The Keap1 BTB/POZ dimerization function is required to sequester Nrf2 in cytoplasm

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

Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain

Itoh, K., Wakabayashi, N., Katoh, Y., Ishii, T., Igarashi, K., Engel, J. D., & Yamamoto, M. (1999) · Genes & Development · doi:10.1101/gad.13.1.76 · Cited by 3,634 · see citing works

Nrf2, a Cap'n'Collar Transcription Factor, Regulates Induction of the Heme Oxygenase-1 Gene

Alam, J., Stewart, D. P., Touchard, C. L., Boinapally, S., Choi, A. M. K., & Cook, J. L. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.37.26071 · Cited by 1,284 · see citing works

Sensitivity to carcinogenesis is increased and chemoprotective efficacy of enzyme inducers is lost in <i>nrf2</i> transcription factor-deficient mice

Ramos-Gomez, M., Kwak, M.-K., Dolan, P. M., Itoh, K., Yamamoto, M., Talalay, P., & Kensler, T. W. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.051618798 · Cited by 1,102 · see citing works

Nrf1 and Nrf2 positively and c-Fos and Fra1 negatively regulate the human antioxidant response element-mediated expression of NAD(P)H:quinone oxidoreductase 1 gene

Radjendirane, V., & Jaiswal, A. K. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.25.14960 · Cited by 1,034 · see citing works

An important function of Nrf2 in combating oxidative stress: Detoxification of acetaminophen

Chan, K., Han, X.-D., & Kan, Y. W. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.081082098 · Cited by 766 · see citing works

The POZ domain: a conserved protein-protein interaction motif.Preprint

Bardwell, V. J., & Treisman, R. (1994) · Genes & Development · doi:10.1101/gad.8.14.1664 · Cited by 749 · see citing works

High Sensitivity of Nrf2 Knockout Mice to Acetaminophen Hepatotoxicity Associated with Decreased Expression of ARE-Regulated Drug Metabolizing Enzymes and Antioxidant Genes

Enomoto, A. (2001) · Toxicological Sciences · doi:10.1093/toxsci/59.1.169 · Cited by 728 · see citing works

Role of NRF2 in Protection Against Hyperoxic Lung Injury in Mice

Cho, H., Jedlicka, A., Reddy, S. P., Kensler, T. W., Yamamoto, M. P., Zhang, L.-Y., & Kleeberger, S. R. (2002) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/ajrcmb.26.2.4501 · Cited by 660 · see citing works

The Cap'n'Collar basic leucine zipper transcription factor Nrf2 (NF-E2 p45-related factor 2) controls both constitutive and inducible expression of intestinal detoxification and glutathione biosynthetic enzymes.

McMahon, M. J., Itoh, K., Yamamoto, M. P., Chanas, S. A., Henderson, C. J., McLellan, L. I., Wolf, C. R., Cavin, C., & Hayes, J. D. (2001) · PubMed · Cited by 657 · see citing works

The kelch repeat superfamily of proteins: propellers of cell function

Adams, J. C., Kelso, R., & Cooley, L. (2000) · Trends in Cell Biology · doi:10.1016/s0962-8924(99)01673-6 · Cited by 603 · see citing works

Regulation of γ-Glutamylcysteine Synthetase Subunit Gene Expression by the Transcription Factor Nrf2

Wild, A. C., Moinova, H., & Mulcahy, R. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.47.33627 · Cited by 595 · see citing works

Potency of Michael reaction acceptors as inducers of enzymes that protect against carcinogenesis depends on their reactivity with sulfhydryl groups

Dinkova‐Kostova, A. T., Massiah, M. A., Bozak, R. E., Hicks, R. J., & Talalay, P. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.051632198 · Cited by 594 · see citing works

Nrf2 is essential for protection against acute pulmonary injury in mice

Chan, K., & Kan, Y. W. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.22.12731 · Cited by 574 · see citing works

Nrf2 and Nrf1 in association with Jun proteins regulate antioxidant response element-mediated expression and coordinated induction of genes encoding detoxifying enzymes

Radjendirane, V., & Jaiswal, A. K. (1998) · Oncogene · doi:10.1038/sj.onc.1202237 · Cited by 566 · 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

Constitutive and β-Naphthoflavone-induced Expression of the Human γ-Glutamylcysteine Synthetase Heavy Subunit Gene Is Regulated by a Distal Antioxidant Response Element/TRE Sequence

Mulcahy, R., Wartman, M. A., Bailey, H. H., & Gipp, J. J. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.11.7445 · Cited by 455 · see citing works

