Nuclear Erythroid Factor 2-mediated Proteasome Activation Delays Senescence in Human Fibroblasts

A biomarker that identifies senescent human cells in culture and in aging skin in vivo.

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An Nrf2/Small Maf Heterodimer Mediates the Induction of Phase II Detoxifying Enzyme Genes through Antioxidant Response Elements

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

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Cell Survival Responses to Environmental Stresses Via the Keap1-Nrf2-ARE Pathway

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Oxidative stress sensor Keap1 functions as an adaptor for Cul3-based E3 ligase to regulate proteasomal degradation of Nrf2

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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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Cellular senescence in cancer and aging.

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Isolation of NF-E2-related factor 2 (Nrf2), a NF-E2-like basic leucine zipper transcriptional activator that binds to the tandem NF-E2/AP1 repeat of the beta-globin locus control region

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

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Evolutionarily conserved transcription factors as regulators of longevity and targets for geroprotection

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PAC1 Gene Knockout Reveals an Essential Role of Chaperone-Mediated 20S Proteasome Biogenesis and Latent 20S Proteasomes in Cellular Homeostasis

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mTORC2 facilitates endothelial cell senescence by suppressing Nrf2 expression via the Akt/GSK-3β/C/EBPα signaling pathway

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Molecular Mechanisms Underlying Hepatocellular Carcinoma Induction by Aberrant NRF2 Activation-Mediated Transcription Networks: Interaction of NRF2-KEAP1 Controls the Fate of Hepatocarcinogenesis

Haque, E., Karim, M. R., Teeli, A. S., Śmiech, M., Leszczyński, P., Winiarczyk, D., Parvanov, E. D., Atanasov, A. G., & Taniguchi, H. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21155378 · Cited by 40

The metabolite alpha-ketobutyrate extends lifespan by promoting peroxisomal function in C. elegans

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The Naked Mole-Rat

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NFE2L2 polymorphisms, mortality, and metabolism in the general population

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NRF2 in age-related musculoskeletal diseases: Role and treatment prospects

Zhang, X., Li, H., Chen, L., Wu, Y., & Li, Y. (2023) · Genes & Diseases · doi:10.1016/j.gendis.2023.101180 · Cited by 38

Pharmacotherapeutic role of astringin against chromium induced nephrotoxicity via modulating TLR4/MyD88, HMGB1/RAGE and NF-κB pathway: A biochemical and pharmacokinetic approach

Han, H., Hayat, M. F., Zahara, S. S., Akbar, A., Alzahrani, K. J., Alsharif, K. F., Alzahrani, F. M., & Al‐Emam, A. (2025) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2025.127666 · Cited by 34

Genetic deletion of Nrf2 promotes immortalization and decreases life span of murine embryonic fibroblasts

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Oxytocin alleviates cellular senescence through oxytocin receptor‐mediated extracellular signal‐regulated kinase/Nrf2 signalling

Cho, S., Kim, A. Y., Kim, J., Choi, D. H., Son, E., & Shin, D. W. (2019) · British Journal of Dermatology · doi:10.1111/bjd.17824 · Cited by 35

Impact of Antioxidant Natural Compounds on the Thyroid Gland and Implication of the Keap1/Nrf2 Signaling Pathway.

Paunkov, A., Chartoumpekis, D., Ziros, P. G., Chondrogianni, N., Kensler, T., & Sykiotis, G. (2019) · Current pharmaceutical design · doi:10.2174/1381612825666190701165821 · Cited by 33

The anti-inflammatory effect of melatonin in SH-SY5Y neuroblastoma cells exposed to sublethal dose of hydrogen peroxide

Nopparat, C., Chantadul, V., Permpoonputtana, K., & Govitrapong, P. (2017) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2017.04.001 · Cited by 35

Cancer chemoprevention via activation of proteostatic modules

Sklirou, A. D., Papanagnou, E., Fokialakis, N., & Trougakos, I. P. (2017) · Cancer Letters · doi:10.1016/j.canlet.2017.10.034 · Cited by 32

