Binding thermodynamics and kinetics guided optimization of potent Keap1–Nrf2 peptide inhibitors

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

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

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

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

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

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

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

Regulatory flexibility in the Nrf2-mediated stress response is conferred by conformational cycling of the Keap1-Nrf2 protein complex

Baird, L., Llères, D., Swift, S., & Dinkova‐Kostova, A. T. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1305687110 · Cited by 386 · see citing works

Kinetic, Thermodynamic, and Structural Characterizations of the Association between Nrf2-DLGex Degron and Keap1

Fukutomi, T., Takagi, K., Mizushima, T., Ohuchi, N., & Yamamoto, M. P. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.01191-13 · 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

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

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

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

Monitoring Keap1–Nrf2 interactions in single live cells

Baird, L., Swift, S., Llères, D., & Dinkova‐Kostova, A. T. (2014) · Biotechnology Advances · doi:10.1016/j.biotechadv.2014.03.004 · Cited by 171 · 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

Peptide inhibitors of the Keap1–Nrf2 protein–protein interaction

Hancock, R., Bertrand, H. C., Tsujita, T., Naz, S., El-Bakry, A., Laoruchupong, J., Hayes, J. D., & Wells, G. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.10.486 · Cited by 147 · see citing works

Nrf2 defense pathway: Experimental evidence for its protective role in epilepsy

Mazzuferi, M., Kumar, G., van Eyll, J. M., Danis, B., Foerch, P., & Kaminski, R. M. (2013) · Annals of Neurology · doi:10.1002/ana.23940 · Cited by 132 · 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

Optimization of Fluorescently Labeled Nrf2 Peptide Probes and the Development of a Fluorescence Polarization Assay for the Discovery of Inhibitors of Keap1-Nrf2 Interaction

Inoyama, D., Chen, Y., Huang, X., Beamer, L. J., Kong, A. T., & Hu, L. (2011) · SLAS DISCOVERY · doi:10.1177/1087057111430124 · Cited by 101 · see citing works

Label-free methods of reporting biomolecular interactions by optical biosensors.

Citartan, M., Gopinath, S., Tominaga, J., & Tang, T.-H. (2013) · In Analysis · doi:10.1039/c3an36828a · Cited by 91 · see citing works

Updated Research and Applications of Small Molecule Inhibitors of Keap1-Nrf2 Protein-Protein Interaction: a Review

Zhuang, C., Miao, Z., Sheng, C., & Zhang, W. (2014) · Current Medicinal Chemistry · doi:10.2174/0929867321666140217104648 · Cited by 65 · see citing works

Diffusion dynamics of the Keap1–Cullin3 interaction in single live cells

Baird, L., & Dinkova‐Kostova, A. T. (2013) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2013.02.065 · Cited by 59 · see citing works

Novel protein–protein interaction inhibitor of Nrf2–Keap1 discovered by structure-based virtual screening

Sun, H.-P., Jiang, Z., Zhang, M.-Y., Lu, M., Yang, T., Pan, Y., Huang, H., Zhang, X., & You, Q. (2013) · MedChemComm · doi:10.1039/c3md00240c · Cited by 59 · see citing works

Insight into the Intermolecular Recognition Mechanism between Keap1 and IKKβ Combining Homology Modelling, Protein-Protein Docking, Molecular Dynamics Simulations and Virtual Alanine Mutation

Jiang, Z., Chu, H., Xi, M., Yang, T., Jia, J.-M., Huang, J., Guo, X., Zhang, X., You, Q., & Sun, H.-P. (2013) · PLoS ONE · doi:10.1371/journal.pone.0075076 · Cited by 52 · see citing works

Privileged scaffolds targeting reverse-turn and helix recognition

Che, Y., & Marshall, G. R. (2007) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.12.1.101 · Cited by 36 · see citing works

Investigation of the intermolecular recognition mechanism between the E3 ubiquitin ligase Keap1 and substrate based on multiple substrates analysis

Jiang, Z., Xu, L., Lu, M., Pan, Y., Huang, H., Zhang, X., Sun, H.-P., & You, Q. (2014) · Journal of Computer-Aided Molecular Design · doi:10.1007/s10822-014-9799-y · Cited by 28 · 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

