Proteasome activation delays aging in vitro and in vivo
Abstract
Aging is a natural biological process that is characterized by a progressive accumulation of macromolecular damage. In the proteome, aging is accompanied by decreased protein homeostasis and function of the major cellular proteolytic systems, leading to the accumulation of unfolded, misfolded, or aggregated proteins. In particular, the proteasome is responsible for the removal of normal as well as damaged or misfolded proteins. Extensive work during the past several years has clearly demonstrated that proteasome activation by either genetic means or use of compounds significantly retards aging. Importantly, this represents a common feature across evolution, thereby suggesting proteasome activation to be an evolutionarily conserved mechanism of aging and longevity regulation. This review article reports on the means of function of these proteasome activators and how they regulate aging in various species.
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GHK should have a positive effect on the ubiquitin proteasome system.
“Thus, it should have a positive effect on this system [13, 14, 46].”
From GHK and DNA: Resetting the human genome to health (2014) · cites this paper as [14]
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“In contrast, animals fed with aip-1 RNAi have a shorter median life span [223].”
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Regulation of the neuronal proteasome by Zif268 (Egr1)
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The proteasome inhibitor PI31 competes with PA28 for binding to 20S proteasomes
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“While proteasomal dysfunction is correlated with age progression and protein aggregation, proteasome activation slows the aging progress down and increases longevity (Chondrogianni et al., 2014).”
BackgroundThe Continuum of Aging and Age-Related Diseases: Common Mechanisms but Different Rates
Franceschi, C., Garagnani, P., Morsiani, C., Conte, M., Santoro, A., Grignolio, A., Monti, D., Capri, M., & Salvioli, S. (2018) · Frontiers in Medicine · doi:10.3389/fmed.2018.00061 · Cited by 945 · see citing works
“A large amount of data indicate that the mechanisms involved in homeostasis and proteostasis collapse with advancing age, favoring the accumulation of the unfolded, misfolded, or aggregated proteins (89).”
BackgroundRegulation of proteasome assembly and activity in health and disease
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The Biology of Aging and Cancer: A Brief Overview of Shared and Divergent Molecular Hallmarks
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“Proteasome activation delays aging in vivo and vitro in a variety of laboratory organisms [84].”
BackgroundMolecular and biological hallmarks of ageing
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Self-citationSulforaphane - role in aging and neurodegeneration
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Self-citationProteasome Activation as a New Therapeutic Approach To Target Proteotoxic Disorders
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“Specifically, the reduction of proteasome activity during aging has been detected in numerous aged human tissues (muscles, lenses, skin, lymphocytes) or other mammalian tissues/organs such as the heart, muscles , spine, brain, liver, adipose tissue and retina (reviewed in [235]).”
Self-citationLi, Y., Xue, Y., Xu, X., Wang, G., Liu, Y., Wu, H., Li, W., Wang, Y., Chen, Z., Zhang, W., et al. (2018) · The EMBO Journal · doi:10.15252/embj.201798786 · Cited by 117 · see citing works
“In line with this, genetic or pharmaceutical activation of the The EMBO Journal Mitochondria regulate proteostasis Yanjun Li et al proteasome retards cell senescence, the cellular basis for aging (Chondrogianni et al , 2014).”
Chondrogianni, N., Voutetakis, K., Καπετάνου, Μ., Delitsikou, V., Papaevgeniou, N., Sakellari, M., Lefaki, M., Filippopoulou, K., & Gonos, E. S. (2014) · Ageing Research Reviews · doi:10.1016/j.arr.2014.12.003 · Cited by 112 · see citing works
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“Aging is a natural process characterized by gradual deterioration of various molecular pathways, continuing loss of homeostatic integrity, and accumulated levels of damaged macromolecules that eventually result in increased death incidence (12).”