Trash Talk: Mammalian Proteasome Regulation at the Transcriptional Level

Kaya, H. E. K., & Radhakrishnan, S. K. (2020) · Trends in Genetics · doi:10.1016/j.tig.2020.09.005 · Cited by 32

Neuroprotective Effects of Protein Tyrosine Phosphatase 1B Inhibition against ER Stress-Induced Toxicity

Jeon, Y., Lee, S., Kim, S., Kwon, Y., Kim, K., Chung, C. G., Lee, S., Lee, S. B., & Kim, H. (2017) · Molecules and Cells · doi:10.14348/molcells.2017.2320 · Cited by 31

Small Molecular Nrf2 Inhibitors as Chemosensitizers for Cancer Therapy

Lin, H., Qiao, Y., Yang, H., Nan, Q., Qu, W., Feng, F., Liu, W., Chen, Y., & Sun, H. (2020) · Future Medicinal Chemistry · doi:10.4155/fmc-2019-0285 · Cited by 30

hPMSCs protects against d-galactose-induced oxidative damage of CD4+ T cells through activating Akt-mediated Nrf2 antioxidant signaling

Xiong, Y., WANG, Y., Zhang, J., Zhao, N., Zhang, A., Zhang, A., Zhao, D., Yu, Z., Yin, Y., Song, L., et al. (2020) · Stem Cell Research & Therapy · doi:10.1186/s13287-020-01993-0 · Cited by 29

Structure and Function of the Ubiquitin–Proteasome System

Chondrogianni, N., & Gonos, E. S. (2012) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-397863-9.00002-x · Cited by 31

Activation of the Nrf2 signaling pathway and neuroprotection of nigral dopaminergic neurons by a novel synthetic compound KMS99220

Lee, J. A., Son, H. J., Choi, J., Kim, J., Han, S. H., Shin, N., Kim, J. H., Kim, S., Heo, J. Y., Kim, D. J., et al. (2017) · Neurochemistry International · doi:10.1016/j.neuint.2017.11.006 · Cited by 30

Targeted de-repression of neuronal Nrf2 inhibits α-synuclein accumulation

Baxter, P. S., Márkus, N. M., Dando, O., He, X., Al-Mubarak, B. R., Qiu, J., & Hardingham, G. E. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-03507-z · Cited by 31

The GSK-3β/Fyn/Nrf2 pathway in fibroblasts and wounds of type 2 diabetes

Bitar, M. S. (2012) · Adipocyte · doi:10.4161/adip.20235 · Cited by 29

Conservation of the Nrf2‐Mediated Gene Regulation of Proteasome Subunits and Glucose Metabolism in Zebrafish

Nguyen, V. T., Fuse, Y., Tamaoki, J., Akiyama, S.-I., Muratani, M., Tamaru, Y., & Kobayashi, M. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/5720574 · Cited by 28

Role of the Ubiquitin–Proteasome in Protein Quality Control and Signaling

Shang, F., & Taylor, A. (2012) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-397863-9.00010-9 · Cited by 29

Pharmacological intervention in a transgenic mouse model improves Alzheimer's-associated pathological phenotype: Involvement of proteasome activation

Mladenović, A., Καπετάνου, Μ., Lončarević‐Vasiljković, N., Todorovic, S. T., Athanasopoulou, S., Jović, M., Prvulović, M., Taoufik, E., Matsas, R., Kanazir, S., et al. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.11.038 · Cited by 29

Modulation of the ubiquitin-proteasome system by marine natural products

Vasilopoulou, M. Α., Ioannou, E., Roussis, V., & Chondrogianni, N. (2021) · Redox Biology · doi:10.1016/j.redox.2021.101897 · Cited by 28

The role of cycloastragenol at the intersection of NRF2/ARE, telomerase, and proteasome activity

Yılmaz, S., Bedіr, E., & Ballar, P. (2022) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2022.06.230 · Cited by 28

