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 2,533 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 1,262 · see citing works

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 · see citing works

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 1,227 · see citing works

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 · see citing works

The Keap1-BTB Protein Is an Adaptor That Bridges Nrf2 to a Cul3-Based E3 Ligase: Oxidative Stress Sensing by a Cul3-Keap1 Ligase

Cullinan, S. B., Gordan, J. D., Jin, J., Harper, J. W., & Diehl, J. A. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.19.8477-8486.2004 · Cited by 986 · see citing works

Ubiquitin-dependent c-Jun degradation in vivo is mediated by the δ domain

Treier, M., Staszewski, L. M., & Bohmann, D. (1994) · Cell · doi:10.1016/s0092-8674(94)90502-9 · Cited by 928 · see citing works

A complex of Cdc4p, Skp1p, and Cdc53p/cullin catalyzes ubiquitination of the phosphorylated CDK inhibitor Sic1p.

Feldman, R. M. R., Correll, C. C., Kaplan, K. B., & Deshaies, R. J. (1997) · Cell · doi:10.1016/s0092-8674(00)80404-3 · Cited by 872 · see citing works

NRF2 and KEAP1 mutations: permanent activation of an adaptive response in cancer

Hayes, J. D., & McMahon, M. J. (2009) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2008.12.008 · Cited by 870 · see citing works

Nrf2–Keap1 regulation of cellular defense mechanisms against electrophiles and reactive oxygen species

Kobayashi, M., & Yamamoto, M. P. (2006) · Advances in Enzyme Regulation · doi:10.1016/j.advenzreg.2006.01.007 · Cited by 855 · see citing works

Decline in transcriptional activity of Nrf2 causes age-related loss of glutathione synthesis, which is reversible with lipoic acid

Suh, J. H., Shenvi, S. V., Dixon, B. M., Liu, H., Jaiswal, A. K., Liu, R.-M., & Hagen, T. M. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0400282101 · Cited by 774 · see citing works

BTB Protein Keap1 Targets Antioxidant Transcription Factor Nrf2 for Ubiquitination by the Cullin 3-Roc1 Ligase

Furukawa, M., & Xiong, Y. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.25.1.162-171.2005 · Cited by 746 · see citing works

Cancer related mutations in <i>NRF2</i> impair its recognition by Keap1-Cul3 E3 ligase and promote malignancy

Shibata, T., Ohta, T., Tong, K. I., Kokubu, A., Odogawa, R., Tsuta, K., Asamura, H., Yamamoto, M., & Hirohashi, S. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0806268105 · Cited by 728 · see citing works

Regulation of Heme Oxygenase-1 Expression through the Phosphatidylinositol 3-Kinase/Akt Pathway and the Nrf2 Transcription Factor in Response to the Antioxidant Phytochemical Carnosol

Martı́n, D., Rojo, A. I., Salinas, M., Díaz, R. G., Gallardo, G., Alam, J., de Galarreta, C. M. R., & Cuadrado, A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m309660200 · Cited by 698 · see citing works

Pharmacological inhibitors of glycogen synthase kinase 3

Meijer, L., Flajolet, M., & Greengard, P. (2004) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2004.07.006 · Cited by 586 · see citing works

Regulation of the antioxidant response element by protein kinase C-mediated phosphorylation of NF-E2-related factor 2

Huang, H.-C., Nguyen, T., & Pickett, C. B. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.220418997 · Cited by 539 · see citing works

Glycogen Synthase Kinase-3β Inhibits the Xenobiotic and Antioxidant Cell Response by Direct Phosphorylation and Nuclear Exclusion of the Transcription Factor Nrf2

Salazar‐Roa, M., Rojo, A. I., Velasco, D., de Sagarra, R. M., & Cuadrado, A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m513737200 · Cited by 523 · see citing works

Sonic hedgehog Signaling Regulates Gli2 Transcriptional Activity by Suppressing Its Processing and Degradation

Pan, Y., Bai, C. B., Joyner, A. L., & Wang, B. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.9.3365-3377.2006 · Cited by 519 · see citing works

Dimerization of Substrate Adaptors Can Facilitate Cullin-mediated Ubiquitylation of Proteins by a “Tethering” Mechanism

McMahon, M. J., Thomas, N., Itoh, K., Yamamoto, M. P., & Hayes, J. D. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m601119200 · Cited by 489 · see citing works

The Transcription Factor Nrf2 Is a Therapeutic Target against Brain Inflammation

Innamorato, N. G., Rojo, A. I., García‐Yagüe, Á. J., Yamamoto, M. P., CEBALLOS, M. L. D., & Cuadrado, A. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.181.1.680 · Cited by 479 · see citing works

The human F box protein β-Trcp associates with the Cul1/Skp1 complex and regulates the stability of β-catenin

Latres, E., Chiaur, D. S., & Pagano, M. (1999) · Oncogene · doi:10.1038/sj.onc.1202653 · Cited by 442 · see citing works

