SCF/β-TrCP Promotes Glycogen Synthase Kinase 3-Dependent Degradation of the Nrf2 Transcription Factor in a Keap1-Independent Manner

β‐catenin is a target for the ubiquitin–proteasome pathway

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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

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

Dual regulation of Snail by GSK-3β-mediated phosphorylation in control of epithelial–mesenchymal transition

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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

A coordinated phosphorylation by Lats and CK1 regulates YAP stability through SCF β-TRCP

Zhao, B., Li, L., Tumaneng, K., Wang, C.-Y., & Guan, K.-L. (2010) · Genes & Development · doi:10.1101/gad.1843810 · Cited by 1,418

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

F-Box Proteins Are Receptors that Recruit Phosphorylated Substrates to the SCF Ubiquitin-Ligase Complex

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Nrf2 Is a Direct PERK Substrate and Effector of PERK-Dependent Cell Survival

Cullinan, S. B., Zhang, D. D., Hannink, M., Arvisais, E. W., Kaufman, R. J., & Diehl, J. A. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.20.7198-7209.2003 · Cited by 1,233

Dietary Phytochemicals Targeting Nrf2 to Enhance the Radiosensitivity of Cancer

Wang, P., Long, F., Lin, H., Wang, S., & Wang, T. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/7848811 · Cited by 22

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Nrf2-Mediated Dichotomy in the Vascular System: Mechanistic and Therapeutic Perspective

Wu, W., Hendrix, A., Nair, S., & Cui, T. (2022) · Cells · doi:10.3390/cells11193042 · Cited by 20

An in vivo drug repurposing screen and transcriptional analyses reveals the serotonin pathway and GSK3 as major therapeutic targets for NGLY1 deficiency

Hope, K. A., Berman, A. R., Peterson, R. T., & Chow, C. Y. (2022) · PLoS Genetics · doi:10.1371/journal.pgen.1010228 · Cited by 20

An inhibitor of interaction between the transcription factor NRF2 and the E3 ubiquitin ligase adapter β-TrCP delivers anti-inflammatory responses in mouse liver

Fernández-Ginés, R., Encinar, J. A., Hayes, J. D., Oliva, B., Rodrı́guez-Franco, M. I., Rojo, A. I., & Cuadrado, A. (2022) · Redox Biology · doi:10.1016/j.redox.2022.102396 · Cited by 20

Phenothiazines: Nrf2 activation and antioxidant effects

Egbujor, M. C., Tucci, P., Buttari, B., Nwobodo, D. C., Marini, P., & Saso, L. (2024) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.23661 · Cited by 20

Apigenin-7-O-β-D-(-6”-p-coumaroyl)-glucopyranoside treatment elicits a neuroprotective effect through GSK-3β phosphorylation-mediated Nrf2 activation

Wang, J., Wang, S., Sun, S., Lu, Y., Gao, K., Guo, C., Li, R., Li, W., Zhao, X., Tang, H., et al. (2020) · Aging · doi:10.18632/aging.104050 · Cited by 19

Interplay between nuclear factor erythroid 2-related factor 2 and inflammatory mediators in COVID-19-related liver injury

Zhu, D., Tan, X., Lu, L., Yu, S., Jian, R.-L., Liang, X., Liao, Y.-X., Fan, W., Barbier-Torres, L., Yang, A., et al. (2021) · World Journal of Gastroenterology · doi:10.3748/wjg.v27.i22.2944 · Cited by 19

Autosomal Dominant Polycystic Kidney Disease Therapies on the Horizon

Zhou, J. X., & Torres, V. E. (2023) · Advances in Kidney Disease and Health · doi:10.1053/j.akdh.2023.01.003 · Cited by 23

Effects of dietary zinc (Zn) levels on growth performance, nutrient composition, muscle development, antioxidant and inflammatory responses in yellow catfish muscle

Xu, X., Song, C.-C., Tan, X.-Y., Zhong, C.-C., & Luo, Z. (2023) · Aquaculture Reports · doi:10.1016/j.aqrep.2023.101640 · Cited by 19

