Proteostasis and the Aging Proteome in Health and Disease
Open accessAbstract
The maintenance of the proteome is essential to preserve cell functionality and the ability to respond and adapt to the changing environment. This is regulated by the proteostasis network, a dedicated set of molecular components comprised of molecular chaperones and protein clearance mechanisms, regulated by cell stress signaling pathways, that prevents the toxicity associated with protein misfolding and accumulation of toxic aggregates in different subcellular compartments and tissues. The efficiency of the proteostasis network declines with age and this failure in protein homeostasis has been proposed to underlie the basis of common age-related human disorders. The current advances in the understanding of the mechanisms and regulation of proteostasis and of the different types of digressions in this process in aging have turned the attention toward the therapeutic opportunities offered by the restoration of proteostasis in age-associated degenerative diseases. Here, we discuss some of the unresolved questions on proteostasis that need to be addressed to enhance healthspan and to diminish the pathology associated with persistent protein damage.
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Aging is associated with impaired activity of the proteasome and mitochondrial Lon proteases and reduced capacity for macromolecule repair.
“aging is associated with impaired activity of the proteasome and mitochondrial Lon proteases [203,204,205] and reduced capacity for macromolecule repair [201,202].”
From Nrf2 and Oxidative Stress: A General Overview of Mechanisms and Implications in Human Disease (2022) · cites this paper as [205]
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Cites
Autophagy fights disease through cellular self-digestion
Mizushima, N., Levine, B., Cuervo, A. M., & Klionsky, D. J. (2008) · Nature · doi:10.1038/nature06639 · Cited by 6,452 · see citing works
Self-citationProtein degradation by the ubiquitin-proteasome pathway in normal and disease states
Lecker, S. H., Goldberg, A. L., & Mitch, W. E. (2006) · Journal of the American Society of Nephrology · doi:10.1681/asn.2006010083 · Cited by 1,234 · see citing works
Endoplasmic reticulum stress in liver disease
Malhi, H., & Kaufman, R. J. (2010) · Journal of Hepatology · doi:10.1016/j.jhep.2010.11.005 · Cited by 1,178 · see citing works
The impact of the unfolded protein response on human disease
Wang, S., & Kaufman, R. J. (2012) · The Journal of Cell Biology · doi:10.1083/jcb.201110131 · Cited by 983 · see citing works
Autophagy gone awry in neurodegenerative diseases
Wong, E. S. P., & Cuervo, A. M. (2010) · Nature Neuroscience · doi:10.1038/nn.2575 · Cited by 883 · see citing works
Self-citationEndoplasmic Reticulum Stress and Type 2 Diabetes
Back, S. H., & Kaufman, R. J. (2012) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-072909-095555 · Cited by 621 · see citing works
Autophagy and aging: keeping that old broom working
Cuervo, A. M. (2008) · Trends in Genetics · doi:10.1016/j.tig.2008.10.002 · Cited by 527 · see citing works
Self-citationCellular Strategies of Protein Quality ControlPreprint
Chen, B., Retzlaff, M., Roos, T. R., & Frydman, J. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a004374 · Cited by 499 · see citing works
Protein Homeostasis and Aging: the importance of exquisite quality control
Koga, H., Kaushik, S., & Cuervo, A. M. (2011) · Ageing research reviews · doi:10.1016/j.arr.2010.02.001 · Cited by 476 · see citing works
Self-citationPharmacological approaches to restore mitochondrial function
Andreux, P. A., Houtkooper, R. H., & Auwerx, J. (2013) · Nature Reviews Drug Discovery · doi:10.1038/nrd4023 · Cited by 383 · see citing works
Mechanism of the eukaryotic chaperonin: protein folding in the chamber of secrets
Spiess, C., Meyer, A. S., Reißmann, S., & Frydman, J. (2004) · Trends in Cell Biology · doi:10.1016/j.tcb.2004.09.015 · Cited by 377 · see citing works
Functions of the proteasome: from protein degradation and immune surveillance to cancer therapy
Goldberg, A. L. (2007) · Biochemical Society Transactions · doi:10.1042/bst0350012 · Cited by 370 · see citing works
