PGAM5 tethers a ternary complex containing Keap1 and Nrf2 to mitochondria

Oxidants, oxidative stress and the biology of ageing

Finkel, T., & Holbrook, N. J. (2000) · Nature · doi:10.1038/35041687 · Cited by 9,413

Mitochondrial formation of reactive oxygen species

Turrens, J. F. (2003) · The Journal of Physiology · doi:10.1113/jphysiol.2003.049478 · Cited by 5,084

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

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

Identification and Characterization of MAVS, a Mitochondrial Antiviral Signaling Protein that Activates NF-κB and IRF3

Seth, R. B., Sun, L., Ea, C.-K., & Chen, Z. J. (2005) · Cell · doi:10.1016/j.cell.2005.08.012 · Cited by 3,329

Purification and Characterization

Tsai, C. S. (2006) · Biomacromolecules · doi:10.1002/0470080124.ch3 · Cited by 2,368

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

Function and regulation of cullin–RING ubiquitin ligases

Petroski, M. D., & Deshaies, R. J. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1547 · Cited by 2,148

Mitochondria: Dynamic Organelles in Disease, Aging, and Development

Chan, D. C. (2006) · Cell · doi:10.1016/j.cell.2006.06.010 · Cited by 1,987

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

Sulforaphane improves mitochondrial metabolism in fibroblasts from patients with fragile X-associated tremor and ataxia syndrome

Napoli, E., Flores, A., Mansuri, Y., Hagerman, R. J., & Giulivi, C. (2021) · Neurobiology of Disease · doi:10.1016/j.nbd.2021.105427 · Cited by 19

PGAM5 promotes tumorigenesis of gastric cancer cells through PI3K/AKT pathway

Meng, L., Hu, P., & Xu, A.-M. (2023) · Pathology - Research and Practice · doi:10.1016/j.prp.2023.154405 · Cited by 18

Differential squamous cell fates elicited by NRF2 gain of function versus KEAP1 loss of function

Takahashi, J. A., Suzuki, T., Sato, M., Nitta, S., Yaguchi, N., Muta, T., Tsuchida, K., Suda, H., Morita, M., Hamada, S., et al. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114104 · Cited by 18

Biological properties of the BCL-2 family protein BCL-RAMBO, which regulates apoptosis, mitochondrial fragmentation, and mitophagy

Kataoka, T. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.1065702 · Cited by 17

Frequency modulated translocational oscillations of Nrf2, a transcription factor functioning like a wireless sensor

Xue, M., Momiji, H., Rabbani, N., Bretschneider, T., Rand, D. A. J., & Thornalley, P. J. (2015) · Biochemical Society Transactions · doi:10.1042/bst20150060 · Cited by 17

6-OHDA-Induced Changes in Parkinson`s Disease-Related Gene Expression are not Affected by the Overexpression of PGAM5 in In Vitro Differentiated Embryonic Mesencephalic Cells

Stępkowski, T. M., Wasyk, I., Grzelak, A., & Kruszewski, M. K. (2015) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-015-0207-5 · Cited by 17

Role of oxeiptosis in disease mechanisms and therapeutic opportunities

Bhuvaneshwari, K., Harithpriya, K., Ganesan, K., Xu, B., & Ramkumar, K. M. (2025) · APOPTOSIS · doi:10.1007/s10495-025-02087-z · Cited by 16

Antioxidants attenuate mitochondrial oxidative damage through the Nrf2 pathway: A promising therapeutic strategy for stroke

Chen, L., Chen, S., Yang, X., & Min, J. (2023) · Journal of Neuroscience Research · doi:10.1002/jnr.25194 · Cited by 17

4-Octyl itaconate inhibits inflammation to attenuate psoriasis as an agonist of oxeiptosis

You, M., Jiang, Q., Huang, H., Ma, F., & Zhou, X. (2023) · International Immunopharmacology · doi:10.1016/j.intimp.2023.110915 · Cited by 16

Tumor suppressor KEAP1 promotes HSPA9 degradation, controlling mitochondrial biogenesis in breast cancer

