Protection against electrophile and oxidant stress by induction of the phase 2 response: Fate of cysteines of the Keap1 sensor modified by inducers

Manipulating the mouse embryo: A laboratory manual

Hogan, B. L. M., Costantini, F. D., & Lacy, E. (1986) · Cited by 4,460

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

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

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

Glutathione and glutathione-dependent enzymes represent a co-ordinately regulated defence against oxidative stress

Hayes, J. D., & McLellan, L. I. (1999) · Free Radical Research · doi:10.1080/10715769900300851 · Cited by 1,528

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

Regulatory Mechanisms Controlling Gene Expression Mediated by the Antioxidant Response Element

Nguyen, T., Sherratt, P. J., & Pickett, C. B. (2003) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.43.100901.140229 · Cited by 1,232

Activation of the OxyR Transcription Factor by Reversible Disulfide Bond Formation

Zheng, M., Åslund, F., & Storz, G. (1998) · Science · doi:10.1126/science.279.5357.1718 · Cited by 1,197

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

Sensitivity to carcinogenesis is increased and chemoprotective efficacy of enzyme inducers is lost in nrf2 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

New Functions of a Well-Known Protein: Prothymosin α Is Involved in Protecting Cells from Apoptosis and Oxidative Stress

Evstafieva, A. G., Karapetian, R. N., Rubtsov, Y. P., Filonov, G. S., Abaeva, I. S., Fateeva, T. V., Melnikov, S. V., Chichkova, N. V., & Vartapetian, A. B. (2005) · Molecular Biology · doi:10.1007/s11008-005-0079-8 · Cited by 1

Mechanisms by which natural polyphenols regulate the expression of cytoprotective genes

Xiao, H. (2010) · Discovery Research Portal (University of Dundee) · Cited by 1

Regulation of oxidoreductase enzymes during inflammation

Ingram, S. (2018) · Cited by 1

Lipid oxidation and nitration products as activators of cytoprotective Nrf2 signaling in the endothelium

Kansanen, E. (2012) · UEF eRepo (University of Eastern Finland) · Cited by 1

Cellular feedback to organotelluranes displays modulation of antioxidant proteins gene expressionPreprint

Pessoto, F. S., Yokomizo, C. H., Cunha, R. L. O. R., & Nantes, I. L. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.01.05.425411 · Cited by 1

Dl-3-n-Butylphthalide Promotes Cardiac Function, Inhibit Oxidative Stress and Myocardial Apoptosis of Chronic Heart Failure Mice via Stimulating Nrf2/HO-1 pathwayPreprint

Wang, Z., Zhang, Y., Yang, C., & Yang, H. (2021) · Research Square · doi:10.21203/rs.3.rs-834507/v1 · Cited by 1

Nrf2: a Transcription Factor that Modifies Susceptibility to Cigarette Smoke-Induced Pulmonary Oxidative Stress and Emphysema

Biswal, S. S., & Kensler, T. W. (2007) · Springer eBooks · doi:10.1007/3-540-32232-9_14 · Cited by 1

Faculty Opinions recommendation of 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.

Lipton, S. A. (2017) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.725601011.793538932 · Cited by 1

Der Einfluss des Transkriptionsfaktors Nuclear Factor-E2 P25-Related Factor 2 auf die Frakturheilung der Maus

Ayub, F. (2013) · Multimedialen Archiv und Publikationsserver der Christian-Albrechts-Universität zu Kiel (Christian-Albrechts-Universität zu Kiel)

Adipocyte protein carbonylation and oxidative stress in obesity-linked mitochondrial dysfunction and insulin resistance.

