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

Replicative aging impedes stress-induced assembly of a key human protein disaggregasePreprint

Mathangasinghe, Y., Alberts, N., Rosado, C. J., Cox, D., Payne, N. L., Ormsby, A. R., Merve, K., Sakson, R., Uthishtran, S., Ruppert, T., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.06.25.497591 · Cited by 8

Global Protein-Turnover Quantification in Escherichia coli Reveals Cytoplasmic Recycling under Nitrogen LimitationPreprint

Gupta, M., Johnson, A. N. T., Cruz, E. R., Costa, E. J., Guest, R. L., Li, H., Hart, E. M., Nguyen, T., Stadlmeier, M., Bratton, B. P., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.08.01.502339 · Cited by 7

Prediction of Protein Half-lives from Amino Acid Sequences by Protein Language ModelsPreprint

Sagawa, T., Kanao, E., Ogata, K., Imami, K., & Ishihama, Y. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.09.10.612367 · Cited by 9

Lycium barbarum Polysaccharide Alleviates Amyloid‐β‐Induced Toxicity in the Caenorhabditis elegans Model

An, L., Wang, W., Chu, J., An, L., Geng, B., Fu, X., Chen, J., & Ma, J. (2024) · Food Frontiers · doi:10.1002/fft2.522 · Cited by 6

The Hallmarks of Ageing in Human Immunodeficiency Virus Infection and the Impact of Antiretroviral Therapy on Telomeres: A Molecular Perspective

Apetroaei, M.-M., Baliou, S., Ιωάννου, Π., Fragkiadaki, P., Ștefan, G., Nedea, M. I., Burcea-Dragomiroiu, G.-T.-A., Velescu, B. Ș., Docea, A. O., Udeanu, D. I., et al. (2025) · Current Issues in Molecular Biology · doi:10.3390/cimb47040273 · Cited by 6

Unveiling Selenoprotein T as a novel regulator of cardiomyocyte senescence: pivotal role of the CD36 receptor in AC16 human cardiomyocytes

Bartolo, A. D., Rago, V., Romeo, N., Cicco, M. D., Lefranc, B., Leprince, J., Passarino, G., Pagliaro, P., Anouar, Y., Rocca, C., et al. (2025) · GeroScience · doi:10.1007/s11357-025-01759-7 · Cited by 7

Proteins with cognition-associated structural changes in a rat model of aging exhibit reduced refolding capacity

Tarbox, H. E., Branch, A., & Fried, S. D. (2025) · Science Advances · doi:10.1126/sciadv.adt3778 · Cited by 8

Kukoamine A from the root bark of Lycium chinense Miller enhances mobility in an aged Caenorhabditis elegans model by regulating mitochondrial function through HSF-1-mediated upregulation of heat shock proteins

Lee, S., Youn, E., Tran, S. H., Bae, W., Nguyen, U. T. T., Ho, P. L., Kim, J. H., Park, K., Kim, C. Y., & Kang, K. (2025) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2025.120469 · Cited by 6

Next-generation sequencing of a combinatorial peptide phage library screened against ubiquitin identifies peptide aptamers that can inhibit the in vitro ubiquitin transfer cascade

Lisowska, M. M., Lickiss, F., Gil-Mir, M., Huart, A.-S., Trybala, Z., Way, L., Hernychová, L., Krejčí, A., Müller, P., Krejčíř, R., et al. (2022) · Frontiers in Microbiology · doi:10.3389/fmicb.2022.875556 · Cited by 6

The Anaphase-Promoting Complex/Cyclosome Is a Cellular Ageing Regulator

Hu, X., Jin, X., Cao, X., & Liu, B. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232315327 · Cited by 7

Small molecules as modulators of the proteostasis machinery: Implication in cardiovascular diseases

Yang, Z., Cao, Y., Kong, L., Xi, J., Liu, S., Zhang, J., & Cheng, W. (2023) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2023.116030 · Cited by 6

Mitochondrial clearance and increased HSF-1 activity are coupled to promote longevity in fasted Caenorhabditis elegans

Tataridas-Pallas, N., Aman, Y., Williams, R., Chapman, H., Cheng, K. J. H., Gomez-Paredes, C., Bates, G. P., & Labbadia, J. P. (2024) · iScience · doi:10.1016/j.isci.2024.109834 · Cited by 7

