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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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“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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Cites
López-Otín, C., Blasco, M. A., Partridge, L., Serrano, M., & Kroemer, G. (2013) · Cell · doi:10.1016/j.cell.2013.05.039 · Cited by 14,982
Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism
Kitada, T., Asakawa, S., Hattori, N., Matsumine, H., Yamamura, Y., Minoshima, S., Yokochi, M., Mizuno, Y., & Shimizu, N. (1998) · Nature · doi:10.1038/33416 · Cited by 5,227
Itoh, K., Chiba, T., Takahashi, S., Ishii, T., Igarashi, K., Katoh, Y., Oyake, T., Hayashi, N., Satoh, K., Hatayama, I., et al. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.6943 · Cited by 3,999
Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice
Hara, T., Nakamura, K., Matsui, M., Yamamoto, A., Nakahara, Y., Suzuki-Migishima, R., Yokoyama, M., Mishima, K., Saito, I., Okano, H., et al. (2006) · Nature · doi:10.1038/nature04724 · Cited by 3,882
Loss of autophagy in the central nervous system causes neurodegeneration in mice
Komatsu, M., Waguri, S., Chiba, T., Murata, S., Iwata, J.-I., Tanida, I., Ueno, T., Koike, M., Uchiyama, Y., Kominami, E., et al. (2006) · Nature · doi:10.1038/nature04723 · Cited by 3,500
Molecular chaperones in protein folding and proteostasis
Hartl, F. U., Bracher, A., & Hayer-Hartl, M. (2011) · Nature · doi:10.1038/nature10317 · Cited by 3,381
Kenyon, C. J. (2010) · Nature · doi:10.1038/nature08980 · Cited by 2,739
Adapting Proteostasis for Disease Intervention
Balch, W. E., Morimoto, R. I., Dillin, A., & Kelly, J. W. (2008) · Science · doi:10.1126/science.1141448 · Cited by 2,495
Genes that act downstream of DAF-16 to influence the lifespan of Caenorhabditis elegans
Murphy, C. T., McCarroll, S. A., Bargmann, C. I., Fraser, A., Kamath, R. S., Ahringer, J., Li, H., & Kenyon, C. (2003) · Nature · doi:10.1038/nature01789 · Cited by 2,280
Structure of 20S proteasome from yeast at 2.4Å resolution
Groll, M., Ditzel, L., Löwe, J., Stock, D., Bochtler, M., Bartunik, H. D., & Huber, R. (1997) · Nature · doi:10.1038/386463a0 · Cited by 2,265
Research works printed but not linked: 1
- Heinemeyer, 2004, The ultimate nanoscale mincer: assembly, structure and active sites of the 20S proteasome core, Cell. Mol. Life Sci., 61, 1562
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Sorted by citations
Sharifi-Rad, M., Anil Kumar, N. V., Zucca, P., Varoni, E. M., Dini, L., Panzarini, E., Rajkovic, J., Tsouh Fokou, P. V., Azzini, E., Peluso, I., et al. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.00694 · Cited by 1,971
“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
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BackgroundRegulation of proteasome assembly and activity in health and disease
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Aunan, J. R., Cho, W. C. S., & Søreide, K. (2017) · Aging and Disease · doi:10.14336/ad.2017.0103 · Cited by 389
“Proteasome activation delays aging in vivo and vitro in a variety of laboratory organisms [84].”