Curtis, J. (2011) · University of Minnesota Digital Conservancy (University of Minnesota)

Antioxidant Adaptive Response of Malignant Glioma Related to Resistance to Antitumor Treatment

Sawa, T., & Akaike, T. (2012) · InTech eBooks · doi:10.5772/23429

Phenotype-dependent regulation of the system XC- cystine/glutamate exchanger by glutathione levels in rat astrocyte primary cultures

Seib, T. (2010)

Modulation of Oxidative Stress by Keap1/Nrf2 Signaling inDrosophila: Implications for Human Diseases

Sykiotis, G. P., Rahman, M. M., & Bohmann, D. (2011) · Wiley eBooks · doi:10.1002/9781118148143.ch22

Principles of Redox Signaling

Chiarugi, P., Taddei, M. L., & Giannoni, E. (2015) · Oxidative stress in applied basic research and clinical practice · doi:10.1007/978-3-319-15539-5_1

Estudo dos polimorfismos Pro198Leu no gene da glutationa peroxidase 1 e -617C/A no gene do fator de transcrição Nrf2 com relação ao estresse oxidativo e ao estado nutricional relativo ao selênio de pacientes com diabetes mellitus tipo 1

de Alencar, L. L. (2014) · doi:10.11606/d.9.2014.tde-27052015-142459

The physiological, pharmacological and toxicological roles of Nrf2 in the kidney

Shelton, L. M. (2015) · University of Liverpool · doi:10.17638/02014505

The Role of the Nrf2-Keap1 Pathway in Autophagy and How it Contributes to Arsenic Carcinogenicity

Lau, A. (2012) · UA Campus Repository (The University of Arizona)

MECHANISTIC STUDY OF USP15-DEPENDENT DEUBIQUITINATION AND CHARACTERIZATION OF NATURAL COMPOUNDS THAT MODULATE THE NRF2-KEAP1 ANTIOXIDANT RESPONSE

Villeneuve, N. (2011) · UA Campus Repository (The University of Arizona)

Antioxidants and Anti-Inflammatory Drugs in the Treatment of Motor Neuron Disease

Esmaeili, M. A., & Kiaei, M. (2014) · Springer eBooks · doi:10.1007/978-3-642-30018-9_132

REVIEW PI3K, RSK, and mTOR Signal Networks for the GST Gene Regulation

Kim, S. G., & Lee, S. J. (2006)

Xenobiotic-metabolizing enzymes elevated in multiple mouse models of slow aging

Steinbaugh, M. J. (2012) · Deep Blue (University of Michigan)

Conformational Heterogeneity and Catalytic Promiscuity in Glutathione Transferases

Honaker, M. T. (2012) · ResearchWorks at the University of Washington (University of Washington)

MODIFICACIÓN DE PROTEÍNAS POR LÍPIDOS ELECTRÓFILOS: SELECTIVIDAD

Biológicas, E. I. (2007)

Overexpression of NF-E2 related factor 2 via viral-mediated gene transfer in vivo.

Imbeault, S. (2009) · cIRcle (University of British Columbia) · doi:10.14288/1.0092076

ROS production is required for follicle-stimulating hormone-induced Nrf2 activation in human epithelial ovarian cancer cells

Jie, M. A., Wang, Q., Hong, L. I. A. O., Yong-bin, Y. A. N. G., Jin, Z., Zhang, Z., Ya-ping, Z. H. U., & Feng, Y. (2013) · Academic Journal of Second Military Medical University · doi:10.3724/sp.j.1008.2012.00935

Potentiation of Cellular Defense Capacity by Phytochemicals Activating NF-E2-Related Factor 2 for the Prevention and/or Treatment of Alzheimer’s Disease

Park, G. H., & Jang, J. (2015) · Springer eBooks · doi:10.1007/978-4-431-55763-0_21

Funktionen der alternsrelevanten Proteine Thioredoxin-1 und Telomerase Reverse Transkriptase in umweltinduzierten Prozessen

Büchner, N. (2010) · Univ. Duesseldorf: Duesseldorfer Dokumenten- und Publikationsserver