Activation of Nrf2/ARE pathway by Anisodamine (654-2) for Inhibition of cellular aging and alleviation of Radiation-Induced lung injury

Guo, H., Chen, J., Yu, H., Dong, L., Yu, R., Li, Q., Song, J., Chen, H., Zhang, H., Pu, J., et al. (2023) · International Immunopharmacology · doi:10.1016/j.intimp.2023.110864 · Cited by 28

Senescence suppressors: their practical importance in replicative lifespan extension in stem cells

Hwang, E. S. (2014) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1685-1 · Cited by 29

Does Nrf2 Play a Role of a Master Regulator of Mammalian Aging?

Zinovkin, R. A., Kondratenko, N. D., & Zinovkina, L. A. (2022) · Biochemistry (Moscow) · doi:10.1134/s0006297922120045 · Cited by 27

Lability of the Nrf2/Keap/ARE Cell Defense System in Different Models of Cell Aging and Age-Related Pathologies

Shilovsky, G. A. (2022) · Biochemistry (Moscow) · doi:10.1134/s0006297922010060 · Cited by 24

Changes in 20S subunit composition are largely responsible for altered proteasomal activities in experimental autoimmune encephalomyelitis

Zheng, J., Dasgupta, A., & Bizzozero, O. A. (2012) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2012.07699.x · Cited by 25

Feedback regulation of proteasome gene expression and its implications in cancer therapy

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Effect of Antioxidants on the Fibroblast Replicative Lifespan In Vitro

Sadowska‐Bartosz, I., & Bartosz, G. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/6423783 · Cited by 24

The profibrotic and senescence phenotype of old lung fibroblasts is reversed or ameliorated by genetic and pharmacological manipulation of Slc7a11 expression

Ritzenthaler, J. D., Torres-González, E., Zheng, Y., Zelko, I. N., van Berkel, V. H., Nunley, D. R., Kidane, B., Halayko, A. J., Summer, R. S., Watson, W. H., et al. (2022) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00593.2020 · Cited by 23

SOD1 deficiency decreases proteasomal function, leading to the accumulation of ubiquitinated proteins in erythrocytes

Homma, T., Kurahashi, T., Lee, J., Kang, E. S., & Fujii, J. (2015) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2015.07.023 · Cited by 23

Biochemical and toxicological evaluation of nano-heparins in cell functional properties, proteasome activation and expression of key matrix molecules

Piperigkou, Z., Καραμάνου, Κ., Afratis, N. A., Bouris, P., Gialeli, C., Belmiro, C. L. R., Pavão, M. S. G., Vynios, D. H., & Tsatsakis, A. M. (2015) · Toxicology Letters · doi:10.1016/j.toxlet.2015.10.005 · Cited by 23

Mechanisms of ubiquitin-independent proteasomal degradation and their roles in age-related neurodegenerative disease

Church, T. R., & Margolis, S. S. (2025) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2024.1531797 · Cited by 25

Involvement of NRF2 and AMPK signaling in aging and progeria: a digest

Petsouki, E., Gerakopoulos, V., Gianniou, D. D., Heiß, E. H., & Trougakos, I. P. (2025) · Redox Biology · doi:10.1016/j.redox.2025.103782 · Cited by 22

The Ginkgo biloba Extract EGb 761 Modulates Proteasome Activity and Polyglutamine Protein Aggregation

Stark, M., & Behl, C. (2014) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2014/940186 · Cited by 22

Metabolic Syndrome, Redox State, and the Proteasomal System

Höhn, A., König, J., & Jung, T. (2016) · Antioxidants and Redox Signaling · doi:10.1089/ars.2016.6815 · Cited by 23

UPS Activation in the Battle Against Aging and Aggregation-Related Diseases: An Extended Review

Papaevgeniou, N., & Chondrogianni, N. (2016) · Methods in molecular biology · doi:10.1007/978-1-4939-3756-1_1 · Cited by 23