Signaling the mitochondrial unfolded protein response
Pellegrino, M. W., Nargund, A. M., & Haynes, C. M. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.02.019 · Cited by 359 · see citing works
The Ribosome as a Hub for Protein Quality Control
Pechmann, S., Willmund, F., & Frydman, J. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.01.020 · Cited by 269 · see citing works
Quality Control of Mitochondrial ProteostasisPreprint
Baker, M. J., Tatsuta, T., & Langer, T. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a007559 · Cited by 260 · see citing works
The Stress of Protein Misfolding: From Single Cells to Multicellular OrganismsPreprint
Gidalevitz, T., Prahlad, V., & Morimoto, R. I. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a009704 · Cited by 254 · see citing works
Self-citationAutophagy in health and disease. 5. Mitophagy as a way of life
Gottlieb, R. A., & Carreira, R. (2010) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00097.2010 · Cited by 228 · see citing works
Regulation of Organismal Proteostasis by Transcellular Chaperone Signaling
van Oosten‐Hawle, P., Porter, R. S., & Morimoto, R. I. (2013) · Cell · doi:10.1016/j.cell.2013.05.015 · Cited by 197 · see citing works
Self-citationAutophagy in Health and Disease
Gözüaçık, D. (2013) · Elsevier eBooks · doi:10.1016/c2010-0-66523-0 · Cited by 194 · see citing works
Protein Homeostasis in Models of Aging and Age-Related Conformational Disease
Kikis, E. A., Gidalevitz, T., & Morimoto, R. I. (2010) · Advances in experimental medicine and biology · doi:10.1007/978-1-4419-7002-2_11 · Cited by 187 · see citing works
Self-citationChaperone networks: Tipping the balance in protein folding diseases
Voisine, C., Pedersen, J. S., & Morimoto, R. I. (2010) · Neurobiology of Disease · doi:10.1016/j.nbd.2010.05.007 · Cited by 163 · see citing works
Self-citationdel Álamo, M., Hogan, D. J., Pechmann, S., Albanèse, V., Brown, P. O., & Frydman, J. (2011) · PLoS Biology · doi:10.1371/journal.pbio.1001100 · Cited by 158 · see citing works
Protein Homeostasis and Aging: Taking Care of Proteins From the Cradle to the Grave
Morimoto, R. I., & Cuervo, A. M. (2009) · The Journals of Gerontology Series A: Biological Sciences and Medical Sciences · doi:10.1093/gerona/gln071 · Cited by 151 · see citing works
Self-citationTargeting endoplasmic reticulum stress in metabolic disease
Cao, S. S., & Kaufman, R. J. (2013) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2013.756471 · Cited by 149 · see citing works
Mitochondrial turnover in the heart
Gottlieb, R. A., & Gustafsson, Å. B. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2010.11.017 · Cited by 135 · see citing works
Selective Autophagy: Talking with the UPS
Park, C., & Cuervo, A. M. (2013) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-013-9623-7 · Cited by 111 · see citing works
Self-citationProtein Homeostasis as a Therapeutic Target for Diseases of Protein Conformation
Calamini, B., & Morimoto, R. I. (2013) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026611212220014 · Cited by 91 · see citing works
Self-citationTargeting unfolded protein response signaling pathways to ameliorate protein misfolding diseases
Ryno, L. M., Wiseman, R. L., & Kelly, J. W. (2013) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2013.04.009 · Cited by 75 · see citing works
XIAP as a prognostic marker of early recurrence of nonmuscular invasive bladder cancer
Li, M., Song, T., Yin, Z.-F., & Na, Y.-Q. (2007) · Chinese Medical Journal · doi:10.1097/00029330-200703020-00007 · Cited by 59 · see citing works
Mitochondrial Therapeutics for Cardioprotection
Carreira, R., Lee, P. P. W., & Gottlieb, R. A. (2011) · Current Pharmaceutical Design · doi:10.2174/138161211796904777 · Cited by 47 · see citing works
Transcellular chaperone signaling: an organismal strategy for integrated cell stress responses
van Oosten‐Hawle, P., & Morimoto, R. I. (2013) · Journal of Experimental Biology · doi:10.1242/jeb.091249 · Cited by 47 · see citing works
Self-citationNew insights into the role of the ubiquitin-proteasome pathway in the regulation of apoptosis.