Regulation of transcription by dimerization of erythroid factor NF-E2 p45 with small Maf proteins

Igarashi, K., Kataokat, K., Itoh, K., Hayashi, N., Nishizawa, M., & Yamamoto, M. (1994) · Nature · doi:10.1038/367568a0 · Cited by 444 · see citing works

Chemoprotection against cancer by Phase 2 enzyme induction

Talalay, P., Fahey, J. W., Holtzclaw, W. D., Prestera, T., & Zhang, Y. (1995) · Toxicology Letters · doi:10.1016/0378-4274(95)03553-2 · Cited by 444 · see citing works

Kelch encodes a component of intercellular bridges in Drosophila egg chambers

Xue, F. (1993) · Cell · doi:10.1016/0092-8674(93)90397-9 · Cited by 440 · see citing works

Mechanism of Heme Oxygenase-1 Gene Activation by Cadmium in MCF-7 Mammary Epithelial Cells

Alam, J., Wicks, C., Stewart, D., Gong, P., Touchard, C. L., Otterbein, S. L., Choi, A. M. K., Burow, M. E., & Tou, J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004729200 · Cited by 406 · see citing works

The BTB/POZ domain: a new protein-protein interaction motif common to DNA- and actin-binding proteins.

Albagli, O., Dhordain, P., Deweindt, C., Lecocq, G., & Leprince, D. (1995) · PubMed · Cited by 377 · see citing works

Role of Transcription Factor Nrf2 in the Induction of Hepatic Phase 2 and Antioxidative Enzymes in vivo by the Cancer Chemoprotective Agent, 3H-1, 2-Dithiole-3-thione

Kwak, M., Itoh, K., Yamamoto, M. P., Sutter, T. R., & Kensler, T. W. (2001) · Molecular Medicine · doi:10.1007/bf03401947 · Cited by 357 · see citing works

All in the Family: the BTB/POZ, KRAB, and SCAN Domains

Collins, T., Stone, J. R., & Williams, A. J. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.11.3609-3615.2001 · Cited by 345 · see citing works

Role of transcription factor Nrf2 in the induction of hepatic phase 2 and antioxidative enzymes in vivo by the cancer chemoprotective agent, 3H-1, 2-dimethiole-3-thione.

Kwak, M.-K., Itoh, K., Yamamoto, M. P., Sutter, T. R., & Kensler, T. W. (2001) · PubMed Central · Cited by 330 · see citing works

The Nrf2 transcription factor contributes both to the basal expression of glutathione S-transferases in mouse liver and to their induction by the chemopreventive synthetic antioxidants, butylated hydroxyanisole and ethoxyquin

Hayes, J. D., Chanas, S. A., Henderson, C. J., McMahon, M. J., Sun, C., Moffat, G. J., Wolf, C. R., & Yamamoto, M. P. (2000) · Biochemical Society Transactions · doi:10.1042/bst0280033 · Cited by 321 · see citing works

Induction of xenobiotic enzymes by the map kinase pathway and the antioxidant or electrophile response element (ARE/EpRE),†,‡

Kong, A., Owuor, E. D., Yu, R., Hebbar, V., Chen, C., Hu, R., & Mandlekar, S. (2001) · Drug Metabolism Reviews · doi:10.1081/dmr-120000652 · Cited by 318 · see citing works

Impaired expression of glutathione synthetic enzyme genes in mice with targeted deletion of the Nrf2 basic-leucine zipper protein

Chan, J. Y., & Kwong, M. (2000) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/s0167-4781(00)00238-4 · Cited by 317 · see citing works

Hemin-induced Activation of the Thioredoxin Gene by Nrf2

Kim, Y. C., Masutani, H., Yamaguchi, Y., Itoh, K., Yamamoto, M. P., & Yodoi, J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100103200 · Cited by 313 · see citing works

Accelerated DNA adduct formation in the lung of the Nrf2 knockout mouse exposed to diesel exhaust

Aoki, Y., Sato, H., Nishimura, N., Takahashi, S., Itoh, K., & Yamamoto, M. (2001) · Toxicology and Applied Pharmacology · doi:10.1006/taap.2001.9176 · Cited by 297 · see citing works

Crystal structure of the BTB domain from PLZF

Ahmad, K. F., Engel, C. K., & Privé, G. G. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.21.12123 · Cited by 296 · see citing works

An Electrophile Responsive Element (EpRE) Regulates β-Naphthoflavone Induction of the Human γ-Glutamylcysteine Synthetase Regulatory Subunit Gene

Moinova, H., & Mulcahy, R. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.24.14683 · Cited by 255 · see citing works