Han, B., Zhen, F., Sun, Y., Sun, B., Wang, H., Liu, W., Huang, J., Liang, X., Wang, Y., Chen, X., et al. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114507 · Cited by 18

Nuclear Cytoplasmic Trafficking of Proteins is a Major Response of Human Fibroblasts to Oxidative Stress

Baqader, N. O., Radulović, M., Crawford, M., Stoeber, K., & Godovac‐Zimmermann, J. (2014) · Journal of Proteome Research · doi:10.1021/pr500638h · Cited by 16

Nrf2 and the Nrf2-Interacting Network in Respiratory Inflammation and Diseases

Carlson, J., Price, L., & Deng, H. (2020) · Progress in inflammation research · doi:10.1007/978-3-030-44599-7_3 · Cited by 17

Dual antioxidant activity and the related mechanisms of a novel pentapeptide GLP4 from the fermented mycelia of Ganoderma lingzhi

Ping, H., Luo, F.-J., Ma, Y.-C., Wang, S.-X., Huang, J., Qin, D., Xue, F.-F., Liu, B.-Y., Wu, Q., Xiao-ling, W., et al. (2022) · Food & Function · doi:10.1039/d2fo01572b · Cited by 15

Ferroptosis: The functions of Nrf2 in human embryonic stem cells

Abraki, S. B., Karamali, F., & Nasr‐Esfahani, M. H. (2023) · Cellular Signalling · doi:10.1016/j.cellsig.2023.110654 · Cited by 16

The role of mitophagy in the development of chronic kidney disease

Yang, K., Li, T., Geng, Y., Zou, X., Peng, F., & Gao, W. (2024) · PeerJ · doi:10.7717/peerj.17260 · Cited by 16

The KEAP1/PGAM5/AIFM1-Mediated oxeiptosis pathway in Alzheimer’s disease

Zhong, F., Xiong, L., Wu, J., Chen, Y., Song, J., Yu, W., & Yang, L. (2024) · Brain Research · doi:10.1016/j.brainres.2024.149173 · Cited by 15

H2S probe CPC inhibits autophagy and promotes apoptosis by inhibiting glutathionylation of Keap1 at Cys434

Li, N., Wang, J., Zang, X., Wang, Z., Zhang, T., Zhao, B., Miao, J., & Lin, Z. (2021) · APOPTOSIS · doi:10.1007/s10495-020-01652-y · Cited by 16

Antimutagenic Activity as a Criterion of Potential Probiotic Properties

Prazdnova, E. V., Mazanko, M. S., Chistyakov, V. A., Bogdanova, A. A., Refeld, A. G., Kharchenko, E. Y., & Chikindas, M. L. (2022) · Probiotics and Antimicrobial Proteins · doi:10.1007/s12602-021-09870-9 · Cited by 15

Lipin-1 is a novel substrate of protein phosphatase PGAM5

Okuno, H., Okuzono, H., Hayase, A., Kumagai, F., Tanii, S., Hino, N., Okada, Y., Tachibana, K., Doi, T., & Ishimoto, K. (2019) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2019.01.031 · Cited by 15

The mitochondrial protein PGAM5 suppresses energy consumption in brown adipocytes by repressing expression of uncoupling protein 1

Sugawara, S., Kanamaru, Y., Sekine, S., Maekawa, L., Takahashi, A., Yamamoto, T. S., Watanabe, K., Fujisawa, T., Hattori, K., & Ichijo, H. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.011508 · Cited by 15

Salmonella Typhimurium persistently infects host via its effector SseJ-induced PHB2-mediated mitophagy

Sun, D., Gou, H., Zhang, Y., Li, J., Dai, C., Shen, H., Chen, K., Wang, Y., Pan, P., Zhu, T., et al. (2025) · Autophagy · doi:10.1080/15548627.2025.2462511 · Cited by 14

Cleaved PGAM5 dephosphorylates nuclear serine/arginine-rich proteins during mitophagy

Baba, T., Tanimura, S., Yamaguchi, A., Horikawa, K., Yokozeki, M., Hachiya, S., Iemura, S., Natsume, T., Matsuda, N., & Takeda, K. (2021) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2021.119045 · Cited by 15