Self-citationImpact of Reactive Species on Amino Acids—Biological Relevance in Proteins and Induced Pathologies
Andrés, C. M. C., Pérez de la Lastra, J. M., Andrés Juan, C., Plou, F. J., & Pérez-Lebeña, E. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232214049 · Cited by 71 · see citing works
Establishment of a suite of assays that support the discovery of proteasome stimulators
Trader, D. J., Simanski, S., Dickson, P., & Kodadek, T. J. (2017) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2017.01.003 · Cited by 64 · see citing works
The burden of trisomy 21 disrupts the proteostasis network in Down syndrome
Aivazidis, S., Coughlan, C. M., Rauniyar, A. K., Jiang, H. L., Liggett, L. A., Maclean, K. N., & Roede, J. R. (2017) · PLoS ONE · doi:10.1371/journal.pone.0176307 · Cited by 62 · see citing works
Nguyen, N. N., Rana, A., Goldman, C., Moore, R., Tai, J., Hong, Y., Shen, J., Walker, D. W., & Hur, J. H. (2019) · Scientific Reports · doi:10.1038/s41598-019-39508-4 · Cited by 62 · see citing works
Keith, S. A., Maddux, S., Zhong, Y., Chinchankar, M. N., Ferguson, A. A., Ghazi, A., & Fisher, A. L. (2016) · PLoS Genetics · doi:10.1371/journal.pgen.1005823 · Cited by 58 · see citing works
“Consistent with the potentially grave consequences resulting from the loss of proteostasis, several cellular mechanisms are known to be triggered when the UPS is inhibited, including the activation of the cap’n’collar family transcription factors, such as skn1, Nrf1, and Nrf2, that control the expression of proteasome…”
BackgroundProtein modification and maintenance systems as biomarkers of ageing
Vanhooren, V., Santos, A. N., Voutetakis, K., Petropoulos, I., Libert, C., Simm, A., Gonos, E. S., & Friguet, B. (2015) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2015.03.009 · Cited by 53 · see citing works
Self-citationCommon Pathogenetic Mechanisms Underlying Aging and Tumor and Means of Interventions
Shen, W., He, J., Hou, T., Si, J., & Chen, S. (2022) · Aging and Disease · doi:10.14336/ad.2021.1208 · Cited by 45 · see citing works
Development and Application of a Sensitive Peptide Reporter to Discover 20S Proteasome Stimulators
Coleman, R. A., & Trader, D. J. (2018) · ACS Combinatorial Science · doi:10.1021/acscombsci.7b00193 · Cited by 45 · see citing works
Proteostasis Decline and Redox Imbalance in Age-Related Diseases: The Therapeutic Potential of NRF2
Buttari, B., Tramutola, A., Rojo, A. I., Chondrogianni, N., Saha, S., Berry, A., Giona, L., Miranda, J. P., Profumo, E., Davinelli, S., et al. (2025) · Biomolecules · doi:10.3390/biom15010113 · Cited by 47 · see citing works
“This, in turn, constantly enhances frailty and increases death probability [60].”
Self-citationProteasome Activation to Combat Proteotoxicity
Jones, C. L., & Tepe, J. J. (2019) · Molecules · doi:10.3390/molecules24152841 · Cited by 41 · see citing works
GHK and DNA: Resetting the human genome to health
Pickart, L., Vasquez-Soltero, J. M., & Margolina, A. (2014) · BioMed Research International · doi:10.1155/2014/151479 · Cited by 39 · see citing works
“Higher activities of the UPS appear to retard aging effects [13, 14].”
BackgroundInfluentialThe Proteasome System in Health and Disease
Coux, O., Zieba, B. A., & Meiners, S. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-38266-7_3 · Cited by 38 · see citing works
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Basic mechanisms of longevity: A case study of Drosophila pro-longevity genes
Николаевна, П. Е., Shaposhnikov, M. V., Садритдинова, А. Ф., Kudryavtseva, A. V., & Moskalev, A. (2015) · Ageing Research Reviews · doi:10.1016/j.arr.2015.08.005 · Cited by 36 · see citing works
Higher expression of somatic repair genes in long-lived ant queens than workers
Lucas, E. R., Privman, E., & Keller, L. (2016) · Aging · doi:10.18632/aging.101027 · Cited by 35 · see citing works
“Subunits of the proteasome involved in the UPS have been found to be associated with lifespan and stress resistance in a range of species, from yeast to humans [23-26].”
BackgroundEssential role of proteasomes in maintaining self-renewal in neural progenitor cells
Zhao, Y., Liu, X., He, Z., Niu, X., Shi, W., Ding, J., Zhang, L., Yuan, T., Li, A., Yang, W., et al. (2016) · Scientific Reports · doi:10.1038/srep19752 · Cited by 33 · see citing works
Fiolek, T. J., Magyar, C. L., Wall, T. J., Davies, S. B., Campbell, M. V., Savich, C. J., Tepe, J. J., & Mosey, R. A. (2021) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2021.127821 · Cited by 32 · see citing works
LRRK2 at the Crossroad of Aging and Parkinson’s Disease
Hur, E., & Lee, B. D. (2021) · Genes · doi:10.3390/genes12040505 · Cited by 30 · see citing works
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 26 · see citing works
Self-citationModulation 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 27 · see citing works
“However, interventions aiming at proteasome activation seem to be beneficial for alleviating the age-related phenotypes [34,35].”