Aβ Oligomer Toxicity-Reducing Therapy for the Prevention of Alzheimer’s Disease: Importance of the Nrf2 and PPARγ Pathways

Araki, W. (2023) · Cells · doi:10.3390/cells12101386 · Cited by 20

Drug repurposing on Alzheimer's disease through modulation of NRF2 neighborhood

Bourdakou, M. M., Fernández-Ginés, R., Cuadrado, A., & Spyrou, G. M. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102881 · Cited by 20

Sustained NRF2 activation in hereditary leiomyomatosis and renal cell cancer (HLRCC) and in hereditary tyrosinemia type 1 (HT1)

Sandhu, I. S., Maksim, N. J., Amouzougan, E. A., Gallion, B. W., Raviele, A. L. J., & Ooi, A. (2015) · Biochemical Society Transactions · doi:10.1042/bst20150041 · Cited by 19

Regulation of the CNC-bZIP transcription factor Nrf2 by Keap1 and the axis between GSK-3 and β-TrCP

Hayes, J. D., Ebisine, K., Sharma, R. S., Chowdhry, S., Dinkova‐Kostova, A. T., & Sutherland, C. D. (2016) · Current Opinion in Toxicology · doi:10.1016/j.cotox.2016.10.003 · Cited by 19

Progressive Rotavirus Infection Downregulates Redox-Sensitive Transcription Factor Nrf2 and Nrf2-Driven Transcription Units

Patra, U., Mukhopadhyay, U., Mukherjee, A., Sarkar, R., & Chawla‐Sarkar, M. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/7289120 · Cited by 19

Sp1 is a substrate of Keap1 and regulates the activity of CRL4AWDR23 ubiquitin ligase toward Nrf2

Siswanto, F. M., Oguro, A., & Imaoka, S. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100704 · Cited by 21

Recent Advances in the Role of Nuclear Factor Erythroid-2-Related Factor 2 in Spinal Cord Injury: Regulatory Mechanisms and Therapeutic Options

Jiang, T., & He, Y. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.851257 · Cited by 19

Inhibition of Microglial GSK3β Activity Is Common to Different Kinds of Antidepressants: A Proposal for an In Vitro Screen to Detect Novel Antidepressant Principles

Kalkman, H. O. (2023) · Biomedicines · doi:10.3390/biomedicines11030806 · Cited by 18

PLK2 protects retinal ganglion cells from oxidative stress by potentiating Nrf2 signaling via GSK‐3β

Fan, Y.-Z., Wang, J., He, N., & Feng, H.-X. (2021) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.22815 · Cited by 18

An Overview of the Posttranslational Modifications and Related Molecular Mechanisms in Diabetic Nephropathy

Cao, Y., Yang, Z., Chen, Y., Jiang, S., Wu, Z. B., Ding, B., Yang, Y., Jin, Z., & Tang, H. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.630401 · Cited by 18

Glycogen Synthase Kinase-3: A Focal Point for Advancing Pathogenic Inflammation in Depression

McCallum, R. T., & Perreault, M. L. (2021) · Cells · doi:10.3390/cells10092270 · Cited by 19

Small molecule and peptide inhibitors of βTrCP and the βTrCP–NRF2 protein–protein interaction

Jaffry, U., & Wells, G. (2023) · Biochemical Society Transactions · doi:10.1042/bst20220352 · Cited by 18

WDR23 regulates the expression of Nrf2-driven drug-metabolizing enzymes

Siswanto, F. M., Oguro, A., Arase, S., & Imaoka, S. (2020) · Drug Metabolism and Pharmacokinetics · doi:10.1016/j.dmpk.2020.06.007 · Cited by 18

Preventing Oxidative Stress in the Liver: An Opportunity for GLP-1 and/or PASK

Hurtado-Carneiro, V., Dongil, P., Pérez-García, A., Álvarez, E., & Sanz, C. (2021) · Antioxidants · doi:10.3390/antiox10122028 · Cited by 18