Calreticulin from Apostichopus japonicus relieves endoplasmic reticulum stress induced by Vibrio splendidus through autophagy

Liang, W., Hu, L., Dai, F., Shi, Y., Yang, L., & Li, C. (2024) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2024.109798 · Cited by 6

Ste20-like kinase, SLK, activates the heat shock factor 1 – Hsp70 pathway

Cybulsky, A. V., Guillemette, J., & Papillon, J. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2016.05.015 · Cited by 6

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

Effects of iron on the aggregation propensity of the N-terminal fibrillogenic polypeptide of human apolipoprotein A-I

Giudice, R. D., Pesce, A., Cozzolino, F., Monti, M., Relini, A., Piccoli, R., Arciello, A., & Monti, D. M. (2018) · BioMetals · doi:10.1007/s10534-018-0101-y · Cited by 6

SEL1L degradation intermediates stimulate cytosolic aggregation of polyglutamine‐expanded protein

Hattori, T., Hanafusa, K., Wada, I., & Hosokawa, N. (2021) · FEBS Journal · doi:10.1111/febs.15761 · Cited by 6

Disruption of Endoplasmic Reticulum Proteostasis in Age-Related Nervous System Disorders

Medinas, D. B., Hazari, Y., & Hetz, C. A. (2021) · Progress in molecular and subcellular biology · doi:10.1007/978-3-030-67696-4_12 · Cited by 7

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

Targeted protein degradation: from small molecules to complex organelles—a Keystone Symposia report

Cable, J., Weber-Ban, E. U., Clausen, T., Walters, K. J., Sharon, M., Finley, D. J., Gu, Y., Hanna, J. W., Feng, Y., Martens, S., et al. (2022) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.14745 · Cited by 6

Brief about hallmarks of aging

Esposto, J., & Balendra, V. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-90235-9.00006-9 · Cited by 6

Chaperonin CCT5 binding with porcine parvovirus NS1 promotes the interaction of NS1 and COPƐ to facilitate viral replication

Du, Q., Zhang, X., Xu, N., Ma, M., Miao, B., Huang, Y., & Tong, D. (2022) · Veterinary Microbiology · doi:10.1016/j.vetmic.2022.109574 · Cited by 6

Vitellogenin accumulation leads to reproductive senescence by impairing lysosomal function

Tang, J., Ma, Y., Chen, Y., Yang, R.-Q., Liu, H., Wang, X., Ni, B., Zou, C., & Zhang, K. (2023) · Science China Life Sciences · doi:10.1007/s11427-022-2242-8 · Cited by 6

Regulation of germline proteostasis by HSF1 and insulin/IGF-1 signaling

Muhammad, T., & Li, J. (2023) · Biochemical Society Transactions · doi:10.1042/bst20220616 · Cited by 5

The PERK Branch of the Unfolded Protein Response Safeguards Protein Homeostasis and Mesendoderm Specification of Human Pluripotent Stem Cells

Liu, F., Liu, Z., Cheng, W., Zhao, Q., Zhang, X., Zhang, H., Yu, M., Xu, H., Gao, Y., Jiang, Q., et al. (2023) · Advanced Science · doi:10.1002/advs.202303799 · Cited by 7

Combating Parkinson’s disease-associated toxicity by modulating proteostasis

Park, Y., & Hoang, Q. Q. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1620082114 · 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

A small molecule autophagy inducer exerts cytoprotection against α-synuclein toxicity

Suresh, S., & Manjithaya, R. R. (2019) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2019.172635 · Cited by 6

Association of intronic polymorphisms (rs1549339, rs13402242) and mRNA expression variations in PSMD1 gene in arsenic-exposed workers

Ahmad, S., Arif, B., Akram, Z., Ahmed, M. W., Khan, A. U., Hussain, M. Z., Rahman, F., Kayani, M. A., & Mahjabeen, I. (2020) · Environmental Science and Pollution Research · doi:10.1007/s11356-019-07422-x · Cited by 6

SLC26A9 is selected for endoplasmic reticulum associated degradation (ERAD) via Hsp70-dependent targeting of the soluble STAS domain