Transcription Factor Nrf2 and Mitochondria – Friends or Foes in the Regulation of Aging Rate

Shilovsky, G. A., & Ashapkin, V. V. (2022) · Biochemistry (Moscow) · doi:10.1134/s0006297922120057 · Cited by 14

Nrf2 deletion results in impaired performance in memory tasks and hyperactivity in mature and aged mice

Gergues, M. M., Moiseyenko, A., Saad, S. Z., Kong, A. T., & Wagner, G. C. (2018) · Brain Research · doi:10.1016/j.brainres.2018.08.033 · Cited by 14

Timely expression of PGAM5 and its cleavage control mitochondrial homeostasis during neurite re-growth after traumatic brain injury

Liang, M.-Z., Lu, T.-H., & Chen, L. (2023) · Cell & Bioscience · doi:10.1186/s13578-023-01052-0 · Cited by 14

Cleavage of mitochondrial homeostasis regulator PGAM5 by the intramembrane protease PARL is governed by transmembrane helix dynamics and oligomeric state

Siebert, V., Silber, M., Heuten, E., Muhle‐Goll, C., & Lemberg, M. K. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102321 · Cited by 14

Therapeutic Targeting of Mitochondrial Plasticity and Redox Control to Overcome Cancer Chemoresistance

Mani, S., Ralph, S. J., Swargiary, G., Rani, M., Wasnik, S., Singh, M., & Devi, A. (2023) · Antioxidants and Redox Signaling · doi:10.1089/ars.2023.0379 · Cited by 12

The Role of NRF2 in Cerebrovascular Protection: Implications for Vascular Cognitive Impairment and Dementia (VCID)

Hu, Y., Zhang, F., Ikonomović, M. D., & Yang, T. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25073833 · Cited by 13

Nrf2-Keap1 Activation, A Promising Strategy in the Prevention of Cancer

Ojo, O. A., Ajiboye, B. O., Fadaka, A. O., Taro, P., & Shariati, M. A. (2016) · Free Radicals and Antioxidants · doi:10.5530/fra.2017.1.1 · Cited by 12

Impaired GPX4 activity elicits ferroptosis in alveolar type II cells promoting PHMG-induced pulmonary fibrosis development

Zhang, W., Sun, Z., Cheng, W., Li, X., Zhang, J., Li, Y., Tan, H., Ji, X., Zhang, L., & Tang, J. (2024) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2024.116680 · Cited by 11

Plasmodium berghei-Mediated NRF2 Activation in Infected Hepatocytes Enhances Parasite Survival

Bindschedler, A., Schmuckli‐Maurer, J., Wacker, R., Kramer, N., Rehmann, R., Caldelari, R., & Heussler, V. T. (2022) · Cellular Microbiology · doi:10.1155/2022/7647976 · Cited by 11

PGAM5 interacts with Bcl-rambo and regulates apoptosis and mitophagy

Hashino, T., Matsubara, H., Xu, J., Tanaka, R., Kusagawa, E., Ueda, Y., Yoshida, H., & Kataoka, T. (2022) · Experimental Cell Research · doi:10.1016/j.yexcr.2022.113342 · Cited by 11

Mitochondria as a signaling Hub and target for phenoptosis shutdown

Zolotukhin, P. V., Belanova, A. A., Prazdnova, E. V., Mazanko, M. S., Batyushin, М. М., Chmyhalo, V. K., & Chistyakov, V. A. (2016) · Biochemistry (Moscow) · doi:10.1134/s0006297916040039 · Cited by 11

Mitochondrial Features of Mouse Myoblasts Are Finely Tuned by Low Doses of Ozone: The Evidence In Vitro

Inguscio, C. R., Pozza, E. D., Dando, I., Boschi, F., Tabaracci, G., Angelini, O., Picotti, P. M., Malatesta, M., & Cisterna, B. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24108900 · Cited by 11

Influence of SkQ1 on expression of Nrf2 gene, ARE-controlled genes of antioxidant enzymes and their activity in rat blood leukocytes under oxidative stress

