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

Aberle, H., Bauer, A., Stappert, J., Kispert, A., & Kemler, R. (1997) · The EMBO Journal · doi:10.1093/emboj/16.13.3797 · Cited by 2,586

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

Zhou, B. P., Deng, J., Xia, W., Xu, J., Li, Y. M., Gunduz, M., & Hung, M.-C. (2004) · Nature Cell Biology · doi:10.1038/ncb1173 · Cited by 1,581

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

Skowyra, D., Craig, K. L., Tyers, M., Elledge, S. J., & Harper, J. W. (1997) · Cell · doi:10.1016/s0092-8674(00)80403-1 · Cited by 1,233

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

NRF2 signaling cascade in amyotrophic lateral sclerosis: bridging the gap between promise and reality

Tarot, P., Lasbleiz, C., & Liévens, J.-C. (2023) · Neural Regeneration Research · doi:10.4103/1673-5374.385283 · Cited by 9

Nrf2, A Target for Precision Oncology in Cancer Prognosis and Treatment

Ngo, H. K. C., Le, H., & Surh, Y. (2023) · Journal of Cancer Prevention · doi:10.15430/jcp.2023.28.4.131 · Cited by 9

Inhibition of sphingomyelin synthase 2 relieves hypoxia-induced cardiomyocyte injury by reinforcing Nrf2/ARE activation via modulation of GSK-3β

Jin, A., Cheng, H., Xia, L., Ye, S., & Yang, C. (2020) · Human & Experimental Toxicology · doi:10.1177/0960327120969958 · Cited by 9

Cardiac NF-κB Acetylation Increases While Nrf2-Related Gene Expression and Mitochondrial Activity Are Impaired during the Progression of Diabetes in UCD-T2DM Rats

Thorwald, M. A., Godoy-Lugo, J. A., Rodríguez, R., Stanhope, K. L., Graham, J. L., Havel, P. J., Forman, H. J., & Ortiz, R. M. (2022) · Antioxidants · doi:10.3390/antiox11050927 · Cited by 9

Protein Phosphorylation and Redox Status: An as Yet Elusive Dyad in Chronic Lymphocytic Leukemia

Pagano, M. A., Frezzato, F., Visentin, A., Trentin, L., & Brunati, A. M. (2022) · Cancers · doi:10.3390/cancers14194881 · Cited by 9

The Contribution of the Nrf2/ARE System to Mechanotransduction in Musculoskeletal and Periodontal Tissues

Fragoulis, A., Tohidnezhad, M., Kubo, Y., Wruck, C. J., Craveiro, R. B., Bock, A., Wolf, M. F., Pufe, T., Jahr, H., & Suhr, F. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24097722 · Cited by 10

Signalling pathways involved in paracetamol-induced hepatotoxicity: new insights on the role of protein tyrosine phosphatase 1B

Mobasher, M. A., & Valverde, Á. M. (2014) · Archives of Physiology and Biochemistry · doi:10.3109/13813455.2014.893365 · Cited by 9

A new copper ionophore DPMQ protects cells against ultraviolet B irradiation by inhibiting the TRPV1 channel

Huang, K., Ma, K., Hung, Y., Lo, L., Lin, K., Liu, P., Hu, M., & Chueh, S. (2018) · Journal of Cellular Physiology · doi:10.1002/jcp.26861 · Cited by 9

Nrf2 Activation Ameliorates Hepatotoxicity Induced by a Heme Synthesis Inhibitor

Taguchi, K., Masui, S., Itoh, T., Miyajima, A., & Yamamoto, M. P. (2018) · Toxicological Sciences · doi:10.1093/toxsci/kfy233 · Cited by 9

Revisiting Neuroblastoma: Nrf2, NF-κB and Phox2B as a Promising Network in Neuroblastoma

Peggion, S., Najem, S., Kolman, J. P., Reinshagen, K., & Raluy, L. P. (2024) · Current Issues in Molecular Biology · doi:10.3390/cimb46040200 · Cited by 8