Liu, C., Goldberg, A. L., & Qiu, X. (2007) · PubMed · Cited by 38 · see citing works
Unfolded protein responses in bacteria and mitochondria: A central role for the ClpXP machine
Truscott, K. N., Bezawork‐Geleta, A., & Dougan, D. A. (2011) · IUBMB Life · doi:10.1002/iub.526 · Cited by 38 · see citing works
The life of proteins: the good, the mostly good and the ugly
Morimoto, R., Driessen, A., Hegde, R., & Langer, T. (2011) · Nature Structural &Molecular Biology · doi:10.1038/nsmb0111-1 · Cited by 28 · see citing works
Self-citationTreating the Periphery to Ameliorate Neurodegenerative Diseases
Reinhart, P. H., & Kelly, J. W. (2011) · Cell · doi:10.1016/j.cell.2011.05.031 · Cited by 13 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Tau in physiology and pathology
Wang, Y., & Mandelkow, E. (2016) · Nature Reviews Neuroscience · doi:10.1038/nrn.2015.1 · Cited by 2,251 · see citing works
Nrf2 and Oxidative Stress: A General Overview of Mechanisms and Implications in Human Disease
Ngo, V., & Duennwald, M. L. (2022) · Antioxidants · doi:10.3390/antiox11122345 · Cited by 1,130 · see citing works
Kaushik, S., & Cuervo, A. M. (2015) · Nature Medicine · doi:10.1038/nm.4001 · Cited by 899 · see citing works
Self-citationMeasuring biological aging in humans: a quest
Ferrucci, L., Gonzalez‐Freire, M., Fabbri, E., Simonsick, E., Tanaka, T., Moore, Z., Salimi, S., Sierra, F., & de Cabo, R. (2020) · Aging Cell · doi:10.1111/acel.13080 · Cited by 781 · see citing works
The aging lung: Physiology, disease, and immunity
Schneider, J. L., Rowe, J. H., Garcia-de-Alba, C., Kim, C. F., Sharpe, A. H., & Haigis, M. C. (2021) · Cell · doi:10.1016/j.cell.2021.03.005 · Cited by 500 · see citing works
Brundel, B. J. J. M., Ai, X., Hills, M. T., Kuipers, M. F., Lip, G. Y. H., & de Groot, N. M. S. (2022) · Nature Reviews Disease Primers · doi:10.1038/s41572-022-00347-9 · Cited by 528 · see citing works
Chaperone-mediated autophagy prevents collapse of the neuronal metastable proteome
Bourdenx, M., Martín-Segura, A., Scrivo, A., Rodriguez-Navarro, J. A., Kaushik, S., Tasset, I., Diaz, A., Storm, N. J., Xin, Q., Juste, Y. R., et al. (2021) · Cell · doi:10.1016/j.cell.2021.03.048 · Cited by 337 · see citing works
Self-citationAging Hallmarks and Progression and Age-Related Diseases: A Landscape View of Research Advancement
Tenchov, R., Sasso, J. M., Wang, X., & Zhou, Q. A. (2024) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.3c00531 · Cited by 276 · see citing works
Interplay of pathogenic forms of human tau with different autophagic pathways
Caballero, B., Wang, Y., Diaz, A., Tasset, I., Juste, Y. R., Stiller, B., Mandelkow, E., Mandelkow, E., & Cuervo, A. M. (2018) · Aging Cell · doi:10.1111/acel.12692 · Cited by 213 · see citing works
Self-citationThe Ubiquitin–Proteasome System in Immune Cells
Çetin, G., Klafack, S., Studencka‐Turski, M., Krüger, E., & Ebstein, F. (2021) · Biomolecules · doi:10.3390/biom11010060 · Cited by 210 · see citing works
ER stress and impaired autophagy flux in neuronal degeneration and brain injury
Yin, Y., Sun, G., Li, E., Kiselyov, K. I., & Sun, D. (2016) · Ageing Research Reviews · doi:10.1016/j.arr.2016.08.008 · Cited by 212 · see citing works
Sierra, F. (2016) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a025163 · Cited by 213 · see citing works
The relationship of autophagy defects to cartilage damage during joint aging in a mouse model
Caramés, B., Olmer, M., Kiosses, W. B., & Lotz, M. K. (2015) · Arthritis & Rheumatology · doi:10.1002/art.39073 · Cited by 204 · see citing works
Proteostasis in cardiac health and disease
Henning, R. H., & Brundel, B. J. J. M. (2017) · Nature Reviews Cardiology · doi:10.1038/nrcardio.2017.89 · Cited by 193 · see citing works
Inflammaging and Cancer: A Challenge for the Mediterranean Diet
Ostan, R., Lanzarini, C., Pini, E., Scurti, M., Vianello, D., Bertarelli, C., Fabbri, C., Izzi, M., Palmas, M. G., Biondi, F., et al. (2015) · Nutrients · doi:10.3390/nu7042589 · Cited by 194 · see citing works
Sirtuins at the crossroads of stemness, aging, and cancer
O'Callaghan, C., & Vassilopoulos, A. (2017) · Aging Cell · doi:10.1111/acel.12685 · Cited by 187 · see citing works