Mechanisms of NRF2 activation to mediate fetal hemoglobin induction and protection against oxidative stress in sickle cell disease

Zhu, X., Oseghale, A., Nicole, L. H., Li, Y., & Pace, B. S. (2019) · Experimental Biology and Medicine · doi:10.1177/1535370219825859 · Cited by 18

A novel yeast model detects Nrf2 and Keap1 interactions with Hsp90

Ngo, V., Brickenden, A. M., Liu, H., Yeung, C., Choy, W., & Duennwald, M. L. (2022) · Disease Models & Mechanisms · doi:10.1242/dmm.049258 · Cited by 16

Hydralazine Revives Cellular and Ocular Lens Health-Span by Ameliorating the Aging and Oxidative-Dependent Loss of the Nrf2-Activated Cellular Stress Response

Chhunchha, B., Kubo, E., Krueger, R. R., & Singh, D. P. (2023) · Antioxidants · doi:10.3390/antiox12010140 · Cited by 18

The Pivotal Role of Nrf2 Signal Axis in Intervertebral Disc Degeneration

Pan, C., Hou, W., Deng, X., Liu, J., Chi, R., Shang, X., Xu, T., & Hao, X. (2023) · Journal of Inflammation Research · doi:10.2147/jir.s432575 · Cited by 17

Phosphorylation and SCF-mediated degradation regulate CREB-H transcription of metabolic targets

Barbosa, S., Carreira, S., Bailey, D., Abaitua, F., & O’Hare, P. (2015) · Molecular Biology of the Cell · doi:10.1091/mbc.e15-04-0247 · Cited by 17

Kelch-like ECH-associated Protein 1-dependent Nuclear Factor-E2–related Factor 2 Activation in Relation to Antioxidation Induced by Sevoflurane Preconditioning

Cai, M., Li, T., Dong, B., Hou, W., Shi, L., & Dong, H. (2016) · Anesthesiology · doi:10.1097/aln.0000000000001485 · Cited by 17

A functionally defined high-density NRF2 interactome reveals new conditional regulators of ARE transactivation

Poh, J., Ponsford, A. H., Boyd, J., Woodsmith, J., Stelzl, U., Wanker, E. E., Harper, N., MacEwan, D. J., & Sanderson, C. M. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101686 · Cited by 17

Dysregulation of nuclear factor erythroid 2-related factor 2 signaling and activation of fibrogenic pathways in hearts of high fat diet-fed rats

Elrashidy, R. A. (2020) · Molecular Biology Reports · doi:10.1007/s11033-020-05360-3 · Cited by 17

Sequestosome 1 (p62) mitigates hypoxia-induced cardiac dysfunction by stabilizing hypoxia-inducible factor 1α and nuclear factor erythroid 2-related factor 2

Ghosh, R., Fatahian, A. N., Tavakoli‐Rouzbehani, O. M., Hathaway, M. A., Mosleh, T., Vinod, V., Vowles, S., Stephens, S. L., Chung, S.-L. D., Cao, I. D., et al. (2024) · Cardiovascular Research · doi:10.1093/cvr/cvae023 · Cited by 18

MTX-211 Inhibits GSH Synthesis through Keap1/NRF2/GCLM Axis and Exerts Antitumor Effects in Bladder Cancer

Hu, B., Chen, R., Jiang, M., Xiong, S., Xie, A., Liu, X., & Fu, B. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24087608 · Cited by 16

Activation of anti-oxidant Nrf2 signaling by substituted trans stilbenes

Deck, L. M., Whalen, L. J., Hunsaker, L. A., Royer, R. E., & Jagt, D. L. V. (2017) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2017.01.005 · Cited by 16

DJ-1 modulates Nrf2-mediated MRP1 expression by activating Wnt3a/β-catenin signalling in A549 cells exposed to cigarette smoke extract and LPS

Zhou, J., Qi, C., Fang, X. H., Wang, Z., Zhang, S., Li, D., & Song, J. (2021) · Life Sciences · doi:10.1016/j.lfs.2021.119089 · Cited by 16