The Nrf2/ARE Pathway as a Potential Therapeutic Target in Neurodegenerative Disease

Calkins, M. J., Johnson, D. A., Townsend, J. A., Vargas, M. R., Dowell, J. A., Williamson, T. P., Kraft, A. D., Lee, J., Li, J., & Johnson, J. A. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2242 · Cited by 440 · see citing works

Nrf2 Enhances Cell Proliferation and Resistance to Anticancer Drugs in Human Lung Cancer

Homma, S., Ishii, Y., Morishima, Y., Yamadori, T., Matsuno, Y., Haraguchi, N., Kikuchi, N., Satoh, H., Sakamoto, T., Hizawa, N., et al. (2009) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-08-2822 · Cited by 417 · see citing works

Redox-regulated Turnover of Nrf2 Is Determined by at Least Two Separate Protein Domains, the Redox-sensitive Neh2 Degron and the Redox-insensitive Neh6 Degron

McMahon, M. J., Thomas, N., Itoh, K., Yamamoto, M. P., & Hayes, J. D. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m403061200 · Cited by 406 · see citing works

Degradation of Mcl-1 by β-TrCP Mediates Glycogen Synthase Kinase 3-Induced Tumor Suppression and Chemosensitization

Ding, Q., He, X., Hsu, J.-M., Xia, W., Chen, C., Li, L., Lee, D., Liu, J.-C., Zhong, Q., Wang, X., et al. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00620-06 · Cited by 396 · see citing works

Phosphorylation of Nrf2 at Multiple Sites by MAP Kinases Has a Limited Contribution in Modulating the Nrf2-Dependent Antioxidant Response

Sun, Z., Huang, Z., & Zhang, D. D. (2009) · PLoS ONE · doi:10.1371/journal.pone.0006588 · Cited by 362 · see citing works

Evidence for the direct involvement of βTrCP in Gli3 protein processing

Wang, B., & Li, Y. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0509927103 · Cited by 273 · see citing works

GSK‐3β down‐regulates the transcription factor Nrf2 after oxidant damage: relevance to exposure of neuronal cells to oxidative stress

Rojo, A. I., de Sagarra, M. R., & Cuadrado, A. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.05124.x · Cited by 241 · see citing works

The rise of antioxidant signaling—The evolution and hormetic actions of Nrf2

Maher, J. M., & Yamamoto, M. P. (2010) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2010.01.011 · Cited by 231 · see citing works

Phosphorylation of Nrf2 in the transcription activation domain by casein kinase 2 (CK2) is critical for the nuclear translocation and transcription activation function of Nrf2 in IMR‐32 neuroblastoma cells

Apopa, P. L., He, X., & Ma, Q. (2008) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.20212 · Cited by 230 · see citing works

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

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

Molecular mechanism of human Nrf2 activation and degradation: Role of sequential phosphorylation by protein kinase CK2

Pi, J., Bai, Y., Reece, J. M., Williams, J. G., Liu, D., Freeman, M. L., Fahl, W. E., Shugar, D., Liu, J., Qu, W., et al. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.03.001 · Cited by 212 · see citing works

Inhibition of PKB/Akt1 by C2-Ceramide Involves Activation of Ceramide-Activated Protein Phosphatase in PC12 Cells

Salinas, M., López‐Valdaliso, R., Martı́n, D., Alvarez, A. M., & Cuadrado, A. (2000) · Molecular and Cellular Neuroscience · doi:10.1006/mcne.1999.0813 · Cited by 199 · see citing works

Nrf2 as a target for cancer chemoprevention

Yu, X. Y., & Kensler, T. W. (2005) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2005.04.017 · Cited by 199 · see citing works

WNT-1 and HGF Regulate GSK3β Activity and β-Catenin Signaling in Mammary Epithelial Cells

Papkoff, J., & Aikawa, M. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.8888 · Cited by 184 · see citing works

Ceramide and Reactive Oxygen Species Generated by H2O2 Induce Caspase-3-independent Degradation of Akt/Protein Kinase B

Martı́n, D., Salinas, M., Fujita, N., Tsuruo, T., & Cuadrado, A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201070200 · Cited by 168 · see citing works

GSK-3β Targets Cdc25A for Ubiquitin-Mediated Proteolysis, and GSK-3β Inactivation Correlates with Cdc25A Overproduction in Human Cancers

Kang, T., Wei, Y., Honaker, Y., Yamaguchi, H., Appella, E., Hung, M., & Piwnica-Worms, H. M. (2008) · Cancer Cell · doi:10.1016/j.ccr.2007.12.002 · Cited by 162 · see citing works

The transcription factor Nrf2 as a new therapeutic target in Parkinson's disease

Cuadrado, A., Moreno-Murciano, P., & Pedraza‐Chaverrí, J. (2009) · Expert Opinion on Therapeutic Targets · doi:10.1517/13543780802716501 · Cited by 135 · see citing works

