SCF/β-TrCP Promotes Glycogen Synthase Kinase 3-Dependent Degradation of the Nrf2 Transcription Factor in a Keap1-Independent Manner

β‐catenin is a target for the ubiquitin–proteasome pathway

Aberle, H., Bauer, A., Stappert, J., Kispert, A., & Kemler, R. (1997) · The EMBO Journal · doi:10.1093/emboj/16.13.3797 · Cited by 2,586

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

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

Dual regulation of Snail by GSK-3β-mediated phosphorylation in control of epithelial–mesenchymal transition

Zhou, B. P., Deng, J., Xia, W., Xu, J., Li, Y. M., Gunduz, M., & Hung, M.-C. (2004) · Nature Cell Biology · doi:10.1038/ncb1173 · Cited by 1,581

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

A coordinated phosphorylation by Lats and CK1 regulates YAP stability through SCF β-TRCP

Zhao, B., Li, L., Tumaneng, K., Wang, C.-Y., & Guan, K.-L. (2010) · Genes & Development · doi:10.1101/gad.1843810 · Cited by 1,418

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 1,284

F-Box Proteins Are Receptors that Recruit Phosphorylated Substrates to the SCF Ubiquitin-Ligase Complex

Skowyra, D., Craig, K. L., Tyers, M., Elledge, S. J., & Harper, J. W. (1997) · Cell · doi:10.1016/s0092-8674(00)80403-1 · Cited by 1,233

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

Regulation of oxidoreductase enzymes during inflammation

Ingram, S. (2018) · Cited by 1

Editorial: Redox-signaling in neurodegenerative diseases: biomarkers, targets, and therapies

Carvalho, A. N., Branco, V., van Horssen, J., & Saso, L. (2023) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2023.1198669 · Cited by 1

Stanniocalcin 2 (STC2) is a potent biomarker of hepatocellular carcinoma with its expression being augmented in Nrf1α-deficient cells, but diminished in Nrf2-deficient cellsPreprint

Bu, Q., Deng, Y., Wang, Q., Deng, R., Hu, S., Pei, Z., & Zhang, Y. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.05.15.540796 · Cited by 1

PRDX1 drives colorectal cancer progression by inhibiting ferroptosis through suppression of Cullin-3-mediated NRF2 degradationPreprint

Yu, X., Song, Y., Wang, X., Sun, Y., Yu, N., Tian, Y., Han, J., & Qu, X. (2024) · Research Square · doi:10.21203/rs.3.rs-4242780/v1 · Cited by 1

Study of the Role of NRF2 in the Progression and Metabolic Adaptation of Glioblastoma

Moubarak, M. M. (2024) · theses.fr (ABES) · doi:10.70675/c7f50cd9za643z437dza037z13798faf9515 · Cited by 2

Protein factors and chemical compounds regulating hypoxic or oxidative stress responses

Oguro, A., Kobayashi, Y., & Imaoka, S. (2015) · Personalized Medicine Universe · doi:10.1016/j.pmu.2015.04.004

Aripiprazole increases NAD(P)H-quinone oxidoreductase-1 and heme oxygenase-1 in PC12 cells

Wien, S.-V. (2015)

Medicinal plants with antioxidant and antiinflammatory properties in cancer prevention

González, P. (2015) · doi:10.7282/t38g8nf4

Oxidative damage and Nrf2 (nuclear factor erythroid 2-related factor 2) protein expression in normal skin and keloid tissues

Whang, K. U., Lee, J. S., Lee, S. Y., An, J. M., Kim, K. O., Kwon, S. B., & Kim, H. J. (2016) · Journal of Dermatological Science · doi:10.1016/j.jdermsci.2016.08.333

PROTEOMIC DISSECTION OF KEAP1/NRF2 SIGNALING TO DETERMINE NEW PATHWAY INTERACTORS IN CANCER

Mulvaney, K. M. (2019) · Carolina Digital Repository (University of North Carolina at Chapel Hill) · doi:10.17615/7v3v-x224

Molecular and Chemical Modulation of NRF2 for Disease Intervention

Harder, B. G. (2017) · UA Campus Repository (The University of Arizona)

NRF2 and RIP140 as new therapeutic targets for X-linked adrenoleukodystrophy (X-ALD): Control of redox/metabolic homeostasis and inflammation

Ranea‐Robles, P. (2017) · Tesis Doctorals en Xarxa (Consorci de Serveis Universitaris de Catalunya)