Nrf2/Keap1/ARE signaling: Towards specific regulation

Ulasov, A. V., Rosenkranz, A. A., Georgiev, G. P., & Sobolev, A. S. (2021) · Life Sciences · doi:10.1016/j.lfs.2021.120111 · Cited by 520 · see citing works

Discovery of a Keap1-dependent peptide PROTAC to knockdown Tau by ubiquitination-proteasome degradation pathway

Lu, M., Liu, T., Jiao, Q., Ji, J., Tao, M., Liu, Y., You, Q., & Jiang, Z. (2018) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2018.01.063 · Cited by 310 · see citing works

KEAP1‐NRF2 protein–protein interaction inhibitors: Design, pharmacological properties and therapeutic potential

Crisman, E., Duarte, P., Daudén, E., Cuadrado, A., Rodrı́guez-Franco, M. I., López, M. G., & Leon, R. M. (2022) · Medicinal Research Reviews · doi:10.1002/med.21925 · Cited by 273 · see citing works

Interfering peptides targeting protein–protein interactions: the next generation of drugs?

Bruzzoni‐Giovanelli, H., Alezra, V., Wolff, N., Dong, C., Tufféry, P., & Rebollo, A. (2017) · Drug Discovery Today · doi:10.1016/j.drudis.2017.10.016 · Cited by 156 · see citing works

Nrf2 activation through the inhibition of Keap1–Nrf2 protein–protein interaction

Lee, S., & Hu, L. (2020) · Medicinal Chemistry Research · doi:10.1007/s00044-020-02539-y · Cited by 136 · see citing works

Discovery and Development of Kelch-like ECH-Associated Protein 1. Nuclear Factor Erythroid 2-Related Factor 2 (KEAP1:NRF2) Protein–Protein Interaction Inhibitors: Achievements, Challenges, and Future Directions

Jiang, Z., Lu, M., & You, Q. (2016) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b00586 · Cited by 126 · see citing works

Advances in targeted degradation of endogenous proteins

Röth, S., Fulcher, L. J., & Sapkota, G. P. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03112-6 · Cited by 92 · see citing works

PROTACs and Other Chemical Protein Degradation Technologies for the Treatment of Neurodegenerative Disorders

Tomoshige, S., & Ishikawa, M. (2020) · Angewandte Chemie International Edition · doi:10.1002/anie.202004746 · Cited by 84 · see citing works

Recent progress in Keap1-Nrf2 protein-protein interaction inhibitors

Mou, Y., Wen, S., Li, Y., Gao, X., Zhang, X., & Jiang, Z. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112532 · Cited by 83 · see citing works

Discovery of a head-to-tail cyclic peptide as the Keap1-Nrf2 protein-protein interaction inhibitor with high cell potency

Lu, M., Jiao, Q., Liu, T., Tan, S.-J., Zhou, H.-S., You, Q., & Jiang, Z. (2017) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2017.10.052 · Cited by 80 · see citing works

Direct Keap1-kelch inhibitors as potential drug candidates for oxidative stress-orchestrated diseases: A review on In silico perspective

Boyenle, I. D., Divine, U. C., Adeyemi, R. O., Ayinde, K. S., Olaoba, O. T., Apu, C., Du, L., Lü, Q., Yin, X., & Adelusi, T. I. (2021) · Pharmacological Research · doi:10.1016/j.phrs.2021.105577 · Cited by 59 · see citing works

Non-small molecule PROTACs (NSM-PROTACs): Protein degradation kaleidoscope

Ma, S., Ji, J., Tong, Y., Zhu, Y., Dou, J., Zhang, X., Xu, S., Zhu, T., Xu, X., You, Q., et al. (2022) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2022.02.022 · Cited by 57 · see citing works

Design, Synthesis, and Structure–Activity Relationships of Indoline-Based Kelch-like ECH-Associated Protein 1-Nuclear Factor (Erythroid-Derived 2)-Like 2 (Keap1-Nrf2) Protein–Protein Interaction Inhibitors

Zhou, H.-S., Hu, L.-B., Zhang, H., Shan, W.-X., Wang, Y., Li, X., Liu, T., Zhao, J., You, Q., & Jiang, Z. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c01116 · Cited by 49 · see citing works

Tackling Undruggable Targets with Designer Peptidomimetics and Synthetic Biologics