Внуков, В. В., Gutsenko, O. I., Milutina, N. P., Корниенко, И. В., Ananyan, A. A., Danilenko, A. O., Panina, S., Plotnikov, A. A., & Makarenko, M. (2015) · Biochemistry (Moscow) · doi:10.1134/s0006297915120081 · Cited by 11

Short Overview on the Involvement of Lipid Peroxidation Product 4-Hydroxynonenal in Diverse Pathways of Cell Death

Jaganjac, M., Marković, A. S., Deiana, N., & Žarković, N. (2025) · Frontiers in Bioscience-Landmark · doi:10.31083/fbl37139 · Cited by 10

Mitophagy suppresses motor neuron necroptotic mitochondrial damage and alleviates necroptosis that converges to SARM1 in acrylamide‐induced dying‐back neuropathy

Wang, S., Yang, Y., Yu, Z., Song, M., Liu, Z. Q., Shan, S., Yong, H., Ni, W., Qiang, Y., Zhang, C., et al. (2023) · Journal of Neurochemistry · doi:10.1111/jnc.15889 · Cited by 10

OAB-14 Attenuated Glymphatic System Disorder, Neuroinflammation and Dyskinesia in Parkinson’s Disease Model Mice Induced by Rotenone

Zhao, X., Cao, R., Tian, X., Liu, P., Liu, D., Yu, X., Zheng, Z., Chen, G., & Zou, L. (2025) · Neurochemical Research · doi:10.1007/s11064-025-04388-w · Cited by 10

Proteomics reveals the importance of the dynamic redistribution of the subcellular location of proteins in breast cancer cells

Pinto, G., Alhaiek, A. A. M., & Godovac‐Zimmermann, J. (2015) · Expert Review of Proteomics · doi:10.1586/14789450.2015.1002474 · Cited by 12

BIRO1, a Cell-Permeable BH3 Peptide, Promotes Mitochondrial Fragmentation and Death of Retinoblastoma Cells

Allaman-Pillet, N., Oberson, A., & Schorderet, D. F. (2014) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-14-0253 · Cited by 11

Redox-Related Epigenetic Mechanisms in Glioblastoma: Nuclear Factor (Erythroid-Derived 2)-Like 2, Cobalamin, and Dopamine Receptor Subtype 4

Schrier, M. S., Trivedi, M. S., & Deth, R. C. (2017) · Frontiers in Oncology · doi:10.3389/fonc.2017.00046 · Cited by 10

Astragalin protects the liver from oxidative damage by modulating the lnc XIST/miR-155-5p/Nrf2 axis

Zhu, K., Zhang, W., Wu, Q., Yang, Q., Gong, Z., Shao, S., & Zhang, W. (2023) · Journal of Functional Foods · doi:10.1016/j.jff.2023.105769 · Cited by 9

Modular Nanotransporters Delivering Biologically Active Molecules to the Surface of Mitochondria

Khramtsov, Y. V., Ulasov, A. V., Slastnikova, T. A., Rosenkranz, A. A., Lupanova, T. N., Georgiev, G. P., & Sobolev, A. S. (2023) · Pharmaceutics · doi:10.3390/pharmaceutics15122687 · Cited by 8

The Ratio of Thioredoxin/Keap1 Protein Level is a Predictor of Distant Metastasis in Colorectal Cancer

Chang, L., Fan, C., Tseng, W., Chein, H., Hsieh, T.-Y., Chen, J., Hwang, C., & Hua, C. (2017) · Biomarkers in Medicine · doi:10.2217/bmm-2017-0107 · Cited by 9

Reactive Oxygen and Nitrogen Species in Biological Systems: Reactions and Regulation by Carotenoids

Landrum, J. T. (2012) · Humana Press eBooks · doi:10.1007/978-1-62703-203-2_4 · Cited by 10

Spatial and temporal dynamics of the cardiac mitochondrial proteome

Lau, E., Huang, D., Cao, Q., Dincer, T. U., Black, C. M., Lin, A. J., Lee, J. M., Wang, D., Liem, D. A., Lam, M. P., et al. (2015) · Expert Review of Proteomics · doi:10.1586/14789450.2015.1024227 · Cited by 10

