S. D., & Dinkova‐Kostova, A. T. (2025) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2024.12.010 · Cited by 103

Dysregulation of the Keap1–Nrf2 pathway in cancer

Leinonen, H. M., Kansanen, E., Pölönen, P., Heinäniemi, M., & Levonen, A. (2015) · Biochemical Society Transactions · doi:10.1042/bst20150048 · Cited by 94

NRF2 and Diabetes: The Good, the Bad, and the Complex

Dodson, M. B., Shakya, A., Anandhan, A., Chen, J., Garcia, J. G. N., & Zhang, D. D. (2022) · Diabetes · doi:10.2337/db22-0623 · Cited by 100

Nrf2 Pathway in Age-Related Neurological Disorders: Insights into MicroRNAs

Paladino, S., Conte, A., Caggiano, R., Pierantoni, G. M., & Faraonio, R. (2018) · Cellular Physiology and Biochemistry · doi:10.1159/000491465 · Cited by 92

RNA Sequence Reveals Mouse Retinal Transcriptome Changes Early after Axonal Injury

Yasuda, M., Tanaka, Y., Ryu, M., Tsuda, S., & Nakazawa, T. (2014) · PLoS ONE · doi:10.1371/journal.pone.0093258 · Cited by 91

Cytoprotection “gone astray’’: Nrf2 and its role in cancer

Schäfer, H., Geismann, C., Arlt, A., & Sebens, S. (2014) · OncoTargets and Therapy · doi:10.2147/ott.s36624 · Cited by 93

Differential transcriptional profiles mediated by exposure to the cannabinoids cannabidiol and Δ9‐tetrahydrocannabinol in BV‐2 microglial cells

Juknat, A., Pietr, M., Kozela, E., Rimmerman, N., Levy, R., Coppola, G., Geschwind, D. H., & Vogel, Z. (2011) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2011.01461.x · Cited by 90

Comprehensive micro-scaled proteome and phosphoproteome characterization of archived retrospective cancer repositories

Friedrich, C., Schallenberg, S., Kirchner, M., Ziehm, M., Niquet, S., Haji, M., Beier, C., Neudecker, J., Klauschen, F., & Mertins, P. (2021) · Nature Communications · doi:10.1038/s41467-021-23855-w · Cited by 96

Antitumorigenic Potential of Linalool Is Accompanied by Modulation of Oxidative Stress: An In Vivo Study in Sarcoma-180 Solid Tumor Model

Jana, S., Patra, K., Sarkar, S., Jana, J., Mukherjee, G., Bhattacharjee, S., & Mandal, D. P. (2014) · Nutrition and Cancer · doi:10.1080/01635581.2014.904906 · Cited by 97

Prognostic significance of 8-hydroxy-2′-deoxyguanosine in solid tumors: a meta-analysis

Qing, X., Shi, D., Lv, X., Wang, B., Chen, S., & Shao, Z. (2019) · BMC Cancer · doi:10.1186/s12885-019-6189-9 · Cited by 92

The Multifaceted Roles of NRF2 in Cancer: Friend or Foe?

Glorieux, C., Enriquez-Lara, C., González, C. D., Aguirre-Martínez, G. V., & Calderón, P. B. (2024) · Antioxidants · doi:10.3390/antiox13010070 · Cited by 97

An overview of the molecular mechanisms and novel roles of Nrf2 in neurodegenerative disorders

Yang, Y., Jiang, S., Yan, J., Li, Y., Xin, Z., Yan, L., & Qu, Y. (2014) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2014.09.002 · Cited by 86

Heme Oxygenase, Inflammation, and Fibrosis: The Good, the Bad, and the Ugly?

Lundvig, D. M. S., Immenschuh, S., & Wagener, F. A. D. T. G. (2012) · Frontiers in Pharmacology · doi:10.3389/fphar.2012.00081 · Cited by 86

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

Molecular mechanisms of Nrf2‐mediated antioxidant response

Li, W., & Kong, A. T. (2008) · Molecular Carcinogenesis · doi:10.1002/mc.20465 · Cited by 797

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 novel Nrf2-interacting factor KAP1 regulates susceptibility to oxidative stress by promoting the Nrf2-mediated cytoprotective response

Maruyama, A., Nishikawa, K., Kawatani, Y., Mimura, J., Hosoya, T., Harada, N., Yamamato, M., & Itoh, K. (2011) · Biochemical Journal · doi:10.1042/bj20101748 · Cited by 30

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 1,087