THE INDUCIBLE NITRIC OXIDE SYNTHASE EXERTS ANTIOXIDANT EFFECTS IN ENDOTHELIAL CELLS VIA A ZINC -DEPENDENT SIGNALING PATHWAY

Forschungsgruppe, A. D., Am, I., Heinrich, M. M. D., & Kolb, V. (2006)

Measurement of sensitivity to DNA damaging agents

Sherin Mathew, T. (2017)

The SenCeeTox® Assay

Keller, D. J., Bauch, C., & Patel, P. (2017) · Springer eBooks · doi:10.1007/978-3-319-50353-0_26

Siah2, which causes a small-eye phenotype by degradation of PHD, regulates the level of Nrf2 escaped from Keap1

Baba, K. (2014) · Institutional Repositories DataBase (IRDB)

Modulators of Nrf2 Activation During Inflammation

Braidy, N. (2020) · Progress in inflammation research · doi:10.1007/978-3-030-44599-7_8

Introducción de respuesta antioxidante vía Nrf2 frente a la toxicidad del MPP+, en astrocitos provenientes de ratas de diferentes edades

Alarcón‐Aguilar, A. (2014) · doi:10.24275/uami.xd07gs71v

Faculty Opinions recommendation of Transcriptional regulation by nrf2.

Ji, L. L. (2021) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.731119952.793582094

DHA for Optimal Health

Meyer, B. J. (2018) · MDPI eBooks · doi:10.3390/books978-3-03842-972-2

Fatty liver disease

van de Wier, B. (2016) · Research Publications (Maastricht University) · doi:10.26481/dis.20160705bw

Two Faces of Nrf2 in Cancer

Yildiz, M., & Seğmen, H. (2022) · IntechOpen eBooks · doi:10.5772/intechopen.102753

Targeting the Transcription Factors of ROS Tumorigenic Pathways as a Therapeutic Strategy in Cancer

Sriramajayam, K., Gokulan, R. C., & Tharmalingam, J. (2022) · Handbook of Oxidative Stress in Cancer: Therapeutic Aspects · doi:10.1007/978-981-16-1247-3_275-1

Faculty Opinions recommendation of Keap1, the cysteine-based mammalian intracellular sensor for electrophiles and oxidants.

Lipton, S. A. (2017) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.726620955.793538940

Faculty Opinions recommendation of A metabolite-derived protein modification integrates glycolysis with KEAP1-NRF2 signalling.

Chandel, N. S. (2018) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.734229651.793552922

Participación de la vía tBHQ-Nrf2 en la protección del daño oxidante por 3NP en ratas viejas

Palacios, A. S. (2014) · doi:10.24275/uami.9g54xh819

Potential Neuroprotective Strategies for Ischemic Injuries

Farooqui, A. A. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-813596-9.00003-1 · Cited by 1

Calidad y proteoma de conidios de Metarhizium anisopliae producidos con atmósferas modificadas

García-Ortiz, N. (2018) · doi:10.24275/uami.nv9352884

Inducción de protección cruzada en los conidios libres al someterlos directamente a condiciones de estrés oxidante

Minjarez, J. M. Á. C. (2019) · doi:10.24275/uami.6q182k43h

Data from The Nuclear Matrix Protein, NRP/B, Enhances Nrf2-Mediated Oxidative Stress Responses in Breast Cancer Cells

Seng, S., Avraham, H. K., Jiang, S., Yang, S., Sekine, M., Kimelman, N., Li, H., & Avraham, S. (2023) · doi:10.1158/0008-5472.c.6496883

Μελέτη της βιολογικής δράσης εκχυλισμάτων γηγενών ποικιλιών οίνου, σε in vitro και in vivo συστήματα με τη χρήση μοριακών τεχνικών

Τέκος, Φ. (2023) · doi:10.12681/eadd/53987

Efecto de los ácidos grasos W-3 sobre el sistema dopaminérgico nigroestriatal ante el daño generado por rotenona, modelo experimental de la enfermedad de Parkinson

