Proteostasis and the Aging Proteome in Health and Disease

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

Protein 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

Endoplasmic 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

Cellular 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

Pharmacological 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

EDEM Function in ERAD Protects against Chronic ER Proteinopathy and Age-Related Physiological Decline in Drosophila

Sekiya, M., Akiko, M.-O., Hearn, S., Sakakibara, Y., Fujisaki, N., Suzuki, E., Ando, K., & Iijima, K. (2017) · Developmental Cell · doi:10.1016/j.devcel.2017.05.019 · Cited by 36

The Effect of Human HSP70 Administration on a Mouse Model of Alzheimer’s Disease Strongly Depends on Transgenicity and Age

Evgen’ev, M. B., Bobkova, N. V., Krasnov, G. S., Garbuz, D. G., Funikov, S. Y., Kudryavtseva, A. V., Куликов, А. М., Samokhin, A. N., Maltsev, A. V., & Nesterova, I. V. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-180987 · Cited by 33

Elamipretide (SS-31) treatment attenuates age-associated post-translational modifications of heart proteins

Whitson, J. D., Martín‐Pérez, M., Zhang, T., Gaffrey, M. J., Merrihew, G. E., Huang, E. L., White, C. C., Kavanagh, T. J., Qian, W., Campbell, M. D., et al. (2021) · GeroScience · doi:10.1007/s11357-021-00447-6 · Cited by 30

The Social Amoeba Dictyostelium discoideum Is Highly Resistant to Polyglutamine Aggregation

Santarriaga, S., Petersen, A. N., Ndukwe, K., Brandt, A. C., Gerges, N. Z., Scaglione, J. B., & Scaglione, K. M. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.676247 · Cited by 32

Natural compounds in the regulation of proteostatic pathways: An invincible artillery against stress, ageing, and diseases

Upadhyay, A. (2021) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2021.01.006 · Cited by 31

Selective fluorescent labeling of cellular proteins and its biological applications

Choi, J. H., Kim, S., Kang, O., Choi, S. Y., Hyun, J. Y., Lee, H. S., & Shin, I. (2024) · Chemical Society Reviews · doi:10.1039/d4cs00094c · Cited by 33

Bushen-Yizhi formula ameliorates cognitive dysfunction through SIRT1/ER stress pathway in SAMP8 mice

Zhang, S., Xu, T., Li, L., Xu, Y., Qu, Z.-L., Wang, X.-C., Huang, S., Luo, Y., Luo, N., Lü, P., et al. (2017) · Oncotarget · doi:10.18632/oncotarget.17638 · Cited by 32

Cancer chemoprevention via activation of proteostatic modules

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

Changes in proteome solubility indicate widespread proteostatic disruption in mouse models of neurodegenerative disease

Pace, M. C., Xu, G. M., Fromholt, S., Howard, J. C., Crosby, K. W., Giasson, B. I., Lewis, J. M., & Borchelt, D. (2018) · Acta Neuropathologica · doi:10.1007/s00401-018-1895-y · Cited by 31

Prevention of aberrant protein aggregation by anchoring the molecular chaperone αB-crystallin to the endoplasmic reticulum

Yamamoto, S., Yamashita, A., Arakaki, N., Nemoto, H., & Yamazaki, T. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.10.151 · Cited by 31

Protein carbonylation in dopaminergic cells exposed to rotenone

Chiaradia, E., Renzone, G., Scaloni, A., Caputo, M., Costanzi, E., Gambelunghe, A., Muzi, G., Avellini, L., Emiliani, C., & Buratta, S. (2019) · Toxicology Letters · doi:10.1016/j.toxlet.2019.04.002 · Cited by 30

Cellular Proteostasis During Influenza A Virus Infection—Friend or Foe?

