The Biology of Proteostasis in Aging and Disease

Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis

Rosen, D. R., Siddique, T., Patterson, D., Figlewicz, D. A., Sapp, P., Hentati, A., Donaldson, D., Goto, J., O'Regan, J. P., Deng, H.-X., et al. (1993) · Nature · doi:10.1038/362059a0 · Cited by 7,062

Protein Misfolding, Functional Amyloid, and Human Disease

Chiti, F., & Dobson, C. M. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.101304.123901 · Cited by 6,497

The Unfolded Protein Response: From Stress Pathway to Homeostatic Regulation

Walter, P., & Ron, D. (2011) · Science · doi:10.1126/science.1209038 · Cited by 5,897

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

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

STRUCTURE AND FUNCTIONS OF THE 20S AND 26S PROTEASOMES

Coux, O., Tanaka, K., & Goldberg, A. L. (1996) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.65.070196.004101 · Cited by 2,438

The amyloid state and its association with protein misfolding diseases.

Knowles, T. P. J., Vendruscolo, M., & Dobson, C. M. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3810 · Cited by 2,382

Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease

Ravikumar, B., Vacher, C., Berger, Z., Davies, J. E., Luo, S., Oroz, L. G., Scaravilli, F., Easton, D. F., Duden, R., O'Kane, C. J., et al. (2004) · Nature Genetics · doi:10.1038/ng1362 · Cited by 2,347

Impaired Degradation of Mutant α-Synuclein by Chaperone-Mediated Autophagy

Cuervo, A. M., Stefanis, L., Fredenburg, R., Lansbury, P. T., & Sulzer, D. (2004) · Science · doi:10.1126/science.1101738 · Cited by 2,024

Identification of subfunctionalized aggregate-remodeling J-domain proteins in Arabidopsis thaliana

Tak, Y., Lal, S. S., Gopan, S., Balakrishnan, M., Satheesh, G., Biswal, A. K., Verma, A. K., Cole, S. J., Brown, R. E., Hayward, R. E., et al. (2022) · Journal of Experimental Botany · doi:10.1093/jxb/erac514 · Cited by 14

Aging: Epigenetic modifications

Mishra, S., Raval, M., Kachhawaha, A. S., Tiwari, B. S., & Tiwari, A. K. (2023) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2023.02.002 · Cited by 14

Links between telomere dysfunction and hallmarks of aging

Li, S., Liu, Z., Zhang, J., & Li, L. (2023) · Mutation Research/Genetic Toxicology and Environmental Mutagenesis · doi:10.1016/j.mrgentox.2023.503617 · Cited by 15

Regulation of HSF1 transcriptional complexes under proteotoxic stress

Fujimoto, M., Takii, R., & Nakai, A. (2023) · BioEssays · doi:10.1002/bies.202300036 · Cited by 14

Recognition of an Ala-rich C-degron by the E3 ligase Pirh2

Wang, X., Li, Y., Yan, X., Yang, Q., Zhang, B., Zhang, Y., Yuan, X., Jiang, C., Chen, D., Liu, Q., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-38173-6 · Cited by 14

Plastic nanoparticles cause proteome stress and aggregation by compromising cellular protein homeostasis ex vivo and in vivo

Jing, B., Wan, W., Hu, B. H., Jin, W., Zhang, Z., Peng, C., Wang, M., Deng, J., Dong, X., Liu, Y., et al. (2023) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2023.115347 · Cited by 17

Prefoldin 2 contributes to mitochondrial morphology and function

Tahmaz, İ., Ghahe, S. S., Stasiak, M., Liput, K. P., Jonak, K., & Topf, U. (2023) · BMC Biology · doi:10.1186/s12915-023-01695-y · Cited by 14

Lipid Droplets Modulate Proteostasis, SQST-1/SQSTM1 Dynamics, and Lifespan in C. elegans

Kumar, A. V., Mills, J., Parker, W. M., Leitão, J. A., Rodriguez, D., Daigle, S. E., Ng, C., Patel, R., Aguilera, J., Johnson, J. R., et al. (2022) · iScience · doi:10.1016/j.isci.2023.107960 · Cited by 16

Crosstalk between protein misfolding and endoplasmic reticulum stress during ageing and their role in age-related disorders