The polyphenolic compound punicalagin protects skin fibroblasts from UVA radiation oxidative damage

Bianchetti, G., Bottoni, P., Tringali, G., Maulucci, G., Tabolacci, E., & Clementi, M. E. (2024) · Current Research in Pharmacology and Drug Discovery · doi:10.1016/j.crphar.2024.100186 · Cited by 9

Nrf2 mediates mitochondrial and NADPH oxidase-derived ROS during mild heat stress at 40 °C

Hraoui, G., Grondin, M., Breton, S., & Averill‐Bates, D. A. (2025) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2025.119897 · Cited by 9

Assembly of PGAM5 into Multimeric Complexes Provides a Mechanism for Allosteric Regulation of Phosphatase Activity

Tipton, P. A., Su, T., & Hannink, M. (2018) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2018.05.017 · Cited by 8

Genetic mapping of renal glutathione suggests a novel regulatory locus on the murine X chromosome and overlap with hepatic glutathione regulation

Gould, R. L., Craig, S. W., McClatchy, S., Churchill, G. A., & Pazdro, R. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.07.035 · Cited by 8

LFHP-1c improves cognitive function after TBI in mice by reducing oxidative stress through the PGAM5-NRF2-KEAP1 ternary complex

Shao, W., Wang, J.-J., Niu, Z.-H., Zhang, K., Wang, S., Wang, Y., Tang, Y., Wang, C., Hou, S., Zhou, D., et al. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e36820 · Cited by 7

Unveiling a novel signalling pathway involving NRF2 and PGAM5 in regulating the mitochondrial unfolded protein response in stressed cardiomyocytes.

Safakli, R., Gray, S., Bernardi, N., & Smyrnias, I. (2024) · International Journal of Biochemistry and Cell Biology · doi:10.1016/j.biocel.2024.106704 · Cited by 7

Programmed Necrosis/Necroptosis: An Inflammatory Form of Cell Death

Chan, F. K.-M. (2013) · Springer eBooks · doi:10.1007/978-1-4614-9302-0_10 · Cited by 7

The Nrf2-Keap1 signalling pathway: Mechanisms of ARE transcription regulation in antioxidant cellular defence

Atia, A., & Abdullah, A. (2014) · International Journal of PharmTech Research · Cited by 7

Neurodegeneration from Drugs and Aging‐Derived Free Radicals

Ramkissoon, A., Shapiro, A. M., Loniewska, M. M., & Wells, P. G. (2013) · Wiley eBooks · doi:10.1002/9781118355886.ch10 · Cited by 6

The Unity of Redox and Structural Remodeling of Brown Adipose Tissue in Hypothyroidism

Aleksic, M., Kalezic, A., Saso, L., Janković, A., Korać, B., & Korać, A. (2021) · Antioxidants · doi:10.3390/antiox10040591 · Cited by 5

Curcumin for protecting mitochondria and downregulating inflammation

Salimi, A., Jamali, Z., & Shirmard, L. R. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-90256-4.00014-x · Cited by 5

Modular Nanotransporters Deliver Anti-Keap1 Monobody into Mouse Hepatocytes, Thereby Inhibiting Production of Reactive Oxygen Species

Khramtsov, Y. V., Ulasov, A. V., Rosenkranz, A. A., Slastnikova, T. A., Lupanova, T. N., Georgiev, G. P., & Sobolev, A. S. (2024) · Pharmaceutics · doi:10.3390/pharmaceutics16101345 · Cited by 5

PGAM5 cleavage and oligomerization equilibrates mitochondrial dynamics under stress by regulating DRP1 function

Nag, S., Szederkenyi, K., Yip, C. M., & McQuibban, G. A. (2025) · Journal of Cell Science · doi:10.1242/jcs.263903 · Cited by 4

Protein Phosphohistidine Phosphatases of the HP Superfamily

Rigden, D. J. (2019) · Methods in molecular biology · doi:10.1007/978-1-4939-9884-5_7 · Cited by 4