Marques, M., Ramos, B., Soares, A. R., & Ribeiro, D. (2019) · Cells · doi:10.3390/cells8030228 · Cited by 30

Does proteostasis get lost in translation? Implications for protein aggregation across the lifespan

Francisco, S., Ferreira, M., Moura, G. R., Soares, A. R., & Santos, M. A. S. (2020) · Ageing Research Reviews · doi:10.1016/j.arr.2020.101119 · Cited by 31

Recombinant HSP70 and mild heat shock stimulate growth of aged mesenchymal stem cells

Andreeva, N. V., Zatsepina, O. G., Garbuz, D. G., Evgen’ev, M. B., & Belyavsky, A. V. (2016) · Cell Stress and Chaperones · doi:10.1007/s12192-016-0691-7 · Cited by 29

α-Synuclein Aggregated with Tau and β-Amyloid in Human Platelets from Healthy Subjects: Correlation with Physical Exercise

Daniele, S., Pietrobono, D., Fusi, J., Gerfo, A. L., Cerri, E., Chico, L., Iofrida, C., Petrozzi, L., Baldacci, F., Giacomelli, C., et al. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00017 · Cited by 28

Terrestrial Microorganisms: Cell Factories of Bioactive Molecules with Skin Protecting Applications

Peyrat, L., Tsafantakis, N., Georgousaki, K., Ouazzani, J., Genilloud, O., Trougakos, I. P., & Fokialakis, N. (2019) · Molecules · doi:10.3390/molecules24091836 · Cited by 31

Insights into the Conserved Regulatory Mechanisms of Human and Yeast Aging

Dahiya, R., Mohammad, T., Alajmi, M. F., Rehman, M. T., Hasan, G. M., Hussain, A., & Hassan, M. I. (2020) · Biomolecules · doi:10.3390/biom10060882 · Cited by 30

Potential roles of natural products in the targeting of proteinopathic neurodegenerative diseases

Dash, R., Jahan, I., Ali, M. C., Mitra, S., Munni, Y. A., Timalsina, B., Hannan, M. A., & Moon, I. S. (2021) · Neurochemistry International · doi:10.1016/j.neuint.2021.105011 · Cited by 28

Phytochemical Study and In Vitro Screening Focusing on the Anti-Aging Features of Various Plants of the Greek Flora

Sklirou, A. D., Angelopoulou, M. T., Argyropoulou, A., Chaita, E., Boka, V.-I., Cheimonidi, C., Niforou, K., Mavrogonatou, E., Pratsinis, H., Kalpoutzakis, E., et al. (2021) · Antioxidants · doi:10.3390/antiox10081206 · Cited by 29

Reviving the protein quality control system: Therapeutic target for cardiac disease in the elderly

Meijering, R. A. M., Henning, R. H., & Brundel, B. J. J. M. (2014) · Trends in Cardiovascular Medicine · doi:10.1016/j.tcm.2014.10.013 · Cited by 27

Yeast at the Forefront of Research on Ageing and Age-Related Diseases

Sampaio‐Marques, B., Burhans, W. C., & Ludovico, P. (2019) · Progress in molecular and subcellular biology · doi:10.1007/978-3-030-13035-0_9 · Cited by 28

Lipids and the hallmarks of ageing: From pathology to interventions

Sharma, R., & Diwan, B. (2023) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2023.111858 · Cited by 31

Crosstalk Between Chaperone-Mediated Protein Disaggregation and Proteolytic Pathways in Aging and Disease

Feleciano, D. R., Juenemann, K., Iburg, M., Brás, I. C., Holmberg, C. I., & Kirstein, J. (2019) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2019.00009 · Cited by 27

Influence of Subcellular Localization and Functional State on Protein Turnover

Yousefi, R., Jevdokimenko, K., Kluever, V., Pacheu‐Grau, D., & Fornasiero, E. F. (2021) · Cells · doi:10.3390/cells10071747 · Cited by 27

Redefining the Scope of Targeted Protein Degradation: Translational Opportunities in Hijacking the Autophagy–Lysosome Pathway

Cassidy, K. B., & Zhao, H. (2021) · Biochemistry · doi:10.1021/acs.biochem.1c00330 · Cited by 25