Hemagirri, M., Chen, Y., Gopinath, S. C. B., Sahreen, S., Adnan, M., & Sasidharan, S. (2023) · Biochimie · doi:10.1016/j.biochi.2023.10.019 · Cited by 15

Potential roles for mitochondria-to-HSF1 signaling in health and disease

Labbadia, J. P. (2023) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2023.1332658 · Cited by 14

Cascade-targeting multifunctional nanochaperone remodels brain microenvironment for synergistic therapy of Alzheimer’s disease

Zhang, X., Hu, H., Li, Q., Zhao, Y., Zhang, Z., Zhao, S., Xu, L., Ma, R., Huang, F., & Shi, L. (2024) · Nano Today · doi:10.1016/j.nantod.2024.102168 · Cited by 14

Distinct types of intramitochondrial protein aggregates protect mitochondria against proteotoxic stress

Bertgen, L., Boekenkamp, J.-E., Schneckmann, T., Koch, C., Räschle, M., Štorchová, Z., & Herrmann, J. M. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114018 · Cited by 14

A sticky situation: Aberrant protein–protein interactions in Parkinson’s disease

Brown, J., & Horrocks, M. H. (2018) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2018.05.006 · Cited by 14

Contribution of the unfolded protein response to breast and prostate tissue homeostasis and its significance to cancer endocrine response

Direito, I., Fardilha, M., & Helguero, L. A. (2018) · Carcinogenesis · doi:10.1093/carcin/bgy182 · Cited by 14

Molecular changes in glaucomatous trabecular meshwork. Correlations with retinal ganglion cell death and novel strategies for neuroprotection

Saccà, S. C., Vernazza, S., Iorio, E. L., Tirendi, S., Bassi, A. M., Gandolfi, S., & Izzotti, A. (2020) · Progress in brain research · doi:10.1016/bs.pbr.2020.06.003 · Cited by 14

Targeted Protein Degradation as a Promising Tool for Epigenetic Upregulation of Fetal Hemoglobin

Verheul, T. C. J., Trinh, V. T., Vázquez, O., & Philipsen, S. (2020) · ChemMedChem · doi:10.1002/cmdc.202000574 · Cited by 14

On the origin of BAG(3) and its consequences for an expansion of BAG3's role in protein homeostasis

Baeken, M. W., & Behl, C. (2021) · Journal of Cellular Biochemistry · doi:10.1002/jcb.29925 · Cited by 14

Surveying Low-Cost Methods to Measure Lifespan and Healthspan in Caenorhabditis elegans

Torres, T. C., Moaddeli, D., Averbukh, M., Coakley, A. J., Dutta, N., Garcia, G., & Higuchi‐Sanabria, R. (2022) · Journal of Visualized Experiments · doi:10.3791/64091 · Cited by 14

Loss of MTCH-1 suppresses age-related proteostasis collapse through the inhibition of programmed cell death factors

Aman, Y., Erinjeri, A. P., Tataridas-Pallas, N., Williams, R., Wellman, R., Chapman, H., & Labbadia, J. P. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111690 · Cited by 14

Regulation of Age-related Decline by Transcription Factors and Their Crosstalk with the Epigenome

Zhou, X., Sen, I., Lin, X.-X., & Riedel, C. G. (2018) · Current Genomics · doi:10.2174/1389202919666180503125850 · Cited by 15

Expression of the amyloid-β peptide in a single pair of C. elegans sensory neurons modulates the associated behavioural response

Sinnige, T., Ciryam, P. S., Casford, S., Dobson, C. M., de Bono, M., & Vendruscolo, M. (2019) · PLoS ONE · doi:10.1371/journal.pone.0217746 · Cited by 18

Pathological changes are associated with shifts in the employment of synonymous codons at the transcriptome level

Fornasiero, E. F., & Rizzoli, S. O. (2019) · BMC Genomics · doi:10.1186/s12864-019-5921-9 · Cited by 15

Protein quality control: from mechanism to disease

Kampinga, H. H., Mayer, M. P., & Mogk, A. (2019) · Cell Stress and Chaperones · doi:10.1007/s12192-019-01040-9 · Cited by 14