Nrf2 Activation, an Innovative Therapeutic Alternative in Cerebral Ischemia

Silva‐Islas, C. A., Ricardo, A., Ana, L., & Perla, D. (2012) · InTech eBooks · doi:10.5772/34324 · Cited by 4

The protective effect and mechanism of dexmedetomidine in inhibiting ferroptosis

Ren, X., & Wang, R. (2025) · Frontiers in Pharmacology · doi:10.3389/fphar.2025.1605363 · Cited by 3

Regulation of Mitochondrial Functions by Transcription Factor NRF2

Reddy, N. M., Qureshi, W., Potteti, H. R., Kalvakolanu, D. V., & Reddy, S. P. (2014) · Respiratory medicine · doi:10.1007/978-1-4939-0829-5_2 · Cited by 4

Identification and validation of protein biomarkers for predicting gastrointestinal stromal tumor recurrence

Sun, J., Li, J., He, Y., Kang, W., & Ye, X. (2024) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2024.02.017 · Cited by 2

Optimization of a Modular Nanotransporter Design for Targeted Intracellular Delivery of Photosensitizer

Alieva, R. T., Ulasov, A. V., Khramtsov, Y. V., Slastnikova, T. A., Lupanova, T. N., Gribova, M. A., Georgiev, G. P., & Rosenkranz, A. A. (2024) · Pharmaceutics · doi:10.3390/pharmaceutics16081083 · Cited by 2

Feed-Forward and Feed-Back Circuits of the NRF2/AP-1 Composite Pathway

Zolotukhin, P. V., & Belanova, A. A. (2016) · InTech eBooks · doi:10.5772/65216 · Cited by 2

Gene expression analysis in peripheral blood cells of patients with hereditary leiomyomatosis and renal cell cancer syndrome (HLRCC): identification of NRF2 pathway activation

Valencia, C. A., Kleine, L. L., Velasco, A. M. P., Barreto, A. Y. C., & Díaz, C. E. A. (2018) · Familial Cancer · doi:10.1007/s10689-017-0068-9 · Cited by 2

MOTS-c attenuates hyperoxia-induced neonatal cardiac injury by inhibiting oxeiptosis via maintaining the KEAP1-PGAM5 interaction

Li, S.-H., Chen, S.-Q., Lu, T., Wang, J.-H., Wang, J., Wu, Y.-X., Pang, Q., & Chen, D. (2026) · Life Sciences · doi:10.1016/j.lfs.2026.124452 · Cited by 1

PGAM5: A Novel Type of Protein Serine/Threonine Phosphatase That Exists in the Mitochondria

Taked, K. (2011) · Journal of Oral Biosciences · doi:10.1016/s1349-0079(11)80014-9 · Cited by 1

PGAM5: A Novel Type of Protein Serine/Threonine Phosphatase That Exists in the Mitochondria

Takeda, K. (2011) · Journal of Oral Biosciences · doi:10.2330/joralbiosci.53.122 · Cited by 1

Basic Leucine Zipper Protein Nuclear Factor Erythroid 2–related Factor 2 as a Potential Therapeutic Target in Brain Related Disorders

Goyal, A., Gopika, S., & Agrawal, N. (2022) · Protein and Peptide Letters · doi:10.2174/0929866529666220622124253 · Cited by 1

Nrf2 Regulates β-cell Mass by Suppressing Cell Death and Promoting ProliferationPreprint

Baumel-Alterzon, S., Katz, L. S., Brill, G., Jean-Pierre, C., Li, Y., Biswal, S. S., Garcı́a-Ocaña, A., & Scott, D. K. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.03.05.434145 · 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

THE PROSURVIVAL ACTIVITIES OF APOPTOSIS-INDUCING FACTOR CONVERGE UPON THE REGULATION OF MITOCHONDRIAL METABOLISM, A NOVEL CELL DEATH PATHWAY, AND THE PROGRESSION OF PROSTATE CANCER

Lenhausen, A. M. (2013) · WakeSpace Scholarship (Wake Forest University)