Age-related macular degeneration: A two-level model hypothesis
Rozing, M. P., Durhuus, J. A., Nielsen, M. K., Subhi, Y., Kirkwood, T. B. L., Westendorp, R. G., & Sørensen, T. L. (2019) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2019.100825 · Cited by 183 · see citing works
Heat shock proteins in neurodegenerative disorders and aging
Leak, R. K. (2014) · Journal of Cell Communication and Signaling · doi:10.1007/s12079-014-0243-9 · Cited by 170 · see citing works
Blue Journal Conference. Aging and Susceptibility to Lung Disease
Thannickal, V. J., Murthy, M., Balch, W. E., Chandel, N. S., Meiners, S., Eickelberg, O., Selman, M., Pardo, A., White, E. S., Levy, B. D., et al. (2015) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.201410-1876pp · Cited by 164 · see citing works
Long-Term Calorie Restriction Enhances Cellular Quality-Control Processes in Human Skeletal Muscle
Yang, L., Licastro, D., Cava, E., Veronese, N., Spelta, F., Rizza, W., Bertozzi, B., Villareal, D. T., Hotamışlıgil, G. S., Holloszy, J. O., et al. (2016) · Cell Reports · doi:10.1016/j.celrep.2015.12.042 · Cited by 167 · see citing works
Nekrasov, E. D., Vigont, V. A., Klyushnikov, S. A., Lebedeva, O. S., Vassina, E. M., Bogomazova, A. N., Chestkov, I. V., Semashko, T. A., Владимировна, К. Е., Suldina, L. A., et al. (2016) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0092-5 · Cited by 156 · see citing works
Martinez, B., Petersen, D., Gaeta, A. L., Stanley, S. P., Caldwell, G. A., & Caldwell, K. A. (2017) · Journal of Neuroscience · doi:10.1523/jneurosci.1294-17.2017 · Cited by 146 · see citing works
Circulating Proteomic Signatures of Chronological Age
Menni, C., Kiddle, S. J., Mangino, M., Viñuela, A., Psatha, M., Steves, C., Sattlecker, M., Buil, A., Newhouse, S., Nelson, S., et al. (2015) · The Journals of Gerontology: Series A · doi:10.1093/gerona/glu121 · Cited by 144 · see citing works
Heat shock proteins and hormesis in the diagnosis and treatment of neurodegenerative diseases
Dattilo, S., Mancuso, C., Koverech, G., Mauro, P. D., Ontario, M. L., Petralia, C. C. T., Petralia, A., Maiolino, L., Serra, A., Calabrese, E. J., et al. (2015) · Immunity & Ageing · doi:10.1186/s12979-015-0046-8 · Cited by 140 · see citing works
Impaired proteostasis during skeletal muscle aging
Fernando, R., Drescher, C., Nowotny, K., Grune, T., & Castro, J. P. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.08.037 · Cited by 134 · see citing works
Sirtuins and FoxOs in osteoporosis and osteoarthritis
Almeida, M., & Porter, R. M. (2019) · Bone · doi:10.1016/j.bone.2019.01.018 · Cited by 129 · see citing works
Multifaceted deregulation of gene expression and protein synthesis with age
Anisimova, A. S., Meerson, M., Gerashchenko, M. V., Kulakovskiy, I. V., Dmitriev, S. E., & Gladyshev, V. N. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2001788117 · Cited by 131 · see citing works
Restricted access: spatial sequestration of damaged proteins during stress and aging
Hill, S. M., Hanzén, S., & Nyström, T. (2017) · EMBO Reports · doi:10.15252/embr.201643458 · Cited by 115 · see citing works
Exogenous Hsp70 delays senescence and improves cognitive function in aging mice
Bobkova, N. V., Evgen’ev, M., Garbuz, D. G., Kulikov, A. M., Morozov, A., Samokhin, A., Velmeshev, D., Medvinskaya, N., Nesterova, I., Pollock, A., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1516131112 · Cited by 118 · see citing works
Editorial: The HSP70 Molecular Chaperone Machines
Goloubinoff, P. (2017) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2017.00001 · Cited by 104 · see citing works
Natural Compounds and Autophagy: Allies Against Neurodegeneration
Stacchiotti, A., & Corsetti, G. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.555409 · Cited by 105 · see citing works
Bustamante, H. A., González, A., Cerda‐Troncoso, C., Shaughnessy, R., Carola Otth, L., Soza, A., & Burgos, P. V. (2018) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2018.00126 · Cited by 98 · see citing works
Frailty biomarkers in humans and rodents: Current approaches and future advances
Kane, A. E., & Sinclair, D. A. (2019) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2019.03.007 · Cited by 101 · see citing works