Nrf2 in human cancers: biological significance and therapeutic potential

Tian, Y. (2024) · American Journal of Cancer Research · doi:10.62347/lzvo6743 · Cited by 9

The role of Nrf2 in immune cells and inflammatory autoimmune diseases: a comprehensive review

Xu, W., Yang, C., & Huang, A. (2024) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2024.2401518 · Cited by 8

A novel β-TrCP1/NRF2 interaction inhibitor for effective anti-inflammatory therapy

García‐Yagüe, Á. J., Cañizares-Moscato, L., Encinar, J. A., Cazalla, E., Fernández-Ginés, R., Escoll, M., Rojo, A. I., & Cuadrado, A. (2025) · Journal of Biomedical Science · doi:10.1186/s12929-025-01157-3 · Cited by 8

NRF2 activation in cancer and overview of NRF2 small molecule inhibitors

Ngo, H. H., Yu, B.-Y., Lee, J., Kim, H. W., & Keum, Y. (2025) · Archives of Pharmacal Research · doi:10.1007/s12272-025-01557-x · Cited by 9

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

Perilipin 5 protects against oxygen-glucose deprivation/reoxygenation-elicited neuronal damage by inhibiting oxidative stress and inflammatory injury via the Akt-GSK-3β-Nrf2 pathway

Huo, K., Ma, K.-G., Guo, Q.-Y., Duan, P., & Xu, J. B. (2022) · International Immunopharmacology · doi:10.1016/j.intimp.2022.108718 · Cited by 8

TRPV1 Modulator Ameliorates Alzheimer‐Like Amyloid‐β Neuropathology via Akt/Gsk3β‐Mediated Nrf2 Activation in the Neuro‐2a/APP Cell Model

Wang, X., Bian, Y., Wong, C. T. T., Lu, J., & Lee, S. M. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/1544244 · Cited by 8

Downregulation of PHLPP1 ameliorates high glucose-evoked injury in retinal ganglion cells by attenuating apoptosis and oxidative stress through enhancement of Nrf2 activation

Zhang, X., Lu, Y. F., He, N., & Wang, F. (2020) · Experimental Cell Research · doi:10.1016/j.yexcr.2020.112344 · Cited by 8

Noncoding RNAs Associated with Therapeutic Resistance in Pancreatic Cancer

Son, S. W., Song, M. G., Yun, B. D., & Park, J. K. (2021) · Biomedicines · doi:10.3390/biomedicines9030263 · Cited by 8

The HO-1/CO System and Mitochondrial Quality Control in Skeletal Muscle

Gasier, H. G., Suliman, H. B., & Piantadosi, C. A. (2021) · Exercise and Sport Sciences Reviews · doi:10.1249/jes.0000000000000277 · Cited by 8

Protein levels in Keap1-Nrf2 system in human failing heart

Konishi, M., Baumgarten, A., Ishida, J., Saitoh, M., Anker, S. D., & Springer, J. (2016) · International Journal of Cardiology · doi:10.1016/j.ijcard.2016.09.128 · Cited by 8

Mutual regulation between β-TRCP mediated REST protein degradation and Kv1.3 expression controls vascular smooth muscle cell phenotype switch

Ye, M., Guo, X., Wang, H., Wang, Y., Qian, X., Deng, H., Wang, W., Yang, S., Ni, Q., Chen, J., et al. (2020) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2020.08.018 · Cited by 8

Nrf2-Mediated Signaling as a Therapeutic Target in Alzheimer’s Disease

Bitra, V. R., Moshapa, F. T., Adiukwu, P. C., & Rapaka, D. (2024) · The Open Neurology Journal · doi:10.2174/011874205x319474240611070113 · Cited by 7

Structural and Dynamic Characterization of Mutated Keap1 for Varied Affinity toward Nrf2: A Molecular Dynamics Simulation Study

