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Proteostasis and the Aging Proteome in Health and Disease
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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 [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
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
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 1,195
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 992
Autophagy gone awry in neurodegenerative diseases
Wong, E., & Cuervo, A. M. (2010) · Nature Neuroscience · doi:10.1038/nn.2575 · Cited by 815
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 636
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
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 515
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
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
Research works printed but not linked: 3
- 2012, Current topics in medicinal chemistry, 12, 2623
- 2009, The Journals of Gerontology Series A: Biological Sciences and Medical Sciences, 64, 167
- 2013, Biochimica et Biophysica Acta. Protein Structure and Molecular Enzymology, 1833, 410
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Tau in physiology and pathology
Wang, Y., & Mandelkow, E. (2016) · Nature Reviews Neuroscience · doi:10.1038/nrn.2015.1 · Cited by 2,251
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
Kaushik, S., & Cuervo, A. M. (2015) · Nature Medicine · doi:10.1038/nm.4001 · Cited by 899
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
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
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 545
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
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
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
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 215
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 218
Sierra, F. (2016) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a025163 · Cited by 226
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
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
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 198
Sirtuins at the crossroads of stemness, aging, and cancer
O'Callaghan, C., & Vassilopoulos, A. (2017) · Aging Cell · doi:10.1111/acel.12685 · Cited by 191
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 188
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 175
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
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 174
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 160
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 144
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
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
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
Sirtuins and FoxOs in osteoporosis and osteoarthritis
Almeida, M., & Porter, R. M. (2019) · Bone · doi:10.1016/j.bone.2019.01.018 · Cited by 131
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 134
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 117
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
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Stacchiotti, A., & Corsetti, G. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.555409 · Cited by 106
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 102
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
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.-L. D., Vidal, R. L., Fuentealba, M., Miedema, T., et al. (2022) · The EMBO Journal · doi:10.15252/embj.2022111952 · Cited by 99
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
Self-citationTranslation elongation rate varies among organs and decreases with age
Gerashchenko, M. V., Peterfi, Z., Yim, S. H., & Gladyshev, V. N. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkaa1103 · Cited by 98
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
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
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
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 92
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 91
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
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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
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
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 93
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Tsakiri, E. N., & Trougakos, I. P. (2014) · International review of cytology · doi:10.1016/bs.ircmb.2014.09.002 · Cited by 80
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Bobela, W., Aebischer, P., & Schneider, B. L. (2015) · Biomolecules · doi:10.3390/biom5042675 · Cited by 75
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 77
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
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 75
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Franceschi, C., Ostan, R., Mariotti, S., Monti, D., & Vitale, G. (2019) · Endocrine Reviews · doi:10.1210/er.2018-00170 · Cited by 74
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 77
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Farr, J. N., & Almeida, M. (2018) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.3564 · Cited by 70
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
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Chiabrando, D., Fiorito, V., Petrillo, S., & Tolosano, E. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00712 · Cited by 68
Too sweet: Problems of protein glycation in the eye
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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 65
Activation-induced autophagy is preserved in CD4+ T-cells in familial longevity
Raz, Y., Guerrero-Ros, I., Maier, A., Slagboom, P. E., Atzmon, G., Barzilai, N., & Macian, F. (2017) · The Journals of Gerontology: Series A · doi:10.1093/gerona/glx020 · Cited by 61
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 66
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 60
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 62
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 64
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
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
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
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 57
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 61
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 58
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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 58
Rodriguez‐Fernandez, I. A., Qi, Y., & Jasper, H. (2019) · Nature Communications · doi:10.1038/s41467-019-08982-9 · Cited by 54
Kevei, É., Pokrzywa, W., & Hoppe, T. (2017) · FEBS Letters · doi:10.1002/1873-3468.12750 · Cited by 53
Mechanisms of protein balance in skeletal muscle
Anthony, T. G. (2016) · Domestic Animal Endocrinology · doi:10.1016/j.domaniend.2016.02.012 · Cited by 59
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
Ahmad, A., Uversky, V. N., & Khan, R. H. (2022) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2022.08.132 · Cited by 53
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 56
Tan, L. P., Register, T. C., & Yammani, R. R. (2020) · Aging and Disease · doi:10.14336/ad.2019.1130 · Cited by 48
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 50
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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 51
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
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 48
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 46
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
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
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 44
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
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Metadata
- 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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