Regulation of lysophosphatidate-induced mechanisms of chemo-resistance

Venkatraman, G. (2015) · ERA: Education and Research Archive (University of Alberta) · doi:10.7939/r3bn9x79k

The Effects of Macrophage Migration Inhibitory Factor on Antioxidant Responses During Cigarette Smoke Exposure

Aladdin, M. (2017)

Contribution to the biochemical characterization of astrocytes expressing a mitochondrial-tagged form of catalase

Bonora, N. (2018) · Gredos (University of Salamanca) · doi:10.14201/gredos.137569

The Involvement of Anti-Oxidative Response and Mitochondrial Dynamics in the Pathogenesis of Friedreich’s Ataxia: Relevance to the Development of Future Therapeutics

Chiang, S. (2019) · The Sydney eScholarship Repository (The University of Sydney)

Nrf2 in the Regulation of Endothelial Cell Homeostasis During Inflammation

Yamazaki, H., & Itoh, K. (2020) · Progress in inflammation research · doi:10.1007/978-3-030-44599-7_4

Регуляция белков циркадных ритмов и Nrf2-опосредованной антиоксидантной защиты: двойная роль киназы гликогенсинтазы 3

Шиловский, Г. А., Putyatina, T. S., Васильевна, М. Г., Селиверстов, А. В., Ashapkin, V. V., Сорокина, Е. В., Markov, A. V., & Skulachev, V. P. (2021) · Biochemistry (Moscow) · doi:10.31857/s0320972521040059

FAIR and bias-free network modules for mechanism-based disease redefinitions

Hassan, A. (2021) · Research Publications (Maastricht University) · doi:10.26481/dis.20210707ah

Reducing neurodegeneration and oxidative damage in Alzheimer's disease: Role of the Nrf2 pathway activation by natural compounds

Villavicencio-Tejo, F., & Quintanilla, R. A. (2023) · Elsevier eBooks · doi:10.1016/b978-0-323-90052-2.00003-2

Transcription Factor NRF2 in Endothelial Functions

Kondratenko, N. D., Zinovkina, L. A., & Zinovkin, R. A. (2023) · Molecular Biology · doi:10.31857/s0026898423060101

A New Mouse Strain with a Mutation in the NFE2L2 (NRF2) Gene

Egorov, E. S., Kondratenko, N. D., Averina, O. A., Permyakov, O. A., Emelyanova, M. A., Prikhodko, A. S., Zinovkina, L. A., Владимирович, С. П., & Zinovkin, R. A. (2023) · Biochemistry (Moscow) · doi:10.1134/s0006297923120039

Study on the correlation between serum levels of oxidative stress regulatory factors and CaOx kidney stonesPreprint

Aihemaitijiang, B., Azhati, J., Tailaiti, A., Ma, B., Liu, R., Chen, C., Maihemuti, M., & Mahemuti, M. (2024) · Research Square · doi:10.21203/rs.3.rs-4182821/v1

Additional file 1 of P2X7 receptor inhibition ameliorates ubiquitin–proteasome system dysfunction associated with Alzheimer’s disease

Bianchi, C., Alvarez‐Castelao, B., Sebastián‐Serrano, Á., Lauro, C. D., Soria-Tobar, L., Nicke, A., Engel, T., & Dı́az-Hernández, M. (2023) · Figshare · doi:10.6084/m9.figshare.23354460

The NRF2 Response to Environmental Stress

Ikumawoyi, V. O., Chen, W.-T., Dodson, M. B., & Zhang, D. D. (2025) · Elsevier eBooks · doi:10.1016/b978-0-323-95488-4.00259-x

Perspective Chapter: Nrf2 at the Realm of Antioxidant Protection in Cardiovascular Systems

Narasimhan, K. K. S., Jayakumar, D., & Kalaiselvi, P. (2025) · Biochemistry · doi:10.5772/intechopen.1012343

NRF2 Dysregulation and Its Implications in Renal Cell Carcinoma

Jang, B., & Kwak, M. (2025) · Drug Targets and Therapeutics · doi:10.58502/dtt.25.0013

GSK-3β/β-TrCP regulates Nrf2-mediated oxidative stress response in Cristaria plicata

Hu, Y., An, J., Qiu, H., Wu, Q., Li, J., Yang, G. Q., Hu, B., & Wen, C. (2025) · iScience · doi:10.1016/j.isci.2025.113995