Up-Regulation of the Human γ-Glutamylcysteine Synthetase Regulatory Subunit Gene Involves Binding of Nrf-2 to an Electrophile Responsive Element

Moinova, H., & Mulcahy, R. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.1109 · Cited by 245 · see citing works

Role of phase 2 enzyme induction in chemoprotection by dithiolethiones

Kwak, M.-K., Egner, P. A., Dolan, P. M., Ramos‐Gómez, M., Groopman, J. D., Itoh, K., Yamamoto, M. P., & Kensler, T. W. (2001) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/s0027-5107(01)00190-7 · Cited by 241 · see citing works

Inhibition of ERK and p38 MAP Kinases Inhibits Binding of Nrf2 and Induction of GCS Genes

Zipper, L. M., & Mulcahy, R. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.3830 · Cited by 238 · see citing works

Phosphatidylinositol 3-Kinase, Not Extracellular Signal-regulated Kinase, Regulates Activation of the Antioxidant-Responsive Element in IMR-32 Human Neuroblastoma Cells

Lee, J., Hanson, J. M., Chu, W. A., & Johnson, J. A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100734200 · Cited by 227 · see citing works

Small Maf (MafG and MafK) Proteins Negatively Regulate Antioxidant Response Element-mediated Expression and Antioxidant Induction of the NAD(P)H:Quinone Oxidoreductase1 Gene

Dhakshinamoorthy, S., & Jaiswal, A. K. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003531200 · Cited by 205 · see citing works

In-Depth Mutational Analysis of the Promyelocytic Leukemia Zinc Finger BTB/POZ Domain Reveals Motifs and Residues Required for Biological and Transcriptional Functions

Melnick, A. M., Ahmad, K. F., Arai, S., Polinger, A., Ball, H. J., Borden, K. L. B., Carlile, G. W., Privé, G. G., & Licht, J. D. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.17.6550-6567.2000 · Cited by 195 · see citing works

Nrf2 and c-Jun regulation of antioxidant response element (ARE)-mediated expression and induction of γ-glutamylcysteine synthetase heavy subunit gene

Jeyapaul, J., & Jaiswal, A. K. (2000) · Biochemical Pharmacology · doi:10.1016/s0006-2952(00)00256-2 · Cited by 193 · see citing works

Drosophila Kelch Is an Oligomeric Ring Canal Actin Organizer

Robinson, D. N., & Cooley, L. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.138.4.799 · Cited by 161 · see citing works

The Rat Quinone Reductase Antioxidant Response Element

Favreau, L. V., & Pickett, C. B. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.41.24468 · Cited by 152 · see citing works

Transcriptional regulation of a rat liver glutathione S-transferase Ya subunit gene. Analysis of the antioxidant response element and its activation by the phorbol ester 12-O-tetradecanoylphorbol-13-acetate.

Nguyen, T. H., Rushmore, T. H., & Pickett, C. B. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)36880-1 · Cited by 150 · see citing works

Dependence of Globin Gene Expression in Mouse Erythroleukemia Cells on the NF-E2 Heterodimer

Kotkow, K. J., & Orkin, S. H. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.8.4640 · Cited by 147 · see citing works

Chemoprotection by Organosulfur Inducers of Phase 2 Enzymes: Dithiolethiones and Dithiins

Kensler, T. W., Curphey, T. J., Maxiutenko, Y., & Roebuck, B. D. (2000) · Drug metabolism and drug interactions · doi:10.1515/dmdi.2000.17.1-4.3 · Cited by 131 · see citing works

Nrf2-Dependent Activation of the Antioxidant Responsive Element by tert-Butylhydroquinone Is Independent of Oxidative Stress in IMR-32 Human Neuroblastoma Cells

Lee, J., Moehlenkamp, J. D., Hanson, J. M., & Johnson, J. A. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.4106 · Cited by 124 · see citing works

Human small Maf proteins form heterodimers with CNC family transcription factors and recognize the NF-E2 motif

Toki, T., Itoh, J., Kitazawa, J., Arai, K., Hatakeyama, K., Akasaka, J.-I., Igarashi, K., Nomura, N., Yokoyama, M., Yamamoto, M. P., et al. (1997) · Oncogene · doi:10.1038/sj.onc.1201024 · Cited by 116 · see citing works

The Essential Role of Phosphatidylinositol 3-Kinase and of p38 Mitogen-Activated Protein Kinase Activation in the Antioxidant Response Element-Mediated rGSTA2 Induction by Decreased Glutathione in H4IIE Hepatoma Cells