Potential role of 20S proteasome in maintaining stem cell integrity of human bone marrow stromal cells in prolonged culture expansion

Lu, L., Song, H., Zhang, W.-G., Liu, X., Zhu, Q., Cheng, X., Yang, G.-J., Li, A., & Xiao, Z. (2012) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2012.04.119 · Cited by 21

Chemical and Physical Approaches to Extend the Replicative and Differentiation Potential of Stem Cells

Hwang, E. S., Ok, J., & Song, S. (2016) · Stem Cell Reviews and Reports · doi:10.1007/s12015-016-9652-x · Cited by 21

Mechanical stress influences the viability and morphology of human parametrial ligament fibroblasts

Hu, M., Hong, L., Hong, S., Min, J., Zhao, Y., Yang, Q. H., Zhang, Q., Tang, J., & Li, Y. (2016) · Molecular Medicine Reports · doi:10.3892/mmr.2016.6052 · Cited by 21

Rejuvenation by Partial Reprogramming of the Epigenome

Mendelsohn, A. R., Larrick, J. W., & Lei, J. L. (2017) · Rejuvenation Research · doi:10.1089/rej.2017.1958 · Cited by 22

Transcription Factor NRF2 in Shaping Myeloid Cell Differentiation and Function

Pfefferlé, M., & Vallelian, F. (2024) · Advances in experimental medicine and biology · doi:10.1007/978-3-031-62731-6_8 · Cited by 18

Reduced Proteasome Activity and Enhanced Autophagy in Blood Cells of Psoriatic Patients

Karabowicz, P., Wroński, A., Ostrowska, H., Waeg, G., Žarković, N., & Skrzydlewska, E. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21207608 · Cited by 20

UBE2E3 regulates cellular senescence and osteogenic differentiation of BMSCs during aging

Liu, Y., Cai, G., Chen, P., Jiang, T., & Xia, Z. (2021) · PeerJ · doi:10.7717/peerj.12253 · Cited by 19

Autophagy-dependent cancer cells circumvent loss of the upstream regulator RB1CC1/FIP200 and loss of LC3 conjugation by similar mechanisms

Towers, C. G., Wodetzki, D., & Thorburn, A. M. (2020) · Autophagy · doi:10.1080/15548627.2020.1741204 · Cited by 18

17β-estradiol inhibits human umbilical vascular endothelial cell senescence by regulating autophagy via p53

Song, S., Wu, S., Wang, Y., Wang, Z. P., Ye, C.-X., Song, R., Song, D., & Ruan, Y. (2018) · Experimental Gerontology · doi:10.1016/j.exger.2018.10.021 · Cited by 18

The Role of Mitochondrial Stress in Muscle Wasting Following Severe Burn Trauma

Ogunbileje, J. O., Herndon, D. N., Murton, A. J., & Porter, C. (2017) · Journal of Burn Care & Research · doi:10.1097/bcr.0000000000000553 · Cited by 18

ARE/Nrf2 Transcription System Involved in Carotenoid, Polyphenol, and Estradiol Protection from Rotenone-Induced Mitochondrial Oxidative Stress in Dermal Fibroblasts

Darawsha, A., Trachtenberg, A., & Sharoni, Y. (2024) · Antioxidants · doi:10.3390/antiox13081019 · Cited by 19

The angiogenic related functions of bone marrow mesenchymal stem cells are promoted by CBDL rat serum via the Akt/Nrf2 pathway

Shen, C., Chen, B., Gu, J., Ning, J., Chen, L., Zeng, J., Yi, B., & Lu, K. (2016) · Experimental Cell Research · doi:10.1016/j.yexcr.2016.04.013 · Cited by 17

FoxO1 Is a Novel Regulator of 20S Proteasome Subunits Expression and Activity

Καπετάνου, Μ., Nespital, T., Tain, L. S., Pahl, A., Partridge, L., & Gonos, E. S. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.625715 · Cited by 19