Assessment of Sacsin Turnover in Patients With ARSACS

Longo, F., Ritis, D. D., Miluzio, A., Fraticelli, D., Baets, J., Scarlato, M., Santorelli, F. M., Biffo, S., & Maltecca, F. (2021) · Neurology · doi:10.1212/wnl.0000000000012962 · Cited by 25

Ketogenic diet administration later in life improves memory by modifying the synaptic cortical proteome via the PKA signaling pathway in aging mice

Acuña-Catalán, D., Shah, S., Wehrfritz, C., Nomura, M., Acevedo, A., Olmos, C., Quiroz, G., Huerta, H., Bons, J., Ampuero, E., et al. (2024) · Cell Reports Medicine · doi:10.1016/j.xcrm.2024.101593 · Cited by 29

Regulatory Roles of miRNAs in Aging

Caravia, X. M., & López-Otı́n, C. (2015) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-22380-3_11 · Cited by 27

Defective proteostasis in induced pluripotent stem cell models of frontotemporal lobar degeneration

Mahali, S., Martinez, R., King, M., Verbeck, A., Harari, O., Benitez, B. A., Horie, K., Sato, C., Temple, S., & Karch, C. M. (2022) · Translational Psychiatry · doi:10.1038/s41398-022-02274-5 · Cited by 33

ALDH2 protects naturally aged mouse retina via inhibiting oxidative stress-related apoptosis and enhancing unfolded protein response in endoplasmic reticulum

Long, P., He, M., Yan, W., Chen, W., Wei, D., Wang, S., Zhang, Z., Ge, W., & Chen, T. (2020) · Aging · doi:10.18632/aging.202325 · Cited by 24

Restoration of LAMP2A expression in old mice leads to changes in the T cell compartment that support improved immune function

Reynolds, C. A., Pelka, S., Gjergjova, F., Tasset, I., Khawaja, R. R., Lindenau, K. L., Krause, G. J., Gavathiotis, E., Cuervo, A. M., & Macián, F. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2322929121 · Cited by 25

Natural Products as Modulators of the Proteostasis Machinery: Implications in Neurodegenerative Diseases

Cuanalo-Contreras, K., & Moreno‐González, I. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20194666 · Cited by 26

Schwann cells ER-associated degradation contributes to myelin maintenance in adult nerves and limits demyelination in CMT1B mice

Volpi, V. G., Ferri, C., Fregno, I., Carro, U. D., Bianchi, F., Scapin, C., Pettinato, E., Soldà, T., Feltri, M. L., Molinari, M., et al. (2019) · PLoS Genetics · doi:10.1371/journal.pgen.1008069 · Cited by 22

How Research on Human Progeroid and Antigeroid Syndromes Can Contribute to the Longevity Dividend InitiativePreprint

Hisama, F. M., Oshima, J., & Martin, G. M. (2016) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a025882 · Cited by 21

Neuroprotective properties of queen bee acid by autophagy induction

Martínez-Chacón, G., Paredes-Barquero, M., Yakhine-Diop, S. M. S., Uribe-Carretero, E., Bargiela, A., Sabater-Arcis, M., Morales-Garcia, J. A., Alarcón-Gil, J., Alegre-Cortés, E., Canales-Cortés, S., et al. (2021) · Cell Biology and Toxicology · doi:10.1007/s10565-021-09625-w · Cited by 22

Concurrent Evolution of Antiaging Gene Duplications and Cellular Phenotypes in Long-Lived Turtles

Glaberman, S. R., Bulls, S. E., Vázquez, J. M., Chiari, Y., & Lynch, V. J. (2021) · Genome Biology and Evolution · doi:10.1093/gbe/evab244 · Cited by 22

The E262K mutation in Lamin A links nuclear proteostasis imbalance to laminopathy‐associated premature aging

Ghosh, D. K., Pande, S., Jeevan Kumar, M., Yesodharan, D., Nampoothiri, S., Radhakrishnan, P., Reddy, C. G., Ranjan, A., & Girisha, K. M. (2022) · Aging Cell · doi:10.1111/acel.13688 · Cited by 20