Cheng, I.-C., Chen, Y., Ku, C., Huang, Y.-W., & Yang, C. (2015) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.5b00300 · Cited by 9

Simvastatin-Mediated Nrf2 Activation Induces Fetal Hemoglobin and Antioxidant Enzyme Expression to Ameliorate the Phenotype of Sickle Cell Disease

Xi, C., Palani, C. D., Takezaki, M., Shi, H., Horuzsko, A., Pace, B. S., & Zhu, X. (2024) · Antioxidants · doi:10.3390/antiox13030337 · Cited by 7

Vigor King mitigates spermatogenic disorders caused by environmental estrogen zearalenone exposure

Zuo, N., Wang, R. T., Bian, W.-M., Liu, X., Han, B. Q., Wang, J., Shen, W., & Li, L. (2024) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2024.116757 · Cited by 7

Modulated Expression of the Protein Kinase GSK3 in Motor and Dopaminergic Neurons Increases Female Lifespan in Drosophila melanogaster

Trostnikov, M. V., Veselkina, E. R., Krementsova, A. V., Boldyrev, S. V., Roshina, N. V., & PASYUKOVA, E. G. (2020) · Frontiers in Genetics · doi:10.3389/fgene.2020.00668 · Cited by 7

Degradation of human Lipin-1 by BTRC E3 ubiquitin ligase

Ishimoto, K., Hayase, A., Kumagai, F., Kawai, M., Okuno, H., Hino, N., Okada, Y., Kawamura, T., Tanaka, T., Hamakubo, T., et al. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2017.04.159 · Cited by 7

Interactive structural analysis of βTrCP1 and PER2 phosphoswitch binding through dynamics simulation assay

Najumuddin, Fakhar, M., Gul, M., & Rashid, S. (2018) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2018.05.020 · Cited by 7

15-Keto prostaglandin E2 induces heme oxygenase-1 expression through activation of Nrf2 in human colon epithelial CCD 841 CoN cells

Lee, J., Zhong, X., Lee, J.-Y., Surh, Y., & Na, H. (2019) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2019.108162 · Cited by 7

WIP Modulates Oxidative Stress through NRF2/KEAP1 in Glioblastoma Cells

Escoll, M., Lastra, D., Robledinos-Antón, N., Wandosell, F. G., Antón, I. M., & Cuadrado, A. (2020) · Antioxidants · doi:10.3390/antiox9090773 · Cited by 7

The role of Nrf2 in autoimmunity and infectious disease: Therapeutic possibilities

Freeborn, R. A., & Rockwell, C. E. (2021) · Advances in pharmacology · doi:10.1016/bs.apha.2020.10.003 · Cited by 7

Redox Signaling and the Onset of the Inflammatory Cascade

Vázquez‐Medina, J. P. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-805417-8.00003-2 · Cited by 8

β-Caryophyllene (CB2 agonist) mitigates rotenone-induced neurotoxicity and apoptosis in SH-SY5Y neuroblastoma cells via modulation of GSK-3β/NRF2/HO-1 axis

Rathod, S., & Agrawal, Y. O. (2025) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-025-04281-x · Cited by 6

Iron-catalyzed oxidative stress compromises cancer promotional effect of BRCA2 haploinsufficiency through mitochondria-targeted ferroptosis

Maeda, Y. K., Motooka, Y., Akatsuka, S., Tanaka, H., Mashimo, T., & Toyokuni, S. (2025) · Redox Biology · doi:10.1016/j.redox.2025.103739 · Cited by 6

Advancements and perspectives of RBX2 as a molecular hallmark in cancer

Tao, Y., Dai, L., Liang, W., Li, X., Lyu, Y., Li, J., Li, Z., Shi, Z., Liang, X., Zhou, S., et al. (2023) · Gene · doi:10.1016/j.gene.2023.147864 · Cited by 6

Acute accumulation of PIM2 and NRF2 and recovery of β5 subunit activity mitigate multiple myeloma cell susceptibility to proteasome inhibitors