The Role of Protein S-Nitrosylation in Protein Misfolding-Associated Diseases

Ju, Y.-J., Lee, H.-W., Choi, J.-W., & Choi, M.-S. (2021) · Life · doi:10.3390/life11070705 · Cited by 14

Imaging of Actin Cytoskeletal Integrity During Aging in C. elegans

Garcia, G., Homentcovschi, S., Kelet, N., & Higuchi‐Sanabria, R. (2021) · Methods in molecular biology · doi:10.1007/978-1-0716-1661-1_5 · Cited by 14

Impaired biogenesis of basic proteins impacts multiple hallmarks of the aging brainPreprint

Fraia, D. D., Marino, A., Lee, J. H., Sacramento, E. K., Baumgart, M., Bagnoli, S., da Silva, P. T., Sahu, A. K., Siano, G., Tiessen, M., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.07.20.549210 · Cited by 13

Lymphoma accelerates T cell and tissue aging

Hesterberg, R. S., Davis, J. T., Handoo, K. J., Elmarsafawi, A. G., Augello, A. C., Cheng, C., Atkins, R. M., Lee, D. H., Yang, C., Yao, J., et al. (2025) · Cancer Cell · doi:10.1016/j.ccell.2025.07.023 · Cited by 14

Human Small Heat Shock Protein B8 Inhibits Protein Aggregation without Affecting the Native Folding Process

Choudhary, D., Mediani, L., Avellaneda, M. J., Bjarnason, S., Alberti, S., Boczek, E. E., Heidarsson, P. O., Mossa, A., Carra, S., Tans, S. J., et al. (2023) · Journal of the American Chemical Society · doi:10.1021/jacs.3c02022 · Cited by 13

Proteostasis regulation through ribosome quality control and no‐go‐decay

Boopathy, L. R. A., Beadle, E., Rico, A. G., & Vera, M. (2023) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1809 · Cited by 14

How ATP suppresses the fibrillation of amyloid peptides: analysis of the free-energy contributions

Minh, T. N., Horinek, D., & Matubayasi, N. (2024) · Physical Chemistry Chemical Physics · doi:10.1039/d4cp00179f · Cited by 13

Human coronaviruses activate and hijack the host transcription factor HSF1 to enhance viral replication

Pauciullo, S., Riccio, A., Santopolo, S., Albecka, A., Papa, G., James, L. C., Piacentini, S., Lanzilli, G., Rossi, A., & Santoro, M. G. (2024) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-024-05370-5 · Cited by 13

Reversible cold-induced lens opacity in a hibernator reveals a molecular target for treating cataracts

Yang, H., Ping, X., Zhou, J., Ailifeire, H., Wu, J., Nadal-Nicolás, F. M., Miyagishima, K. J., Bao, J., Huang, Y., Cui, Y., et al. (2024) · Journal of Clinical Investigation · doi:10.1172/jci169666 · Cited by 15

Tmc1 Is a Dynamically Regulated Effector of the Rpn4 Proteotoxic Stress Response

Guerra-Moreno, Á., & Hanna, J. W. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.726398 · Cited by 13

Emerging roles of RNA modifications in genome integrity

Lee, S. Y., Kim, J. J., & Miller, K. M. (2020) · Briefings in Functional Genomics · doi:10.1093/bfgp/elaa022 · Cited by 14

Improved correction of F508del-CFTR biogenesis with a folding facilitator and an inhibitor of protein ubiquitination

Goeckeler-Fried, J. L., Denny, R. A., Joshi, D., Hill, C., Larsen, M. B., Chiang, A., Frizzell, R. A., Wipf, P., Sorscher, E. J., & Brodsky, J. L. (2021) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2021.128243 · Cited by 13

Truncation-Driven Lateral Association of α-Synuclein Hinders Amyloid Clearance by the Hsp70-Based Disaggregase

Franco, A., Cuéllar, J., Fernández-Higuero, J. Á., de la Arada, I., Orozco, N., Valpuesta, J., Prado, A., & Muga, A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222312983 · Cited by 13

The CRTC-CREB axis functions as a transcriptional sensor to protect against proteotoxic stress in Drosophila