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 132 · see citing works

Nrf2 promotes neuronal cell differentiation

Zhao, F. L., Wu, T., Lau, A., Jiang, T., Huang, Z., Wang, X.-J., Chen, W., Wong, P. K., & Zhang, D. D. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.06.029 · Cited by 103 · see citing works

Role of microglial redox balance in modulation of neuroinflammation

Innamorato, N. G., Lastres‐Becker, I., & Cuadrado, A. (2009) · Current Opinion in Neurology · doi:10.1097/wco.0b013e32832a3225 · Cited by 100 · see citing works

β-TrCP-Mediated Ubiquitination and Degradation of PHLPP1 Are Negatively Regulated by Akt

Li, X., Liu, J., & Gao, T. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00681-09 · Cited by 98 · see citing works

Polyubiquitination of Prolactin Receptor Stimulates Its Internalization, Postinternalization Sorting, and Degradation via the Lysosomal Pathway

Varghese, B., Barrière, H., Carbone, C. J., Banerjee, A., Swaminathan, G., Plotnikov, A., Xu, P., Peng, J., Goffin, V., Lukács, G. L., et al. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.00350-08 · Cited by 90 · see citing works

β-Trcp mediates ubiquitination and degradation of the erythropoietin receptor and controls cell proliferation

Meyer, L., Deau, B., Forejtníková, H., Dumènil, D., Margottin-Goguet, F., Lacombe, C., Mayeux, P., & Verdier, F. (2007) · Blood · doi:10.1182/blood-2006-10-055350 · Cited by 74 · see citing works

Novel insights into FGD3, a putative GEF for Cdc42, that undergoes SCFFWD1/β‐TrCP‐mediated proteasomal degradation analogous to that of its homologue FGD1 but regulates cell morphology and motility differently from FGD1

Hayakawa, M., Matsushima, M., Hagiwara, H., Oshima, T., Fujino, T., Ando, K., Kikugawa, K., Tanaka, H., Miyazawa, K., & Kitagawa, M. (2008) · Genes to Cells · doi:10.1111/j.1365-2443.2008.01168.x · Cited by 58 · see citing works

Regulated Proteolysis of Xom Mediates Dorsoventral Pattern Formation during Early Xenopus Development

Zhu, Z., & Kirschner, M. W. (2002) · Developmental Cell · doi:10.1016/s1534-5807(02)00270-8 · Cited by 38 · see citing works

In Vitro Reconstitution of SCF Substrate Ubiquitination with Purified Proteins

Petroski, M. D., & Deshaies, R. J. (2005) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(05)98013-0 · Cited by 36 · see citing works

The FWD1/β‐TrCP‐mediated degradation pathway establishes a ‘turning off switch’ of a Cdc42 guanine nucleotide exchange factor, FGD1

Hayakawa, M., Kitagawa, H., Miyazawa, K., Kitagawa, M., & Kikugawa, K. (2005) · Genes to Cells · doi:10.1111/j.1365-2443.2005.00834.x · Cited by 31 · see citing works

UV-induced degradation of securin is mediated by SKP1-CUL1-βTrCP E3 ubiquitin ligase

Limón‐Mortés, M. C., Mora‐Santos, M., Espina, Á. G., Pintor‐Toro, J. A., López-Román, A., Tortolero, M., & Romero, F. (2008) · Journal of Cell Science · doi:10.1242/jcs.020552 · Cited by 29 · see citing works

Role of nrf2 in oxidative stress and toxicity

Ma, Q. (2013) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-011112-140320 · Cited by 4,903 · see citing works

Transcriptional Regulation by Nrf2

Tonelli, C., Chio, I. I. C., & Tuveson, D. A. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7342 · Cited by 2,206 · see citing works

The Nrf2 regulatory network provides an interface between redox and intermediary metabolism

Hayes, J. D., & Dinkova‐Kostova, A. T. (2014) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2014.02.002 · Cited by 2,158 · see citing works

The PI3K–AKT network at the interface of oncogenic signalling and cancer metabolism

Hoxhaj, G., & Manning, B. D. (2020) · Nature Reviews Cancer · doi:10.1038/s41568-019-0216-7 · Cited by 2,137 · see citing works

The KEAP1-NRF2 system: a thiol-based sensor-effector apparatus for maintaining redox homeostasis

Yamamoto, M., Kensler, T. W., & Motohashi, H. (2018) · Physiological Reviews · doi:10.1152/physrev.00023.2017 · Cited by 1,968 · see citing works

Nrf2 signaling pathway: pivotal roles in inflammation

Ahmed, S. M. U., Luo, L., Namani, A., Wang, X. J., & Tang, X. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2016.11.005 · Cited by 1,794 · see citing works