Sogabe, K., Nakamura, S., Higa, Y., Miki, H., Oda, A., Maruhashi, T., Sumitani, R., Oura, M., Takahashi, M., Nakamura, M., et al. (2024) · International Journal of Hematology · doi:10.1007/s12185-023-03705-9 · Cited by 6

Effects of Akt Activator SC79 on Human M0 Macrophage Phagocytosis and Cytokine Production

Lee, R. J., Adappa, N. D., & Palmer, J. N. (2024) · Cells · doi:10.3390/cells13110902 · Cited by 7

The Role of FBXW Subfamily of F-box Proteins in Tumorigenesis

Lau, A. W., Liu, Y., Tron, A. E., Inuzuka, H., & Wei, W. (2014) · Springer eBooks · doi:10.1007/978-3-319-05026-3_2 · Cited by 6

Aucubin provides protection against cerebral ischaemia-reperfusion injury by suppressing neuronal apoptosis, oxidative stress, and inflammation through the modulation of the AKT-GSK-3β-Nrf2 signal cascade

Fang, Y., Lian, Q., Zhang, X., Sun, F., Jia, S., & Zhao, W. (2024) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2024.116829 · 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

CDGSH iron sulfur domain 2 mitigates apoptosis, oxidative stress and inflammatory response caused by oxygen–glucose deprivation/reoxygenation in HT22 hippocampal neurons by Akt-Nrf2-activated pathway

Ren, X., Yu, J., Guo, L., & Zhang, Z. (2022) · Metabolic Brain Disease · doi:10.1007/s11011-022-01043-z · Cited by 5

New insights into the regulation of Cystathionine beta synthase (CBS), an enzyme involved in intellectual deficiency in Down syndrome

Conan, P., Léon, A., Caroff, N., Rollet, C., Chaïr, L., Martin, J., Bihel, F. J. ‐., Mignen, O., Voisset, C., & Friocourt, G. (2023) · Frontiers in Neuroscience · doi:10.3389/fnins.2022.1110163 · Cited by 5

The KEAP1-NRF2 system and neurodegenerative diseases

Uruno, A., & Yamamoto, M. P. (2023) · Antioxidants and Redox Signaling · doi:10.1089/ars.2023.0005 · Cited by 8

Aripiprazole increases NAD(P)H–quinone oxidoreductase-1 and heme oxygenase-1 in PC12 cells

Kaneko, Y. S., Takayanagi, T., Nagasaki, H., Kodani, Y., Nakashima, A., Mori, K., Suzuki, A., Itoh, M., Kondo, K., Nagatsu, T., et al. (2014) · Journal of Neural Transmission · doi:10.1007/s00702-014-1350-8 · Cited by 5

Dual targeting of Keap1 and Gsk-3 by hexaraphane in the regulation of transcription factor Nrf2

García‐Yagüe, Á. J., Cueto-Diaz, E. J., Escoll, M., Okunishi, I., Hayes, J. D., Rodrı́guez-Franco, M. I., Rojo, A. I., & Cuadrado, A. (2025) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2025.07.051 · Cited by 4

TRPA1 activation prompts lysosome-mediated Nrf2 degradation enhancing the killing of colorectal cancer cells

Eskandari, N., Delisi, D., Saatloo, M. V., Keceli, G., Pinheiro, N., Eblen, S. T., Paolocci, N., & Gentile, S. (2025) · Redox Biology · doi:10.1016/j.redox.2025.103942 · Cited by 4

Anticancer Effect of C19-Position Substituted Geldanamycin Derivatives Targeting NRF2-NQO1-activated Esophageal Squamous Cell Carcinoma

Oshikiri, H., Taguchi, K., Hirose, W., Taniyama, Y., Kamei, T., Siegel, D. M., Ross, D., Kitson, R. R. A., Baird, L., & Yamamoto, M. P. (2024) · Molecular and Cellular Biology · doi:10.1080/10985549.2024.2438817 · Cited by 4