Serrano‐García, N. (2015) · doi:10.24275/uami.tm70mv223

Coenzyme Q0, a quinone derivative from Antrodia camphorata, inhibits epithelial-mesenchymal transition by activating the Nrf2 signaling pathway in TGF-β-stimulated adult retinal pigment epithelial cells to improve age-related macular degeneration and proliferative vitreoretinopathy

Yang, H., Yen, H., Chang, I.-C., Vadivalagan, C., Chen, S.-J., Lee, C.-C., Jane, W., Hseu, J., & Hseu, Y. (2023) · Journal of Functional Foods · doi:10.1016/j.jff.2023.105978

Identification of novel Nrf2-activating neuroprotective agents: Elucidation of structural congeners of (-)-galiellalactone and congener-based novel Nrf2 activators

Kim, T., Kim, H. S., Bang, Y., Kwon, Y., Kim, J., Choi, H. J., & Suh, Y. (2024) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2024.107109

Additional file 2 of Loss-of-function mutations in KEAP1 drive lung cancer progression via KEAP1/NRF2 pathway activation

Gong, M., Li, Y., Ye, X., Zhang, L., Wang, Z., Xu, X., Shen, Y., & Zheng, C. (2020) · Figshare · doi:10.6084/m9.figshare.12552329

Breast Cancer

Ross, I. A. (2024) · Springer eBooks · doi:10.1007/978-3-031-63681-3_8

The Impact of Gut Hormones and the Gut-Adipose-Liver Axis in Metabolic Syndrome: An Overview of Nrf2 Involvement in the Signaling Pathways

Sonakar, A. K., Kumar, A. V., Kalita, B. C., Garg, V. K., Buttar, H. S., Kashyap, D., & Wilson, D. W. (2024) · Advances in biochemistry in health and disease · doi:10.1007/978-3-031-75686-3_15

Identification of Keap1a and Keap1b in Grass Carp (Ctenopharyngodon Idellus) and Response of Keap1-Nrf2 Signaling Pathway to Heat Stress Oxidative StressPreprint

Feng, J., Liu, H., Yang, Y., Yu, H., Yang, M., Tian, M., Lai, M., Wu, Y., & Du, A. (2025) · SSRN Electronic Journal · doi:10.2139/ssrn.5139638

Protective Effects of Ginsenosides Rg3, Rk1, Rg5 and Antioxi-Dants in Black Ginseng on Alcohol-Induced Fatty Liver Via the Keap1–Nrf2–Ho-1 PathwayPreprint

Oh, H.-B., Jeong, D.-E., Cho, J.-H., Yoon, H.-B., Lee, D., Yoo, J.-H., Hwang, D.-I., Kim, D.-W., Park, Y.-G., Oh, H., et al. (2025) · SSRN Electronic Journal · doi:10.2139/ssrn.5251627

Ellagic acid mediates cardioprotection against adrenaline-induced toxicity via PI3K/AKT and Keap1-NRF2 axes

Aldayel, T. S., Haleka, S. A. A., Ebaid, H. M., El‐Fadeal, N. M. A., Abdelrazek, H. M. A., El-Hak, H. N. G., Darwish, K. M., & Rashwan, H. M. (2025) · Scientific Reports · doi:10.1038/s41598-025-21317-7 · Cited by 1

Investigating dimethyl fumarate derivatives as drugs against oxidative stress using the molecular docking with KEAP1 protein

Emamian, S., Hosseini, J., & Ali-Asgari, S. (2025) · فصلنامه علوم پزشکی دانشگاه آزاد اسلامی واحد پزشکی تهران · doi:10.61882/iau.35.4.406

Post-Transcriptional Regulation of Nrf2: Novel Mechanisms beyond Keap1

Wu, T. (2013) · UA Campus Repository (The University of Arizona)