Interplay between Nrf2 and NF-κB in Neuroinflammatory Diseases

Liddell, J. R. (2017) · Journal of Clinical & Cellular Immunology · doi:10.4172/2155-9899.1000489 · Cited by 16

Cardiac Aging – Benefits of Exercise, Nrf2 Activation and Antioxidant Signaling

Narasimhan, M., & Rajasekaran, N. S. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-981-10-4307-9_13 · Cited by 17

Model organisms for investigating the functional involvement of NRF2 in non-communicable diseases

Rojo, A. I., Buttari, B., Cadenas, S., Carlos, A. R., Cuadrado, A., Falcão, A. S., López, M. G., Georgiev, M. I., Grochot‐Przeczek, A., Gumeni, S., et al. (2024) · Redox Biology · doi:10.1016/j.redox.2024.103464 · Cited by 16

Oxidative Stress Induced by Nuclear Factor Erythroid 2-Related Factor 2 (NRF2) Dysfunction Aggravates Chronic Inflammation Through the NAD+/SIRT3 Axis and Promotes Renal Injury in Diabetes

Li, R., Yan, X., Zhao, Y., Liu, H., Song, J., Yuan, Y., Li, Q., & Su, J. (2025) · Antioxidants · doi:10.3390/antiox14030267 · Cited by 19

MicroRNA‐135a alleviates oxygen‐glucose deprivation and reoxygenation‐induced injury in neurons through regulation of GSK‐3β/Nrf2 signaling

Liu, X., Li, M., Hou, M.-S., Huang, W., & Song, J. (2018) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.22159 · Cited by 15

The untapped potential of targeting NRF2 in neurodegenerative disease

Chen, W.-T., & Dodson, M. B. (2023) · Frontiers in Aging · doi:10.3389/fragi.2023.1270838 · Cited by 18

Subcellular distribution and Nrf2/Keap1-interacting properties of Glutathione S-transferase P in hepatocellular carcinoma

Bartolini, D., Stabile, A. M., Migni, A., Gurrado, F., Lioci, G., Franco, F., Mandarano, M., Svegliati‐Baroni, G., Cristina, M. D., Bellezza, G., et al. (2024) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2024.110043 · Cited by 17

Dysregulation of Nrf2 Signaling in Diabetes: An Opportunity for a Multitarget Approach

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Signaling pathways and their potential therapeutic utility in esophageal squamous cell carcinoma

Kadian, L. K., Arora, M., Prasad, C. P., Pramanik, R., & Chauhan, S. S. (2022) · Clinical & Translational Oncology · doi:10.1007/s12094-021-02763-x · Cited by 17

The complex role of NRF2 in cancer: A genomic view

Praslicka, B. J., Kerins, M. J., & Ooi, A. (2016) · Current Opinion in Toxicology · doi:10.1016/j.cotox.2016.09.003 · Cited by 14

FBXW8 regulates G1 and S phases of cell cycle progression by restricting β‐TrCP1 function

Islam, S., Dutta, P., Chopra, K., Rapole, S., Chauhan, R., & Santra, M. K. (2021) · FEBS Journal · doi:10.1111/febs.15828 · Cited by 14

CaMKK2 alleviates myocardial ischemia/reperfusion injury by inhibiting oxidative stress and inflammation via the action on the AMPK-AKT-GSK-3β/Nrf2 signaling cascade

Li, C.-L., Hao, J., Qiu, H., & Xin, H. (2023) · Inflammation Research · doi:10.1007/s00011-023-01756-6 · Cited by 18

The bridge between cell survival and cell death: reactive oxygen species-mediated cellular stress

Acar, N. V., & Özgül, R. K. (2023) · EXCLI journal · doi:10.17179/excli2023-6221 · Cited by 19

NRF2 Modulators of Plant Origin and Their Ability to Overcome Multidrug Resistance in Cancers

Wadowski, P., Juszczak, M., & Woźniak, K. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252111500 · Cited by 14