Nrf2 Regulates the Expression of CYP2D6 by Inhibiting the Activity of Krüppel-Like Factor 9 (KLF9)

Siswanto, F. M., Handayani, M. D. N., Firmasyah, R. D., Oguro, A., & Imaoka, S. (2023) · Current Drug Metabolism · doi:10.2174/0113892002271342231013095255 · Cited by 4

Transcription Factor NRF2 in Endothelial Functions

Kondratenko, N. D., Zinovkina, L. A., & Zinovkin, R. A. (2023) · Molecular Biology · doi:10.1134/s0026893323060092 · Cited by 4

Transcription factor NF-E2-related factor 2 plays a critical role in acute lung injury/acute respiratory distress syndrome (ALI/ARDS) by regulating ferroptosis

Deng, J., Li, N., Hao, L., Li, S., Nie, A., Zhang, J., & Hu, X. (2024) · PeerJ · doi:10.7717/peerj.17692 · Cited by 4

GSKIP protects cardiomyocytes from hypoxia/reoxygenation-induced injury by enhancing Nrf2 activation via GSK-3β inhibition

Li, Y., Cheng, G., & Yang, G. (2020) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2020.06.029 · Cited by 4

Sulfhydryl-Reactive Phytochemicals as Dual Activators of Transcription Factors NRF2 and HSF1

Dinkova‐Kostova, A. T., Zhang, Y., Naidu, S. D., Kostov, R. V., Pheely, A., & Calabrese, V. (2013) · Springer eBooks · doi:10.1007/978-3-319-00581-2_6 · Cited by 4

Antioxidant defense of Nrf2vspro-inflammatory system of NF-κB during the amoebic liver infection in hamster

Aldaba-Muruato, L. R., Muñoz‐Ortega, M. H., Campos-Esparza, M. D. R., Macías-Pérez, J. R., MÁRQUEZ-MUÑOZ, N. A., VILLALOBOS-SANTOS, A. G., & Ventura‐Juárez, J. (2016) · Parasitology · doi:10.1017/s0031182016001967 · Cited by 4

Nuclear factor erythroid 2-related factor 2 (Nrf2) inhibition revisited: advances and unmet challenges

Lu, M., Yang, Z., Xin, Y., Zhang, Y., Jiang, S., Zhu, J., You, Q., Zhao, Z., & Jiang, Z. (2026) · Journal of Advanced Research · doi:10.1016/j.jare.2026.05.030 · Cited by 3

Nuclear factor erythroid 2-related factor 2 in Alzheimer's disease

Murphy, K. E., & Park, J. J. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-815868-5.00015-3 · Cited by 3

Pharmacological effects of methysticin and L-sulforaphane through the Nrf2/ARE signaling pathway in MLO-Y4 osteocytes: in vitro study

Dittmar, M. C., Tohidnezhad, M., Fragoulis, A., Bücker, A., Stein, M., Pufe, T., & Kubo, Y. (2024) · Annals of Anatomy - Anatomischer Anzeiger · doi:10.1016/j.aanat.2024.152260 · Cited by 3

Study on the response mechanism of MicroRNA novel-13 and novel-44 to Vibrio parahaemolyticus infection in Pinctada fucata martensii

Li, C., Zhang, Q., Zhang, B., Liang, H. Y., Ma, L. N., & Salman, M. (2025) · BMC Veterinary Research · doi:10.1186/s12917-024-04467-0 · Cited by 3

Cisplatin-induced acute kidney injury increased brain 5-hydroxytryptamine levels partly due to the hippuric acid–induced upregulation of CYP2D4 expression and function in the brain of rats

Lu, L.-J., Hu, N., Chen, H., Wang, S., Deng, Y. J., Lin, Z., Wang, Z., Zhu, X., Liu, X., Liu, L., et al. (2025) · Drug Metabolism and Disposition · doi:10.1016/j.dmd.2025.100068 · Cited by 3

