Monoacidic Inhibitors of the Kelch-like ECH-Associated Protein 1: Nuclear Factor Erythroid 2-Related Factor 2 (KEAP1:NRF2) Protein–Protein Interaction with High Cell Potency Identified by Fragment-Based Discovery

Analysis of Relative Gene Expression Data Using Real-Time Quantitative PCR and the 2−ΔΔCT Method

Livak, K. J., & Schmittgen, T. D. (2001) · Methods · doi:10.1006/meth.2001.1262 · Cited by 180,860 · see citing works

<i>Coot</i> : model-building tools for molecular graphics

Emsley, P., & Cowtan, K. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904019158 · Cited by 30,571 · see citing works

Refinement of Macromolecular Structures by the Maximum-Likelihood Method

Murshudov, G. N., Vagin, A. A., & Dodson, E. J. (1997) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444996012255 · Cited by 14,671 · see citing works

An Nrf2/Small Maf Heterodimer Mediates the Induction of Phase II Detoxifying Enzyme Genes through Antioxidant Response Elements

Itoh, K., Chiba, T., Takahashi, S., Ishii, T., Igarashi, K., Katoh, Y., Oyake, T., Hayashi, N., Satoh, K., Hatayama, I., et al. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.6943 · Cited by 3,999 · see citing works

Cell Survival Responses to Environmental Stresses Via the Keap1-Nrf2-ARE Pathway

Kensler, T. W., Wakabayashi, N., & Biswal, S. (2007) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.46.120604.141046 · Cited by 3,630 · 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

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

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

Fumaric acid esters exert neuroprotective effects in neuroinflammation via activation of the Nrf2 antioxidant pathway

Linker, R. A., Lee, D.-H., Ryan, S., van Dam, A. M., Conrad, R., Bista, P., Zeng, W., Hronowsky, X., Buko, A., Chollate, S., et al. (2011) · Brain · doi:10.1093/brain/awq386 · Cited by 1,155 · see citing works

Genetic ablation of Nrf2 enhances susceptibility to cigarette smoke–induced emphysema in mice

Rangasamy, T., Cho, C. Y., Thimmulappa, R. K., Zhen, L., Srisuma, S., Kensler, T. W., Yamamoto, M. P., Petrache, I., Tuder, R. M., & Biswal, S. S. (2004) · Journal of Clinical Investigation · doi:10.1172/jci21146 · Cited by 993 · 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

Bardoxolone Methyl and Kidney Function in CKD with Type 2 Diabetes

Pergola, P. E., Raskin, P., Toto, R. D., Meyer, C. J., Huff, J. W., Grossman, E. B., Krauth, M., Ruiz, S., Audhya, P., Christ-Schmidt, H., et al. (2011) · New England Journal of Medicine · doi:10.1056/nejmoa1105351 · Cited by 890 · see citing works

Keap1 Recruits Neh2 through Binding to ETGE and DLG Motifs: Characterization of the Two-Site Molecular Recognition Model

Tong, K. I., Katoh, Y., Kusunoki, H., Itoh, K., Tanaka, T., & Yamamoto, M. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.8.2887-2900.2006 · Cited by 759 · see citing works

Structural basis for defects of Keap1 activity provoked by its point mutations in lung cancer

Padmanabhan, B., Tong, K. I., Ohta, T., Nakamura, Y., Scharlock, M., Ohtsuji, M., Kang, M.-I., Kobayashi, A., Yokoyama, S., & Yamamoto, M. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.01.013 · Cited by 735 · see citing works

Functional antioxidant responsive elements

Wasserman, W. W., & Fahl, W. E. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.10.5361 · Cited by 705 · 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

Structure of the Keap1:Nrf2 interface provides mechanistic insight into Nrf2 signaling

Lo, S., Li, X., Henzl, M. T., Beamer, L. J., & Hannink, M. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601243 · Cited by 604 · see citing works

Direct measurement of NAD(P)H:quinone reductase from cells cultured in microtiter wells: A screening assay for anticarcinogenic enzyme inducers

Prochaska, H. J., & Santamaria, A. B. (1988) · Analytical Biochemistry · doi:10.1016/0003-2697(88)90292-8 · Cited by 495 · see citing works

Different Electrostatic Potentials Define ETGE and DLG Motifs as Hinge and Latch in Oxidative Stress Response

Tong, K. I., Padmanabhan, B., Kobayashi, A., Shang, C., Hirotsu, Y., Yokoyama, S., & Yamamoto, M. P. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00753-07 · Cited by 447 · 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

Targeting Nrf2 with the triterpenoid CDDO- imidazolide attenuates cigarette smoke-induced emphysema and cardiac dysfunction in mice