Swenson, C., Mandava, G., Thomas, D. M., & Moellering, R. E. (2024) · Chemical Reviews · doi:10.1021/acs.chemrev.4c00423 · Cited by 48 · see citing works

Recapitulating the Binding Affinity of Nrf2 for KEAP1 in a Cyclic Heptapeptide, Guided by NMR, X-ray Crystallography, and Machine Learning

Ortet, P. C., Muellers, S. N., Viarengo‐Baker, L. A., Streu, K., Szymczyna, B. R., Beeler, A. B., Allen, K. N., & Whitty, A. (2021) · Journal of the American Chemical Society · doi:10.1021/jacs.0c09799 · Cited by 45 · see citing works

Beyond canonical PROTAC: biological targeted protein degradation (bioTPD)

Wang, H., Zhou, R., Xu, F., Yang, K., Zheng, L., Zhao, P., Shi, G., Dai, L., Xu, C., Yu, L., et al. (2023) · Biomaterials Research · doi:10.1186/s40824-023-00385-8 · Cited by 46 · see citing works

Discovery of a Potent Kelch-Like ECH-Associated Protein 1-Nuclear Factor Erythroid 2-Related Factor 2 (Keap1–Nrf2) Protein–Protein Interaction Inhibitor with Natural Proline Structure as a Cytoprotective Agent against Acetaminophen-Induced Hepatotoxicity

Lu, M., Zhang, X., Wu, F., Tan, S.-J., Zhao, J., You, Q., & Jiang, Z. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b00818 · Cited by 41 · see citing works

Modified Peptide Inhibitors of the Keap1–Nrf2 Protein–Protein Interaction Incorporating Unnatural Amino Acids

Georgakopoulos, N., Talapatra, S. K., Gatliff, J., Kozielski, F., & Wells, G. (2018) · ChemBioChem · doi:10.1002/cbic.201800170 · Cited by 40 · see citing works

Discovery of 2-oxy-2-phenylacetic acid substituted naphthalene sulfonamide derivatives as potent KEAP1-NRF2 protein-protein interaction inhibitors for inflammatory conditions

Lu, M., Shao, H.-L., Liu, T., You, Q., & Jiang, Z. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112734 · Cited by 38 · see citing works

Inhibiting the Keap1/Nrf2 Protein‐Protein Interaction with Protein‐Like Polymers

Carrow, K. P., Hamilton, H. L., Hopps, M. P., Li, Y., Qiao, B., Payne, N. C., Thompson, M. P., Zhang, X., Magassa, A., Fattah, M. A., et al. (2024) · Advanced Materials · doi:10.1002/adma.202311467 · Cited by 37 · see citing works

Baicalein disrupts the KEAP1-NRF2 interaction to alleviate oxidative stress injury by inhibiting M1 macrophage polarization

Chi, F., Cheng, C., Liu, K., Sun, T., Zhang, M., Hou, Y., & Bai, G. (2024) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2024.12.036 · Cited by 36 · see citing works

Polar Recognition Group Study of Keap1-Nrf2 Protein–Protein Interaction Inhibitors

Lu, M., Tan, S.-J., Ji, J., Chen, Z., Yuan, Z., You, Q., & Jiang, Z. (2016) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.5b00407 · Cited by 34 · see citing works

A systematic molecular dynamics approach to the study of peptide Keap1–Nrf2 protein–protein interaction inhibitors and its application to p62 peptides

Lu, M., Yuan, Z., Jiang, Y.-L., Chen, Z., You, Q., & Jiang, Z. (2016) · Molecular BioSystems · doi:10.1039/c6mb00030d · Cited by 33 · see citing works

Protein-Based Degraders: From Chemical Biology Tools to Neo-Therapeutics

Ou, L., Setegne, M. T., Elliot, J., Shen, F., & Dassama, L. M. K. (2025) · Chemical Reviews · doi:10.1021/acs.chemrev.4c00595 · Cited by 30 · see citing works

Perfluoroarene-based peptide macrocycles that inhibit the Nrf2/Keap1 interaction

Steel, R., O'Connell, M. A., & Searcey, M. (2018) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2018.03.003 · Cited by 29 · see citing works

Cyclic Peptide Keap1–Nrf2 Protein–Protein Interaction Inhibitors: Design, Synthesis, and In Vivo Treatment of Acute Lung Injury