Needham, P. G., Goeckeler-Fried, J. L., Zhang, C., Sun, Z., Wetzel, A. R., Bertrand, C. A., & Brodsky, J. L. (2021) · Biochemical Journal · doi:10.1042/bcj20210644 · Cited by 6

The intriguing dose-dependent effect of selected amphiphilic compounds on insulin amyloid aggregation: Focus on a cholesterol-based detergent, Chobimalt

Šipošová, K., Petrenko, V. I., Garcarova, I., Sedláková, D., Almásy, L., Kyzyma, O. A., Kriechbaum, M., & Musatov, A. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.955282 · Cited by 6

Modeling SILAC Data to Assess Protein Turnover in a Cellular Model of Diabetic Nephropathy

Camillo, B. D., Puricelli, L., Iori, E., TOFFOLO, G. M., Tessari, P., & Arrigoni, G. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24032811 · Cited by 5

The Molecular Chaperone HSP90 Promotes Notch Signaling in the Germline ofCaenorhabditis elegans

Lissemore, J. L., Connors, E. M., Liu, Y., Li, Q., Yang, B., Edgley, M. L., Flibotte, S., Taylor, J. C., Au, V., Moerman, D. G., et al. (2018) · G3 Genes Genomes Genetics · doi:10.1534/g3.118.300551 · Cited by 6

Species-specific mitochondria dynamics and metabolism regulate the timing of neuronal developmentPreprint

Iwata, R., Casimir, P., Erkol, E., Boubakar, L., Planque, M., Ditkowska, M., Vints, K., Poovathingal, S. K., Gaspariunaite, V., Bird, M., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.12.27.474246 · Cited by 6

Ubiquitin-Proteasome System in the Different Stages of Dominantly Inherited Alzheimer’s DiseasePreprint

McDade, E., Liu, H., Bui, Q. V. P., Hassenstab, J. J., Gordon, B. A., Benzinger, T. L. S., Shen, Y., Timsina, J., Wang, L., Sung, Y. J., et al. (2024) · Research Square · doi:10.21203/rs.3.rs-4202125/v1 · Cited by 6

Neurodegeneration emerges at a cellular tipping point between aggregate accumulation and removalPreprint

Cotton, M. W., Venkatesan, S., Beckwith, J. S., Böken, D., Xu, C. K., Fertan, E., Breiter, J. C., Berkowicz, L. E., Salazar, L. S., Schulze, A. T. V., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.09.08.674880 · Cited by 7

DNA Methylation in Aging and Alzheimer's Disease

Cheng, R., Shu, J., Chen, H., Li, M., Cheng, X., & Liu, L. (2024) · Human Brain · doi:10.37819/hb.3.2027 · Cited by 5

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

A network of P-body and Whi3 condensates adjusts cell fate decisions to cellular context

Peskett, T. R., Farcas, A.-M., Lee, S. S., & Barral, Y. (2025) · Molecular Cell · doi:10.1016/j.molcel.2025.09.001 · Cited by 8

The drug discovery and therapeutic nano-strategies targeting cellular senescence

Wang, Y., Liu, M., Chen, X., Wang, S., Li, J., Sun, Y., Zheng, X., Zhang, J.-X., & Li, H. (2025) · Materials Today Bio · doi:10.1016/j.mtbio.2025.102480 · Cited by 6

Multiplex neurodegeneration proteotoxicity platform reveals DNAJB6 promotes non-toxic FUS condensate gelation and inhibits neurotoxicity

Resnick, S. J., Qamar, S., Krishna, P., Korben, V. A., Ausserwöger, H., Miller, A., Esposito, P., Varela, J. A., Sheng, J., Huang, L., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-65178-0 · Cited by 7

Perturbation of multiprotein complexes in skeletal muscle induces protective proteases in the CNS that degrade pathogenic proteins

Rai, M., Baddeley, H. J. E., Chuang, C.-L., Platt, A., Curley, M., Finkelstein, D., & Demontis, F. (2025) · npj Aging · doi:10.1038/s41514-025-00288-z · Cited by 5

The mouse nicotinamide mononucleotide adenylyltransferase chaperones diverse pathological amyloid client proteins