Kang, K. W., Ryu, J. H., & Kim, S. G. (2000) · Molecular Pharmacology · doi:10.1124/mol.58.5.1017 · Cited by 110 · see citing works

Overlapping antioxidant response element and PMA responseelement sequences mediate basal and β-naphthoflavone-induced expression of the human γ-glutamylcysteine synthetase catalytic subunit gene

Wild, A. C., Gipp, J. J., & Mulcahy, R. (1998) · Biochemical Journal · doi:10.1042/bj3320373 · Cited by 108 · see citing works

The N-terminal POZ Domain of GAGA Mediates the Formation of Oligomers That Bind DNA with High Affinity and Specificity

Espinás, M. L., Jiménez-Garcı́a, E., Vaquero, A., Canudas, S., Bernués, J., & Azorı́n, F. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.23.16461 · Cited by 106 · see citing works

Characterization of Mayven, a Novel Actin-binding Protein Predominantly Expressed in Brain

Soltysik-Española, M., Rogers, R. A., Jiang, S., Kim, T., Gaedigk, R., White, R. A., Avraham, H. K., & Avraham, S. (1999) · Molecular Biology of the Cell · doi:10.1091/mbc.10.7.2361 · Cited by 99 · see citing works

ENC-1 : A Novel Mammalian Kelch -Related Gene Specifically Expressed in the Nervous System Encodes an Actin-Binding Protein

Hernandez, M., Andrés-Barquin, P. J., Martı́nez, S., Bulfone, A., Rubenstein, J. L. R., & Israel, M. A. (1997) · Journal of Neuroscience · doi:10.1523/jneurosci.17-09-03038.1997 · Cited by 97 · see citing works

Structure-function studies of the BTB/POZ transcriptional repression domain from the promyelocytic leukemia zinc finger oncoprotein.

Li, X., Peng, H., Schultz, D., López-Guisa, J. M., Rauscher, F. J., & Marmorstein, R. (1999) · PubMed · Cited by 96 · see citing works

A human homologue of Drosophila kelch associates with myosin‐VIIa in specialized adhesion junctions

Velichkova, M., Guttman, J. A., Warren, C. M., Eng, L., Kline, K., Vogl, A. W., & Hasson, T. (2002) · Cell Motility and the Cytoskeleton · doi:10.1002/cm.10025 · Cited by 90 · see citing works

Human MafG Is a Functional Partner for p45 NF-E2 in Activating Globin Gene Expression

Blank, V., Kim, M. J., & Andrews, N. C. (1997) · Blood · doi:10.1182/blood.v89.11.3925 · Cited by 83 · see citing works

TCF11/Nrf1 overexpression increases the intracellular glutathione level and can transactivate the γ-glutamylcysteine synthetase (GCS) heavy subunit promoter

Myhrstad, M. C. W., Husberg, C., Murphy, P., Nordström, O., Blomhoff, R., Moskaug, J. Ø., & Kolstø, A. (2001) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/s0167-4781(00)00276-1 · Cited by 64 · see citing works

Actin-Binding Properties and Colocalization with Actin During Spermiogenesis of Mammalian Sperm Calicin1

Lécuyer, C., Dacheux, J., Hermand, E., Mazeman, E., Rousseaux, J., & Rousseaux‐Prévost, R. (2000) · Biology of Reproduction · doi:10.1095/biolreprod63.6.1801 · Cited by 62 · see citing works

Isolation and characterization of IPP, a novel human gene encoding an actin-binding, kelch-like protein

Kim, I. F., Mohammadi, E., & Huang, R. C. C. (1999) · Gene · doi:10.1016/s0378-1119(99)00006-2 · Cited by 41 · 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

The selective autophagy substrate p62 activates the stress responsive transcription factor Nrf2 through inactivation of Keap1

Komatsu, M., Kurokawa, H., Waguri, S., Taguchi, K., Kobayashi, A., Ichimura, Y., Sou, Y., Ueno, I., Sakamoto, A., Tong, K. I., et al. (2010) · Nature Cell Biology · doi:10.1038/ncb2021 · Cited by 2,422 · 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

Nrf2–Keap1 defines a physiologically important stress response mechanism

Motohashi, H., & Yamamoto, M. (2004) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2004.09.003 · Cited by 1,725 · see citing works

Nrf2:INrf2 (Keap1) signaling in oxidative stress

Kaspar, J. W., Niture, S. K., & Jaiswal, A. K. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.07.035 · Cited by 1,646 · 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

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

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

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 signaling in coordinated activation of antioxidant gene expression