Unfolded protein response IRE1/XBP1 signaling is required for healthy mammalian brain aging
Cabral-Miranda, F., Tamburini, G., Martínez, G., Ardiles, Á. O., Medinas, D. B., Gerakis, Y., Hung, M., Vidal, R. L., Fuentealba, M., Miedema, T., et al. (2022) · EMBO Journal · doi:10.15252/embj.2022111952 · Cited by 80 · see citing works
A farnesyltransferase inhibitor activates lysosomes and reduces tau pathology in mice with tauopathy
Hernández, I., Luna, G., Rauch, J. N., Reis, S. A., Giroux, M., Karch, C. M. M., Boctor, D., Sibih, Y., Storm, N. J., Díaz, A., et al. (2019) · Science Translational Medicine · doi:10.1126/scitranslmed.aat3005 · Cited by 95 · see citing works
Self-citationTranslation elongation rate varies among organs and decreases with age
Gerashchenko, M. V., Péterfi, Z., Yim, S. H., & Gladyshev, V. N. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa1103 · Cited by 95 · see citing works
Extensive accumulation of misfolded protein aggregates during natural aging and senescence
Cuanalo-Contreras, K., Schulz, J., Mukherjee, A., Park, K.-W., Armijo, E., & Soto, C. (2023) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.1090109 · Cited by 92 · see citing works
Pride, H., Yu, Z., Sunchu, B., Mochnick, J., Coles, A., Zhang, Y., Buffenstein, R., Hornsby, P. J., Austad, S. N., & Pérez, V. (2015) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2015.01.046 · Cited by 91 · see citing works
Proteomics and metabolomics in ageing research: from biomarkers to systems biology
Hoffman, J. M., Lyu, Y., Pletcher, S. D., & Promislow, D. (2017) · Essays in Biochemistry · doi:10.1042/ebc20160083 · Cited by 90 · see citing works
Interventions for age-related diseases: Shifting the paradigm
Figueira, I., Fernandes, A. M. A., Mladenović, A., Lopez-Contreras, A. J., Henriques, C. M., Selman, C., Ferreiro, E. B., Gonos, E. S., Trejo, J. L., Misra, J., et al. (2016) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2016.09.009 · Cited by 87 · see citing works
ER Stress Response in Human Cellular Models of Senescence
Matos, L., Gouveia, A., & Almeida, H. (2014) · The Journals of Gerontology Series A · doi:10.1093/gerona/glu129 · Cited by 88 · see citing works
Tauopathies: Deciphering Disease Mechanisms to Develop Effective Therapies
Silva, M. C., & Haggarty, S. J. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21238948 · Cited by 87 · see citing works
Differentiation Drives Widespread Rewiring of the Neural Stem Cell Chaperone Network
Vonk, W. I. M., Rainbolt, T. K., Dolan, P. T., Webb, A. E., Brunet, A., & Frydman, J. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.03.009 · Cited by 84 · see citing works
A distinct astrocyte subtype in the aging mouse brain characterized by impaired protein homeostasis
Lee, E., Jung, Y., Park, Y. R., Lim, S., Choi, Y.-J., Lee, S. Y., Kim, C. H., Mun, J. Y., & Chung, W. (2022) · Nature Aging · doi:10.1038/s43587-022-00257-1 · Cited by 85 · see citing works
Influence of the Mediterranean Diet on Healthy Aging
Andreo-López, M. C., Contreras-Bolívar, V., Muñoz‐Torres, M., García-Fontana, B., & García‐Fontana, C. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24054491 · Cited by 86 · see citing works
The Amazing Ubiquitin-Proteasome System: Structural Components and Implication in Aging
Tsakiri, E. N., & Trougakos, I. P. (2014) · International review of cytology · doi:10.1016/bs.ircmb.2014.09.002 · Cited by 78 · see citing works
Αlpha-Synuclein as a Mediator in the Interplay between Aging and Parkinson’s Disease
Bobela, W., Aebischer, P., & Schneider, B. L. (2015) · Biomolecules · doi:10.3390/biom5042675 · Cited by 75 · see citing works
Ayyadevara, S., Balasubramaniam, M., Parcon, P. A., Barger, S. W., Griffin, W. S. T., Alla, R., Tackett, A. J., Mackintosh, S. G., Petricoin, E. F., Zhou, W., et al. (2016) · Aging Cell · doi:10.1111/acel.12501 · Cited by 76 · see citing works
Cavinato, M. S., Kozieł, R., Romani, N., Weinmüllner, R., Jenewein, B., Hermann, M., Dubrac, S., Ratzinger, G., Grillari, J., Schmuth, M., et al. (2016) · The Journals of Gerontology Series A · doi:10.1093/gerona/glw150 · Cited by 76 · see citing works