Mécanismes de la toxicité cardiaque induite par les rayonnements ionisants

Pousa, A. Q., & Vozenin, M. (2016) · Archives des Maladies du Coeur et des Vaisseaux - Pratique · doi:10.1016/j.amcp.2016.10.003

The Role of Prostaglandin H Synthase (PHS) Bioactivation and Nuclear Factor Erythroid 2-related Factor 2 (Nrf2)-Mediated Protection in Endogenous and Methamphetamine-initiated Neurotoxicity

Ramkissoon, A. (2012) · TSpace (University of Toronto)

Characterization of PGAM5

Wilkins, J. M. (2013) · MOspace Institutional Repository (University of Missouri) · doi:10.32469/10355/44044

Oxidative and energetic stress: regulation of Nrf2 and mitochondrial biogenesis for slowed aging interventions

Bruns, D. R., Hamilton, K. L., Miller, B. F., Wilusz, C. J., & Pagliassotti, M. J. (2007) · Digital Collections of Colorado (Colorado State University) · doi:10.25675/3.020021

Apoptosis-Inducing Factor Mediates Metabolism and Oxidative Stress Signaling through Functionally Uncoupled Mechanisms to the Benefit of Tumorigenesis

Scott, A. J. (2019) · NDSU Repository (North Dakota State University)

Targeting Mitochondrial Metabolism as a Key Vulnerability in Artemisinin-Resistant Plasmodium falciparum Malaria

Fidock, D. A. (2020)

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

Cleavage of PGAM5 by the intramembrane protease PARL is governed by transmembrane helix dynamics and oligomeric statePreprint

Siebert, V., Silber, M., Heuten, E., Muhle‐Goll, C., & Lemberg, M. K. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.11.19.469224

La sustracción internacional de menores en la jurisprudencia española

Moreno, G. P. (2002) · Revista de Derecho de Familia: doctrina, jurisprudencia, legislación

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

Faculty Opinions recommendation of Mitochondrial phosphoglycerate mutase 5 uses alternate catalytic activity as a protein serine/threonine phosphatase to activate ASK1.

Choi, E. (2009) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.1166101.627014

Mitochondria-derived Vesicles mediate Mito-nuclear Trafficking of CargoPreprint

Rajeev, T., Shil, D., Bhattacharjee, S., Ramesh, L., Samuel, V., Nair, N., Marib, A., Jayakumar, M., Gayathri, S., Surendran, A., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.05.04.592299

Additional file 2 of Timely expression of PGAM5 and its cleavage control mitochondrial homeostasis during neurite re-growth after traumatic brain injury

Liang, M.-Z., Lu, T.-H., & Chen, L. (2024) · Figshare · doi:10.6084/m9.figshare.26591456

Additional file 1 of Timely expression of PGAM5 and its cleavage control mitochondrial homeostasis during neurite re-growth after traumatic brain injury

Liang, M.-Z., Lu, T.-H., & Chen, L. (2024) · Figshare · doi:10.6084/m9.figshare.26591453

Amyloid precursor protein interacts with the mitochondrial phosphatase PGAM5 and regulates mitochondrial respirationPreprint

Shukla, K., Zhang, Z., Plafker, K. S., Matsuzaki, S., Salinas-Salinas, C., Thomason, Y. M., Houmam, S., Barber, D., Faakye, A., Humphries, K. M., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.01.20.700642

High-throughput mitochondrial morphology screen identifies PGS1 as a functional suppressor of mitochondrial fragmentation in patient-derived OPA1 mutant fibroblasts

Cretin, E. (2021) · theses.fr (ABES) · doi:10.70675/5eaca89az9b6az4b80z9614z08ea32bd2ac6

The antioxidant transcription factor NRF2 as a new regulator of the extracellular matrix in human skin fibroblasts

Salamito, M. (2020) · theses.fr (ABES) · doi:10.70675/06c757bdz04c8z4119za1e4z46921f1528b1

Superoxide dismutase mimics : an integrated approach from chemical design to bioactivity in cells

Bouvet, J. (2023) · theses.fr (ABES) · doi:10.70675/12c2d6a7ze53cz41eezb98azd3f258c882a7