Yin, Y., Ma, P., Wang, S., Zhang, Y., Han, R., Huo, C., Wu, M., & Deng, H. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-05122-y · Cited by 14

Shape matters: the complex relationship between aggregation and toxicity in protein-misfolding diseases

Ries, H. M., & Nussbaum-Krammer, C. I. (2016) · Essays in Biochemistry · doi:10.1042/ebc20160008 · Cited by 12

High-Reynolds Microfluidic Sorting of Large Yeast Populations

Keinan, E., Abraham, A. C., Cohen, A., Alexandrov, A. I., Mintz, R., Cohen, M., Reichmann, D., Kaganovich, D., & Nahmias, Y. (2018) · Scientific Reports · doi:10.1038/s41598-018-31726-6 · Cited by 13

Non-Proteasomal UbL-UbA Family of Proteins in Neurodegeneration

Jantrapirom, S., Piccolo, L. L., & Yamaguchi, M. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20081893 · Cited by 13

Protein turnover models for LC–MS data of heavy water metabolic labeling

Sadygov, R. G. (2021) · Briefings in Bioinformatics · doi:10.1093/bib/bbab598 · Cited by 14

Efficient Heat Shock Response Affects Hyperthermia-Induced Radiosensitization in a Tumor Spheroid Control Probability Assay

Chen, O., Michlíková, S., Eckhardt, L., Wondrak, M., Mendoza, A. M. D., Krause, M., McLeod, D. D., & Kunz‐Schughart, L. A. (2021) · Cancers · doi:10.3390/cancers13133168 · Cited by 12

Structural basis for the inhibition of IAPP fibril formation by the co-chaperonin prefoldin

Törner, R., Kupreichyk, T., Gremer, L., Debled, E. C., Fenel, D., Schemmert, S., Gans, P., Willbold, D., Schoehn, G., Hoyer, W., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-30042-y · Cited by 12

The role of heat shock proteins in preventing amyloid toxicity

Törner, R., Kupreichyk, T., Hoyer, W., & Boisbouvier, J. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.1045616 · Cited by 12

Cross-sectional study and bioinformatics analysis to reveal the correlations of osteoporosis in patients with Parkinson's disease

Ma, C., Yu, R., Li, J., Xiao, E., Guo, J., Wang, X., Li, G., & Liu, P. (2023) · Experimental Gerontology · doi:10.1016/j.exger.2023.112111 · Cited by 12

The heat shock factor code: Specifying a diversity of transcriptional regulatory programs broadly promoting stress resilience

Alasady, M. J., & Mendillo, M. L. (2024) · Cell Stress and Chaperones · doi:10.1016/j.cstres.2024.10.006 · Cited by 14

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

Tissue-Specific Upregulation of Drosophila Insulin Receptor (InR) Mitigates Poly(Q)-Mediated Neurotoxicity by Restoration of Cellular Transcription Machinery

Raj, K., & Sarkar, S. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-1160-3 · Cited by 12

Proteostatic stress as a nodal hallmark of replicative aging

Moreno, D. F., & Aldea, M. (2020) · Experimental Cell Research · doi:10.1016/j.yexcr.2020.112163 · Cited by 12

Recent advances in bioanalytical methods to measure proteome stability in cells

Zhang, S., Greening, D. W., & Hong, Y. (2021) · The Analyst · doi:10.1039/d0an01547d · Cited by 13

Interactions of amyloidogenic proteins with mitochondrial protein import machinery in aging-related neurodegenerative diseases

Reed, A. L., Mitchell, W., Alexandrescu, A. T., & Alder, N. N. (2023) · Frontiers in Physiology · doi:10.3389/fphys.2023.1263420 · Cited by 13

Deletion of the transcription factors Hsf1, Msn2 and Msn4 in yeast uncovers transcriptional reprogramming in response to proteotoxic stress

Mühlhofer, M., Offensperger, F., Reschke, S., Wallmann, G., Csaba, G., Berchtold, E., Riedl, M., Blum, H., Haslbeck, M., Zimmer, R., et al. (2024) · FEBS Letters · doi:10.1002/1873-3468.14821 · Cited by 14

Effects of Quercetin on Neurodegenerative and Compensatory Processes in the Nigrostriatal System in a Model of the Preclinical Stage of Parkinson’s Disease in Rats