Coping with Protein Quality Control Failure
Pilla, E., Schneider, K., & Bertolotti, A. (2017) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-111315-125334 · Cited by 72 · see citing works
The Aging Thyroid: A Reappraisal Within the Geroscience Integrated Perspective
Franceschi, C., Ostan, R., Mariotti, S., Monti, D., & Vitale, G. (2019) · Endocrine Reviews · doi:10.1210/er.2018-00170 · Cited by 72 · see citing works
Aging Fits the Disease Criteria of the International Classification of Diseases
Khaltourina, D. A., Matveyev, Y., Alekseev, A., Cortese, F., & Ioviţă, A. (2020) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2020.111230 · Cited by 71 · see citing works
The Spectrum of Fundamental Basic Science Discoveries Contributing to Organismal Aging
Farr, J. N., & Almeida, M. (2018) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.3564 · Cited by 69 · see citing works
Small heat-shock proteins and their role in mechanical stress
Collier, M. P., & Benesch, J. L. P. (2020) · Cell Stress and Chaperones · doi:10.1007/s12192-020-01095-z · Cited by 65 · see citing works
Unraveling the Role of Heme in Neurodegeneration
Chiabrando, D., Fiorito, V., Petrillo, S., & Tolosano, E. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00712 · Cited by 65 · see citing works
Too sweet: Problems of protein glycation in the eye
Bejarano, E., & Taylor, A. (2018) · Experimental Eye Research · doi:10.1016/j.exer.2018.08.017 · Cited by 64 · see citing works
Global and tissue-specific aging effects on murine proteomes
Keele, G. R., Zhang, J., Szpyt, J., Korstanje, R., Gygi, S. P., Churchill, G. A., & Schweppe, D. K. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112715 · Cited by 63 · see citing works
Activation-Induced Autophagy Is Preserved in CD4+ T-Cells in Familial Longevity
Raz, Y., Guerrero‐Ros, I., Maier, A. B., Slagboom, P. E., Atzmon, G., Barzilai, N., & Macián, F. (2017) · The Journals of Gerontology Series A · doi:10.1093/gerona/glx020 · Cited by 63 · see citing works
Mitochondria and α-Synuclein: Friends or Foes in the Pathogenesis of Parkinson’s Disease?
Faustini, G., Bono, F., Valerio, A., Pizzi, M., Spano, P., & Bellucci, A. (2017) · Genes · doi:10.3390/genes8120377 · Cited by 63 · see citing works
Hark, T. J., Rao, N. R., Castillon, C., Basta, T., Smukowski, S. N., Bao, H., Upadhyay, A., Bomba-Warczak, E. K., Nomura, T., O'Toole, E. T., et al. (2020) · Cell Systems · doi:10.1016/j.cels.2020.11.007 · Cited by 59 · see citing works
Sklirou, A. D., Gaboriaud‐Kolar, N., Papassideri, I. S., Skaltsounis, A., & Trougakos, I. P. (2017) · Scientific Reports · doi:10.1038/s41598-017-11662-7 · Cited by 61 · see citing works
Aging, Metabolism, and Cancer Development: from Peto’s Paradox to the Warburg Effect
Tidwell, T., Søreide, K., & Hagland, H. R. (2017) · Aging and Disease · doi:10.14336/ad.2017.0713 · Cited by 63 · see citing works
Surviving protein quality control catastrophes – from cells to organisms
Schneider, K., & Bertolotti, A. (2015) · Journal of Cell Science · doi:10.1242/jcs.173047 · Cited by 57 · see citing works
New considerations on hormetic response against oxidative stress
Luna-López, A., González-Puertos, V. Y., López-Díazguerrero, N., & Königsberg, M. (2014) · Journal of cell communication and signaling · doi:10.1007/s12079-014-0248-4 · Cited by 52 · see citing works
Emanuele, E., Minoretti, P., Sanchis‐Gomar, F., Pareja-Galeano, H., Yilmaz, Y. N., Garatachea, N., & Lucía, A. (2014) · Rejuvenation Research · doi:10.1089/rej.2014.1607 · Cited by 56 · see citing works
Stem Cell Aging in Lifespan and Disease: A State-of-the-Art Review
Sameri, S., Samadi, P., Dehghan, R., Salem, E., Hosseini, N. F., & Amini, R. (2020) · Current Stem Cell Research & Therapy · doi:10.2174/1574888x15666200213105155 · Cited by 55 · see citing works
A new model to investigate UVB-induced cellular senescence and pigmentation in melanocytes
Martic, I., Wedel, S., Jansen‐Dürr, P., & Cavinato, M. S. (2020) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2020.111322 · Cited by 55 · see citing works
Heat Shock Proteins and Ferroptosis
Liu, Y., Zhou, L., Xu, Y., Li, K., Zhao, Y., Qiao, H., Xu, Q., & Zhao, J. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.864635 · Cited by 55 · see citing works