BackgroundSelf-citationThe 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 27 · see citing works
A Genetic Screen for Saccharomyces cerevisiae Mutants That Fail to Enter Quiescence
Li, L., Miles, S., & Breeden, L. L. (2015) · G3 Genes Genomes Genetics · doi:10.1534/g3.115.019091 · Cited by 25 · see citing works
Ogłuszka, M., Szostak, A., PAS, M. F. W. T., Poławska, E., Urbański, P., Blicharski, T., Pareek, C. S., Juszczuk‐Kubiak, E., Dunkelberger, J., Horbańczuk, J. O., et al. (2017) · Genes & Nutrition · doi:10.1186/s12263-017-0552-8 · Cited by 25 · see citing works
“Omega-6 and omega-3 fatty acids are polyunsaturated fatty acids (PUFA), which belong to the essential fatty acid family and must be obtained from food sources [3].”
Decreased lipid absorption due to reduced pancreatic lipase activity in aging male mice
Yamamoto, K., Kitano, Y., Shuang, E., Hatakeyama, Y., Sakamoto, Y., Honma, T., & Tsuduki, T. (2014) · Biogerontology · doi:10.1007/s10522-014-9512-5 · Cited by 24 · see citing works
UPS Activation in the Battle Against Aging and Aggregation-Related Diseases: An Extended Review
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Self-citationResponse Mechanisms to Oxidative Stress in Yeast and Filamentous Fungi
Zadrąg‐Tęcza, R., Maślanka, R., Bednarska, S., & Kwolek‐Mirek, M. (2018) · Springer eBooks · doi:10.1007/978-3-030-00683-9_1 · Cited by 19 · see citing works
Approaches for extending human healthspan: from antioxidants to healthspan pharmacology
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“Further, proteasomal function has been reported to decline with age (Chondrogianni et al., 2014).”
BackgroundProteasome function is not impaired in healthy aging of the lung
Caniard, A., Ballweg, K., Lukas, C., Yildirim, A. Ö., Eickelberg, O., & Meiners, S. (2015) · Aging · doi:10.18632/aging.100820 · Cited by 18 · see citing works
“During aging, proteasome activity declines in several tissues such as in brain, liver, muscle, lymphocytes, and heart [14,15].”
BackgroundLangerak, S., Kim, M.-J., Lamberg, H., Godinez, M., Main, M., Winslow, L., O’Connor, M. B., & Zhu, C. C. (2018) · Biology Open · doi:10.1242/bio.029454 · Cited by 16 · see citing works
“Despite the important roles of proteasome in regulating normal protein homeostasis and thereby the ageing process, the activity of proteasome has been found to decline inevitably over time (Chondrogianni et al., 2014).”
InfluentialProtein kinase C activator bryostatin‐1 modulates proteasome function
Khan, T. K., & Nelson, T. J. (2018) · Journal of Cellular Biochemistry · doi:10.1002/jcb.26887 · Cited by 15 · see citing works
“A growing body of evidence shows that cellular and molecular pathways of compromised proteasome activity are linked with aging and age-related diseases.3–5 Furthermore, there is strong evidence that neurodegenerative diseases (Alzheimer's disease, Parkinson's disease, Huntington's disease, amyotrophic lateral sclerosi…”
MethodLamin B receptor plays a key role in cellular senescence induced by inhibition of the proteasome
En, A., Takauji, Y., Miki, K., Ayusawa, D., & Fujii, M. (2019) · FEBS Open Bio · doi:10.1002/2211-5463.12775 · Cited by 15 · see citing works
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 14 · see citing works
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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 13 · see citing works
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Toxicant-mediated redox control of proteostasis in neurodegeneration
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Cekała, K., Trepczyk, K., Sowik, D., Karpowicz, P., Giełdoń, A., Witkowska, J., Giżyńska, M., Jankowska, E., & Wieczerzak, E. (2022) · Biomolecules · doi:10.3390/biom12060777 · Cited by 11 · see citing works
“Hence, increasing the proteasomal degradation in a controlled manner appears attractive as a potential therapeutic method [9].”