Ekimova, I. V., & Плаксина, Д. В. (2017) · Neuroscience and Behavioral Physiology · doi:10.1007/s11055-017-0508-x · Cited by 12

Mitogen-activated protein kinases, Fus3 and Kss1, regulate chronological lifespan in yeast

Aluru, M. R., McKinney, T., Venero, A.-K. L., Choudhury, S., & Torres, M. P. (2017) · Aging · doi:10.18632/aging.101350 · Cited by 13

Decreased Protein Quality Control Promotes the Cognitive Dysfunction Associated With Aging and Environmental Insults

Jin, H., Komita, M., & Aoe, T. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00753 · Cited by 12

Toxicant-mediated redox control of proteostasis in neurodegeneration

Aivazidis, S., Anderson, C. C., & Roede, J. R. (2018) · Current Opinion in Toxicology · doi:10.1016/j.cotox.2018.12.007 · Cited by 13

Application of Caenorhabditis elegans for Research on Endoplasmic Reticulum Stress

Xu, Y., & Park, Y. (2018) · Preventive Nutrition and Food Science · doi:10.3746/pnf.2018.23.4.275 · Cited by 12

Redefining proteostasis transcription factors in organismal stress responses, development, metabolism, and health

Jones, L., Chen, Y., & van Oosten‐Hawle, P. (2020) · Biological Chemistry · doi:10.1515/hsz-2019-0385 · Cited by 13

Designing Novel Therapies to Mend Broken Hearts: ATF6 and Cardiac Proteostasis

Blackwood, E. A., Bilal, A. S., Stauffer, W. T., Arrieta, A., & Glembotski, C. C. (2020) · Cells · doi:10.3390/cells9030602 · Cited by 12

Effects of chronic intermittent hypoxia on left cardiac function in young and aged mice

Qin, W. D., Xu, X., Chen, L., Wang, T., Xie, L., Yu, F., Song, S.-F., Sheng, Z.-Q., & Tong, J. (2022) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00256.2021 · Cited by 12

Molecular chaperones: functional mechanisms and nanotechnological applications

Fernández-Fernández, M. R., Sot, B., & Valpuesta, J. (2016) · Nanotechnology · doi:10.1088/0957-4484/27/32/324004 · Cited by 12

Methodologies to monitor protein turnover at the inner nuclear membrane

Tsai, P.-L., Zhao, C., & Schlieker, C. D. (2019) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2018.12.033 · Cited by 12

A brain atlas of synapse protein lifetime across the mouse lifespanPreprint

Bulovaite, E., Qiu, Z., Kratschke, M., Zgraj, A., Fricker, D. G., Tuck, E. J., Gokhale, R., Jami, S. A., Merino‐Serrais, P., Husi, E., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.12.16.472938 · Cited by 11

Long ant life span is maintained by a unique heat shock factorPreprint

Glastad, K. M., Roessler, J. M., Gospočić, J., Bonasio, R., & Berger, S. L. (2023) · Genes & Development · doi:10.1101/gad.350250.122 · Cited by 12

Natural Products in Aging: Cellular Mechanisms and Emerging Therapeutics for Age‐Related Disorders

Dixit, V., Chaubey, K. K., Dayal, D., Chole, P. B., Manjunath, B. T., Bachheti, R. K., Gupta, P. C., Bachheti, A., & Worku, L. A. (2025) · Journal of Aging Research · doi:10.1155/jare/6868732 · Cited by 11

Enhancing healthspan with Ashwagandha (Withania somnifera): a comprehensive review of its multifaceted geroprotective benefits

Vittal, M., & Vinciguerra, M. (2025) · Biogerontology · doi:10.1007/s10522-025-10320-0 · Cited by 11

Assessing glymphatic-associated fluid dynamics in psychiatric disorders: evidence from neuroimaging - a review

Zhang, X., Hatoum, L., Ying, J., & Huang, C. (2025) · Psychoradiology · doi:10.1093/psyrad/kkaf031 · Cited by 11

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

HSP70 mediates a crosstalk between the estrogen and the heat shock response pathways

Silveira, M. A. D., Khadangi, F., Mersaoui, S. Y., Naik, D., Masson, J., & Bilodeau, S. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.102872 · Cited by 13