Preparing for an Aging World: Engaging Biogerontologists, Geriatricians, and the Society
Nikolich‐Žugich, J., Goldman, D. P., Cohen, P. R., Cortese, D. A., Fontana, L., Kennedy, B. K., Mohler, M. J., Olshansky, S. J., Perls, T. T., Perry, D. P., et al. (2015) · The Journals of Gerontology Series A · doi:10.1093/gerona/glv164 · Cited by 54 · see citing works
Rodriguez‐Fernandez, I. A., Qi, Y., & Jasper, H. (2019) · Nature Communications · doi:10.1038/s41467-019-08982-9 · Cited by 53 · see citing works
Kevei, É., Pokrzywa, W., & Hoppe, T. (2017) · FEBS Letters · doi:10.1002/1873-3468.12750 · Cited by 52 · see citing works
Mechanisms of protein balance in skeletal muscle
Anthony, T. G. (2016) · Domestic Animal Endocrinology · doi:10.1016/j.domaniend.2016.02.012 · Cited by 57 · see citing works
The Autophagy-Lysosomal Pathways and Their Emerging Roles in Modulating Proteostasis in Tumors
Dong, Z., & Cui, H. (2018) · Cells · doi:10.3390/cells8010004 · Cited by 50 · see citing works
Ahmad, A., Uversky, V. N., & Khan, R. H. (2022) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2022.08.132 · Cited by 52 · see citing works
Terracina, S. A., Petrella, C., Francati, S., Lucarelli, M., Barbato, C., Minni, A., Ralli, M., Greco, A., Tarani, L., Fiore, M., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232415674 · Cited by 50 · see citing works
Tan, L. P., Register, T. C., & Yammani, R. R. (2020) · Aging and Disease · doi:10.14336/ad.2019.1130 · Cited by 47 · see citing works
Emerging potential of cannabidiol in reversing proteinopathies
Dash, R., Ali, M. C., Jahan, I., Munni, Y. A., Mitra, S., Hannan, M. A., Timalsina, B., Oktaviani, D. F., Choi, H. J., & Moon, I. S. (2020) · Ageing Research Reviews · doi:10.1016/j.arr.2020.101209 · Cited by 49 · see citing works
Protein homeostasis in aging and cancer
Chen, X., Shen, T., Fang, S.-J., Sun, X.-M., Li, G., & Li, Y. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1143532 · Cited by 47 · see citing works
Evgen’ev, M. B., Krasnov, G. S., Nesterova, I. V., Garbuz, D. G., Карпов, В. Л., Morozov, A. V., Snezhkina, A. V., Samokhin, A. N., Sergeev, A., Куликов, А. М., et al. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170398 · Cited by 45 · see citing works
Proteostasis disruption and senescence in Alzheimer’s disease pathways to neurodegeneration
Thapa, R., Bhat, A. A., Shahwan, M. J., Ali, H., Padmapriya, G., Bansal, P., Rajotiya, S., Barwal, A., Prasad, G. V. S., Pramanik, A., et al. (2024) · Brain Research · doi:10.1016/j.brainres.2024.149202 · Cited by 44 · see citing works
Glioblastoma: Targeting the autophagy in tumorigenesis
Yang, K., Niu, L., Bai, Y., & Le, W. (2019) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2019.09.012 · Cited by 44 · see citing works
Causal Relationships Between Glycemic Traits and Myopia
Li, F., Zhu, M., Shao, Y., Lü, F., Yi, Q., & Huang, X. (2023) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.64.3.7 · Cited by 43 · see citing works
Sir2 links the unfolded protein response and the heat shock response in a stress response network
Weindling, E., & Bar‐Nun, S. (2015) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2015.01.021 · Cited by 43 · see citing works
Proteome Stability as a Key Factor of Genome Integrity
Gumeni, S., Evangelakou, Z., Gorgoulis, V. G., & Trougakos, I. P. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18102036 · Cited by 41 · see citing works
Kenche, H., Ye, Z., Vedagiri, K., Richards, D. M., Gao, X., Tew, K. D., Townsend, D. M., & Blumental‐Perry, A. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.712331 · Cited by 40 · see citing works
Proteasome mapping reveals sexual dimorphism in tissue‐specific sensitivity to protein aggregations
Jenkins, E. C., Shah, N., Gomez-Jenkins, M., Casalena, G., Zhao, D., Kenny, T. C., Guariglia, S. R., Manfredi, G., & Germain, D. (2020) · EMBO Reports · doi:10.15252/embr.201948978 · Cited by 40 · see citing works
Ageing, Age-Related Cardiovascular Risk and the Beneficial Role of Natural Components Intake