Zou, J., Yan, J., Lu, Y., Zhou, Y., Zhang, K., Han, Q., Han, D., Gai, C., Chai, X., Zhao, Q., et al. (2024) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c00065 · Cited by 29 · see citing works

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

Lee, S., Abed, D. A., Nguyen, M.-U., Verzi, M. P., & Hu, L. (2022) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2022.114380 · Cited by 27 · see citing works

A cell-active cyclic peptide targeting the Nrf2/Keap1 protein–protein interaction

Iegre, J., Krajčovičová, S., Gunnarsson, A., Wissler, L., Käck, H., Łuchniak, A., Tångefjord, S., Narjes, F., & Spring, D. R. (2023) · Chemical Science · doi:10.1039/d3sc04083f · Cited by 26 · see citing works

Advances in KEAP1-based PROTACs as emerging therapeutic modalities: Structural basis and progress

Chen, J., Feng, D., Zhu, R., Li, H., & Chen, L. (2025) · Redox Biology · doi:10.1016/j.redox.2025.103781 · Cited by 26 · see citing works

Molecular similarity guided optimization of novel Nrf2 activators with 1,2,4-oxadiazole core

Xu, L., Zhang, X., Jiang, Z., & You, Q. (2016) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2016.05.056 · Cited by 19 · see citing works

Prediction of Binding Energy of Keap1 Interaction Motifs in the Nrf2 Antioxidant Pathway and Design of Potential High-Affinity Peptides

Karttunen, M., Choy, W., & Cino, E. A. (2018) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.8b03295 · Cited by 19 · see citing works

Rational cyclization-based minimization of entropy penalty upon the binding of Nrf2-derived linear peptides to Keap1: A new strategy to improve therapeutic peptide activity against sepsis

Chen, K., Huang, L., & Shen, B. (2018) · Biophysical Chemistry · doi:10.1016/j.bpc.2018.11.002 · Cited by 19 · see citing works

Design, Synthesis, and Initial Evaluation of Affinity-Based Small-Molecule Probes for Fluorescent Visualization and Specific Detection of Keap1

Lu, M., Zhou, H.-S., You, Q., & Jiang, Z. (2016) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b00775 · Cited by 18 · see citing works

Computational Prediction of Cyclic Peptide Structural Ensembles and Application to the Design of Keap1 Binders

Lopez, F., Miao, J., Damjanovic, J., Bischof, L., Braun, M. B., Ling, Y., Hartmann, M. D., Lin, Y., & Kritzer, J. A. (2023) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.3c01337 · Cited by 17 · see citing works

Exploring new strategies for grafting binding peptides onto protein loops using a consensus‐designed tetratricopeptide repeat scaffold

Madden, S. K., Perez‐Riba, A., & Itzhaki, L. S. (2019) · Protein Science · doi:10.1002/pro.3586 · Cited by 17 · see citing works

Identification of novel and selective non-peptide inhibitors targeting the polo-box domain of polo-like kinase 1

Chen, Y., Li, Z., Liu, Y., Lin, T., Sun, H., Yang, D., & Jiang, C. (2018) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2018.08.030 · Cited by 16 · see citing works

The structural and functional impacts of rationally designed cyclic peptides on self-assembly-mediated functionality

Kurita, T., & Numata, K. (2024) · Physical Chemistry Chemical Physics · doi:10.1039/d4cp02759k · Cited by 13 · see citing works

Screening approaches for the identification of Nrf2-Keap1 protein-protein interaction inhibitors targeting hot spot residues

Asano, W., Hantani, R., Uhara, T., Debaene, F., Nomura, A., Yamaguchi, K., Adachi, T., Otake, K., Harada, K., & Hantani, Y. (2023) · SLAS DISCOVERY · doi:10.1016/j.slasd.2023.11.001 · Cited by 11 · see citing works

Design, synthesis and biological evaluation of phosphopeptides as Polo-like kinase 1 Polo-box domain inhibitors

Lin, T., Min, H.-P., Jiang, C., Niu, M., Fang, Y., Xu, L., & Di, B. (2018) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2018.05.014 · Cited by 8 · see citing works

PROTACs and Other Chemical Protein Degradation Technologies for the Treatment of Neurodegenerative Disorders

Tomoshige, S., & Ishikawa, M. (2020) · Angewandte Chemie · doi:10.1002/ange.202004746 · Cited by 8 · see citing works