Critical role of lysosomes in the dysfunction of human Cardiac Stem Cells obtained from failing hearts

Gianfranceschi, G., Caragnano, A., Piazza, S., Manini, I., Ciani, Y., Verardo, R., Toffoletto, B., Finato, N., Livi, U., Beltrami, C. A., et al. (2016) · International Journal of Cardiology · doi:10.1016/j.ijcard.2016.04.155 · Cited by 22

Importance of the subcellular location of protein deposits in neurodegenerative diseases

Bertolotti, A. (2018) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2018.03.004 · Cited by 21

Impaired autophagic activity and ATG4B deficiency are associated with increased endoplasmic reticulum stress-induced lung injury

Maciel, M., Hernández-Barrientos, D., Herrera, I., Selman, M., Pardo, A., & Cabrera, S. (2018) · Aging · doi:10.18632/aging.101532 · Cited by 21

Human aldehyde dehydrogenase 3A1 (ALDH3A1) exhibits chaperone-like function

Voulgaridou, G.-P., Tsochantaridis, I., Mantso, T., Franco, R., Panayiotidis, M. I., & Pappa, A. (2017) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2017.05.017 · Cited by 20

Structural Determinant of β-Amyloid Formation: From Transmembrane Protein Dimerization to β-Amyloid Aggregates

Papadopoulos, N., Suelves, N., Perrin, F., Vadukul, D. M., Vrancx, C., Constantinescu, S. N., & Kienlen-Campard, P. (2022) · Biomedicines · doi:10.3390/biomedicines10112753 · Cited by 20

Modulation of Pancreatic Islets' Function and Survival During Aging Involves the Differential Regulation of Endoplasmic Reticulum Stress by p21 and CHOP

Mihailidou, C., Chatzistamou, I., Papavassiliou, A. G., & Kiaris, H. (2016) · Antioxidants and Redox Signaling · doi:10.1089/ars.2016.6671 · Cited by 22

Clinical implications of extracellular vesicles in neurodegenerative diseases

Vinaiphat, A., & Sze, S. K. (2019) · Expert Review of Molecular Diagnostics · doi:10.1080/14737159.2019.1657407 · Cited by 20

Characteristic Hallmarks of Aging and the Impact on Carcinogenesis

Fiore, M., Terracina, S. A., Ferraguti, G., Petrella, C., Bruno, S. M., Blaconà, G., Certo, M. G. D., Minni, A., Greco, A., Musacchio, A., et al. (2022) · Current Cancer Drug Targets · doi:10.2174/1568009622666220816120353 · Cited by 21

Improved resilience and proteostasis mediate longevity upon DAF-2 degradation in old age

Molière, A., Park, J. Y. C., Goyala, A., Vayndorf, E. M., Zhang, B., Hsiung, K. C., Jung, Y., Kwon, S., Statzer, C., Meyer, D. H., et al. (2024) · GeroScience · doi:10.1007/s11357-024-01232-x · Cited by 19

Down Syndrome, Ageing and Epigenetics

Gensous, N., Franceschi, C., Salvioli, S., Garagnani, P., & Bacalini, M. G. (2019) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-981-13-3681-2_7 · Cited by 19

Quantitative analysis of global protein stability rates in tissues

McClatchy, D. B., Martínez-Bartolomé, S., Gao, Y., Lavallée-Adam, M., & Yates, J. R. (2020) · Scientific Reports · doi:10.1038/s41598-020-72410-y · Cited by 19

Early Generation of New PrPSc on Blood Vessels after Brain Microinjection of Scrapie in Mice

Chesebro, B. W., Striebel, J. F., Rangel, A., Phillips, K. L., Hughson, A. G., Caughey, B. W., & Race, B. (2015) · mBio · doi:10.1128/mbio.01419-15 · Cited by 21

Inhibition of chaperone-mediated autophagy prevents glucotoxicity in the Caenorhabditis elegans mev-1 mutant by activation of the proteasome

Eisermann, D. J., Wenzel, U., & Fitzenberger, E. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2017.01.043 · Cited by 18