Jaiswal, A. K. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.02.074 · Cited by 1,254 · 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

Keap1-dependent proteasomal degradation of transcription factor Nrf2 contributes to the negative regulation of antioxidant response element-driven gene expression

McMahon, M., Itoh, K., Yamamoto, M., & Hayes, J. D. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300931200 · Cited by 1,141 · 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

Mechanistic Studies of the Nrf2-Keap1 Signaling Pathway

Zhang, D. D. (2006) · Drug Metabolism Reviews · doi:10.1080/03602530600971974 · Cited by 1,091 · 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 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

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

Oxidative and Electrophilic Stresses Activate Nrf2 through Inhibition of Ubiquitination Activity of Keap1

Kobayashi, A., Kang, M.-I., Watai, Y., Tong, K. I., Shibata, T., Uchida, K., & Yamamoto, M. P. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.26.1.221-229.2006 · Cited by 933 · 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

Keap1-null mutation leads to postnatal lethality due to constitutive Nrf2 activation

Wakabayashi, N., Itoh, K., Wakabayashi, J., Motohashi, H., Noda, S., Takahashi, S., Imakado, S., KOTSUJI, T., Otsuka, F., Roop, D. R., et al. (2003) · Nature Genetics · doi:10.1038/ng1248 · Cited by 881 · 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

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

Molecular mechanism activating nrf2–keap1 pathway in regulation of adaptive response to electrophiles

Itoh, K., Tong, K. I., & Yamamoto, M. P. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.02.075 · Cited by 866 · 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

A Noncanonical Mechanism of Nrf2 Activation by Autophagy Deficiency: Direct Interaction between Keap1 and p62

Lau, A., Wang, X.-J., Zhao, F. L., Villeneuve, N. F., Wu, T., Jiang, T., Sun, Z., White, E., & Zhang, D. D. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.00248-10 · Cited by 851 · see citing works

The Keap1–Nrf2–ARE Pathway As a Potential Preventive and Therapeutic Target: An Update

Lu, M., Ji, J., Jiang, Z., & You, Q. (2016) · Medicinal Research Reviews · doi:10.1002/med.21396 · Cited by 801 · see citing works

Stress-activated cap’n’collar transcription factors in aging and human disease

Sykiotis, G. P., & Bohmann, D. (2010) · Science Signaling · doi:10.1126/scisignal.3112re3 · Cited by 776 · 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

Expression of Nrf2 in Neurodegenerative Diseases

Ramsey, C. P., Glass, C. A., Montgomery, M. B., Lindl, K. A., Ritson, G. P., Chia, L. A., Hamilton, R. L., Chu, C. T., & Jordan-Sciutto, K. L. (2007) · Journal of Neuropathology and Experimental Neurology · doi:10.1097/nen.0b013e31802d6da9 · Cited by 760 · 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

Small Molecule Modulators of <scp>K</scp> eap1‐ <scp>N</scp> rf2‐ <scp>ARE</scp> Pathway as Potential Preventive and Therapeutic Agents

Magesh, S., Chen, Y., & Hu, L. (2012) · Medicinal Research Reviews · doi:10.1002/med.21257 · Cited by 760 · 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

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

Modulation of Gene Expression by Cancer Chemopreventive Dithiolethiones through the Keap1-Nrf2 Pathway

Kwak, M.-K., Wakabayashi, N., Itoh, K., Motohashi, H., Yamamoto, M. P., & Kensler, T. W. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m211898200 · Cited by 661 · see citing works

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

Chen, W., Sun, Z., Wang, X.-J., Jiang, T., Huang, Z., Fang, D., & Zhang, D. D. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.04.029 · Cited by 638 · see citing works

The Dual Roles of NRF2 in Cancer

Menegon, S., Columbano, A., & Giordano, S. (2016) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2016.05.002 · Cited by 633 · 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

Increased Protein Stability as a Mechanism That Enhances Nrf2-mediated Transcriptional Activation of the Antioxidant Response Element

Nguyen, T., Sherratt, P. J., Huang, H.-C., Yang, C. S., & Pickett, C. B. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m207293200 · Cited by 615 · 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

Basic Principles and Emerging Concepts in the Redox Control of Transcription Factors

Brigelius-Flohé, R., & Flohé, L. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3534 · Cited by 577 · see citing works

Cellular mechanisms of redox cell signalling: role of cysteine modification in controlling antioxidant defences in response to electrophilic lipid oxidation products

Levonen, A., Landar, A. L., Ramachandran, A., CEASER, E. K., Dickinson, D. A., Zanoni, G., Morrow, J. D., & Darley-Usmar, V. M. (2004) · Biochemical Journal · doi:10.1042/bj20031049 · Cited by 559 · see citing works