ZO-2 blocks the localization of PGAM5 protein to the mitochondrial membrane and suppresses pancreatic cancer malignancy through metabolic reprogramming

Yu, S., Ke, M., Ma, M., Jiang, T., Li, X., & Xie, K. (2026) · Genes & Diseases · doi:10.1016/j.gendis.2026.102290

Targeted degradation of hepatic KEAP1 mitigates drug-induced liver injury via dual boosting NRF2 and PGAM5 signaling

Deng, Y., Xu, L., Niu, X., Li, J., Xiong, Y., Zhu, G., Lu, Z., Xu, C., Wang, X., Wang, P., et al. (2026) · Redox Biology · doi:10.1016/j.redox.2026.104296

The Discovery of GSK3227634: A Potent Inhaled Inhibitor of the KEAP1/NRF2 Protein–Protein Interaction for the Treatment of Chronic Obstructive Pulmonary Disease

Callahan, J. F., Davies, T. G., Bantscheff, M., Bédard, S., Boehm, J. D., Booth-Genthe, C. L., Concha, N. O., Copley, R. C. B., Davis, A., Davis, R., et al. (2026) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6c01820

Phosphoglycerate mutase 5 regulates lipid metabolism and mitochondrial homeostasis in hepatocellular cancer cells

Guttula, P. K., Muthusamy, G., Liu, C., Devora, P. A., Sasaki, E., Butsch, T., Gandhi, H., Moran, J., Gartia, M. R., & Johnston, A. N. (2026) · Cellular Signalling · doi:10.1016/j.cellsig.2026.112833

TRIM25 facilitates mitochondrial dysfunction and extracellular matrix degradation by enhancing USP7‐driven ENO1 deubiquitination during intervertebral disc degeneration

Liu, X., Zhang, W., Feng, H., Lai, L., Cao, C., Yang, G., Gao, Y., Wang, B., Wang, H., Yu, B., et al. (2026) · Clinical and Translational Medicine · doi:10.1002/ctm2.70785

Hydrogen peroxide sensing and signaling in physiology and disease: implications for therapy

Mailloux, R. J. (2026) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-026-02905-z

ED-71 ameliorates oxeiptosis-associated signaling in BMSCs under diabetic osteoporosis by alleviating PKM2-associated metabolic dysregulation and mitochondrial dysfunction.

Yuan, R., Cui, Y.-J., Sun, J., Liu, H.-R., Guo, J., Qi, Y.-P., Du, J., & Li, M.-Q. (2026) · Cellular Signalling · doi:10.1016/j.cellsig.2026.112946

Targeting metabolic cell death in cancer to reverse drug resistance

Liu, T., Dang, Y., Zhang, W., Liu, Y., Ji, Y., Lu, P., Zou, H., Yang, W., & JIANG, J. (2026) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2026.189737

Mitochondrial proteins Anti-oxidant gene expression

Lo, S.-C., Hannink, M., Stress, O., & Ligases, U. (2008)

A PGAM5–KEAP1–Nrf2 complex is required for stress-induced mitochondrial retrograde trafficking

O'Mealey, G. B., Plafker, K. S., Berry, W. L., Janknecht, R., Chan, J. Y., & Plafker, S. M. (2017) · Journal of Cell Science · doi:10.1242/jcs.203216 · Cited by 99

PGAM5, a Bcl-X L-interacting Protein, Is a Novel Substrate for the Redox-regulated Keap1-dependent

Complex, U. L., Lo, S.-C., & Hannink, M. (2013)

PGAM5, a Bcl‐XL‐interacting protein, is a novel substrate for the redox‐regulated Keap1‐dependent ubiquitin ligase complex.

Lo, S., & Hannink, M. (2007) · The FASEB Journal · doi:10.1096/fasebj.21.6.a1022 · Cited by 1

The spatiotemporal regulation of the Keap1–Nrf2 pathway and its importance in cellular bioenergetics

Dinkova‐Kostova, A. T., Baird, L., Holmström, K. M., Meyer, C. J., & Abramov, A. Y. (2015) · Biochemical Society Transactions · doi:10.1042/bst20150003 · Cited by 86