BackgroundMolecular and biological hallmarks of ageing
Aunan, J. R., Watson, M. M., Hagland, H. R., & Søreide, K. (2016) · British journal of surgery · doi:10.1002/bjs.10053 · Cited by 341
Kelmer Sacramento, E., Kirkpatrick, J. M., Mazzetto, M., Baumgart, M., Bartolome, A., Di Sanzo, S., Caterino, C., Sanguanini, M., Papaevgeniou, N., Lefaki, M., et al. (2020) · Molecular Systems Biology · doi:10.15252/msb.20209596 · Cited by 236
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Santín-Márquez, R., Alarcón‐Aguilar, A., López‐Díazguerrero, N. E., Chondrogianni, N., & Königsberg, M. (2019) · GeroScience · doi:10.1007/s11357-019-00061-7 · Cited by 160
Self-citationProteasome Activation as a New Therapeutic Approach To Target Proteotoxic Disorders
Njomen, E., & Tepe, J. J. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b00101 · Cited by 133
Gonos, E. S., Καπετάνου, Μ., Sereikaitė, J., Bartosz, G., Naparło, K., Grzesik, M., & Sadowska‐Bartosz, I. (2018) · Aging · doi:10.18632/aging.101450 · Cited by 135
“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
“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 115
Self-citationPapaevgeniou, N., Sakellari, M., Jha, S., Tavernarakis, N., Holmberg, C. I., Gonos, E. S., & Chondrogianni, N. (2016) · Antioxidants and Redox Signaling · doi:10.1089/ars.2015.6494 · Cited by 75
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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
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 66
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 61
“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 60
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
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Coleman, R. A., & Trader, D. J. (2018) · ACS Combinatorial Science · doi:10.1021/acscombsci.7b00193 · Cited by 45
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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 49
“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 43
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
“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 41
Andrés, C. M. C., de la Lastra, J. M. P., Andrés, C., Plou, F. J., & Pérez‐Lebeña, E. (2023) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.23455 · Cited by 44
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Proshkina, E., 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 38
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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
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
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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
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“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 28
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Li, L., Miles, S., & Breeden, L. L. (2015) · G3 Genes Genomes Genetics · doi:10.1534/g3.115.019091 · Cited by 25
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
“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
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Papaevgeniou, N., & Chondrogianni, N. (2016) · Methods in molecular biology · doi:10.1007/978-1-4939-3756-1_1 · Cited by 23
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 20
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Gruber, J., & Halliwell, B. B. (2017) · Essays in Biochemistry · doi:10.1042/ebc20160091 · Cited by 20
Kaku, H., & Rothstein, T. L. (2020) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2020.00032 · Cited by 18
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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 19
“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
“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
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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
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
Stelmakh, A., Abrahamovych, O., & Cherkas, A. (2016) · Medical Hypotheses · doi:10.1016/j.mehy.2016.09.008 · Cited by 14
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
Self-citationJin, Y., Sun, G., Chen, B., Feng, S., Tang, M., Wang, H., Zhang, Y., Wang, Y., An, Y., Xiao, Y., et al. (2025) · BMC Biology · doi:10.1186/s12915-025-02143-9 · Cited by 14
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Aivazidis, S., Anderson, C. C., & Roede, J. R. (2018) · Current Opinion in Toxicology · doi:10.1016/j.cotox.2018.12.007 · Cited by 13
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
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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 12
“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].”
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Pandurangan, S., Pooranachithra, M., Ramudu, K. N., Balamurugan, K., & Ayyadurai, N. (2020) · ACS Applied Bio Materials · doi:10.1021/acsabm.0c00755 · Cited by 11
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 11
Zhang, Y., Huang, X., Zhao, X., Hu, Y., Sun, H., & Kong, W. (2017) · ORL · doi:10.1159/000468944 · Cited by 10
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Drabikowski, K. (2019) · Current Issues in Molecular Biology · doi:10.21775/cimb.035.145 · Cited by 9
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
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 8
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 9
“During aging, irreversible and deleterious processes are triggered by accumulation of damaged cellular macromolecules [1, 2].”
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Sedláček, J. (2024) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.4c00408 · Cited by 6
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Wu, S. (2017) · The Chinese Journal of Physiology · doi:10.4077/cjp.2017.bag496 · Cited by 6
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Wang, F., Ma, L., Wang, Q., Hammock, B. D., Xiao, G., & Liu, R. (2024) · Biosensors · doi:10.3390/bios14070322 · Cited by 5
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Sakellari, M., Chondrogianni, N., & Gonos, E. S. (2019) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2019.04.114 · Cited by 5
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
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Panagiotidou, E., & Chondrogianni, N. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-38266-7_15 · Cited by 5
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
“…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
“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
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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 5
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
Voutetakis, K., Delitsikou, V., Magouritsas, M. G., & Gonos, E. S. (2017) · New Biotechnology · doi:10.1016/j.nbt.2017.03.002 · Cited by 2
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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
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El, M. H. A. (2015) · Chemotherapy Open access · doi:10.4172/2167-7700.1000142 · Cited by 1
“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
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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
“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
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
“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
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
“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
Thibaudeau, T. A. (2019) · The Research Repository @ WVU (West Virginia University) · doi:10.33915/etd.3780
Multi-omic analysis of the aging mouse brain
Kluever, V. (2021) · eDiss (Georg-August-Universität Göttingen) · 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].”
Metadata
- 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
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › 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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