NRF2 and the Hallmarks of Cancer

Rojo de la Vega, M., Chapman, E., & Zhang, D. D. (2018) · Cancer Cell · doi:10.1016/j.ccell.2018.03.022 · Cited by 1,672 · see citing works

The Molecular Mechanisms Regulating the KEAP1-NRF2 Pathway

Baird, L., & Yamamoto, M. P. (2020) · Molecular and Cellular Biology · doi:10.1128/mcb.00099-20 · Cited by 1,600 · see citing works

Therapeutic targeting of the NRF2 and KEAP1 partnership in chronic diseases

Cuadrado, A., Rojo, A. I., Wells, G., Hayes, J. D., Cousin, S. P., Rumsey, W. L., Attucks, O. C., Franklin, S., Levonen, A., Kensler, T. W., et al. (2019) · Nature Reviews Drug Discovery · doi:10.1038/s41573-018-0008-x · Cited by 1,474 · see citing works

An Overview of Nrf2 Signaling Pathway and Its Role in Inflammation

Saha, S., Buttari, B., Panieri, E., Profumo, E., & Saso, L. (2020) · Molecules · doi:10.3390/molecules25225474 · Cited by 1,419 · see citing works

Nrf2 Redirects Glucose and Glutamine into Anabolic Pathways in Metabolic Reprogramming

Mitsuishi, Y., Taguchi, K., Kawatani, Y., Shibata, T., Nukiwa, T., Aburatani, H., Yamamoto, M., & Motohashi, H. (2012) · Cancer Cell · doi:10.1016/j.ccr.2012.05.016 · Cited by 1,395 · see citing works

The emerging role of the Nrf2–Keap1 signaling pathway in cancerPreprint

Jaramillo, M. C., & Zhang, D. D. (2013) · Genes & Development · doi:10.1101/gad.225680.113 · Cited by 1,304 · see citing works

Dissecting molecular cross-talk between Nrf2 and NF-κB response pathways

Wardyn, J. D., Ponsford, A. H., & Sanderson, C. M. (2015) · Biochemical Society Transactions · doi:10.1042/bst20150014 · Cited by 1,200 · see citing works

Nrf2 and Oxidative Stress: A General Overview of Mechanisms and Implications in Human Disease

Ngo, V., & Duennwald, M. L. (2022) · Antioxidants · doi:10.3390/antiox11122345 · Cited by 1,130 · see citing works

The cytoprotective role of the Keap1–Nrf2 pathway

Baird, L., & Dinkova‐Kostova, A. T. (2011) · Archives of Toxicology · doi:10.1007/s00204-011-0674-5 · Cited by 1,029 · see citing works

The Nrf2 cell defence pathway: Keap1-dependent and -independent mechanisms of regulation

Bryan, H. K., Olayanju, A., Goldring, C. E., & Park, B. K. (2012) · Biochemical Pharmacology · doi:10.1016/j.bcp.2012.11.016 · Cited by 1,026 · see citing works

Molecular basis of the Keap1–Nrf2 system

Suzuki, T., & Yamamoto, M. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.06.006 · Cited by 995 · see citing works

The emerging role of Nrf2 in mitochondrial function

Dinkova-Kostova, A. T., & Abramov, A. Y. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.04.036 · Cited by 983 · see citing works

Regulation of Nrf2—an update

Niture, S. K., Khatri, R., & Jaiswal, A. K. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.02.008 · Cited by 873 · see citing works

Hydrogen peroxide sensing, signaling and regulation of transcription factors

Marinho, H. S., Real, C., Cyrne, L., Soares, H., & Antunes, F. (2014) · Redox Biology · doi:10.1016/j.redox.2014.02.006 · Cited by 851 · see citing works

Mechanisms of activation of the transcription factor Nrf2 by redox stressors, nutrient cues, and energy status and the pathways through which it attenuates degenerative disease

Tebay, L. E., Robertson, H., Durant, S. T., Vitale, S. R., Penning, T. M., Dinkova-Kostova, A. T., & Hayes, J. D. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.06.021 · Cited by 837 · see citing works

Nrf2, the Master Regulator of Anti-Oxidative Responses

Vomund, S., Schäfer, A., Parnham, M., Brüne, B., & Von Knethen, A. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18122772 · Cited by 752 · see citing works

Toward clinical application of the Keap1-Nrf2 pathway

Suzuki, T., Motohashi, H., & Yamamoto, M. (2013) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2013.04.005 · Cited by 680 · see citing works

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 · see citing works

p62 links autophagy and Nrf2 signaling

Jiang, T., Harder, B. G., de la Vega, M. R., Wong, P. K., Chapman, E., & Zhang, D. D. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.06.014 · Cited by 642 · see citing works

NRF2 and NF-қB interplay in cerebrovascular and neurodegenerative disorders: Molecular mechanisms and possible therapeutic approaches