Rysz, J., Franczyk, B., Rysz-Górzyńska, M., & Gluba-Brzózka, A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms23010183 · Cited by 41 · see citing works
Urbán, V. S., Ceglédi, A., & Mikala, G. (2022) · GeroScience · doi:10.1007/s11357-022-00698-x · Cited by 40 · see citing works
The Effect of Polyphenols on Protein Degradation Pathways: Implications for Neuroprotection
Hajieva, P. (2017) · Molecules · doi:10.3390/molecules22010159 · Cited by 39 · see citing works
Franco, M. L., Melero, C., Sarasola, E., Acebo, P., Luque, A., Calatayud-Baselga, I., García‐Barcina, M., & Vilar, M. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.722587 · Cited by 37 · see citing works
Targeting Protein Quality Control Mechanisms by Natural Products to Promote Healthy Ageing
Wedel, S., Manola, M. S., Cavinato, M. S., Trougakos, I. P., & Jansen‐Dürr, P. (2018) · Molecules · doi:10.3390/molecules23051219 · Cited by 39 · see citing works
The 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
Prion Properties of SOD1 in Amyotrophic Lateral Sclerosis and Potential TherapyPreprint
Sibilla, C., & Bertolotti, A. (2017) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a024141 · Cited by 37 · see citing works
DEGRONOPEDIA: a web server for proteome-wide inspection of degrons
Szulc, N. A., Stefaniak, F., Piechota, M., Soszyńska, A., Piórkowska, G., Cappannini, A., Bujnicki, J. M., Maniaci, C., & Pokrzywa, W. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae238 · Cited by 35 · see citing works
Hexapeptide-11 is a novel modulator of the proteostasis network in human diploid fibroblasts
Sklirou, A. D., Ralli, M., Dominguez, M., Papassideri, I. S., Skaltsounis, A., & Trougakos, I. P. (2015) · Redox Biology · doi:10.1016/j.redox.2015.04.010 · Cited by 35 · see citing works
Role of cellular senescence in inflammatory lung diseases
Xie, C. H., Yalikun, M., Luo, Q., & Dong, J. (2023) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2023.02.001 · Cited by 31 · see citing works
Derailed protein turnover in the aging mammalian brain
Rao, N. R., Upadhyay, A., & Savas, J. N. (2024) · Molecular Systems Biology · doi:10.1038/s44320-023-00009-2 · Cited by 30 · see citing works
Genetics and Pharmacology of Longevity
Castillo-Quan, J. I., Kinghorn, K. J., & Bjedov, I. (2015) · Advances in genetics · doi:10.1016/bs.adgen.2015.06.002 · Cited by 37 · see citing works
Cullin-3–RING ubiquitin ligase activity is required for striated muscle function in mice
Papizan, J. B., Vidal, A., Bezprozvannaya, S., Bassel‐Duby, R., & Olson, E. N. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.002104 · Cited by 34 · see citing works
Essential 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
- Authors
- Morimoto, R. I., & Cuervo, A. M.
- Affiliations
- Northwestern University (US)
- Albert Einstein College of Medicine (US)
- Venue
- The Journals of Gerontology Series A: Biological Sciences and Medical Sciences
- Publisher
- Oxford University Press (OUP)
- Published
- 2014-05-14
- Volume
- 69
- Issue
- Suppl 1
- Pages
- S33-S38
- ISSN
- 1079-5006 (ISSN-L)
- 1758-535X
- PMC
- PMC4022129
- OpenAlex
- W2136597136
- Cited by
- 277
- References
- 33
- Citations by year
- 2026: 15 · 2025: 19 · 2024: 14 · 2023: 24 · 2022: 19 · 2021: 25 · 2020: 24 · 2019: 26 · 2018: 25 · 2017: 30 · 2016: 20 · 2015: 26 · 2014: 9
- FWCI
- 11.62
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- The Journals of Gerontology Series A (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Institute on Aging (AG 026647, P01AG031782, AG031782, AG21904)
- National Institute of General Medical Sciences (GM081192, GM 038109)
- National Institute of Diabetes and Digestive and Kidney Diseases (DK090408)
- National Institute of Neurological Disorders and Stroke (NS038370, NS-047331, P50NS038370, R01NS047331)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- 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
- Keywords
- proteostasis, molecular chaperones, protein misfolding, protein aggregates, age-related diseases, degenerative diseases, healthspan, stress signaling pathways
- MeSH terms
- Aging, Chronic Disease, Homeostasis, Humans, Signal Transduction, Protein Folding, Molecular Chaperones, Proteome
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