Transcriptional regulatory networks of the proteasome in mammalian systems

Καπετάνου, Μ., Athanasopoulou, S., & Gonos, E. S. (2021) · IUBMB Life · doi:10.1002/iub.2586 · Cited by 18

Factors determining the sensitivity to proteasome inhibitors of multiple myeloma cells

Pelon, M., Krzemiński, P., Tracz‐Gaszewska, Z., & Misiewicz-Krzemińska, I. (2024) · Frontiers in Pharmacology · doi:10.3389/fphar.2024.1351565 · Cited by 15

Effect of Nrf2 loss on senescence and cognition of tau-based P301S mice

Riordan, R., Wang, R., Yu, Z., Ross, G., Valerio, J., Dimas-Muñoz, J., Heredia, V., Magnusson, K. R., Galván, V., & Pérez, V. (2023) · GeroScience · doi:10.1007/s11357-023-00760-2 · Cited by 15

Beneficial Effects of Elderly Tailored Mediterranean Diet on the Proteasomal Proteolysis

Athanasopoulou, S., Chondrogianni, N., Santoro, A., Asimaki, K., Delitsikou, V., Voutetakis, K., Fabbri, C., Pietruszka, B., Kałuża, J., Franceschi, C., et al. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.00457 · Cited by 15

Pan-cancer analysis of genomic and transcriptomic data reveals the prognostic relevance of human proteasome genes in different cancer types

Larsson, P., Pettersson, D., Engqvist, H., Rönnerman, E. W., Forssell-Aronsson, E. B., Kovács, A., Karlsson, P., Helou, K., & Parris, T. Z. (2022) · BMC Cancer · doi:10.1186/s12885-022-10079-4 · Cited by 17

Defining regorafenib as a senomorphic drug: therapeutic potential in the age-related lung disease emphysema

Park, J.-J., Oh, K., Lee, G.-W., Bang, G., Park, J., Kim, H.-B., Kim, J. Y., Shin, E., & Kim, E. (2023) · Experimental & Molecular Medicine · doi:10.1038/s12276-023-00966-6 · Cited by 15

Polygonatum polysaccharide ameliorates D-galactose-induced cognitive dysfunction in aging rats by inhibiting ferroptosis through activation of Nrf2

Xiao, L., Wen, H., Peng, S., Chen, B., Tang, B., & Liu, B. (2024) · Neuroscience Letters · doi:10.1016/j.neulet.2024.137873 · Cited by 13

Healthspan improvement and anti-aggregation effects induced by a marine-derived structural proteasome activator

Vasilopoulou, M. Α., Gioran, A., Theodoropoulou, M. C., Koutsaviti, A., Roussis, V., Ioannou, E., & Chondrogianni, N. (2022) · Redox Biology · doi:10.1016/j.redox.2022.102462 · Cited by 17

The Interplay between Autophagy and Redox Signaling in Cardiovascular Diseases

Boťanská, B., Dovinová, I., & Barančı́k, M. (2022) · Cells · doi:10.3390/cells11071203 · Cited by 13

Proteasome Biology: Chemistry and Bioengineering Insights

Račková, L., & Csekes, E. (2020) · Polymers · doi:10.3390/polym12122909 · Cited by 14

Implications of Senescent Cell Burden and NRF2 Pathway in Uremic Calcification: A Translational Study

Laget, J., Hobson, S., Muyor, K., Duranton, F., Cortijo, I., Bartochowski, P., Jover, B. F., Lajoix, A., Söderberg, M. P., Ebert, T., et al. (2023) · Cells · doi:10.3390/cells12040643 · 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

Therapy-induced senescence in breast cancer: an overview

Narayanan, C. S., & Lindsay, A. J. (2024) · Exploration of Targeted Anti-tumor Therapy · doi:10.37349/etat.2024.00254 · Cited by 12

Mitochondrial permeabilization without caspase activation mediates the increase of basal apoptosis in cells lacking Nrf2

Ariza, J., González-Reyes, J. A., Jódar, L., Díaz‐Ruiz, A., de Cabo, R., & Villalba, J. M. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.03.015 · Cited by 12