Kelch-like ECH-associated Protein 1/Nuclear Factor Erythroid 2-related Factor 2 Pathway and Its Interplay with Oncogenes in Lung Tumorigenesis

Bae, T., & Kwak, M. (2024) · Journal of Cancer Prevention · doi:10.15430/jcp.24.021 · Cited by 15

Nrf2-related gene expression is impaired during a glucose challenge in type II diabetic rat hearts

Thorwald, M. A., Godoy-Lugo, J. A., Rodriguez, G. J., Rodriguez, M. A., Jamal, M., Kinoshita, H., Nakano, D., Nishiyama, A., Forman, H. J., & Ortiz, R. M. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.10.405 · Cited by 16

Sulfiredoxin-1 protects retinal ganglion cells from high glucose-induced oxidative stress and inflammatory injury by potentiating Nrf2 signaling via the Akt/GSK-3β pathway

Zhu, F., Shao, J., Tian, Y., & Xu, Z. (2021) · International Immunopharmacology · doi:10.1016/j.intimp.2021.108221 · Cited by 14

Comparison of toxic effects of atorvastatin and gemfibrozil on Daphnia magna

Hu, L., Ding, R., & Nie, X. (2021) · Comparative Biochemistry and Physiology Part C Toxicology & Pharmacology · doi:10.1016/j.cbpc.2021.109224 · Cited by 14

Selective Elimination of NRF2-Activated Cells by Competition With Neighboring Cells in the Esophageal Epithelium

Hirose, W., Horiuchi, M., Li, D., Motoike, I. N., Zhang, L., Nishi, H., Taniyama, Y., Kamei, T., Suzuki, M., Kinoshita, K., et al. (2022) · Cellular and Molecular Gastroenterology and Hepatology · doi:10.1016/j.jcmgh.2022.09.004 · Cited by 15

The role of modulation of antioxidant enzyme systems in the treatment of neurodegenerative diseases

Obuobi, S. A. O., Karatayev, S., Chai, C. L. L., Ee, P. L. R., & Mátyus, P. (2016) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.1080/14756366.2016.1205047 · Cited by 15

Role of Nrf2 in Oxidative and Inflammatory Processes in Obesity and Metabolic Diseases

Bayliak, M. M., & Abrat, O. (2020) · Progress in inflammation research · doi:10.1007/978-3-030-44599-7_7 · Cited by 14

The Effects of Ginsenosides on the Nrf2 Signaling Pathway

Ashrafizadeh, M., Ahmadi, Z., Yaribeygi, H., Sathyapalan, T., Jamialahmadi, T., & Sahebkar, A. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-73234-9_20 · Cited by 13

Alleviating effect of lycorine on CFA‑induced arthritic pain via inhibition of spinal inflammation and oxidative stress

Hu, Y.-D., Yue, Y.-F., Chen, T., Wang, Z., Ding, J.-Q., Xie, M., Dai, L., Zhu, H., & Cheng, M. (2023) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2023.11940 · Cited by 13

β-hydroxybutyrate recapitulates the beneficial effects of ketogenic metabolic therapy in polycystic kidney disease

Torres, J. A., Holznecht, N. J., Asplund, D. A., Kroes, B. C., Amarlkhagva, T., Haeffner, M. M., Sharpe, E. H., Koestner, S., Strubl, S., Schimmel, M. F., et al. (2024) · iScience · doi:10.1016/j.isci.2024.110773 · Cited by 13

Loss of PHLDA1 has a protective role in OGD/R-injured neurons via regulation of the GSK-3β/Nrf2 pathway

Yang, F., & Chen, R. (2021) · Human & Experimental Toxicology · doi:10.1177/09603271211014596 · Cited by 13

Monitoring Nrf2/ARE Pathway Activity with a New Zebrafish Reporter System

Badenetti, L., Manzoli, R., Rubin, M., Cozza, G., & Moro, E. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24076804 · Cited by 13

Nrf2 in Host Defense: Over the Rainbow

Cho, H., Kwak, M., & Pi, J. (2013) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2013/975839 · Cited by 13