Transcription factor NRF2: New therapeutic approach to modify Parkinson's disease progression

Rojo, A. I., Esteras, N., Cuadrado, A., & Lastres‐Becker, I. (2025) · Handbook of behavioral neuroscience · doi:10.1016/b978-0-443-21992-4.00025-7

Additional file 1 of Panax quinquefolius saponin inhibits vascular smooth muscle cell calcification via activation of nuclear factor-erythroid 2-related factor 2

Lu, X., Liu, X., Liang, E., Yang, R., Liu, Y., Liu, X., Yan, F., & Xing, Y. (2024) · Figshare · doi:10.6084/m9.figshare.26584083

Additional file 3 of Panax quinquefolius saponin inhibits vascular smooth muscle cell calcification via activation of nuclear factor-erythroid 2-related factor 2

Lu, X., Liu, X., Liang, E., Yang, R., Liu, Y., Liu, X., Yan, F., & Xing, Y. (2024) · Figshare · doi:10.6084/m9.figshare.26584089

Additional file 2 of P2X7 receptor inhibition ameliorates ubiquitin–proteasome system dysfunction associated with Alzheimer’s disease

Bianchi, C., Alvarez‐Castelao, B., Sebastián‐Serrano, Á., Lauro, C. D., Soria-Tobar, L., Nicke, A., Engel, T., & Dı́az-Hernández, M. (2023) · Figshare · doi:10.6084/m9.figshare.23354463

Additional file 6 of Panax quinquefolius saponin inhibits vascular smooth muscle cell calcification via activation of nuclear factor-erythroid 2-related factor 2

Lu, X., Liu, X., Liang, E., Yang, R., Liu, Y., Liu, X., Yan, F., & Xing, Y. (2023) · Figshare · doi:10.6084/m9.figshare.26584098

Additional file 2 of Panax quinquefolius saponin inhibits vascular smooth muscle cell calcification via activation of nuclear factor-erythroid 2-related factor 2

Lu, X., Liu, X., Liang, E., Yang, R., Liu, Y., Liu, X., Yan, F., & Xing, Y. (2024) · Figshare · doi:10.6084/m9.figshare.26584086

Additional file 4 of Panax quinquefolius saponin inhibits vascular smooth muscle cell calcification via activation of nuclear factor-erythroid 2-related factor 2

Lu, X., Liu, X., Liang, E., Yang, R., Liu, Y., Liu, X., Yan, F., & Xing, Y. (2024) · Figshare · doi:10.6084/m9.figshare.26584092

Additional file 5 of Panax quinquefolius saponin inhibits vascular smooth muscle cell calcification via activation of nuclear factor-erythroid 2-related factor 2

Lu, X., Liu, X., Liang, E., Yang, R., Liu, Y., Liu, X., Yan, F., & Xing, Y. (2024) · Figshare · doi:10.6084/m9.figshare.26584095

Additional file 1 of Dysregulation of SOX17/NRF2 axis confers chemoradiotherapy resistance and emerges as a novel therapeutic target in esophageal squamous cell carcinoma

Hsieh, C.-H., Kuan, W.-H., Chang, W.-L., Kuo, I.-Y., Liu, H., Shieh, D.-B., Liu, H., Tan, B. C., & Wang, Y.-C. (2022) · Figshare · doi:10.6084/m9.figshare.21435555

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

Studies of biological pathways involved in radioresistance of glioblastoma stem cells after hadron irradiation

Salma, R. (2023) · theses.fr (ABES) · doi:10.70675/2252f851zd8fez441cz9a73z91038dc14cac

ZIP7 Drives Glycolytic Reprogramming and Lactate-Mediated Immune Remodeling in Lung Adenocarcinoma Through GSK3β-NRF2 Signaling

Tang, Z., Shi, Y., Jiang, X., Jiang, S., Maihemuti, N., Zhang, J., Tang, B., & Xu, Z. S. (2026) · Biomedicines · doi:10.3390/biomedicines14061262 · Cited by 1

Beyond KEAP1: The Context-Specific NRF2 Partner Code in Disease and Therapy

Kwag, S.-J., Lee, J., Lee, S.-J., Hwang, J.-M., & Hah, Y. (2026) · Antioxidants · doi:10.3390/antiox15060759

Nrf2 signaling pathway and its molecular regulatory mechanism

Pan, Y., Zhang, X., Lu, Y., Qin, H., Chen, R., & Fan, H. (2026) · Journal of Zhejiang University SCIENCE B · doi:10.1631/jzus.b2500053