Sussan, T. E., Rangasamy, T., Blake, D. J., Malhotra, D., El-Haddad, H., Bedja, D., Yates, M. S., Kombairaju, P., Yamamoto, M., Liby, K. T., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0804333106 · Cited by 346 · see citing works

Nrf2‐deficient mice are highly susceptible to cigarette smoke‐induced emphysema

Iizuka, T., Ishii, Y., Itoh, K., Kiwamoto, T., Kimura, T., Matsuno, Y., Morishima, Y., Hegab, A. E., Homma, S., Nomura, A., et al. (2005) · Genes to Cells · doi:10.1111/j.1365-2443.2005.00905.x · Cited by 336 · see citing works

Modification of Keap1 Cysteine Residues by Sulforaphane

Hu, C., Eggler, A. L., Mesecar, A. D., & van Breemen, R. B. (2011) · Chemical Research in Toxicology · doi:10.1021/tx100389r · Cited by 312 · see citing works

Structural basis for Cul3 protein assembly with the BTB-Kelch family of E3 ubiquitin ligases

Canning, P., Cooper, C. D. O., Krojer, T., Murray, J. W., Pike, A. C. W., Chaikuad, A., Keates, T., Thangaratnarajah, C., Hojzan, V., Marsden, B. D., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.437996 · Cited by 284 · see citing works

Structure of the BTB Domain of Keap1 and Its Interaction with the Triterpenoid Antagonist CDDO

Cleasby, A., Yon, J. R., Day, P. J., Richardson, C. J., Tickle, I. J., Williams, P. A., Callahan, J. F., Carr, R. A. E., Concha, N. O., Kerns, J. K., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0098896 · Cited by 265 · see citing works

Discovery of Potent Keap1–Nrf2 Protein–Protein Interaction Inhibitor Based on Molecular Binding Determinants Analysis

Jiang, Z., Lu, M., Xu, L., Yang, T., Xi, M., Xu, X., Guo, X., Zhang, X., You, Q., & Sun, H.-P. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm5000529 · Cited by 263 · see citing works

Crystal Structure of the Kelch Domain of Human Keap1

Li, X., Zhang, D. D., Hannink, M., & Beamer, L. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m410073200 · Cited by 249 · see citing works

Small molecules inhibit the interaction of Nrf2 and the Keap1 Kelch domain through a non-covalent mechanism

Marcotte, D. J., Zeng, W., Hus, J., McKenzie, A., Hession, C., Jin, P., Bergeron, C., Lugovskoy, A. A., Enyedy, I. J., Cuervo, H., et al. (2013) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2013.04.019 · Cited by 245 · see citing works

Nrf2 protects against airway disorders

Cho, H., & Kleeberger, S. R. (2009) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2009.07.024 · Cited by 237 · 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

Fragment-based lead discovery grows up

Baker, M. (2012) · Nature Reviews Drug Discovery · doi:10.1038/nrd3926 · Cited by 214 · see citing works

Covalent Modification at Cys151 Dissociates the Electrophile Sensor Keap1 from the Ubiquitin Ligase CUL3

Rachakonda, G., Xiong, Y., Sekhar, K. R., Stamer, S. L., Liebler, D. C., & Freeman, M. L. (2008) · Chemical Research in Toxicology · doi:10.1021/tx700302s · Cited by 210 · see citing works

Discovery of a small-molecule inhibitor and cellular probe of Keap1–Nrf2 protein–protein interaction

Hu, L., Magesh, S., Chen, L., Wang, L., Lewis, T. A., Chen, Y., Khodier, C., Inoyama, D., Beamer, L. J., Emge, T. J., et al. (2013) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2013.03.013 · Cited by 206 · see citing works

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

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

Cul3-mediated Nrf2 ubiquitination and antioxidant response element (ARE) activation are dependent on the partial molar volume at position 151 of Keap1

Eggler, A. L., Small, E., Hannink, M., & Mesecar, A. D. (2009) · Biochemical Journal · doi:10.1042/bj20090471 · Cited by 178 · see citing works

Keap Calm, and Carry on Covalently

Wilson, A. J., Kerns, J. K., Callahan, J. F., & Moody, C. J. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm400224q · Cited by 171 · see citing works

Targeting the Nrf2 pathway against cardiovascular disease

Li, J., Ichikawa, T., Janicki, J. S., & Cui, T. (2009) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728220903025762 · Cited by 168 · see citing works

Rapid Identification of Keap1–Nrf2 Small-Molecule Inhibitors through Structure-Based Virtual Screening and Hit-Based Substructure Search

Zhuang, C., Narayanapillai, S. C., Zhang, W., Sham, Y. Y., & Xing, C. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm4017174 · Cited by 156 · see citing works