Huang, C., Lu, J., Ma, X., Qiang, J., Wang, C., Liu, C., Fang, Y., Zhang, Y., Jiang, L., Li, D., et al. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.101912 · Cited by 5

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

Biomolecular Markers of Brain Aging

Li, M., An, H., Wang, W., & Wei, D. (2023) · Advances in experimental medicine and biology · doi:10.1007/978-981-99-1627-6_9 · Cited by 7

Elucidation of Site-Specific Ubiquitination on Chaperones in Response to Mutant Huntingtin

Panda, P., Sarohi, V., Basak, T., & Kasturi, P. (2023) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-023-01446-1 · Cited by 5

Systematic analysis of proteome turnover in an organoid model of pancreatic cancer by dSILO

Ross, A. B., Gorhe, D., Kim, J. K., Hodapp, S. J., DeVine, L., Chan, K. M., Chio, I. I. C., Jovanović, M., & Pereira, M. A. (2024) · Cell Reports Methods · doi:10.1016/j.crmeth.2024.100760 · Cited by 5

Systematic Analysis of Biological Processes Reveals Gene Co-expression Modules Driving Pathway Dysregulation in Alzheimer’s Disease

Adeoye, T., Shah, S. I., & Ullah, G. (2024) · Aging and Disease · doi:10.14336/ad.2024.0429 · Cited by 7

Energetics of cosolvent effect on peptide aggregation

Matubayasi, N., & Masutani, K. (2019) · Biophysics and Physicobiology · doi:10.2142/biophysico.16.0_185 · Cited by 5

The Impact of Hidden Structure on Aggregate Disassembly by Molecular Chaperones

Shoup, D. W., Roth, A., Puchalla, J., & Rye, H. S. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.915307 · Cited by 5

Solvatochromic sensors detect proteome aggregation in stressed liver tissues with hepatic cancer and cirrhosis

Jing, B., Li, J., Guo, K., Zeng, L., Sui, J., Zhang, Z., Wang, Z., Jin, H., Sun, J., Xue, Z., et al. (2023) · Journal of Materials Chemistry B · doi:10.1039/d3tb00984j · Cited by 5

MIL-CELL: a tool for multi-scale simulation of yeast replication and prion transmission

Hall, D. R. (2023) · European Biophysics Journal · doi:10.1007/s00249-023-01679-4 · Cited by 5

Broad proteomics analysis of seeding-induced aggregation of α-synuclein in M83 neurons reveals remodeling of proteostasis mechanisms that might contribute to Parkinson’s disease pathogenesis

Lumpkin, C. J., Patel, H., Potts, G. K., Chaurasia, S., Gibilisco, L., Srivastava, G. P., Lee, J. Y., Brown, N. J., Amarante, P., Williams, J. D., et al. (2024) · Molecular Brain · doi:10.1186/s13041-024-01099-1 · Cited by 5

PrP-C1 fragment in cattle brains reveals features of the transmissible spongiform encephalopathy associated PrPsc

Serra, F., Müller, J., Gray, J., Lüthi, R., Dudas, S., Czub, S., & Seuberlich, T. (2017) · Brain Research · doi:10.1016/j.brainres.2017.01.015 · Cited by 5

ATP alters protein folding and function of Escherichia coli uridine phosphorylase

Liu, Y., Lin, T.-H., & Liu, P.-F. (2017) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2017.09.007 · Cited by 5

Urinary Congophilia Confirmed With the CapCord Test Is Associated With Pregnancy Outcomes in Women With Early-Onset Pre-eclampsia

Cai, B., Yuan, X., Li, X., Xu, J., & Du, J. (2021) · Frontiers in Medicine · doi:10.3389/fmed.2021.700157 · Cited by 5

dCubilin/dAMN- mediated protein reabsorption in Drosophila nephrocytes modulates longevity

Feng, X., Hong, X., Fan, Q., Chen, L., Li, J., Deng, J., Gong, S., Hou, F. F., & Zhang, F. (2021) · Disease Models & Mechanisms · doi:10.1242/dmm.047464 · Cited by 5

Inhibitor Combinations Reveal Wiring of the Proteostasis Network in Prostate Cancer Cells