Coordination of ER and oxidative stress signaling: The PERK/Nrf2 signaling pathway

Cullinan, S. B., & Diehl, J. A. (2006) · The International Journal of Biochemistry &amp; Cell Biology · doi:10.1016/j.biocel.2005.09.018 · Cited by 554 · see citing works

Cancer Chemoprevention Mechanisms Mediated Through the Keap1–Nrf2 Pathway

Hayes, J. D., McMahon, M. J., Chowdhry, S., & Dinkova‐Kostova, A. T. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3221 · Cited by 540 · 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

Scaffolding of Keap1 to the actin cytoskeleton controls the function of Nrf2 as key regulator of cytoprotective phase 2 genes

Kang, M.-I., Kobayashi, A., Wakabayashi, N., Kim, S.-G., & Yamamoto, M. P. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0308347100 · Cited by 536 · see citing works

Nrf2 as a novel molecular target for chemoprevention

Lee, J., & Surh, Y. (2004) · Cancer Letters · doi:10.1016/j.canlet.2004.09.042 · Cited by 514 · see citing works

Physiological Significance of Reactive Cysteine Residues of Keap1 in Determining Nrf2 Activity

Yamamoto, T., Suzuki, T., Kobayashi, A., Wakabayashi, J., Maher, J. M., Motohashi, H., & Yamamoto, M. P. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01704-07 · Cited by 515 · see citing works

Discovery of the Negative Regulator of Nrf2, Keap1: A Historical Overview

Itoh, K., Mimura, J., & Yamamoto, M. P. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3222 · Cited by 513 · 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

Two-site substrate recognition model for the Keap1-Nrf2 system: A hinge and latch mechanism

Tong, K. I., Kobayashi, A., Katsuoka, F., & Yamamoto, M. (2006) · Biological Chemistry · doi:10.1515/bc.2006.164 · Cited by 473 · see citing works

Nrf2 Defends the Lung from Oxidative Stress

Cho, H., Reddy, S. P., & Kleeberger, S. R. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.76 · Cited by 463 · see citing works

Degradation of transcription factor Nrf2 via the ubiquitin-proteasome pathway and stabilization by cadmium

Stewart, D., Killeen, E., Naquin, R., Alam, S., & Alam, J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m209195200 · Cited by 463 · see citing works

The pathways and molecular mechanisms regulating Nrf2 activation in response to chemical stress

Nguyen, T., Yang, C. S., & Pickett, C. B. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.04.033 · Cited by 463 · see citing works

Modifying specific cysteines of the electrophile-sensing human Keap1 protein is insufficient to disrupt binding to the Nrf2 domain Neh2

Eggler, A. L., Liu, G., Pezzuto, J. M., van Breemen, R. B., & Mesecar, A. D. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0502402102 · Cited by 459 · see citing works

Regulation of the Nrf2–Keap1 Antioxidant Response by the Ubiquitin Proteasome System: An Insight into Cullin-Ring Ubiquitin Ligases

Villeneuve, N. F., Lau, A., & Zhang, D. D. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3211 · Cited by 423 · see citing works

Identification of Sensor Cysteines in Human Keap1 Modified by the Cancer Chemopreventive Agent Sulforaphane

Hong, F., Freeman, M. L., & Liebler, D. C. (2005) · Chemical Research in Toxicology · doi:10.1021/tx0502138 · Cited by 404 · see citing works

The Keap1–Nrf2 pathway: promising therapeutic target to counteract ROS-mediated damage in cancers and neurodegenerative diseases

Deshmukh, P. H., Unni, S., Krishnappa, G., & Padmanabhan, B. (2016) · Biophysical Reviews · doi:10.1007/s12551-016-0244-4 · Cited by 397 · see citing works

Nrf2 signaling and cell survival

Niture, S. K., Kaspar, J. W., Shen, J., & Jaiswal, A. K. (2009) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2009.06.009 · Cited by 397 · see citing works

Heme oxygenase-1 induction by NRF2 requires inactivation of the transcriptional repressor BACH1

Reichard, J. F., Motz, G. T., & Puga, A. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm638 · Cited by 393 · see citing works

Activation of NRF2 by Nitrosative Agents and H2O2 Involves KEAP1 Disulfide Formation

Fourquet, S., Guérois, R., Biard, D. S. F., & Tolédano, M. B. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.051714 · Cited by 378 · see citing works