Transcriptomic characterization of Lonrf1 at the single-cell level under pathophysiological conditions

Li, D., Wang, T., Aratani, S., Omori, S., Tamatani, M., Johmura, Y., & Nakanishi, M. (2023) · The Journal of Biochemistry · doi:10.1093/jb/mvad021 · Cited by 12

p97/VCP Promotes the Recycling of Endocytic Cargo

Kawan, M., Körner, M., Schlösser, A., & Buchberger, A. (2023) · Molecular Biology of the Cell · doi:10.1091/mbc.e23-06-0237 · Cited by 10

The Hsp70 and JDP proteins: Structure-function perspective on molecular chaperone activity

Ciesielski, S. J., Young, C., Ciesielska, E. J., & Ciesielski, G. L. (2023) · The Enzymes · doi:10.1016/bs.enz.2023.07.008 · Cited by 11

A multi‐layered network model identifies Akt1 as a common modulator of neurodegeneration

Na, D., Lim, D., Hong, J., Lee, H., Cho, D., Yu, M., Shaker, B., Ren, J. T., Lee, B., Song, J. G., et al. (2023) · Molecular Systems Biology · doi:10.15252/msb.202311801 · Cited by 14

Pharmacological inhibition of USP14 delays proteostasis-associated aging in a proteasome-dependent but foxo-independent manner

Lim, J. J., Noh, S., Kang, W., Hyun, B., Lee, B., & Hyun, S. (2024) · Autophagy · doi:10.1080/15548627.2024.2389607 · Cited by 12

Human umbilical cord mesenchymal stem cells-derived extracellular vesicles ameliorate kidney ischemia-reperfusion injury by suppression of senescent tubular epithelial cells: experimental study

Ma, M., Zeng, J., Zhu, M., Li, H., Lin, T., Yang, H., Wei, X. C., & Song, T. (2024) · International Journal of Surgery · doi:10.1097/js9.0000000000002074 · Cited by 11

Too old for healthy aging? Exploring age limits of longevity treatments

Chaudhari, P., & Ermolaeva, M. (2024) · npj Metabolic Health and Disease · doi:10.1038/s44324-024-00040-3 · Cited by 13

TMBIM-2 orchestrates systemic mitochondrial stress response via facilitating Ca2+ oscillations

Li, J., Cui, J., Li, X., Zhu, D., Chen, Z., Huang, X., Wang, Y., Wu, Q., & Tian, Y. (2025) · The Journal of Cell Biology · doi:10.1083/jcb.202408050 · Cited by 11

Interaction-component analysis of the effects of urea and its alkylated derivatives on the structure of T4-lysozyme

Yamamori, Y., & Matubayasi, N. (2017) · The Journal of Chemical Physics · doi:10.1063/1.4985222 · Cited by 11

Ub and Down: Ubiquitin Exercise for the Elderly

Höhfeld, J., & Hoppe, T. (2018) · Trends in Cell Biology · doi:10.1016/j.tcb.2018.03.002 · Cited by 11

Distinct temporal actions of different types of unfolded protein responses during aging

Sheng, Y., Yang, G., Markovich, Z., Han, S. M., & Xiao, R. (2020) · Journal of Cellular Physiology · doi:10.1002/jcp.30215 · Cited by 11

H2S contributed from CSE during cellular senescence suppresses inflammation and nitrosative stress

Gupta, K., Mathew, A. B., Chakrapani, H., & Saini, D. K. (2022) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2022.119388 · Cited by 11

Oral Therapy for the Treatment of Transthyretin-Related Amyloid Cardiomyopathy

Nuvolone, M., Girelli, M., & Merlini, G. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232416145 · Cited by 11

Branched-Chain Amino Acid Assembly into Amyloid-like Fibrils Provides a New Paradigm for Maple Syrup Urine Disease Pathology

Kreiser, T., Sogolovsky-Bard, I., Zaguri, D., Shaham‐Niv, S., Bar‐Yosef, D. L., & Gazit, E. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242115999 · Cited by 11

Uncoupling the Trade-Off between Somatic Proteostasis and Reproduction in Caenorhabditis elegans Models of Polyglutamine Diseases

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