Potential Neuroprotective Strategies for Ischemic Injury

Farooqui, A. A. (2010) · Springer eBooks · doi:10.1007/978-1-4419-6652-0_3

ANALYSIS OF ELECTROPHILE-INDUCED NRF2 GENE ACTIVATION

Hong, F. (2005) · UA Campus Repository (The University of Arizona)

Regulatory impact of phytochemicals on metabolic diseases by targeting Nrf2-ARE signaling mechanism

Gambhir, L., Pokhriyal, A., Kapoor, N., & Kandwal, P. (2025) · Elsevier eBooks · doi:10.1016/b978-0-443-31698-2.00012-6

NRF2 controls a diverse network of antiviral effectors with p62 acting as a central restriction factor effective across virus families

Pedersen, A., Blay‐Cadanet, J., Storgaard, J., Hernáez, B., Thyrsted, J., Bach-Nielsen, C. S., Twayana, K. S., Jørgensen, S. E., Río-Bergé, C., Poulsen, C., et al. (2026) · Redox Biology · doi:10.1016/j.redox.2026.104135

Les allergies cutanées aux fragrances : mécanisme d'action et rôle du facteur de transcription Nrf2. Du modèle 2D au modèle 3D.

Raffalli, C. (2018) · theses.fr (ABES) · doi:10.70675/4900e006zd72bz460czbce9z30cd5e7312bc

Coopération entre les isoformes TAp73 et la signalisation TGF-β dans la régulation de l'expression de la NO Synthase inductible

Cabrié, A. (2017) · theses.fr (ABES) · doi:10.70675/df567380z9a01z4262z9a43z7666c8df7b0f

Le donneur de rein décédé, principes physiopathologiques et innovations thérapeutiques

Kerforne, T. (2018) · theses.fr (ABES) · doi:10.70675/f25441cfz0e1bz40f5zbae0z0ea1d0037f9f

The Elucidation of Hydrogen Sulfide Signalling Through Persulfidation

Kouroussis, E. (2019) · theses.fr (ABES) · doi:10.70675/7d7beb54z2f84z43cdz8a1fz2342abbe3731

Impact de différentes classes de pesticides sur les fonctions immunitaires innées des macrophages et des kératinocytes humains HaCaT : mise en évidence de la contribution des kératinocytes dans le contrôle de la polarisation des macrophages

Parny, M. (2020) · theses.fr (ABES) · doi:10.70675/43001866z792bz4ef1z9593ze927a52316f6

Cysteine-rich peptide for chiral self-assembly: a multi-functional antioxidant with novel SH-mediated ROS-responsive disassembly from natural medicine

Zhang, X., Cao, Z., Zhao, R., Guo, Y., Ren, J., Sun, Z., Ye, R., He, J., Chen, Y., Wiedmer, S. Κ., et al. (2026) · Materials Horizons · doi:10.1039/d6mh00128a

Discovery of a novel covalent allosteric site CYS434 in Keap1 and its ligand for the treatment of acute lung injury

Shi, Y., Tie, X., Tao, G., Jia, Y., Huang, Q., Lu, G., & Wu, Y. (2026) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2026.118716

A review on Nrf2 and antioxidant metalloproteins

Hossain, A. M. S., Qudratovna, Q. M., Kholnazarov, B., Odaka, A., Nakane, D., & Akitsu, T. (2026) · European Journal of Chemistry · doi:10.5155/eurjchem.17.2.176-187.2773

Neuroprotective Potential of Nardostachys jatamansi Extract via Keap1–Nrf2 Pathway Regulation in Parkinson’s Disease

Krishnappa, G., Aouti, S., Sreedevi, S., Sridhar, A., Murugesan, K., Srinivasan, R., Gothe, S., Kumar, S., Gokulakrishnan, K., Bharath, M. M. S., et al. (2026) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-026-05821-8

Protein–Protein Interactions: Emerging Drug Targets

Silverman, R. B., Xue, F., & Juncosa, J. I. (2026) · Elsevier eBooks · doi:10.1016/b978-0-443-15862-9.00010-2