Development of Keap1-interactive small molecules that regulate Nrf2 transcriptional activity

Georgakopoulos, N., Gatliff, J., & Wells, G. (2016) · Current Opinion in Toxicology · doi:10.1016/j.cotox.2016.08.002 · Cited by 8 · see citing works

Peptide-Based PROTACs: Transitioning from Static Paradigm to a Dynamic Landscape within Targeted Protein Degradation

Lu, X., & Hu, Q. (2026) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.6c00029 · Cited by 6 · see citing works

Design, synthesis and evaluation of -amino acid-containing peptidomimetics targeting the polo-box domain of polo-like kinase 1

Li, Z., Zhang, Z., Chen, Y., Tang, S., Lin, T., Huang, J., Лі, Б., & Jiang, C. (2019) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2019.02.022 · Cited by 6 · see citing works

In Cellulo Peptide Cyclization via Gene‐Encoded Proximity‐Induced Proline‐Isothiocyanate Crosslinking

Huang, Z., Jiang, S., Ren, J., Zhao, L., Zhang, Z., Qin, H., Gong, C., & Xuan, W. (2025) · Angewandte Chemie International Edition · doi:10.1002/anie.202517565 · Cited by 4 · see citing works

The emerging role of proteolysis targeting chimeras (PROTACs) in the treatment of Alzheimer’s disease

George, N., Akhtar, M. J., Balushi, K. A. A., Safi, S. Z., Azmi, S. N. H., & Khan, S. A. (2023) · Medicinal Chemistry Research · doi:10.1007/s00044-023-03026-w · Cited by 3 · see citing works

Development of p62-Keap1 protein–protein interaction inhibitors as doxorubicin-sensitizers against non-small cell lung cancer

Yasuda, D., Yoshida, I., Imamura, R. M., Katagishi, D., Takahashi, K., Kojima, H., Okabe, T., Ichimura, Y., Komatsu, M., Mashino, T., et al. (2022) · Results in Chemistry · doi:10.1016/j.rechem.2022.100609 · Cited by 3 · see citing works

In Cellulo Peptide Cyclization via Gene‐Encoded Proximity‐Induced Proline‐Isothiocyanate Crosslinking

Huang, Z., Jiang, S., Ren, J., Zhao, L., Zhang, Z., Qin, H., Gong, C., & Xuan, W. (2025) · Angewandte Chemie · doi:10.1002/ange.202517565 · Cited by 1 · see citing works

Macrocyclic peptides and peptidomimetics as modulators of protein–protein interactions

Parmar, R., Shrivastava, V., Kaur, G., Goyal, B., & Jain, R. (2026) · RSC Medicinal Chemistry · doi:10.1039/d6md00640j · Cited by 1 · see citing works

Discovery and Development of Keap1-Nrf2 Protein-Protein Interaction Inhibitors

Jiang, Z., & You, Q. (2018) · Springer eBooks · doi:10.1007/978-981-13-0773-7_10 · Cited by 1 · see citing works

Exploring the binding of rationally engineered tandem-repeat proteins to E3 ubiquitin ligase Keap1

Madden, S. K., & Itzhaki, L. S. (2021) · Protein Engineering Design and Selection · doi:10.1093/protein/gzab027 · Cited by 1 · see citing works

Computational design of diverse nuclear factor erythroid 2 activators with cellular antioxidative activity

Yuwen, M., Gao, X., Ba, J., Wu, J., Kang, J. Y., Ye, S., & Zhu, C. (2025) · iScience · doi:10.1016/j.isci.2025.112621

Design and optimisation of meta-substituted bis(arylsulfonamido)benzene inhibitors through a molecular hybridisation strategy targeting the Keap1-Nrf2 protein-protein interaction

Lee, S., Ali, A. R., Abed, D. A., & Hu, L. (2026) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.1080/14756366.2026.2622777

Protein-protein interaction inhibitors in cancer

Hardcastle, I. R., Goujon-Ricci, J., & Thompson, W. I. (2026) · Elsevier eBooks · doi:10.1016/b978-0-443-29808-0.00067-4

BindingDB Entry 50011439: Design, Synthesis, and Structure-Activity Relationships of Indoline-Based Kelch-like ECH-Associated Protein 1-Nuclear Factor (Erythroid-Derived 2)-Like 2 (Keap1-Nrf2) Protein-Protein Interaction Inhibitors.