Shkedi, A., Adkisson, M., Schroeder, A., Eckalbar, W. L., Kuo, S.-Y., Neckers, L. Μ., & Gestwicki, J. E. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c01342 · Cited by 5

GPI-anchored Gas1 protein regulates cytosolic proteostasis in budding yeast

Wang, Y., Ruan, L., & Li, R. (2024) · G3 Genes Genomes Genetics · doi:10.1093/g3journal/jkad263 · Cited by 5

Why and How Do We Age? A Single Answer to Two Questions

Golubev, A. G. (2019) · Advances in Gerontology · doi:10.1134/s2079057019010065 · Cited by 5

Quantification of Insoluble Protein Aggregation in Caenorhabditis elegans during Aging with a Novel Data-Independent Acquisition Workflow

Xie, X., Chamoli, M., Bhaumik, D., Sivapatham, R., Angeli, S., Andersen, J. K., Lithgow, G. J., & Schilling, B. (2020) · Journal of Visualized Experiments · doi:10.3791/61366 · Cited by 5

Assessment of the Efficacy of Preventive Therapy with Chaperone Inducer U133 in a Model of the Preclinical Stage of Parkinson’s Disease in Elderly Rats

Belan, D. V., Полоник, С. Г., & Ekimova, I. V. (2021) · Neuroscience and Behavioral Physiology · doi:10.1007/s11055-021-01120-3 · Cited by 5

We Are What We Eat: Ubiquitin–Proteasome System (UPS) Modulation Through Dietary Products

Panagiotidou, E., & Chondrogianni, N. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-38266-7_15 · Cited by 5

Disease-associated protein seeding suggests a dissociation between misfolded protein accumulation and neurodegeneration in prion disease

Alibhai, J. D., Diack, A. B., & Manson, J. C. (2017) · Prion · doi:10.1080/19336896.2017.1378289 · Cited by 5

A multiplex platform to identify mechanisms and modulators of proteotoxicity in neurodegenerationPreprint

Resnick, S. J., Qamar, S., Sheng, J., Huang, L. H., Nixon‐Abell, J., Melore, S. M., Chung, C. W., Li, X., Wang, J., Zhang, N. R., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.09.19.508444 · Cited by 5

The Calpain Proteolytic System

Baudry, M., Su, W., & Bi, X. (2022) · Elsevier eBooks · doi:10.1016/b978-0-12-821618-7.00223-6 · Cited by 5

Systematic Approach Identifies Multiple Transcription Factor Perturbations That Rejuvenate Replicatively Aged Human Skin FibroblastsPreprint

Sengstack, J., Zheng, J., Mobaraki, M., Lin, J., Deng, C., & Li, H. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.11.20.517270 · Cited by 6

Proteostasis is a key driver of the pathogenesis in Apicomplexa

Mitra, P., & Deshmukh, A. S. (2024) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2024.119824 · Cited by 4

Calorie restriction and rapamycin distinctly restore non-canonical ORF translation in the muscles of aging mice

Mittal, N., Ataman, M., Tintignac, L. A. J., Ham, D. J., Jörin, L., Schmidt, A., Sinnreich, M., Rüegg, M. A., & Zavolan, M. (2024) · npj Regenerative Medicine · doi:10.1038/s41536-024-00369-9 · Cited by 6

Xeroderma pigmentosum protein XPD controls caspase-mediated stress responses

Wei, H., Weaver, Y. M., & Weaver, B. P. (2024) · Nature Communications · doi:10.1038/s41467-024-53755-8 · Cited by 4

Proteasome Activators and Ageing: Restoring Proteostasis Using Small Molecules

Upadhyay, A., & Joshi, V. (2024) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-031-66768-8_2 · Cited by 5

Lessons in longevity from blood stem cells under protein stress

Catic, A. (2025) · Trends in Cell Biology · doi:10.1016/j.tcb.2025.06.006 · Cited by 5

Episodic transport of protein aggregates achieves a positive size selectivity in aggresome formation

Fang, R., Bai, L., Verheijen, B. M., Li, B., Dong, K. D., Paulo, J. A., Zhou, M., Chu, Y.-C., Song, Y., Sherman, M. Y., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-62751-5 · Cited by 4

Insolubilome profiling defines molecular features that influence protein insolubility with aging