Oxidative stress: mechanisms, implications and emerging therapeutic strategies

Namratha, B., Martis, G. J., Sushma, S., Hakkimane, S. S., & Gaonkar, S. L. (2026) · Advances in Redox Research · doi:10.1016/j.arres.2026.100191

Inter-domain distance analysis reveals conformational changes in the Keap1-Nrf2 stress sensor system

Saito, R., Kawabata, T., Yamashita, S., Oki, K., Fujii, T., Kawauchi, H., Doi, Y., Irie, M., Torizawa, T., Kinoshita, K., et al. (2026) · Redox Biology · doi:10.1016/j.redox.2026.104379

Natural Histidine Derivatives—From Basic Research to Potential Applications in Cosmetics and Nutricosmetics

Gołaś, E., & Maciejczyk, M. (2026) · Antioxidants · doi:10.3390/antiox15091118

Cross-species bioanalytical assessment of the oxidative stress and xenobiotic metabolism modes of action for environmental water samples – A multi-layered approach to testing and modelling

Lungu-Mitea, S., Mandava, G., Horackova, J., Golovko, O., Toušová, Z., Bednář, D., Ahrens, L., Hilscherová, K., & Lundqvist, J. (2026) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2026.120709

Dual promoter architecture of NFE2L2 underlies isoform-specific translational control of NRF2

Sznarkowska, A., Urban-Wójciuk, Z., Dziadosz-Brzezińska, A., Cieśla, M., Kusiński, S., Wakimian, K., Szabelska-Beręsewicz, A., Chruściel, E., Papak, I., Marek-Trzonkowska, N., et al. (2026) · Redox Biology · doi:10.1016/j.redox.2026.104405

Subtype-Conditioned NRF2–KEAP1 Signaling in Breast Cancer: A Narrative Review and Hypothesis-Generating Framework from Chemoprevention to Therapy Resistance

Choi, H. Y., Kwon, H., & Hah, Y. (2026) · Antioxidants · doi:10.3390/antiox15101223

Cysteine-based molecular switches: a focus on KEAP1 and BACH1 in regulating the antioxidant response

Feng, J., & Dinkova‐Kostova, A. T. (2026) · Archives of Toxicology · doi:10.1007/s00204-026-04562-1

Redox regulation of plant transcription factors

Rudresh, H. S., Vaishnavi, S. L., Kumar, H. S. S., & Sharathchandra, R. G. (2026) · Elsevier eBooks · doi:10.1016/b978-0-443-33748-2.00039-2

BindingDB Entry 50038443: Noxious compounds activate TRPA1 ion channels through covalent modification of cysteines.

BindingDB (2012) · UC San Diego · doi:10.7270/q2d21zhq

BindingDB Entry 50020149: Optimization of the C2 substituents on the 1,4-bis(arylsulfonamido)naphthalene-N,N'-diacetic acid scaffold for better inhibition of Keap1-Nrf2 protein-protein interaction.

BindingDB (2024) · UC San Diego · doi:10.7270/q2cf9vjf

BindingDB Entry 50005673: 3-aroylmethylene-2,3,6,7-tetrahydro-1H-pyrazino[2,1-a]isoquinolin-4(11bH)-ones as potent Nrf2/ARE inducers in human cancer cells and AOM-DSS treated mice.

BindingDB (2020) · UC San Diego · doi:10.7270/q2z322kj

BindingDB Entry 50020415: Optimization and evaluation of pyridinyl vinyl sulfones as Nrf2 activator for the antioxidant and anti-inflammatory effects.

BindingDB (2024) · UC San Diego · doi:10.7270/q25x2fd0

BindingDB Entry 50008721: Structure-Activity and Structure-Conformation Relationships of Aryl Propionic Acid Inhibitors of the Kelch-like ECH-Associated Protein 1/Nuclear Factor Erythroid 2-Related Factor 2 (KEAP1/NRF2) Protein-Protein Interaction.