The Role of Keap1 in Cellular Protective Responses

Dinkova‐Kostova, A. T., Holtzclaw, W. D., & Kensler, T. W. (2005) · Chemical Research in Toxicology · doi:10.1021/tx050217c · Cited by 378 · see citing works

Molecular Mechanism of Nrf2 Activation by Oxidative Stress

Kang, K. W., Lee, S. J., & Kim, S. G. (2005) · Antioxidants and Redox Signaling · doi:10.1089/ars.2005.7.1664 · Cited by 361 · see citing works

The role of chalcones in suppression of NF-κB-mediated inflammation and cancer

Yadav, V. R., Prasad, S., Sung, B., & Aggarwal, B. B. (2010) · International Immunopharmacology · doi:10.1016/j.intimp.2010.12.006 · Cited by 342 · see citing works

The Nrf2–Keap1 defence pathway: Role in protection against drug-induced toxicity

Copple, I. M., Goldring, C. E., Kitteringham, N. R., & Park, B. K. (2007) · Toxicology · doi:10.1016/j.tox.2007.10.029 · 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

Discovery of direct inhibitors of Keap1–Nrf2 protein–protein interaction as potential therapeutic and preventive agents

Abed, D. A., Goldstein, M., Albanyan, H., Jin, H., & Hu, L. (2015) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2015.05.008 · Cited by 330 · see citing works

Atypical protein kinase C mediates activation of NF-E2-related factor 2 in response to oxidative stress

Numazawa, S., Ishikawa, M., Yoshida, A., Tanaka, S., & Yoshida, T. (2003) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00043.2003 · Cited by 316 · 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

PGAM5 tethers a ternary complex containing Keap1 and Nrf2 to mitochondria

Lo, S.-C., & Hannink, M. (2008) · Experimental Cell Research · doi:10.1016/j.yexcr.2008.02.014 · Cited by 300 · 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

Chemoprevention through the Keap1–Nrf2 signaling pathway by phase 2 enzyme inducers

Kwak, M.-K., Wakabayashi, N., & Kensler, T. W. (2004) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2004.06.041 · Cited by 311 · see citing works

Targeting NRF2 signaling for cancer chemoprevention

Kwak, M.-K., & Kensler, T. W. (2009) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2009.08.028 · Cited by 306 · see citing works

Nrf2-ARE stress response mechanism: A control point in oxidative stress-mediated dysfunctions and chronic inflammatory diseases

Singh, S., Vrishni, S., Singh, B. K., Rahman, I., & Kakkar, P. (2010) · Free Radical Research · doi:10.3109/10715762.2010.507670 · Cited by 294 · 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

NRF2 Blockade Suppresses Colon Tumor Angiogenesis by Inhibiting Hypoxia-Induced Activation of HIF-1α

Kim, T., Hur, E.-G., Kang, S., Kim, J., Thapa, D., Lee, Y. M., Ku, S., Jung, Y., & Kwak, M. (2011) · Cancer Research · doi:10.1158/0008-5472.can-10-3007 · Cited by 292 · see citing works

Importance of phase 2 gene regulation in protection against electrophile and reactive oxygen toxicity and carcinogenesis

Talalay, P., Dinkova‐Kostova, A. T., & Holtzclaw, W. D. (2003) · Advances in Enzyme Regulation · doi:10.1016/s0065-2571(02)00038-9 · Cited by 289 · see citing works

Nrf2 Mediates the Induction of Ferritin H in Response to Xenobiotics and Cancer Chemopreventive Dithiolethiones

Pietsch, E. C., Chan, J. Y., Torti, F. M., & Torti, S. V. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210664200 · Cited by 284 · see citing works

Enhancing Expression of Nrf2-Driven Genes Protects the Blood–Brain Barrier after Brain Injury

Zhao, J., Moore, A. N., Redell, J. B., & Dash, P. K. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.1683-07.2007 · Cited by 274 · see citing works

Heme Oxygenase-1: An Anti-Inflammatory Effector in Cardiovascular, Lung, and Related Metabolic Disorders

Ryter, S. W. (2022) · Antioxidants · doi:10.3390/antiox11030555 · Cited by 281 · see citing works

Induction of the Nrf2-driven Antioxidant Response Confers Neuroprotection during Mitochondrial Stress in Vivo

Shih, A. Y., Imbeault, S., Barakauskas, V., Erb, H., Jiang, L., Li, P., & Murphy, T. H. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414635200 · Cited by 273 · see citing works