NRF2-mediated persistent adaptation of oesophageal adenocarcinoma cells to HER2 inhibition

Zhang, W., Lang, J., Chattrakarn, S., Wong, C. W., Li, S.-Y., Kan, K., Liu, H., Gu, W., Zhang, J., Westermarck, J. K., et al. (2025) · Oncogene · doi:10.1038/s41388-025-03459-0 · Cited by 3

The Role of Nonneuronal Nrf2 Pathway in Ischemic Stroke: Damage Control and Potential Tissue Repair

Yang, T., Sun, Y., & Zhang, F. (2016) · Springer series in translational stroke research · doi:10.1007/978-3-319-32337-4_18 · Cited by 3

Sulforaphane alleviates hypoxic vestibular vertigo (HVV) by increasing NO production via upregulating the expression of NRF2

Zhou, L., Hu, C., Li, Y., & Wang, B. (2022) · Bioengineered · doi:10.1080/21655979.2022.2030592 · Cited by 3

Identification of NRF2 Activation as a Prognostic Biomarker in T-Cell Acute Lymphoblastic Leukaemia

Villa‐Morales, M., Pérez-Gómez, L., Pérez-Gómez, E., López‐Nieva, P., Fernández‐Navarro, P., & Santos, J. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241210350 · Cited by 4

Key Transcription Factors Linking Macular Degeneration and Alzheimer’s Disease

Eichenbaum, J. W. (2019) · World Journal of Ophthalmology & Vision Research · doi:10.33552/wjovr.2019.01.000516 · Cited by 3

Neurochemical Aspects of Oxidative and Nitrosative Stress

Farooqui, A. A. (2014) · Springer eBooks · doi:10.1007/978-3-319-04111-7_6 · Cited by 3

Behavioral Risk Factors

Thiriet, M. (2018) · Biomathematical and biomechanical modeling of the circulatory and ventilatory systems · doi:10.1007/978-3-319-89315-0_6 · Cited by 3

Adenosine/A 2A R/PKA signaling regulates HO-1-mediated anti-inflammatory responses during Leishmania donovani infection

Das, T., Brahmachari, P., & Ukil, A. (2025) · mBio · doi:10.1128/mbio.02581-25 · Cited by 2

Modulation of the Receptor Tyrosine Kinase TIE2/Tek Pathway by NRF2 Activation in Neurovascular Endothelial Cells

Cazalla, E., García‐Yagüe, Á. J., Pajares, M., Jiménez-Villegas, J., Escoll, M., Rojo, A. I., & Cuadrado, A. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27020770 · Cited by 2

Aging-associated GSK3β overexpression exacerbates hepatic ischemia-reperfusion injury through Nrf2 deficiency-induced hepatocyte ferroptosis

Wu, Y., Zhang, Y., Zhang, S., Yang, H., & Ci, X. (2026) · Life Sciences · doi:10.1016/j.lfs.2026.124214 · Cited by 2

1,1-Diethoxyethane enhances aerobic respiration in human mitochondria via activation of AMP-activated protein kinase

Huu, T. N., Thanh, H. D., Kim, M., Sah, D. K., Trinh, V. H., Yoon, H.-J., Choi, J. M., Lee, G.-H., Kim, S., & Lee, S.-R. (2026) · Communications Biology · doi:10.1038/s42003-026-09797-3 · Cited by 2

NRF2 as a Therapeutic Target in Dermatological Disorders: Mechanisms and Molecules

Khiar-Fernández, I., Khiar‐Fernández, N., Pereyra-Rodríguez, J.-J., & Fernández, I. (2026) · Pharmaceuticals · doi:10.3390/ph19030497 · Cited by 6

AMPK as a regulatory node in cell death

Rong, D., You, S., & Shen, H. (2026) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2026.02.006 · Cited by 3