Comparison of the transcriptome in circulating leukocytes in early lactation between primiparous and multiparous cows provides evidence for age-related changes

Buggiotti, L., Cheng, Z., Salavati, M., Wathes, C., Fahey, A. G., Crisà, A., Fouladi, A., Wylie, A. R. G., Vanlierde, A., Fogh, A., et al. (2021) · BMC Genomics · doi:10.1186/s12864-021-07977-5 · Cited by 21

Two human metabolites rescue a C. elegans model of Alzheimer’s disease via a cytosolic unfolded protein response

Joshi, P., Perni, M., Limbocker, R., Mannini, B., Casford, S., Chia, S., Habchi, J., Labbadia, J. P., Dobson, C. M., & Vendruscolo, M. (2021) · Communications Biology · doi:10.1038/s42003-021-02218-7 · Cited by 17

HspB1 Overexpression Improves Life Span and Stress Resistance in an Invertebrate Model

Alexander, C. C., Munkácsy, E., Tillmon, H., Fraker, T. L., Scheirer, J. L., Holstein, D. M., Lozano, D., Khan, M. H., Gidalevitz, T., Lechleiter, J. D., et al. (2021) · The Journals of Gerontology Series A · doi:10.1093/gerona/glab296 · Cited by 17

Dietary glycemia as a determinant of health and longevity

Whitcomb, E. A., Chiu, C., & Taylor, A. (2015) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2015.08.005 · Cited by 16

Atrial fibrillation

Brundel, B. J. J. M., Ai, X., Hills, M. T., Kuipers, M. F., Lip, G. Y. H., & de Groot, N. M. S. (2016) · Nature Reviews Disease Primers · doi:10.1038/nrdp.2016.17 · Cited by 18

Haplodeficiency of Cathepsin D does not affect cerebral amyloidosis and autophagy in APP / PS 1 transgenic mice

Cheng, S., Wani, W. Y., Hottman, D. A., Jeong, A., Cao, D., LeBlanc, K. J., Säftig, P., Zhang, J., & Li, L. (2017) · Journal of Neurochemistry · doi:10.1111/jnc.14048 · Cited by 15

Inmunopatología de la enfermedad pulmonar obstructiva crónica

Martínez-Aguilar, N. E., Vargas-Camaño, M. E., Hernández-Pliego, R. R., Chaia-Semerena, G. M., & Perez-Chavira, M. R. (2017) · Revista Alergia México · doi:10.29262/ram.v64i3.263 · Cited by 17

Beneficial Effects of Elderly Tailored Mediterranean Diet on the Proteasomal Proteolysis

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

Cross-species functional modules link proteostasis to human normal aging

Komljenović, A., Li, H., Sorrentino, V., Kutalik, Z., Auwerx, J. H., & Robinson‐Rechavi, M. (2019) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1007162 · Cited by 19

Impact of Sample Preparation Strategies on the Quantitative Accuracy of Low-Abundance Serum Proteins in Shotgun Proteomics

Katsavelis, D., van der Hart, M. G. C., Wolters, J. C., Permentier, H. P., Horvatovich, P. L., & Cremers, T. I. F. H. (2025) · Journal of Proteome Research · doi:10.1021/acs.jproteome.5c00572 · Cited by 15

Physics-based modeling provides predictive understanding of selectively promiscuous substrate binding by Hsp70 chaperones

Nordquist, E. B., English, C. A., Clérico, E. M., Sherman, W., Gierasch, L. M., & Chen, J. (2021) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1009567 · Cited by 14

Proteomics for comprehensive characterization of extracellular vesicles in neurodegenerative disease

Vinaiphat, A., & Sze, S. K. (2022) · Experimental Neurology · doi:10.1016/j.expneurol.2022.114149 · Cited by 14

The Critical Role of Biomarkers for Drug Development Targeting the Biology of Aging

Owen, M., Bose, N., Nisenbaum, L., Partrick, K. A., & Fillit, H. M. (2023) · The Journal of Prevention of Alzheimer s Disease · doi:10.14283/jpad.2023.111 · Cited by 15