Anticancer potential of metformin: focusing on gastrointestinal cancers

Khezri, M. R., Malekinejad, H., Zolbanin, N. M., & Ghasemnejad‐Berenji, M. (2021) · Cancer Chemotherapy and Pharmacology · doi:10.1007/s00280-021-04256-8 · Cited by 12

Nrf2-Keap1 Activation, A Promising Strategy in the Prevention of Cancer

Ojo, O. A., Ajiboye, B. O., Fadaka, A. O., Taro, P., & Shariati, M. A. (2016) · Free Radicals and Antioxidants · doi:10.5530/fra.2017.1.1 · Cited by 12

Upregulation of Glutaredoxin 2 alleviates oxygen-glucose deprivation/reoxygenation-induced apoptosis and ROS production in neurons by enhancing Nrf2 signaling via modulation of GSK-3β

Wen, J., Li, X., Zheng, S., & Xiao, Y. (2020) · Brain Research · doi:10.1016/j.brainres.2020.146946 · Cited by 12

NRF2 Dysregulation and Therapeutic Insights Across Chronic Kidney Diseases

Lim, T. S. T., Ng, K. H., & Zhang, Y. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26157471 · Cited by 14

AMPK-Mediated Phosphorylation of Nrf2 at S374/S408/S433 Favors Its βTrCP2-Mediated Degradation in KEAP1-Deficient Cells

Petsouki, E., Ender, S., Cabrera, S. N. S., & Heiß, E. H. (2023) · Antioxidants · doi:10.3390/antiox12081586 · Cited by 14

Dysregulation of intracellular redox homeostasis by the SARS-CoV-2 ORF6 protein

Angelis, M. D., Anichini, G., Palamara, A. T., Nencioni, L., & Savellini, G. G. (2023) · Virology Journal · doi:10.1186/s12985-023-02208-7 · Cited by 11

Glutathione S-transferase: A keystone in Parkinson's disease pathogenesis and therapy

Padhan, P., Simran, S., Kumar, N., & Verma, S. (2024) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2024.103981 · Cited by 12

Berberine triggers apoptosis through the PI3K/Akt pathways and Nrf2 by inducing ROS in papillary thyroid cancer

Li, J., Zhu, Z., Ni, J., Ye, L., Huang, X., Dong, J., Lu, Y., & Yue, L. (2025) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2025.110481 · Cited by 11

Elucidating the mechanistic interplay of AMPK and Nrf2 in MASLD: A focus on dietary phytochemical modulation of lipid and redox homeostasis

Yu, C. H. J., & Rupasinghe, H. P. V. (2025) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2025.152300 · Cited by 12

GM‐CSF suppresses antioxidant signaling and drives IL‐1β secretion through NRF2 downregulation

Carlo, S. D., Häcker, G. A., & Gentle, I. E. (2022) · EMBO Reports · doi:10.15252/embr.202154226 · Cited by 11

Dissecting the Keap1/Nrf2 pathway through proteomics

Tamir, T. Y., Mulvaney, K. M., & Major, M. B. (2016) · Current Opinion in Toxicology · doi:10.1016/j.cotox.2016.10.007 · Cited by 11

Therapeutic Potential of the Activators of the Nuclear Factor Erythroid 2-Related Factor 2–Antioxidant Response Element Pathway in Brain Disorders

Kume, T. (2017) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.b17-00091 · Cited by 11

Regulation of NRF2 by Na+/K+-ATPase: implication of tyrosine phosphorylation of Src

Nam, L. B., & Keum, Y. (2020) · Free Radical Research · doi:10.1080/10715762.2020.1735633 · Cited by 11

Paraoxonase 2 protects against oxygen-glucose deprivation/reoxygenation-induced neuronal injury by enhancing Nrf2 activation via GSK-3β modulation

Bai, J., Jia, P., Zhang, Y., Wang, K., & Wu, G. (2021) · Human & Experimental Toxicology · doi:10.1177/0960327121996032 · Cited by 11