Sivandzade, F., Prasad, S., Bhalerao, A., & Cucullo, L. (2019) · Redox Biology · doi:10.1016/j.redox.2018.11.017 · Cited by 639 · see citing works

Transcription Factor NRF2 as a Therapeutic Target for Chronic Diseases: A Systems Medicine Approach

Cuadrado, A., Manda, G., Hassan, A., Alcaraz, M. J., Barbas, C., Daiber, A., Ghezzi, P., León, R., López, M. G., Oliva, B., et al. (2018) · Pharmacological Reviews · doi:10.1124/pr.117.014753 · Cited by 632 · see citing works

Emerging roles of Nrf2 and phase II antioxidant enzymes in neuroprotection

Zhang, M., An, C., Gao, Y., Leak, R. K., Chen, J., & Zhang, F. (2012) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2012.09.003 · Cited by 622 · see citing works

Molecular and Cellular Mechanisms of Cardiovascular Disorders in Diabetes

Shah, M. S., & Brownlee, M. (2016) · Circulation Research · doi:10.1161/circresaha.116.306923 · Cited by 601 · see citing works

Structural basis of Keap1 interactions with Nrf2

Canning, P., Sorrell, F. J., & Bullock, A. N. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.05.034 · Cited by 605 · see citing works

ROS in Cancer: The Burning Question

Chio, I. I. C., & Tuveson, D. A. (2017) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2017.03.004 · Cited by 532 · see citing works

The Keap1-Nrf2 System: A Mediator between Oxidative Stress and Aging

Yu, C., & Xiao, J.-H. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/6635460 · Cited by 537 · see citing works

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 · see citing works

AMPK Facilitates Nuclear Accumulation of Nrf2 by Phosphorylating at Serine 550

Joo, M. S., Kim, W., Lee, K. Y., Kim, J. H., Koo, J. H., & Kim, S. G. (2016) · Molecular and Cellular Biology · doi:10.1128/mcb.00118-16 · Cited by 503 · see citing works

GSK-3: Functional Insights from Cell Biology and Animal Models

Kaidanovich‐Beilin, O., & Woodgett, J. R. (2011) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2011.00040 · Cited by 487 · see citing works

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 474 · see citing works

The complexity of the Nrf2 pathway: beyond the antioxidant response

Huang, Y. S., Li, W., Su, Z., & Kong, A. T. (2015) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2015.08.001 · Cited by 449 · see citing works

Nrf2–ARE signaling in cellular protection: Mechanism of action and the regulatory mechanisms

Shaw, P., & Chattopadhyay, A. (2019) · Journal of Cellular Physiology · doi:10.1002/jcp.29219 · Cited by 431 · see citing works

Stress-sensing mechanisms and the physiological roles of the Keap1–Nrf2 system during cellular stress

Suzuki, T., & Yamamoto, M. P. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.r117.800169 · Cited by 402 · see citing works

RXRα Inhibits the NRF2-ARE Signaling Pathway through a Direct Interaction with the Neh7 Domain of NRF2

Wang, H., Liu, K., Geng, M., Gao, P., Wu, X., Hai, Y., Li, Y., Li, Y., Luo, L., Hayes, J. D., et al. (2013) · Cancer Research · doi:10.1158/0008-5472.can-12-3386 · Cited by 382 · see citing works

The multifaceted role of Nrf2 in mitochondrial function

Holmström, K. M., Kostov, R. V., & Dinkova-Kostova, A. T. (2016) · Current Opinion in Toxicology · doi:10.1016/j.cotox.2016.10.002 · Cited by 368 · see citing works

Hrd1 suppresses Nrf2-mediated cellular protection during liver cirrhosisPreprint

Wu, T., Zhao, F. L., Gao, B., Tan, C., Yagishita, N., Nakajima, T., Wong, P. K., Chapman, E., Fang, D., & Zhang, D. D. (2014) · Genes & Development · doi:10.1101/gad.238246.114 · Cited by 355 · see citing works

The role of Nrf2 signaling in counteracting neurodegenerative diseases

Dinkova‐Kostova, A. T., Kostov, R. V., & Kazantsev, A. G. (2018) · The FEBS Journal · doi:10.1111/febs.14379 · Cited by 342 · see citing works

What Are the bona fide GSK3 Substrates?