Age-related disruption of the proteome and acetylome in mouse hearts is associated with loss of function and attenuated by elamipretide (SS-31) and nicotinamide mononucleotide (NMN) treatment

Whitson, J. D., Johnson, R. S., Wang, L., Bammler, T. K., Imai, S., Zhang, H., Fredrickson, J., Latorre-Esteves, E. S., Bitto, A., MacCoss, M. J., et al. (2022) · GeroScience · doi:10.1007/s11357-022-00564-w · Cited by 13

Pulse labeling reveals the tail end of protein folding by proteome profiling

Zhu, M., Kuechler, E. R., Wong, R. W. K., Calabrese, G., Sitarik, I. M., Rana, V., Stoynov, N., O’Brien, E. P., Gsponer, J., & Mayor, T. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111096 · Cited by 13

Proteasome-dependent degradation of intracellular carbamylated proteins

Desmons, A., Okwieka, A., Doué, M., Gorisse, L., Vuiblet, V., Piétrement, C., Gillery, P., & Jaisson, S. (2019) · Aging · doi:10.18632/aging.102002 · Cited by 13

DDQ anti-aging properties expressed with improved mitophagy in mutant tau HT22 neuronal cells

Pradeepkiran, J. A., Rawat, P., Reddy, A. P., Orlov, E., & Reddy, P. H. (2024) · Mitochondrion · doi:10.1016/j.mito.2024.101843 · Cited by 12

Total proteome turbidity assay for tracking global protein aggregation in the natural cellular environment

Shmueli, M. D., Hizkiahou, N., Peled, S., Gazit, E., & Segal, D. (2017) · Journal of Biological Methods · doi:10.14440/jbm.2017.148 · Cited by 13

PIP3-binding proteins promote age-dependent protein aggregation and limit survival in C. elegans

Ayyadevara, S., Balasubramaniam, M., Johnson, J. E., Alla, R., Mackintosh, S. G., & Reis, R. J. S. (2016) · Oncotarget · doi:10.18632/oncotarget.10549 · Cited by 12

Complex Inclusion Bodies and Defective Proteome Hubs in Neurodegenerative Disease: New Clues, New Challenges

Upadhyay, A., Sundaria, N., Dhiman, R., Prajapati, V. K., Prasad, A., & Mishra, A. (2021) · The Neuroscientist · doi:10.1177/1073858421989582 · Cited by 12

Targeting Shp2 as a therapeutic strategy for neurodegenerative diseases

Pang, J., Cen, C.-Q., Tian, Y., Cao, X., Hao, L., Tao, X., & Cao, Z. (2025) · Translational Psychiatry · doi:10.1038/s41398-024-03222-1 · Cited by 12

Hepatic Global Transcriptomic Profiles of Holstein Cows According to Parity Reveal Age-Related Changes in Early Lactation

Cheng, Z., Ferris, C. P., Crowe, M. A., Ingvartsen, K. L., Grelet, C., Vanlierde, A., Foldager, L., Becker, F. O., & Wathes, D. C. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24129906 · Cited by 13

Transgenic sensors reveal compartment-specific effects of aggregation-prone proteins on subcellular proteostasis during aging

Curley, M., Rai, M., Chuang, C.-L., Pagala, V., Stephan, A., Coleman, Z., Robles‐Murguia, M., Wang, Y., Peng, J., & Demontis, F. (2024) · Cell Reports Methods · doi:10.1016/j.crmeth.2024.100875 · Cited by 11

Proteostasis signatures in human diseases

Lim, C. M., & Vendruscolo, M. (2025) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1013155 · Cited by 12

Polyamines sustain epithelial regeneration in aged intestines by modulating protein homeostasis

Minetti, A., Omrani, O., Brenner, C., Cansiz, F., Imada, S., Rösler, J., Khawaled, S., Allies, G., Meckelmann, S. W., Gebert, N., et al. (2025) · Nature Cell Biology · doi:10.1038/s41556-025-01804-9 · Cited by 11