Stress Resistance Screen in a Human Primary Cell Line Identifies Small Molecules That Affect Aging Pathways and Extend Caenorhabditis elegans ’ Lifespan

Zhang, P., Zhai, Y., Cregg, J. M., Ang, K. K. H., Arkin, M. R., & Kenyon, C. J. (2019) · G3 Genes Genomes Genetics · doi:10.1534/g3.119.400618 · Cited by 12

Root hydrotropism and thigmotropism in Arabidopsis thaliana are differentially controlled by redox status

Ponce, G., Corkidi, G., Eapen, D., Lledı́as, F., Cárdenas, L., & Cassab, G. I. (2017) · Plant Signaling & Behavior · doi:10.1080/15592324.2017.1305536 · Cited by 11

Neuron-specific proteasome activation exerts cell non-autonomous protection against amyloid-beta (Aβ) proteotoxicity in Caenorhabditis elegans

Panagiotidou, E., Gioran, A., Bano, D., & Chondrogianni, N. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102817 · Cited by 12

Effect of Selected Antioxidants on the In Vitro Aging of Human Fibroblasts

Bartosz, G., Pieńkowska, N., & Sadowska‐Bartosz, I. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25031529 · Cited by 11

The NRF2/ID2 Axis in Vascular Smooth Muscle Cells: Novel Insights into the Interplay between Vascular Calcification and Aging

Xu, M., Wei, X., Wang, J., Li, Y., Huang, Y., Cheng, A., He, F., Zhang, L., Zhang, C., & Liu, Y. (2024) · Aging and Disease · doi:10.14336/ad.2024.0075 · Cited by 10

SiO 2 /hyaluronic acid nanoparticles carry CaO 2 , DOX and p53 plasmid to effectively achieve ion interference/chemical/gene multimodal therapy of lung cancer

Yi, Z., Huang, X., Lin, N., Yu, F., Chen, Y.-X., Guan, M.-H., Yi, W., & Lai, F. (2023) · Biomaterials Science · doi:10.1039/d2bm02075k · Cited by 9

Signaling pathways of dietary energy restriction and metabolism on brain physiology and in age-related neurodegenerative diseases

Xie, K., Καπετάνου, Μ., Sidiropoulou, K., Bano, D., Gonos, E. S., Mladenović, A., & Ehninger, D. (2020) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2020.111364 · Cited by 9

Interactions Between the Ubiquitin–Proteasome System, Nrf2, and the Cannabinoidome as Protective Strategies to Combat Neurodegeneration: Review on Experimental Evidence

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Nrf2-Mediated Pathway Activated by Prunus spinosa L. (Rosaceae) Fruit Extract: Bioinformatics Analyses and Experimental Validation

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EGF/EGFR signaling axis is a significant regulator of the proteasome expression and activity in colon cancer cells

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Complement C3a Suppresses Spinal Cord Neural Stem Cell Activation by Inhibiting UCHL1 via the NF-κB p65/Nrf2 Pathway

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Anti-ageing properties of Khelma Longevity™: treatment of human fibroblasts increases proteasome levels and decreases the levels of oxidized proteins

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Applications of Nanotechnology in Alzheimer’s Disease

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Proteasomal activation ameliorates neuronal phenotypes linked to FBXO11-deficiency

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Proteasome-mediated ubiquitination in neural regeneration

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THE AGING PROTEASOME AND ITS ACTIVATION AS A NOVEL ANTI-AGING STRATEGY

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Proteasome activation as a novel anti-aging strategy

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Nrf2-Mediated Fibroblast Reprogramming Drives Cellular Senescence by Targeting the Matrisome

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Preincubation with the Proteasome Inhibitor MG‐132 Enhances Proteasome Activity via the Nrf2 Transcription Factor in Aging Human Skin Fibroblasts

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Proteasomal activation by Nrf2 extends lifespan in human fibroblasts

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