AstexViewerTM †: a visualisation aid for structure-based drug design

Hartshorn, M. J. (2002) · Journal of Computer-Aided Molecular Design · doi:10.1023/a:1023813504011 · Cited by 145 · see citing works

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

Shimozono, R., Asaoka, Y., Yoshizawa, Y., Aoki, T., Noda, H., Yamada, M., Kaino, M., & Mochizuki, H. (2013) · Molecular Pharmacology · doi:10.1124/mol.112.084269 · Cited by 131 · see citing works

Anti-inflammatory Effect of a Cell-Penetrating Peptide Targeting the Nrf2/Keap1 Interaction

Steel, R., Cowan, J., Payerne, E., O'Connell, M. A., & Searcey, M. (2012) · ACS Medicinal Chemistry Letters · doi:10.1021/ml300041g · Cited by 111 · see citing works

The titerless infected-cells preservation and scale-up (TIPS) method for large-scale production of NO-sensitive human soluble guanylate cyclase (sGC) from insect cells infected with recombinant baculovirus

Wasilko, D. J., Lee, S. E., Stutzman-Engwall, K. J., Reitz, B. A., Emmons, T. L., Mathis, K. J., Bienkowski, M. J., Tomasselli, A. G., & Fischer, H. (2009) · Protein Expression and Purification · doi:10.1016/j.pep.2009.01.002 · Cited by 101 · see citing works

Characterization of RA839, a Noncovalent Small Molecule Binder to Keap1 and Selective Activator of Nrf2 Signaling

Winkel, A. F., Engel, C. K., Margerie, D., Kannt, A., Szillat, H., Glombik, H., Kallus, C., Ruf, S. G., Güssregen, S., Riedel, J., et al. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.678136 · Cited by 101 · see citing works

Proteomic Analysis Shows Synthetic Oleanane Triterpenoid Binds to mTOR

Yore, M. M., Kettenbach, A. N., Sporn, M. B., Gerber, S. A., & Liby, K. T. (2011) · PLoS ONE · doi:10.1371/journal.pone.0022862 · Cited by 99 · see citing works

A Selective Antagonist Reveals a Potential Role of G Protein–Coupled Receptor 55 in Platelet and Endothelial Cell Function

Kargl, J., Brown, A. J., Andersen, L., Dorn, G., Schicho, R., Waldhoer, M., & Heinemann, Á. (2013) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.113.204180 · Cited by 98 · see citing works

Automated Protein–Ligand Crystallography for Structure‐Based Drug Design

Mooij, W. T. M., Hartshorn, M. J., Tickle, I. J., Sharff, A., Verdonk, M. L., & Jhoti, H. (2006) · ChemMedChem · doi:10.1002/cmdc.200600074 · Cited by 96 · see citing works

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

Jiang, Z., Xu, L., Lu, M., Chen, Z., Yuan, Z., Xu, X., Guo, X., Zhang, X., Sun, H.-P., & You, Q. (2015) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b00185 · Cited by 94 · see citing works

Fragment-Based Drug Discovery Targeting Inhibitor of Apoptosis Proteins: Discovery of a Non-Alanine Lead Series with Dual Activity Against cIAP1 and XIAP

Chessari, G., Buck, I. M., Day, J. E. H., Day, P. J., Iqbal, A., Johnson, C. N., Lewis, E. J., Martins, V., Miller, D., Reader, M., et al. (2015) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b00706 · Cited by 90 · see citing works

Fragment Screening Using X-Ray Crystallography

Davies, T. G., & Tickle, I. J. (2011) · Topics in current chemistry · doi:10.1007/128_2011_179 · Cited by 82 · see citing works

Structural insights into the similar modes of Nrf2 transcription factor recognition by the cytoplasmic repressor Keap1

Padmanabhan, B., Tong, K. I., Kobayashi, A., Yamamoto, M. P., & Yokoyama, S. (2008) · Journal of Synchrotron Radiation · doi:10.1107/s090904950705114x · Cited by 31 · see citing works

Modulating Role of Endogenous Reduced Glutathione in Tert-Butyl Hydroperoxide-Induced Cell Injury in Isolated Rat Hepatocytes

Nishida, K., Ohta, Y., & Ishiguro, I. (1997) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(97)00116-0 · Cited by 21 · see citing works

Twenty years on: the impact of fragments on drug discovery

Erlanson, D. A., Fesik, S. W., Hubbard, R. E., Jahnke, W., & Jhoti, H. (2016) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2016.109 · Cited by 1,000 · see citing works

Recent advances in the development of protein–protein interactions modulators: mechanisms and clinical trials

Lu, H., Zhou, Q., He, J., Jiang, Z., Peng, C., Tong, R., & Shi, J. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00315-3 · Cited by 891 · see citing works