The Interplay Between Proteostasis Systems and Parkinson’s Disease

Lázaro, D. F., & Outeiro, T. F. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-38266-7_9 · Cited by 10

RhoA Activation Sensitizes Cells to Proteotoxic Stimuli by Abrogating the HSF1-Dependent Heat Shock Response

Meijering, R. A. M., Wiersma, M., van Marion, D. M. S., Zhang, D., Hoogstra‐Berends, F., Dijkhuis, A., Schmidt, M., Wieland, T., Kampinga, H. H., Henning, R. H., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0133553 · Cited by 9

The impact of proteostasis dysfunction secondary to environmental and genetic causes on neurodegenerative diseases progression and potential therapeutic intervention

Elmatboly, A. M., Sherif, A., Deeb, D. A., Benmelouka, A. Y., Bin-Jumah, M. N., Aleya, L., & Abdel‐Daim, M. M. (2020) · Environmental Science and Pollution Research · doi:10.1007/s11356-020-07914-1 · Cited by 9

Protein aggregation activates erratic stress response in dietary restricted yeast cells

Bhadra, A. K., Das, E., & Roy, I. (2016) · Scientific Reports · doi:10.1038/srep33433 · Cited by 9

Tumor burden negatively impacts protein turnover as a proteostatic process in noncancerous liver, heart, and muscle, but not brain

Brown, J. L., Lawrence, M. M., Borowik, A., Oliver, L. A., Peelor, F. F., Remmen, H. V., & Miller, B. F. (2021) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01026.2020 · Cited by 8

Organ-specific translation elongation rates measured by in vivo ribosome profilingPreprint

Gerashchenko, M. V., Péterfi, Z., & Gladyshev, V. N. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/279257 · Cited by 8

Hormesis and brain diseases

Lim, V. J. T., Tabassum, N. I., Orian, J. M., Arumugam, T. V., & Weng, E. F.-J. (2025) · Progress in brain research · doi:10.1016/bs.pbr.2025.05.003 · Cited by 7

Trehalose Promotes Clearance of Proteotoxic Aggregation of Neurodegenerative Disease-Associated Aberrant Proteins

Kumar, P., Kinger, S., Dubey, A. R., Jagtap, Y. A., Choudhary, A., Prasad, A., Jha, H. C., Dhiman, R., Gutti, R. K., & Mishra, A. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03824-8 · Cited by 7

Neurodegeneration & imperfect ageing: Technological limitations and challenges?

Sundaria, N., Upadhyay, A., Prasad, A., Prajapati, V. K., Poluri, K. M., & Mishra, A. (2021) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2021.111574 · Cited by 7

Ageing, Metabolic Dysfunction, and the Therapeutic Role of Antioxidants

Santos, A. L., & Sinha, S. (2023) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-031-26576-1_15 · Cited by 8

Lysine deserts and cullin-RING ligase receptors: Navigating untrodden paths in proteostasis

Szulc, N. A., Piechota, M. J., Biriczová, L., Thapa, P. S., & Pokrzywa, W. (2023) · iScience · doi:10.1016/j.isci.2023.108344 · Cited by 7

Caloric restriction induces heat shock response and inhibits B16F10 cell tumorigenesis both in vitro and in vivo

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

Remodeling Tau and Prion Proteins Using Nanochaperons

Bhattacharyya, S., Kim, K., & Teizer, W. (2017) · Advanced Biosystems · doi:10.1002/adbi.201700108 · Cited by 7

Proteostasis Takes Center Stage in Pulmonary Fibrosis

Budinger, G. R. S. (2019) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2018-0400ed · Cited by 7

Multi-scale model suggests the trade-off between protein and ATP demand as a driver of metabolic changes during yeast replicative ageing

Schnitzer, B., Österberg, L., Skopa, I., & Cvijović, M. (2022) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1010261 · Cited by 8

Polyalanine Expansion in PABPN1 Alters the Structure and Dynamics of Its Nuclear Aggregates in Differentiated Muscle Cells