Sutherland, C. D. (2011) · International Journal of Alzheimer s Disease · doi:10.4061/2011/505607 · Cited by 349 · see citing works

Keap1, the cysteine-based mammalian intracellular sensor for electrophiles and oxidants

Dinkova‐Kostova, A. T., Kostov, R. V., & Canning, P. (2016) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2016.08.005 · Cited by 332 · see citing works

Dissecting the Crosstalk Between Nrf2 and NF-κB Response Pathways in Drug-Induced Toxicity

Gao, W., Guo, L., Yang, Y., Wang, Y., Xia, S., Gong, H., Zhang, B., & Yan, M. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.809952 · Cited by 328 · see citing works

Nrf2—a therapeutic target for the treatment of neurodegenerative diseases

Johnson, D. A., & Johnson, J. A. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.07.147 · Cited by 328 · see citing works

Degradation of proteins by PROTACs and other strategies

Wang, Y., Jiang, X., Feng, F., Liu, W., & Sun, H. (2020) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2019.08.001 · Cited by 335 · see citing works

NRF2 as a regulator of cell metabolism and inflammation in cancer

He, F., Antonucci, L., & Karin, M. (2020) · Carcinogenesis · doi:10.1093/carcin/bgaa039 · Cited by 318 · see citing works

Molecular Basis of Electrophilic and Oxidative Defense: Promises and Perils of Nrf2

Ma, Q., & He, X. (2012) · Pharmacological Reviews · doi:10.1124/pr.110.004333 · Cited by 317 · see citing works

Targeting cell signaling in allergic asthma

Athari, S. S. (2019) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-019-0079-0 · Cited by 318 · see citing works

Redox Control of Microglial Function: Molecular Mechanisms and Functional Significance

Rojo, A. I., McBean, G. J., Cindrić, M., Egea, J., López, M. G., Rada, P., Žarković, N., & Cuadrado, A. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5745 · Cited by 313 · see citing works

Fumarate Is Cardioprotective via Activation of the Nrf2 Antioxidant Pathway

Ashrafian, H., Czibik, G., Bellahcene, M., Aksentijević, D., Smith, A. C., Mitchell, S. J., Dodd, M. S., Kirwan, J., Byrne, J. J., Ludwig, C., et al. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.01.017 · Cited by 303 · see citing works

The KEAP1-NRF2 pathway: Targets for therapy and role in cancer

Adinolfi, S., Patinen, T., Deen, A. J., Pitkänen, S., Härkönen, J., Kansanen, E., Küblbeck, J., & Levonen, A. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102726 · Cited by 301 · see citing works

Oncogenic KRAS Confers Chemoresistance by Upregulating NRF2

Tao, S., Wang, S., Moghaddam, S. J., Ooi, A., Chapman, E., Wong, P. K., & Zhang, D. D. (2014) · Cancer Research · doi:10.1158/0008-5472.can-14-1439 · Cited by 291 · see citing works

Role of Oxidative Stress in Reperfusion following Myocardial Ischemia and Its Treatments

Xiang, M., Lu, Y., Xin, L., Gao, J., Shang, C., Jiang, Z., Lin, H., Fang, X., Qu, Y., Wang, Y., et al. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/6614009 · Cited by 301 · see citing works

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

Furfaro, A. L., Traverso, N., Domenicotti, C., Piras, S., Moretta, L., Marinari, U. M., Pronzato, M. A., & Nitti, M. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/1958174 · Cited by 295 · see citing works

The Role of Nrf2 in Cardiovascular Function and Disease

Satta, S., Mahmoud, A. M., Wilkinson, F. L., Alexander, M. Y., & White, S. J. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/9237263 · Cited by 299 · see citing works

Wogonin, a plant derived small molecule, exerts potent anti-inflammatory and chondroprotective effects through the activation of ROS/ERK/Nrf2 signaling pathways in human Osteoarthritis chondrocytes

Khan, N. M., Haseeb, A., Ansari, M. Y., Devarapalli, P., Haynie, S., & Haqqi, T. M. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.02.041 · Cited by 289 · see citing works

The Nrf2-antioxidant response element pathway: a target for regulating energy metabolism

Vomhof‐DeKrey, E. E., & Picklo, M. J. (2012) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2012.03.005 · Cited by 283 · see citing works

NRF2 addiction in cancer cells

Kitamura, H., & Motohashi, H. (2018) · Cancer Science · doi:10.1111/cas.13537 · Cited by 275 · see citing works

Proteostasis, oxidative stress and aging

Korovila, I., Hugo, M., Castro, J. P., Weber, D., Höhn, A., Grune, T., & Jung, T. (2017) · Redox Biology · doi:10.1016/j.redox.2017.07.008 · Cited by 274 · see citing works

Shaping the Nrf2-ARE-related pathways in Alzheimer’s and Parkinson’s diseases

Fão, L., Mota, S. I., & Rego, A. C. (2019) · Ageing Research Reviews · doi:10.1016/j.arr.2019.100942 · Cited by 270 · see citing works

Role of Nrf2 and Its Activators in Respiratory Diseases

Liu, Q., Gao, Y., & Ci, X. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/7090534 · Cited by 273 · see citing works

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 265 · see citing works

Involvement of Nrf2 in myocardial ischemia and reperfusion injury

Shen, Y., Liu, X., Shi, J., & Xiang, W. (2018) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2018.11.190 · Cited by 257 · see citing works

An innovative NRF2 nano-modulator induces lung cancer ferroptosis and elicits an immunostimulatory tumor microenvironment