Targeting the Interaction of NRF2 and β-TrCP with Molecular Glues

O’Donovan, D. H., Winter-Holt, J. J., Collie, G. W., Cuomo, M. E., McGarry, D., Fox, M., Seong, B. K. A., Grazini, U., Barton, P., Longmire, D., et al. (2026) · ACS Chemical Biology · doi:10.1021/acschembio.5c01006 · Cited by 2

Targeting NRF2 addiction in cancer: synthetic lethal strategies beyond direct inhibition

Gebru, M. T., & Stokoe, D. (2026) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2026.1856014 · Cited by 2

Inhibition of NRF2 signaling overcomes acquired resistance to arsenic trioxide in FLT3-mutated Acute Myeloid Leukemia

Jebanesan, D. Z. P., Illangeswaran, R. S. S., Rajamani, B. M., Vidhyadharan, R. T., Das, S., Bijukumar, N. K., Balakrishnan, B., Mathews, V., Velayudhan, S. R., & Balasubramanian, P. (2024) · Annals of Hematology · doi:10.1007/s00277-024-05742-8 · Cited by 2

The deubiquitinating enzyme USP35 regulates the stability of NRF2 protein

Zhang, D., Li, J., Zhang, C., Xue, J., Li, P., Shang, K., Zhang, X., & Lang, B. (2024) · Open Life Sciences · doi:10.1515/biol-2022-0935 · Cited by 2

Nrf2 signaling pathway activation through Keap1-dependent and -independent mechanisms in response to acute benzo[a]pyrene exposure in Mytilus coruscus

Chen, Y., Zhu, L., Ye, Y., Song, M., Wang, W., Shen, B. Q., Guo, B., Yan, X., & Qi, P. (2025) · Aquatic Toxicology · doi:10.1016/j.aquatox.2025.107513 · Cited by 2

Targeting the Keap1/Nrf2 axis in cancer: molecular mechanisms and pharmacological interventions

Xia, Y., Xu, Z., Yuan, X., & Chu, Q. (2025) · Investigational New Drugs · doi:10.1007/s10637-025-01578-9 · Cited by 2

NRF2 and Age-Dependent RPE Degeneration

Chen, Y., Zhao, Z., Sternberg, P. W., & Cai, J. (2012) · InTech eBooks · doi:10.5772/28167 · Cited by 2

The GSK3-NRF2 Axis in Suicide

Kalkman, H. O. (2021) · Psychiatry International · doi:10.3390/psychiatryint2010008 · Cited by 2

Sensing Oxidative Stress: The NRF2 Signaling Pathway

de la Vega, M. R., Dodson, M. B., & Zhang, D. D. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-801238-3.95613-7 · Cited by 1

Scope of Theoretical Approaches Studying the Ligand-Nrf2 Interactions

Soriano-Ursua, M. A., Ocampo-Néstor, A. L., Rosalez, M. N., Farfán‐García, E. D., Madrigal‐Santillán, E., Morales‐González, Á., & Morales‐González, J. A. (2024) · IntechOpen eBooks · doi:10.5772/intechopen.1007160 · Cited by 1

Cyclic vinyl sulfones activate NRF2 to protect from oxidative stress-induced programmed necrosis

Davidovich, P. B., Nikolaev, D., Khadiullina, R., Gurzhiy, V. V., & Bulatov, E. (2024) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2024.130058 · Cited by 1

Exploring the Impact of NRF2 Signaling on Atherosclerosis: Insights Into Hydrogen Sulfide, NLRP3 Inflammasome, microRNAs, and HO‐1

Shao, C., Feng, X., Hao, R., Chen, Y., Zhang, T., Yan, S., Chen, Y., Wang, X., & Luo, H. (2025) · Cell Biochemistry and Function · doi:10.1002/cbf.70149 · Cited by 1

GSK3β-mediated NRF2 degradation drives Escherichia coli-induced ferroptosis in the bovine endometrium

Yuan, C., Dong, P., Wang, J., Mao, P., Wang, Z., Dong, J., Guo, L., Liu, K., Cui, L., Li, J., et al. (2025) · Veterinary Research · doi:10.1186/s13567-025-01675-w · Cited by 2