Computational approaches to pleiotropic drug design for intestinal ischemia-reperfusion injury

Hezekiah, O. S., Afolabi, O. A., Ajike, R. A., Oyekunle, O. S., Ezekiel Oladele, O. J. O., & KOMOLAFE, A. I. (2026) · In Silico Research in Biomedicine · doi:10.1016/j.insi.2026.100511

Feasibility Study of Intratumoral NRF2 Expression as a Predictive Biomarker for the Effectiveness of Immunotherapy in Patients with Non-Small Cell Lung Cancer Treated with PD-1 Inhibitor

Jin, Y., Inoue, Y., Shimada, H., Hara, T., Yamashita, S., Yamamoto, M., & Matsubara, O. (2026) · Cancers · doi:10.3390/cancers18142202

LRRK2 and Nrf2 regulation in Parkinson’s disease: Mechanistic insights and therapeutic potential

Sunkersett, E., Kumar, D., Kumar, K., & Prajapati, V. K. (2026) · Advances in pharmacology · doi:10.1016/bs.apha.2026.07.003

Molecular and cellular processes connecting type 2 diabetes to Alzheimer’s disease, focusing on oxidative stress, metabolic dysfunction, and neurodegeneration

Ono, R. M. D. S., Lima, J. E. B. D. F., de Lira, J. A. S. P., Sanches, F. C., Piassi, L. D. O., Coelho, L. B. V., Moreira, N. C. D. S., & Sakamoto‐Hojo, E. T. (2026) · Genetics and Molecular Biology · doi:10.1590/1678-4685-gmb-2025-0233

Beta-Caryophyllene Prevents Ouabain-Induced Neurodegeneration and Behavioral Alterations Through PKA/GSK-3β Pathway

Guerra, J. M. D. S., Souza-Pereira, A., Maidana, L. M., Lins, M. P., Pereira, G. L. M., Dahleh, M. M. M., Prigol, M., Furian, A. F., Oliveira, M. S., & Rambo, L. M. (2026) · Neurochemical Research · doi:10.1007/s11064-026-04843-2

LIN-23 Affects C. elegans Pathogen and Stress Resistance by Modulating SKN-1 ActivityPreprint

Tavizon, L. A., Gabaldón, C., Cruz, M. R., Munsey, O., & Garsin, D. A. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.07.22.740106

Pathogenesis and role of ferroptosis mediated by Nrf2 signaling pathway in ischemic stroke

Ying, N., Wang, Y., Li, Z., Yu, X., Xu, X., Guo, Z., Fu, Z., Deng, Y., Liu, L., & Guo, T. (2026) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2026.154363

A targetable ALDH3A2-NRF2 axis mediates KEAP1-mutant tumour development via ferroptosis inhibition

Yang, L., Zhuang, X., Han, J., Cui, W., Zhang, Y., Wang, Z., Song, D., Zhou, C., Huang, S., Cui, K., et al. (2026) · Cell Death and Differentiation · doi:10.1038/s41418-026-01850-2

PI3Kinase based degradation of NRF2 signaling in chemo-radiation resistant HNSCCPreprint

Yadollahi, P., Li, Y., Saab, K., Essien, F. N., Yebra, I., Dayoub, H., Patel, R., Lai, S. Y., Myers, J. N., Skinner, H. D., et al. (2026) · Research Square · doi:10.21203/rs.3.rs-10606918/v1

Heme Oxygenase-1 in Bone Remodeling: Molecular Mechanisms and Therapeutic Implications

Pattananandecha, T., Apichai, S., Saenjum, C., & Surh, Y. (2026) · Biomolecules · doi:10.3390/biom16091224

NRF2 signalling in endometriosis: A hormone-independent axis for fertility-preserving therapeutic innovation

Chen, S., Lu, Y., Wang, L., Weng, A., Miao, Y., Feng, L., Wang, Z., Xu, M., Liang, X., & Wang, Y. (2026) · Pharmacological Research · doi:10.1016/j.phrs.2026.108453

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

Crosstalk Between Nrf2 and Metabolic Pathways: Redox Regulation, Glutaminolysis, and Cellular Proliferation

Oria, R. S., Umeano, V. A., CHUKWU, V. O., Inyang, H. O., & Usin, S. G. (2026) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-026-02185-y