Stephan, A., Graça, F. A., Pagala, V., Hunt, L. C., Chuang, C.-L., Grime, J., Alford, D., Wang, X., High, A. A., Peng, J., et al. (2026) · Developmental Cell · doi:10.1016/j.devcel.2026.01.015 · Cited by 4

Supervised learning of protein variant effects across large‐scale mutagenesis datasets

Schulze, T. K., Blaabjerg, L. M., Cagiada, M., & Lindorff‐Larsen, K. (2026) · Protein Science · doi:10.1002/pro.70526 · Cited by 11

Multiplexed Photo-Cross-Linking Reveals Comprehensive Midnolin Interactome: Insights into Ubiquitin-Independent Degradation and Functional Diversity

Xu, Y., Zhao, W., Fu, J., Liu, Z., Nie, H., Zhang, J., Guo, J., Tan, M., & Chen, X. (2026) · Journal of the American Chemical Society · doi:10.1021/jacs.5c22099 · Cited by 4

Dietary Bioactives in Alzheimer’s Disease: A Critical Appraisal of Clinical Trials and Future Nutritional Strategies

Kumari, A., & Zeng, X.-A. (2026) · Nutrients · doi:10.3390/nu18060907 · Cited by 4

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-v · Cited by 4

The yeast molecular chaperone, Hsp104, influences transthyretin aggregate formation

Knier, A., Davis, E. E., Buchholz, H. E., Dorweiler, J. E., Flannagan, L. E., & Manogaran, A. L. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.1050472 · Cited by 4

Bovine serum albumin prevents human hemoglobin aggregation and retains its chaperone-like activity

Khan, S. S., & Naeem, A. (2023) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2023.2192802 · Cited by 5

Fountain of youth—Targeting autophagy in aging

Danics, L., Abbas, A. A., Kis, B., & Pircs, K. (2023) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2023.1125739 · Cited by 4

Disruption of Proteostasis by Natural Products and Synthetic Compounds That Induce Pervasive Unfolding of Proteins: Therapeutic Implications

Vilaboa, N. E., López, J. A., de Mesa, M., Escudero-Duch, C., Winfield, N., Bayford, M., & Voellmy, R. W. (2023) · Pharmaceuticals · doi:10.3390/ph16040616 · Cited by 4

Lanosterol elevates cytoprotective response through induced-proteasomal degradation of aberrant proteins

Kinger, S., Jagtap, Y. A., Dubey, A. R., Kumar, P., Choudhary, A., Dhiman, R., Prajapati, V. K., Chitkara, D., Poluri, K. M., & Mishra, A. (2023) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2023.119631 · Cited by 4

Distinct patterns of proteostasis network gene expression are associated with different prognoses in melanoma patients

Wellman, R., Jacobson, D. H., Secrier, M., & Labbadia, J. P. (2024) · Scientific Reports · doi:10.1038/s41598-023-50640-0 · Cited by 4

Evolution and impact of molecular glue research: a bibliometric analysis from 2000 to 2023

Li, D., Cheng, J., Yuan, Z., & Deng, K. (2024) · Frontiers in Oncology · doi:10.3389/fonc.2024.1401257 · Cited by 4

Statistical Survey of Chemical and Geometric Patterns on Protein Surfaces as a Blueprint for Protein‐Mimicking Nanoparticles

(2024) · doi:10.1002/sstr.202400086 · Cited by 4

Non-cell-autonomous regulation of germline proteostasis by insulin/IGF-1 signaling-induced dietary peptide uptake via PEPT-1

Muhammad, T., Edwards, S. L., Morphis, A. C., Johnson, M. V., Oliveira, V., Chamera, T., Liu, S., Nguyen, N. G. T., & Li, J. (2024) · The EMBO Journal · doi:10.1038/s44318-024-00234-x · Cited by 6

The middle domain of Hsp104 can ensure substrates are functional after processing

Buchholz, H. E., Dorweiler, J. E., Guereca, S., Wisniewski, B. T., Shorter, J., & Manogaran, A. L. (2024) · PLoS Genetics · doi:10.1371/journal.pgen.1011424 · Cited by 4