BackgroundSakamoto, K., Fujimoto, R., Nakagawa, S., Kamiyama, E., Kanai, K., Kawai, Y., Kojima, H., Hirasawa, A., Wakamatsu, K., & Masutani, T. (2023) · International Journal of Cosmetic Science · doi:10.1111/ics.12876 · Cited by 11 · see citing works
“The artificially elevated expression of proteasomes in yeast, nematodes, Drosophila, and human cells has also been reported to extend the life span of these species [11, 14, 15].”
BackgroundEnhanced Cellular Uptake and Sustained Transdermal Delivery of Collagen for Skin Regeneration
Pandurangan, S., Pooranachithra, M., Ramudu, K. N., Balamurugan, K., & Ayyadurai, N. (2020) · ACS Applied Bio Materials · doi:10.1021/acsabm.0c00755 · Cited by 11 · see citing works
Evaluation of quantitative biomarkers of aging in human PBMCs
Owen, B. M., Phie, J. K. P., Huynh, J., Needham, S., & Fraser, C. (2023) · Frontiers in Aging · doi:10.3389/fragi.2023.1260502 · Cited by 10 · see citing works
Zhang, Y., Huang, X., Zhao, X., Hu, Y., Sun, H., & Kong, W. (2017) · ORL · doi:10.1159/000468944 · Cited by 10 · see citing works
Ubiquitin and SUMO Modifications in Caenorhabditis elegans Stress Response
Drabikowski, K. (2019) · Current Issues in Molecular Biology · doi:10.21775/cimb.035.145 · Cited by 10 · see citing works
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 · see citing works
Self-citationYamamuro, A., Oshima, Y., Iyama, T., Ishimaru, Y., & Yoshioka, Y. (2024) · Journal of Pharmacological Sciences · doi:10.1016/j.jphs.2024.03.002 · Cited by 7 · see citing works
Novelle, M. G., Davis, A., Price, N. L., Ali, A., Fürer-Galbán, S., Zhang, Y., Becker, K. G., Bernier, M., & de Cabo, R. (2015) · Aging · doi:10.18632/aging.100732 · Cited by 7 · see citing works
“During aging, irreversible and deleterious processes are triggered by accumulation of damaged cellular macromolecules [1, 2].”
BackgroundActivation of the 26S Proteasome to Reduce Proteotoxic Stress and Improve the Efficacy of PROTACs
Sedláček, J. (2024) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.4c00408 · Cited by 6 · see citing works
Promising Potential of Curcumin and Related Compounds for Antiviral Drug Discovery
Sharma, A., Sharma, T., Bhaskar, R., Ola, M., Sharma, A. K., & Sharma, P. C. (2024) · Medicinal Chemistry · doi:10.2174/0115734064277371240325105016 · Cited by 6 · see citing works
The Effects of Two Different Multivitamins on Aging Mice
Wu, S. (2017) · The Chinese Journal of Physiology · doi:10.4077/cjp.2017.bag496 · Cited by 6 · see citing works
Evaluation of the Immune Response of Patulin by Proteomics
Wang, F., Ma, L., Wang, Q., Hammock, B. D., Xiao, G., & Liu, R. (2024) · Biosensors · doi:10.3390/bios14070322 · Cited by 5 · see citing works
Protein synthesis inhibition induces proteasome assembly and function
Sakellari, M., Chondrogianni, N., & Gonos, E. S. (2019) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2019.04.114 · Cited by 5 · see citing works
Self-citationEFFECTS AND MECHANISMS OF A NEW MULTIVITAMIN ON CHRONIC METABOLIC SYNDROMES AND AGING
Wu, S., Jiang, X., Liu, Y., Chen, L., & Tao, J. (2016) · African Journal of Traditional Complementary and Alternative Medicines · doi:10.21010/ajtcam.v14i1.7 · Cited by 5 · see citing works
We Are What We Eat: Ubiquitin–Proteasome System (UPS) Modulation Through Dietary Products
Panagiotidou, E., & Chondrogianni, N. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-38266-7_15 · Cited by 5 · see citing works
Self-citationMariner, B. L., Rodriguez, A. S., Heath, O. C., & McCormick, M. A. (2023) · GeroScience · doi:10.1007/s11357-023-00938-8 · Cited by 4 · see citing works
“…phenotypes in yeast, worms and flies, indicating that further research exploring this process in mammals is of great interest to the aging field [3, 4, 8–10 , Although there is great interest in the treatment potential of UPS activators, there are few known pharmacological agents that can do so…”
BackgroundMariner, B. L., Felker, D. P., Cantergiani, R. J., Peterson, J., & McCormick, M. A. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242216163 · Cited by 4 · see citing works
“Elevated activity of the UPS system has been shown to increase lifespan in multiple model organisms [5,7,11–15].”