BindingDB (2021) · UC San Diego · doi:10.7270/q2pk0kkb

BindingDB Entry 50016274: Structure-activity relationships of 1,4-bis(arylsulfonamido)-benzene or naphthalene-N,N'-diacetic acids with varying C2-substituents as inhibitors of Keap1-Nrf2 protein-protein interaction.

BindingDB (2023) · UC San Diego · doi:10.7270/q2f193rh

BindingDB Entry 50007273: Optimization of Vinyl Sulfone Derivatives as Potent Nuclear Factor Erythroid 2-Related Factor 2 (Nrf2) Activators for Parkinson's Disease Therapy.

BindingDB (2021) · UC San Diego · doi:10.7270/q2tt4v8s

BindingDB Entry 50002315: DESIGNER Extracts as Tools to Balance Estrogenic and Chemopreventive Activities of Botanicals for Women's Health.

BindingDB (2020) · UC San Diego · doi:10.7270/q2jh3psg

BindingDB Entry 50017423: Fragment-Guided Discovery of Pyrazole Carboxylic Acid Inhibitors of the Kelch-like ECH-Associated Protein 1: Nuclear Factor Erythroid 2 Related Factor 2 (KEAP1:NRF2) Protein-Protein Interaction.

BindingDB (2023) · UC San Diego · doi:10.7270/q2js9vjf

BindingDB Entry 50022224: NRF2 inhibitors: Recent progress, future design and therapeutic potential.

BindingDB (2025) · UC San Diego · doi:10.7270/q27h1q92

BindingDB Entry 50022982: Structure-Guided Conformational Restriction Leading to High-Affinity, Selective, and Cell-Active Tetrahydroisoquinoline-Based Noncovalent Keap1-Nrf2 Inhibitors.

BindingDB (2026) · UC San Diego · doi:10.7270/q2154nx4

BindingDB Entry 50047646: 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.

BindingDB (2017) · UC San Diego · doi:10.7270/q25t3ndt

BindingDB Entry 50006108: Rapid identification of Keap1-Nrf2 small-molecule inhibitors through structure-based virtual screening and hit-based substructure search.

BindingDB (2020) · UC San Diego · doi:10.7270/q261139g

ANALYSIS OF PROTEIN ADDUCTION KINETICS AND THE EFFECTS OF PROTEIN ADDUCTION ON C-JUN N-TERMINAL KINASE SIGNALING

Orton, C. R. (2006) · UA Campus Repository (The University of Arizona)

Shp-2 als neuer Regulator der Telomerase Reversen Transkriptase im Endothel

Jakob, S. (2010) · Univ. Duesseldorf: Duesseldorfer Dokumenten- und Publikationsserver

NEUROPROTECTIVE STUDIES ON THE MPTP AND SOD1 MOUSE MODELS OF NEURODEGENERATIVE DISEASES

Fontanilla, C. V. (2012) · IUScholarWorks (Indiana University) · doi:10.7912/c2/2043

Identification and Characterization of Quinone-Thioether Protein Adducts In Vivo

Labenski, M. (2008) · UA Campus Repository (The University of Arizona)

Protection against electrophile and oxidative stress by induction of phase 2 genes: the quest for the elusive sensor that responds to inducers

Holtzclaw, W. D., Dinkova‐Kostova, A. T., & Talalay, P. (2004) · Advances in Enzyme Regulation · doi:10.1016/j.advenzreg.2003.11.013 · Cited by 145

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

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Direct evidence that sulfhydryl groups of Keap1 are the sensors regulating induction of phase 2 enzymes that protect against carcinogens and oxidants

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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

NRF2 Cysteine Residues Are Critical for Oxidant/Electrophile-Sensing, Kelch-Like ECH-Associated Protein-1-Dependent Ubiquitination-Proteasomal Degradation, and Transcription Activation

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