Mallon, S. D., Bos, E., Sheikhhassani, V., Shademan, M., Voortman, L. M., Mashaghi, A., Sharp, T. H., & Raz, V. (2025) · The FASEB Journal · doi:10.1096/fj.202501097r · Cited by 6

Effects of heterologous human tau protein expression in yeast models of proteotoxic stress response

Zubčić, K., Franić, D., Pravica, M., Hof, P. R., Šimić, G., & Boban, M. (2023) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.14304 · Cited by 5

Short-term changes in diet composition do not affect in vivo hepatic protein synthesis in rats

Estrada, A. L., Hudson, W. M., Kim, P., Stewart, C. M., Peelor, F. F., Wei, Y., Wang, D., Hamilton, K. L., Miller, B. F., & Pagliassotti, M. J. (2017) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00209.2017 · Cited by 6

Isolation of an Extract from the Soft Coral Symbiotic Microorganism Salinispora arenicola Exerting Cytoprotective and Anti-Aging Effects

Louka, X. P., Sklirou, A. D., Goff, G. L., Lopes, P., Papanagnou, E., Manola, M. S., Benayahu, Y., Ouazzani, J., & Trougakos, I. P. (2021) · Current Issues in Molecular Biology · doi:10.3390/cimb44010002 · Cited by 6

Prevention of Atrial Fibrillation: Putting Proteostasis Derailment Back on Track

Kishore, P., Collinet, A. C. T., & Brundel, B. J. J. M. (2023) · Journal of Clinical Medicine · doi:10.3390/jcm12134352 · Cited by 6

Gene expression in the liver of female, but not male mice treated with rapamycin resembles changes observed under dietary restriction

Yu, Z., Sunchu, B., Fok, W. C., Alshaikh, N., & Pérez, V. (2015) · SpringerPlus · doi:10.1186/s40064-015-0909-7 · Cited by 6

Heptamer Peptide Disassembles Native Amyloid in Human Plasma Through Heat Shock Protein 70

Cunningham, T. J., Greenstein, J. I., Yao, L., Fischer, I., & Connors, T. M. (2018) · Rejuvenation Research · doi:10.1089/rej.2017.2049 · Cited by 6

Non‐lethal proteasome inhibition activates pro‐tumorigenic pathways in multiple myeloma cells

Skorda, A., Sklirou, A. D., Sakellaropoulos, T., Gianniou, D. D., Kastritis, E., Terpos, E., Tsitsilonis, O., Florea, B. I., Overkleeft, H. S., Dimopoulos, M. A., et al. (2019) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.14653 · Cited by 6

Proteome solubility is differentially reshaped by thermal stress and regulators of ubiquitination

Hunt, L. C., Stephan, A., Poudel, S., Yu, K., Kavdia, K., Pagala, V., Wang, W., Fu, Y., Wang, Y., Wang, X., et al. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.110517 · Cited by 5

NAD⁺ as a central metabolic hub Regulating the hallmarks of aging: Mechanisms and therapeutic implications

Pei, Z., Liang, F., Wang, X., & Li, H. (2026) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2026.112174 · Cited by 7

Perspective Proteostasis and the Aging Proteome in Health and Disease

Gerontol, C. J., Biol, A., Med, S. T., (s):s–s, S. J., Morimoto, R., & Cuervo, A. M. (2014)

The proteostasis network and its decline in ageing

Hipp, M. S., Kasturi, P., & Hartl, F. U. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0101-y · Cited by 1,642

S3–02–01: Proteostasis: monitoring the health of the proteome in biology, aging and disease

Morimoto, R. I. (2013) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2013.04.218 · Cited by 2

Dysregulated proteostasis

Al-Mufti, Y., Cranwell, S., & Samant, R. S. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-91617-2.00004-3 · Cited by 1

Proteolysis dysfunction in the process of aging and age-related diseases

Frankowska, N., Lisowska, K., & Witkowski, J. M. (2022) · Frontiers in Aging · doi:10.3389/fragi.2022.927630 · Cited by 67