Design principles to tailor Hsp104 therapeutics

Lin, J., Carman, P. J., Gambogi, C. W., Kendsersky, N. M., Chuang, E., Gates, S. N., Yokom, A. L., Rizo, A. N., Southworth, D. R., & Shorter, J. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.115005 · Cited by 4

An Update on the Molecular Pillars of Aging

García‐Velázquez, L., & Arias, C. (2020) · Springer eBooks · doi:10.1007/978-3-030-40955-5_1 · Cited by 4

The Chaperone Inducer U133 Eliminates Anhedonia and Prevents Neurodegeneration in Monoaminergic Emotiogenic Brain Structures in a Preclinical Model of Parkinson’s Disease in Aged Rats

Ekimova, I. V., Пази, М. Б., Belan, D. V., Полоник, С. Г., & Pastukhov, Y. F. (2021) · Journal of Evolutionary Biochemistry and Physiology · doi:10.1134/s0022093021050148 · Cited by 4

The effect of stress on biophysical characteristics of misfolded protein aggregates in living Saccharomyces cerevisiae cells

Schnitzer, B., Welkenhuysen, N., Leake, M. C., Shashkova, S., & Cvijović, M. (2022) · Experimental Gerontology · doi:10.1016/j.exger.2022.111755 · Cited by 4

Longitudinal Serum Protein Analysis of Women with a High Risk of Developing Breast Cancer Reveals Large Interpatient Versus Small Intrapatient Variations: First Results from the TESTBREAST Study

Hagenaars, S. C., Dekker, L. J. M., Ravesteijn, B., van Vlierberghe, R., Romijn, F. P. H. T. M., Verhoeff, L., Witkamp, A. J., Schenk, K., Keymeulen, K., Menke‐Pluijmers, M. B. E., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232012399 · Cited by 4

Myelinosome organelles in pathological retinas: ubiquitous presence and dual role in ocular proteostasis maintenance

Yéfimova, M. (2022) · Neural Regeneration Research · doi:10.4103/1673-5374.355753 · Cited by 4

Nuclear Magnetic Resonance Spectroscopy to Analyse Protein Folding and Dynamics

Saibo, N. V., Boral, S., Saha, R., Das, A. K., & De, S. (2023) · Springer eBooks · doi:10.1007/978-981-99-2079-2_4 · Cited by 4

The GET pathway is a major bottleneck for maintaining proteostasis in Saccharomyces cerevisiae

Josefson, R., Kumar, N., Hao, X., Liu, B., & Nyström, T. (2023) · Scientific Reports · doi:10.1038/s41598-023-35666-8 · Cited by 4

Some mechanistic underpinnings of molecular adaptations of SARS-COV-2 spike protein by integrating candidate adaptive polymorphisms with protein dynamics

Ose, N. J., Campitelli, P., Modi, T., Kazan, I. C., Kumar, S., & Ozkan, S. B. (2023) · eLife · doi:10.7554/elife.92063 · Cited by 9

Molecular Regulation of Transforming Growth Factor-β1-induced Thioredoxin-interacting Protein Ubiquitination and Proteasomal Degradation in Lung Fibroblasts: Implication in Pulmonary Fibrosis

Taleb, S. J., Ye, Q., Baoyinna, B., Dedad, M., Pisini, D., Parinandi, N. L., Cantley, L. C., Zhao, J., & Zhao, Y. (2024) · Journal of Respiratory Biology and Translational Medicine · doi:10.35534/jrbtm.2024.10002 · Cited by 4

Proteostasis impairment in protein-misfolding and -aggregation diseases

Hipp, M. S., Park, S.-H., & Hartl, F. U. (2014) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.05.003 · Cited by 683

Shaping proteostasis at the cellular, tissue, and organismal level

Sala, A. J., Bott, L. C., & Morimoto, R. I. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201612111 · Cited by 256

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

Proteostasis and the Aging Proteome in Health and Disease

Morimoto, R. I., & Cuervo, A. M. (2014) · The Journals of Gerontology Series A: Biological Sciences and Medical Sciences · doi:10.1093/gerona/glu049 · Cited by 277

Functional Modules of the Proteostasis NetworkPreprint

Jayaraj, G. G., Hipp, M. S., & Hartl, F. U. (2019) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a033951 · Cited by 254