Hsieh, C., Hsieh, H.-C., Shih, F.-H., Wang, P., Yang, L., Shieh, D.-B., & Wang, Y. (2021) · Theranostics · doi:10.7150/thno.57803 · Cited by 260 · see citing works

NRF2, a Superstar of Ferroptosis

Yan, R., Lin, B., Jin, W., Tang, L., Hu, S., & Cai, R. (2023) · Antioxidants · doi:10.3390/antiox12091739 · Cited by 260 · see citing works

Oxidative stress in Alzheimer’s disease: current knowledge of signaling pathways and therapeutics

Dhapola, R., Beura, S. K., Sharma, P., Singh, S. K., & HariKrishnaReddy, D. (2024) · Molecular Biology Reports · doi:10.1007/s11033-023-09021-z · Cited by 270 · see citing works

Glutathione biosynthesis is a metabolic vulnerability in PI(3)K/Akt-driven breast cancer

Lien, E. C., Lyssiotis, C. A., Juvekar, A., Hu, H., Asara, J. M., Cantley, L. C., & Toker, A. (2016) · Nature Cell Biology · doi:10.1038/ncb3341 · Cited by 249 · see citing works

Nuclear Heme Oxygenase-1 (HO-1) Modulates Subcellular Distribution and Activation of Nrf2, Impacting Metabolic and Anti-oxidant Defenses

Biswas, C., Shah, N., Muthu, M., La, P., Fernando, A. P., Sengupta, S., Yang, G., & Dennery, P. A. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.567685 · Cited by 259 · see citing works

Activated AMPK boosts the Nrf2/HO-1 signaling axis—A role for the unfolded protein response

Zimmermann, K., Baldinger, J., Mayerhofer, B., Atanasov, A. G., Dirsch, V. M., & Heiß, E. H. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.03.030 · Cited by 255 · see citing works

The Crosstalk between Nrf2 and Inflammasomes

Hennig, P., Garstkiewicz, M., Grossi, S., Filippo, M. D., French, L. E., & Beer, H. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19020562 · Cited by 256 · see citing works

Glutathione synthesis and its role in redox signaling

Zhang, H., & Forman, H. J. (2012) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2012.03.017 · Cited by 248 · see citing works

Regulation of Nrf2 signaling and longevity in naturally long-lived rodents

Lewis, K. N., Wason, E., Edrey, Y. H., Kristan, D. M., Nevo, E., & Buffenstein, R. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1417566112 · Cited by 248 · see citing works

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

Lee, J. H., Khor, T. O., Shu, L., Su, Z., Fuentes, F., & Kong, A. T. (2012) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2012.09.008 · Cited by 248 · see citing works

Nrf2/ARE pathway activation, HO-1 and NQO1 induction by polychlorinated biphenyl quinone is associated with reactive oxygen species and PI3K/AKT signaling

Li, L., Dong, H., Song, E., Xu, X., Liu, L., & Song, Y. (2013) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2013.12.005 · Cited by 244 · see citing works

Nrf2: a dark horse in Alzheimer's disease treatment

Osama, A., Zhang, J., Yao, J., Yao, X., & Fang, J. (2020) · Ageing Research Reviews · doi:10.1016/j.arr.2020.101206 · Cited by 251 · see citing works

Nrf2—a Promising Therapeutic Target for Defensing Against Oxidative Stress in Stroke

Zhang, R., Xu, M., Wang, Y., Xie, F., Zhang, G., & Qin, X. (2016) · Molecular Neurobiology · doi:10.1007/s12035-016-0111-0 · Cited by 243 · see citing works

Targeting Neddylation Pathways to Inactivate Cullin-RING Ligases for Anticancer Therapy

Zhao, Y., Morgan, M. A., & Sun, Y. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5795 · Cited by 242 · see citing works

Roles of Oxidative Stress and Nrf2 Signaling in Pathogenic and Non-Pathogenic Cells: A Possible General Mechanism of Resistance to Therapy

Hammad, M., Raftari, M., Cesário, R., Salma, R., Godoy, P. R. D. V., Emami, S. N., & Haghdoost, S. (2023) · Antioxidants · doi:10.3390/antiox12071371 · Cited by 245 · see citing works

New Insights into the Physiological Role of Endoplasmic Reticulum-Associated Degradation

Qi, L., Tsai, B., & Arvan, P. R. (2017) · Trends in Cell Biology · doi:10.1016/j.tcb.2016.12.002 · Cited by 234 · see citing works

Sulforaphane reactivates cellular antioxidant defense by inducing Nrf2/ARE/Prdx6 activity during aging and oxidative stress

Kubo, E., Chhunchha, B., Singh, P., Sasaki, H., & Singh, D. P. (2017) · Scientific Reports · doi:10.1038/s41598-017-14520-8 · Cited by 231 · see citing works