Keap1 Mutations and Nrf2 Pathway Activation in Epithelial Ovarian Cancer

Konstantinopoulos, P. A., Spentzos, D., Fountzilas, E., Francoeur, N. J., Sanisetty, S., Grammatikos, A. P., Hecht, J. L., & Cannistra, S. A. (2011) · Cancer Research · doi:10.1158/0008-5472.can-10-4668 · Cited by 272 · 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

Beyond repression of Nrf2: An update on Keap1

Kopacz, A., Klóska, D., Forman, H. J., Józkowicz, A., & Grochot‐Przeczek, A. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.03.023 · Cited by 262 · see citing works

Macrophage achieves self-protection against oxidative stress-induced ageing through the Mst-Nrf2 axis

Wang, P., Geng, J., Gao, J., Zhao, H., Li, J., Shi, Y., Yang, B., Chen, X., Linghu, Y., Sun, X., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-08680-6 · Cited by 265 · 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 263 · see citing works

Tumor cell survival pathways activated by photodynamic therapy: a molecular basis for pharmacological inhibition strategies

Broekgaarden, M., Weijer, R., van Gulik, T. M., Hamblin, M. R., & Heger, M. (2015) · Cancer and Metastasis Reviews · doi:10.1007/s10555-015-9588-7 · Cited by 261 · see citing works

Erk Activation Is Required for Nrf2 Nuclear Localization during Pyrrolidine Dithiocarbamate Induction of Glutamate Cysteine Ligase Modulatory Gene Expression in HepG2 Cells

Zipper, L. M. (2003) · Toxicological Sciences · doi:10.1093/toxsci/kfg083 · Cited by 252 · see citing works

The Nrf2-ARE Pathway: A Valuable Therapeutic Target for the Treatment of Neurodegenerative Diseases

Gururaj Joshi, A., & Johnson, J. A. (2012) · Recent Patents on CNS Drug Discovery · doi:10.2174/157488912803252023 · Cited by 246 · 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 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

Keap1 Regulates the Oxidation-Sensitive Shuttling of Nrf2 into and out of the Nucleus via a Crm1-Dependent Nuclear Export Mechanism

Velichkova, M., & Hasson, T. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.11.4501-4513.2005 · Cited by 237 · 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

Activation of the Nrf2–ARE signaling pathway: a promising strategy in cancer prevention

Giudice, A., & Montella, M. (2006) · BioEssays · doi:10.1002/bies.20359 · Cited by 232 · see citing works

Keap1 is a forked-stem dimer structure with two large spheres enclosing the intervening, double glycine repeat, and C-terminal domains

Ogura, T., Tong, K. I., Mio, K., Maruyama, Y., Kurokawa, H., Sato, C., & Yamamoto, M. P. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0914036107 · Cited by 232 · see citing works

A strategy for cancer prevention: Stimulation of the Nrf2-ARE signaling pathway

Zhang, Y., & Gordon, G. (2004) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.885.3.7 · 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

Mechanism of the Nrf2/Keap1/ARE signaling system

Tkachev, V., Брониславовна, М. Е., & Зенков, Н. К. (2011) · Biochemistry (Moscow) · doi:10.1134/s0006297911040031 · Cited by 228 · see citing works

Dietary Regulation of Keap1/Nrf2/ARE Pathway: Focus on Plant-Derived Compounds and Trace Minerals

Stefanson, A. L., & Bakovic, M. (2014) · Nutrients · doi:10.3390/nu6093777 · Cited by 226 · see citing works

Reactive Oxygen Production Induced by the Gut Microbiota: Pharmacotherapeutic Implications

Jones, R. M., Mercante, J. W., & Neish, A. S. (2012) · Current Medicinal Chemistry · doi:10.2174/092986712799828283 · Cited by 228 · see citing works

Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain

Itoh, K., Wakabayashi, N., Katoh, Y., Ishii, T., Igarashi, K., Engel, J. D., & Yamamoto, M. (1999) · Genes &amp; Development · doi:10.1101/gad.13.1.76 · Cited by 3,634 · 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

Scaffolding of Keap1 to the actin cytoskeleton controls the function of Nrf2 as key regulator of cytoprotective phase 2 genes

Kang, M.-I., Kobayashi, A., Wakabayashi, N., Kim, S.-G., & Yamamoto, M. P. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0308347100 · Cited by 536 · 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

Chapter 3 Site-Specific Modification of the Electrophile Sensor Protein Keap1 and Activation of Nrf2-Dependent Gene Expression

Liebler, D. C., Hong, F., Sekhar, K. R., & Freeman, M. L. (2006) · Advances in molecular toxicology · doi:10.1016/s1872-0854(06)01003-4 · Cited by 3 · see citing works