Cancer degronopathies and protein-fate biomarkers in drug resistance and cancer progression: signalling mechanisms, measurement and translational limits

Li, J., Liu, S., Fu, L., Bo, Q., Bai, Y., & Dai, X. (2026) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2026.1960932

Aberrant NRF2-Dependent Cytoprotection Subverts Stress Homeostasis and Promotes Tumor Progression

Feng, G., Yang, Y., Wang, H., Du, M., Xia, Q., & Dong, L. (2026) · Current Issues in Molecular Biology · doi:10.3390/cimb48101022

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

Targeting Nrf2 signaling in Parkinson's disease: Mechanisms, strategies, and therapeutic perspectives

Cao, Y., 张建革, & Shoujiao, P. (2026) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2026.10.027

Stanniocalcin-1 and −2: The insulin-like growth factor system and beyond

Bossow, K. A., Kjeldsen, C. M. N., & Oxvig, C. (2026) · Molecular Biology Reports · doi:10.1007/s11033-026-12940-2

Early PEG-bHb resuscitation for hemorrhagic shock: Attenuation of acute kidney injury via the Nrf2/HO-1 pathway

Yu, H., You, G., Chen, Y., Li, W., Zhang, X., Zhou, H., Zhao, L., & Wang, Y. (2026) · Life Sciences · doi:10.1016/j.lfs.2026.124747

BindingDB Entry 50010105: Nuclear Factor Erythroid 2-Related Factor 2 (Nrf2) Inhibition: An Emerging Strategy in Cancer Therapy.

BindingDB (2021) · UC San Diego · doi:10.7270/q2639t70

BindingDB Entry 50048290: Activation of anti-oxidant Nrf2 signaling by substituted trans stilbenes.

BindingDB (2018) · UC San Diego · doi:10.7270/q23t9kdn

BindingDB Entry 50013255: Tuning melatonin receptor subtype selectivity in oxadiazolone-based analogues: Discovery of QR2 ligands and NRF2 activators with neurogenic properties.

BindingDB (2022) · UC San Diego · doi:10.7270/q2p272wn

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

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

Theoretical Considerations Regarding the Role of Hyperinsulinemia and Insulin/IGF Signaling in Cancer Metabolic Reprogramming: Potential Mechanisms and Therapeutic Vulnerabilities

Chae, B. S. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27219598

NRF2 in hypertrophic scarring: A stage-dependent redox hub poised between resolution and persistence

Thangboonjit, W., Pluempreecha, M., Soingam, T., & Panich, U. (2026) · Redox Biology · doi:10.1016/j.redox.2026.104460

Targeted protein degradation in cancer: strategies for undruggable targets and progress towards clinical translation

Tang, J., Cheng, Z., Xie, T., Zhuang, Y., Hu, H., Li, C., Wang, H., Feng, C., & Tu, C. (2026) · Biomarker Research · doi:10.1186/s40364-026-01032-9

SCF/-TrCP Promotes Glycogen Synthase Kinase 3-Dependent Degradation of the Nrf2 Transcription Factor in a Keap1-Independent Manner

Rada, P., Rojo, A. I., Chowdhry, S., Mcmahon, M., Hayes, J. D., & Cuadrado, A. (2011)

Structural and functional characterization of Nrf2 degradation by glycogen synthase kinase 3/β-TrCP

Cuadrado, A. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.04.029 · Cited by 272

Structural and Functional Characterization of Nrf2 Degradation by the Glycogen Synthase Kinase 3/β-TrCP Axis

Rada, P., Rojo, A. I., Evrard‐Todeschi, N., Innamorato, N. G., Cotte, A., Jaworski, T., Tobón-Velasco, J. C., Devijver, H., García‐Mayoral, M. F., LEUVEN, F. V., et al. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.00180-12 · Cited by 485

Nrf2 is controlled by two distinct β-TrCP recognition motifs in its Neh6 domain, one of which can be modulated by GSK-3 activity

Chowdhry, S., Zhang, Y., McMahon, M., Sutherland, C., Cuadrado, A., & Hayes, J. D. (2013) · Oncogene · doi:10.1038/onc.2012.388 · Cited by 657

Nrf2 is controlled by two distinct β-TrCP recognition motifs in its Neh6 domain, one of which can be modulated by GSK-3 activity. Oncogene 2013

Chowdhry, S., Zhang, Y., Mcmahon, M., Cuadrado, A., & Hayes, J. D. (2016)