BackgroundMethodInfluentialWiemer, M., & Osiewacz, H. D. (2014) · F1000Research · doi:10.12688/f1000research.5337.1 · Cited by 4 · see citing works
Proteasome Modulation: A Way to Delay Aging?
Chondrogianni, N., Vasilopoulou, M. Α., Καπετάνου, Μ., & Gonos, E. S. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-801238-3.11461-8 · Cited by 4 · see citing works
Self-citationFrederico, É. H. F. F., de Sá-Caputo, D. D. C., Moreira-Marconi, E., Guimarães, C. A. S., Cardoso, A. L. B. D., Dionello, C. D. F., Morel, D. S., Sousa-Gonçalves, C. R., Paineiras-Domingos, L. L., Costa-Cavalcanti, R. G., et al. (2017) · African Journal of Traditional Complementary and Alternative Medicines · doi:10.21010/ajtcam.v14i4s.7 · Cited by 3 · see citing works
Voutetakis, K., Delitsikou, V., Magouritsas, M. G., & Gonos, E. S. (2017) · New Biotechnology · doi:10.1016/j.nbt.2017.03.002 · Cited by 2 · see citing works
“These in vitro studies indicated that proteasome activation is feasible and results in significant delay of senescence in human cells [13].”
BackgroundSelf-citationDetienne, G., de Walle, P. V., Haes, W. D., Cockx, B., Braeckman, B. P., Schoofs, L., & Temmerman, L. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/421818 · Cited by 2 · see citing works
Ubiquitin Proteasome System as Target for Tumor Therapy
El, M. H. A. (2015) · Chemotherapy Open access · doi:10.4172/2167-7700.1000142 · Cited by 1 · see citing works
“Activation of ubiquitin-proteasome system is an essential step in the degradation process of normal, damaged, or mis-folded proteins [40-42].”
BackgroundShetty, V., Shetty, N. J., Jha, S. K., & Chaubey, R. C. (2022) · Journal of Vector Borne Diseases · doi:10.4103/0972-9062.335770 · Cited by 1 · see citing works
Chinchankar, M. N., Taylor, W. B., Ko, S. H., Apple, E. C., Rodriguez, K. A., Chen, L., & Fisher, A. L. (2023) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2023.194957 · Cited by 1 · see citing works
The accelerated organ senescence and proteotoxicity in thyrotoxicosis mice
Qin, F., Xia, W., Feng, Z., Tan, Y., Zhang, Y., Liu, D., & Zhang, G. (2023) · Journal of Cellular Physiology · doi:10.1002/jcp.31108 · Cited by 1 · see citing works
“Although the decrease of proteasome activity and its association with aging have also been confirmed (Chondrogianni et al., 2014), the dysregulation of ubiquitin proteasome system (UPS) in thyrotoxicosis organism is unknown.”
BackgroundSex programs functional protein level dimorphism in the zebrafish gastrointestinal tract
Niksirat, H., Siino, V., Steinbach, C., & Levander, F. (2025) · Aquaculture Reports · doi:10.1016/j.aqrep.2025.102775 · Cited by 1 · see citing works
Murillo-Cancho, A. F., Martín‐Latorre, M. D. M., Lozano‐Paniagua, D., & Soriano, B. J. N. (2025) · Nutrición clínica y dietética hospitalaria/Nutrición clínica, dietética hospitalaria · doi:10.12873/451murillo · Cited by 1 · see citing works
“It acts by inhibiting acetyltransferases and activating key signaling pathways such as AMPK, SIRT1, and FOXO3a, in addition to modulating autophagic factors related to lysosomal biogenesis, thereby contributing to cellular longevity and maintaining proteostasis 1,23 .”
Ubiquitin and SUMO Modifications in Caenorhabditis elegans Stress Response
Drabikowski, K. (2019) · Caister Academic Press eBooks · doi:10.21775/9781912530120.21 · Cited by 1 · see citing works
Induction of proteostasis pathways in a C. elegans model of exercisePreprint
Randall, L., & Lithgow, G. J. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.02.21.639525 · Cited by 1 · see citing works
“Because the proteasome is known to become dysfunctional with age (20,44), we first tested whether chronic exercise in C. elegans was able to counteract it.”