Protective effects of Ganoderma lucidum polysaccharide peptides against cisplatin-induced toxicity

Hou, Z., Ji, W., Yang, S., Zhang, Y., Yang, T., Wang, L.-F., Luo, H., Lin, D., Yang, B., Chen, X., et al. (2026) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2026.121210 · Cited by 1

Multi-pathway and gut microbiota mechanisms underlying the antioxidant effects of formononetin

薛梅, Kong, L., Chen, Y., Hou, L., & Hou, J. (2026) · South African Journal of Botany · doi:10.1016/j.sajb.2026.04.023 · Cited by 1

Nitric oxide redox signaling as a convergent mechanism in aging and fibrosis

Guo, X., Cao, Y., Liu, L., Peng, Y., Du, Y., Yang, F., & Huang, D. (2026) · Ageing Research Reviews · doi:10.1016/j.arr.2026.103156 · Cited by 1

Multiple Modes of Nrf2 Regulation and Transcriptional Response

Mathew, S. T., & Hammarsten, O. (2016) · InTech eBooks · doi:10.5772/65295 · Cited by 1

Sulforaphane and mitochondria

Zyla, K., & Plafker, S. M. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-821562-3.00042-3 · Cited by 1

Photoperiod affects oxidative stress in the liver of Cricetulus barabensis through the Nrf2-Keap1 signaling pathway

Wang, X.-C., Wang, Z., Wang, C.-L., Xue, H.-L., Wu, M., Chen, L., Fan, C., Xu, J.-H., & Xu, L. (2023) · Biological Rhythm Research · doi:10.1080/09291016.2023.2252221 · Cited by 1

ncRNAs Orchestrate Chemosensitivity Induction by Neddylation Blockades

Pérez-González, A., Ramírez‐Díaz, I., Guzmán-Linares, J., Sarvari, P., Sarvari, P., & Rubio, K. (2024) · Cancers · doi:10.3390/cancers16040825 · Cited by 1

A new mouse strain with mutation in the NFE2L2 (NRF2 gene

Egorov, E. S., Kondratenko, N. D., Averina, O. A., Permyakov, O. A., Emelyanova, M., Prikhodko, A. S., Zinovkina, L. A., Владимирович, С. П., & Zinovkin, R. A. (2023) · Biochemistry (Moscow) · doi:10.31857/s0320972523120035 · Cited by 1

USP37 as a novel regulator of NRF2 protein stability and chemoresistance in HCC

Zhang, S., Ding, F., Jia, F., & Lu, X. (2025) · Discover Oncology · doi:10.1007/s12672-025-01913-9 · Cited by 1

Regulation of Antioxidant Nrf2 Signaling: An Important Pathway in COPD

Chatterjee, N., & Chatterjee, D. (2019) · Springer eBooks · doi:10.1007/978-981-32-9366-3_7 · Cited by 1

Reactive oxygen species, redox signaling, and regulation of vascular endothelial signaling

Allen, K. N., & Vázquez‐Medina, J. P. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-816196-8.00011-4 · Cited by 1

Nuclear factor erythroid 2-related factor 2-mediated antioxidant response as an indicator of oxidative stress

Wang, H., Liu, S., Guo, J., Deng, T., Fu, J., Xu, Y., Qu, W., Zhang, Q., & Pi, J. (2021) · Elsevier eBooks · doi:10.1016/b978-0-323-85215-9.00035-0 · Cited by 1

Regulation of NRF2 signaling pathway and the hallmarks of aging: An overview

Medoro, A., Scapagnini, G., & Davinelli, S. (2023) · Elsevier eBooks · doi:10.1016/b978-0-443-19247-0.00004-7 · Cited by 1

Targeting Nrf2 in inflammation and cancer

Cowan, J. (2014) · UEA Digital Repository (University of East Anglia) · Cited by 1

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)