BindingDB (2022) · UC San Diego · doi:10.7270/q2vd7329

BindingDB Entry 50001273: Design, synthesis and biological evaluation of phosphopeptides as Polo-like kinase 1 Polo-box domain inhibitors.

BindingDB (2020) · UC San Diego · doi:10.7270/q2cc1364

BindingDB Entry 50012263: Discovery of 2-oxy-2-phenylacetic acid substituted naphthalene sulfonamide derivatives as potent KEAP1-NRF2 protein-protein interaction inhibitors for inflammatory conditions.

BindingDB (2022) · UC San Diego · doi:10.7270/q2fj2mgn

BindingDB Entry 50009857: Design, Synthesis, and Initial Evaluation of Affinity-Based Small-Molecule Probes for Fluorescent Visualization and Specific Detection of Keap1.

BindingDB (2021) · UC San Diego · doi:10.7270/q2bk1gwd

BindingDB Entry 50001541: Discovery of a head-to-tail cyclic peptide as the Keap1-Nrf2 protein-protein interaction inhibitor with high cell potency.

BindingDB (2020) · UC San Diego · doi:10.7270/q2pk0jnt

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 50010098: Polar Recognition Group Study of Keap1-Nrf2 Protein-Protein Interaction Inhibitors.

BindingDB (2021) · UC San Diego · doi:10.7270/q2zk5m5r

BindingDB Entry 50018333: Recent progress in Keap1-Nrf2 protein-protein interaction inhibitors.

BindingDB (2024) · UC San Diego · doi:10.7270/q2b85dbt

BindingDB Entry 50021293: Cyclic Peptide Keap1-Nrf2 Protein-Protein Interaction Inhibitors: Design, Synthesis, and In Vivo Treatment of Acute Lung Injury.

BindingDB (2025) · UC San Diego · doi:10.7270/q2pk0msf

BindingDB Entry 50001682: Discovery of a Keap1-dependent peptide PROTAC to knockdown Tau by ubiquitination-proteasome degradation pathway.

BindingDB (2020) · UC San Diego · doi:10.7270/q2qz2dh7

BindingDB Entry 50008207: Discovery of a Potent Kelch-Like ECH-Associated Protein 1-Nuclear Factor Erythroid 2-Related Factor 2 (Keap1-Nrf2) Protein-Protein Interaction Inhibitor with Natural Proline Structure as a Cytoprotective Agent against Acetaminophen-Induced Hepatotoxicity.

BindingDB (2021) · UC San Diego · doi:10.7270/q2cr5xq3

BindingDB Entry 50047995: Discovery and Development of Kelch-like ECH-Associated Protein 1. Nuclear Factor Erythroid 2-Related Factor 2 (KEAP1:NRF2) Protein-Protein Interaction Inhibitors: Achievements, Challenges, and Future Directions.

BindingDB (2018) · UC San Diego · doi:10.7270/q2377bpq

BindingDB Entry 50002729: Perfluoroarene-based peptide macrocycles that inhibit the Nrf2/Keap1 interaction.

BindingDB (2020) · UC San Diego · doi:10.7270/q2qc065n

Peptide inhibitors of the Keap1–Nrf2 protein–protein interaction with improved binding and cellular activity

Hancock, R., Schaap, M., Pfister, H., & Wells, G. (2013) · Organic &amp; Biomolecular Chemistry · doi:10.1039/c3ob40249e · Cited by 91 · 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

Modified Peptide Inhibitors of the Keap1–Nrf2 Protein–Protein Interaction Incorporating Unnatural Amino Acids

Georgakopoulos, N., Talapatra, S. K., Gatliff, J., Kozielski, F., & Wells, G. (2018) · ChemBioChem · doi:10.1002/cbic.201800170 · Cited by 40 · see citing works

Discovery and Development of Keap1-Nrf2 Protein-Protein Interaction Inhibitors

Jiang, Z., & You, Q. (2018) · Springer eBooks · doi:10.1007/978-981-13-0773-7_10 · Cited by 1 · see citing works

Recent progress in Keap1-Nrf2 protein-protein interaction inhibitors

Mou, Y., Wen, S., Li, Y., Gao, X., Zhang, X., & Jiang, Z. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112532 · Cited by 83 · see citing works