The Keap1-Nrf2 system and diabetes mellitus

Uruno, A., Yagishita, Y., & Yamamoto, M. (2015) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2014.12.012 · Cited by 231 · see citing works

Antioxidants in Translational Medicine

Schmidt, H. H. H. W., Stocker, R., Vollbracht, C., Paulsen, G., Riley, D. P., Daiber, A., & Cuadrado, A. (2015) · Antioxidants and Redox Signaling · doi:10.1089/ars.2015.6393 · Cited by 231 · see citing works

Nrf2/ARE Signaling Pathway: Key Mediator in Oxidative Stress and Potential Therapeutic Target in ALS

Petri, S., Körner, S., & Kiaei, M. (2012) · Neurology Research International · doi:10.1155/2012/878030 · Cited by 227 · see citing works

Molecular and Chemical Regulation of the Keap1-Nrf2 Signaling Pathway

Keum, Y., & Choi, B. Y. (2014) · Molecules · doi:10.3390/molecules190710074 · Cited by 224 · see citing works

Roles of Nrf2 in cell proliferation and differentiation

Murakami, S., & Motohashi, H. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.06.030 · Cited by 221 · see citing works

HO-1 Induction in Cancer Progression: A Matter of Cell Adaptation

Nitti, M., Piras, S., Marinari, U. M., Moretta, L., Pronzato, M. A., & Furfaro, A. L. (2017) · Antioxidants · doi:10.3390/antiox6020029 · Cited by 222 · see citing works

NRF2 targeting: a promising therapeutic strategy in chronic obstructive pulmonary disease

Boutten, A., Goven, D., Artaud-Macari, É., Boczkowski, J., & Bonay, M. (2011) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2011.02.006 · Cited by 223 · see citing works

Oxidative stress and chronic inflammation in osteoarthritis: can NRF2 counteract these partners in crime?

Marchev, A. S., Dimitrova, P. A., Burns, A. J., Kostov, R. V., Dinkova‐Kostova, A. T., & Georgiev, M. I. (2017) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.13407 · Cited by 223 · see citing works

Modulation of proteostasis by transcription factor NRF2 and impact in neurodegenerative diseases

Pajares, M., Cuadrado, A., & Rojo, A. I. (2017) · Redox Biology · doi:10.1016/j.redox.2017.01.006 · Cited by 219 · see citing works

Mechanisms of induction of cytosolic and microsomal glutathione transferase (GST) genes by xenobiotics and pro-inflammatory agents

Higgins, L. G., & Hayes, J. D. (2011) · Drug Metabolism Reviews · doi:10.3109/03602532.2011.567391 · Cited by 217 · see citing works

NRF2 activation promotes the recurrence of dormant tumour cells through regulation of redox and nucleotide metabolism

Fox, D. B., Garcia, N. M. G., McKinney, B. J., Lupo, R., Noteware, L. C., Newcomb, R., Liu, J., Locasale, J. W., Hirschey, M. D., & Alvarez, J. V. (2020) · Nature Metabolism · doi:10.1038/s42255-020-0191-z · Cited by 214 · see citing works

A Perspective on Nrf2 Signaling Pathway for Neuroinflammation: A Potential Therapeutic Target in Alzheimer's and Parkinson's Diseases

Saha, S., Buttari, B., Profumo, E., Tucci, P., & Saso, L. (2022) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2021.787258 · Cited by 206 · see citing works

Activation of Nrf2 signaling by natural products-can it alleviate diabetes?

Matzinger, M., Fischhuber, K., & Heiß, E. H. (2017) · Biotechnology Advances · doi:10.1016/j.biotechadv.2017.12.015 · Cited by 205 · see citing works

Nrf2: Molecular and epigenetic regulation during aging

Silva‐Palacios, A., Ostolga-Chavarría, M., Zazueta, C., & Königsberg, M. (2018) · Ageing Research Reviews · doi:10.1016/j.arr.2018.06.003 · Cited by 195 · see citing works

The KEAP1–NRF2 System as a Molecular Target of Cancer Treatment

Taguchi, K., & Yamamoto, M. (2020) · Cancers · doi:10.3390/cancers13010046 · Cited by 195 · see citing works

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

Rojo, A. I., Medina‐Campos, O. N., Rada, P., Zúñiga-Toalá, A., López-Gazcón, A., Espada, S., Pedraza‐Chaverrí, J., & Cuadrado, A. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.11.003 · Cited by 195 · see citing works

The Dual Role of Nrf2 in Nonalcoholic Fatty Liver Disease: Regulation of Antioxidant Defenses and Hepatic Lipid Metabolism

Chambel, S. S., Santos-Gonçalves, A., & Duarte, T. L. (2015) · BioMed Research International · doi:10.1155/2015/597134 · Cited by 192 · see citing works

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 265 · see citing works

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 474 · see citing works

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 · see citing works

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)