Nrf2 induces malignant transformation of hepatic progenitor cells by inducing β-catenin expression

Fragoulis, A., Schenkel, J., Schröder, N., Brandt, E. F., Weiand, M., Neu, T., Ramadori, P., Caspers, T., Kant, S., Pufe, T., et al. (2022) · Redox Biology · doi:10.1016/j.redox.2022.102453 · Cited by 11

PML-Nuclear Bodies Regulate the Stability of the Fusion Protein Dendra2-Nrf2 in the Nucleus

Burroughs, A. F., Eluhu, S., Whalen, D. S., Goodwin, J. S., Sakwe, A. M., & Arinze, I. (2018) · Cellular Physiology and Biochemistry · doi:10.1159/000490033 · Cited by 11

NRF2 at the crossroads of Parkinson’s disease and aging: Mechanistic insights and translational perspectives

García‐Yagüe, Á. J., Esteras, N., Dinkova‐Kostova, A. T., Rojo, A. I., Shiels, P. G., Dinnyés, A., Tamas, V., van Goor, H., & Lastres‐Becker, I. (2026) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2026.01.023 · Cited by 12

Panax quinquefolius saponin inhibits vascular smooth muscle cell calcification via activation of nuclear factor-erythroid 2-related factor 2

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Nfe2l3 promotes neuroprotection and long-distance axon regeneration after injury in vivo

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Lycium barbarum polysaccharides exert an antioxidative effect on rat chondrocytes by activating the nuclear factor (erythroid-derived 2)-like 2 signaling pathway

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Heme oxygenase promotes B‐Raf‐dependent melanosphere formation

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Nuclear lamins and progerin are dispensable for antioxidant Nrf2 response to arsenic and cadmium

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Flavonoids as Modulators of Nrf2 Signaling Pathway in Alleviating Cisplatin-Induced Organ Toxicity

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Overexpression of angiotensinogen downregulates aquaporin 1 expression via modulation of Nrf2–HO-1 pathway in renal proximal tubular cells of transgenic mice

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Phytochemicals to regulate oxidative and electrophilic stress through Nrf2 activation

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Decreasing REDD1 expression protects against high glucose-induced apoptosis, oxidative stress and inflammatory injury in podocytes through regulation of the AKT/GSK-3β/Nrf2 pathway

Wang, X., Yang, J., Wang, W., Li, Y., & Yang, Y. (2023) · Immunopharmacology and Immunotoxicology · doi:10.1080/08923973.2023.2183351 · Cited by 9

SCF/-TrCP Promotes Glycogen Synthase Kinase 3-Dependent Degradation of the Nrf2 Transcription Factor in a Keap1-Independent Manner

Rada, P., Rojo, A. I., Chowdhry, S., Mcmahon, M., Hayes, J. D., & Cuadrado, A. (2011)

Structural and functional characterization of Nrf2 degradation by glycogen synthase kinase 3/β-TrCP

Cuadrado, A. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.04.029 · Cited by 272

Structural and Functional Characterization of Nrf2 Degradation by the Glycogen Synthase Kinase 3/β-TrCP Axis

Rada, P., Rojo, A. I., Evrard‐Todeschi, N., Innamorato, N. G., Cotte, A., Jaworski, T., Tobón-Velasco, J. C., Devijver, H., García‐Mayoral, M. F., LEUVEN, F. V., et al. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.00180-12 · Cited by 485

Nrf2 is controlled by two distinct β-TrCP recognition motifs in its Neh6 domain, one of which can be modulated by GSK-3 activity

Chowdhry, S., Zhang, Y., McMahon, M., Sutherland, C., Cuadrado, A., & Hayes, J. D. (2013) · Oncogene · doi:10.1038/onc.2012.388 · Cited by 657

Nrf2 is controlled by two distinct β-TrCP recognition motifs in its Neh6 domain, one of which can be modulated by GSK-3 activity. Oncogene 2013

Chowdhry, S., Zhang, Y., Mcmahon, M., Cuadrado, A., & Hayes, J. D. (2016)