Effect of SOD1 Overexpression on the 20S Proteasome during Aging
London, J., & Marie, L. P. (2016) · Natural Science · doi:10.4236/ns.2016.86034
Specificity of Protein Carbonylation and Its Relevance in Aging
Cabiscol, E., Tamarit, J., & Ros, J. (2017) · Wiley eBooks · doi:10.1002/9781119374947.ch14
Multi-omic analysis of the aging mouse brain
Kluever, V. (2021) · doi:10.53846/goediss-9022
Antioxidants as modulators of the ubiquitin–proteasome system against aging and proteinopathies
Panagiotidou, E., Gioran, A., & Chondrogianni, N. (2023) · Elsevier eBooks · doi:10.1016/b978-0-443-19247-0.00007-2
Self-citationAlotaibi, F. M., Almazam, . A., Alotaibi, ., Emam, . M., Alqahtani, . S., Alheggi, . I., Alanazi, . F., Alharbi, . K., Alhamed, . A., Ali, . I. A., et al. (2021) · International Journal of Health Sciences · doi:10.53730/ijhs.v5ns1.15088
“Proteasome dysfunction correlates with aging and protein aggregation, while proteasome activation has been shown to slow aging and enhance longevity (Chondrogianni et al., 2014).”
Anthricin-induced hyperactive proteasome and its molecular mechanism
Sakamoto, K., Fujimoto, R., Kamiyama, E., & Hirokawa, T. (2024) · Biochemistry and Biophysics Reports · doi:10.1016/j.bbrep.2024.101830
“Some studies suggest that high proteasome activity is correlated with longevity [23].”
BackgroundLarsson, P., Pettersson, D., Engqvist, H., Rönnerman, E. W., Forssell-Aronsson, E. B., Kovács, A., Karlsson, P., Helou, K., & Parris, T. Z. (2022) · Figshare · doi:10.6084/m9.figshare.21162570
Larsson, P., Pettersson, D., Engqvist, H., Rönnerman, E. W., Forssell-Aronsson, E. B., Kovács, A., Karlsson, P., Helou, K., & Parris, T. Z. (2022) · Figshare · doi:10.6084/m9.figshare.21162567
Protein aggregation in progressive myoclonus epilepsies and related syndromes
Žerovnik, E. (2026) · Exploration of neuroscience · doi:10.37349/en.2026.1006136
Challenges and Limitations in Targeting Oxidative Stress
Pandey, M., Pooja, Nirban, S., Roy, M., Kumari, R., Gorain, B., Jain, N., & Verma, R. K. (2026) · Oxidative stress in applied basic research and clinical practice · doi:10.1007/978-3-032-19837-2_12
The p53-PA200 Feedback Loop Modulates Age-Dependent Tumorigenesis
Jiang, C.-Y., Wang, Y.-L., Lv, N., Cai, B., & Jiang, T.-X. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27198783
“Proteasome activity declines with advancing age, leading to accumulation of misfolded or aggregated proteins and gradually destabilizing protein homeostasis [19,20].”
- Authors
- Chondrogianni, N., Sakellari, M., Lefaki, M., Papaevgeniou, N., & Gonos, E. S.
- Affiliations
- National Hellenic Research Foundation (GR)
- Örebro University (SE)
- Corresponding author
- Chondrogianni, Niki
- Venue
- Free Radical Biology and Medicine
- Publisher
- Elsevier BV
- Published
- 2014-06
- Volume
- 71
- Pages
- 303-320
- ISSN
- 0891-5849 (ISSN-L)
- OpenAlex
- W2018028939
- Cited by
- 94
- References
- 300
- Citations by year
- 2026: 3 · 2025: 5 · 2024: 6 · 2023: 8 · 2022: 9 · 2021: 5 · 2020: 8 · 2019: 10 · 2018: 10 · 2017: 10 · 2016: 9 · 2015: 6 · 2014: 5
- FWCI
- 1.11
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Free Radical Biology and Medicine (publishedVersion)
- PubMed (publishedVersion)
- National Hellenic Research Foundation Helios Repository (National Hellenic Research Foundation) (submittedVersion)
- Funders
- European Commission
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Aging › Genetics, Aging, and Longevity in Model Organisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Keywords
- proteasome activation, aging, longevity, proteostasis, proteasome activator, protein aggregation, protein misfolding, proteasome inhibitors
- MeSH terms
- Aging, Animals, Antioxidants, Drosophila melanogaster, Enzyme Activation, Free Radicals, Humans, Longevity, Nuclear Proteins, Saccharomyces cerevisiae, Caenorhabditis elegans, Proteasome Endopeptidase Complex, Mice, Rats, Proteolysis
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