Targeted protein degradation: expanding the toolbox

Schapira, M., Calabrese, M. F., Bullock, A. N., & Crews, C. M. (2019) · Nature Reviews Drug Discovery · doi:10.1038/s41573-019-0047-y · Cited by 960 · see citing works

Nrf2 Activation Promotes Lung Cancer Metastasis by Inhibiting the Degradation of Bach1

Lignitto, L., LeBoeuf, S. E., Homer, H., Jiang, S., Askenazi, M., Karakousi, T. R., Pass, H. I., Bhutkar, A. J., Tsirigos, A., Ueberheide, B., et al. (2019) · Cell · doi:10.1016/j.cell.2019.06.003 · Cited by 573 · see citing works

WD40 repeat domain proteins: a novel target class?

Schapira, M., Tyers, M., Torrent, M., & Arrowsmith, C. H. (2017) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2017.179 · Cited by 335 · see citing works

Environmental cystine drives glutamine anaplerosis and sensitizes cancer cells to glutaminase inhibition

Muir, A., Danai, L. V., Gui, D. Y., Waingarten, C. Y., Lewis, C. A., & Vander Heiden, M. G. (2017) · eLife · doi:10.7554/elife.27713 · Cited by 311 · see citing works

Homo-PROTACs: bivalent small-molecule dimerizers of the VHL E3 ubiquitin ligase to induce self-degradation

Maniaci, C., Hughes, S. J., Testa, A., Chen, W., Lamont, D. J., Rocha, S., Alessi, D. R., Romeo, R., & Ciulli, A. (2017) · Nature Communications · doi:10.1038/s41467-017-00954-1 · Cited by 245 · see citing works

Activation of the NRF2 antioxidant program generates an imbalance in central carbon metabolism in cancer

Sayin, V. I., LeBoeuf, S. E., Singh, S. X., Davidson, S. M., Biancur, D., Guzelhan, B. S., Alvarez, S. W., Wu, W. L., Karakousi, T. R., Zavitsanou, A. M., et al. (2017) · eLife · doi:10.7554/elife.28083 · Cited by 231 · see citing works

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

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

Harnessing the E3 Ligase KEAP1 for Targeted Protein Degradation

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

Small molecules inhibiting Keap1-Nrf2 protein-protein interactions: A novel approach to activate Nrf2 function

Zhuang, C., Wu, Z., Xing, C., & Miao, Z. (2017) · MedChemComm · doi:10.1039/c6md00500d · Cited by 84 · see citing works

Small molecules targeting protein–protein interactions for cancer therapy

Wu, D., Li, Y., Zheng, L., Xiao, H., Ouyang, L., Wang, G., & Sun, Q. (2023) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2023.05.035 · Cited by 71 · see citing works

Phenyl Bis-Sulfonamide Keap1-Nrf2 Protein–Protein Interaction Inhibitors with an Alternative Binding Mode

Georgakopoulos, N., Talapatra, S., Dikovskaya, D., Dayalan Naidu, S., Higgins, M., Gatliff, J., Ayhan, A., Nikoloudaki, R., Schaap, M., Valko, K., et al. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c00457 · Cited by 33 · see citing works

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

Cuadrado, A., Cazalla, E., Bach, A., Bathish, B., Naidu, S. D., DeNicola, G. M., Dinkova-Kostova, A. T., Fernández-Ginés, R., Grochot-Przeczek, A., Hayes, J. D., et al. (2025) · Redox Biology · doi:10.1016/j.redox.2025.103569 · Cited by 28 · see citing works

Drug-Repositioning Screening for Keap1-Nrf2 Binding Inhibitors using Fluorescence Correlation Spectroscopy

Yoshizaki, Y., Mori, T., Ishigami‐Yuasa, M., Kikuchi, E., Takahashi, D., Zeniya, M., Nomura, N., Mori, Y., Araki, Y., Ando, F., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-04233-3 · Cited by 20 · see citing works

Molecular Basis of the KEAP1-NRF2 Signaling Pathway

Suzuki, T., Takahashi, J. A., & Yamamoto, M. P. (2023) · Molecules and Cells · doi:10.14348/molcells.2023.0028 · Cited by 309 · see citing works

Molecular mechanisms of Nrf2‐mediated antioxidant response

Li, W., & Kong, A. T. (2008) · Molecular Carcinogenesis · doi:10.1002/mc.20465 · Cited by 786 · see citing works

Molecular Mechanisms Activating the Nrf2-Keap1 Pathway of Antioxidant Gene Regulation

Kobayashi, M., & Yamamoto, M. P. (2005) · Antioxidants and Redox Signaling · doi:10.1089/ars.2005.7.385 · Cited by 1,075 · 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