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

Proteostasis and Mitochondrial Role on Psychiatric and Neurodegenerative Disorders: Current Perspectives

Olivero, P., Lozano, C., Sotomayor‐Zárate, R., Meza-Concha, N., Marcelo Arancibia, M., Córdova, C., González‐Arriagada, W. A., Ramírez-Barrantes, R., & Marchant, I. (2018) · Neural Plasticity · doi:10.1155/2018/6798712 · Cited by 19

Biological Evaluation and In Silico Study of Benzoic Acid Derivatives from Bjerkandera adusta Targeting Proteostasis Network Modules

Georgousaki, K., Tsafantakis, N., Gumeni, S., Lambrinidis, G., González-Menéndez, V., Tormo, J. R., Genilloud, O., Trougakos, I. P., & Fokialakis, N. (2020) · Molecules · doi:10.3390/molecules25030666 · Cited by 20

J-domain proteins interaction with neurodegenerative disease-related proteins

Ayala, S., & Kirstein, J. (2021) · Experimental Cell Research · doi:10.1016/j.yexcr.2021.112491 · Cited by 21

Emerging molecular mediators and targets for age-related skeletal muscle atrophy

Brown, L. A., Guzman, S. D., & Brooks, S. V. (2020) · Translational research · doi:10.1016/j.trsl.2020.03.001 · Cited by 22

Human chaperones untangle fibrils of the Alzheimer protein TauPreprint

Ferrari, L., Geerts, W. J. C., van Wezel, M. D., Kos, R., Konstantoulea, A., van Bezouwen, L. S., Förster, F. G., & Rüdiger, S. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/426650 · Cited by 19

Endoplasmic reticulum stress-induced senescence in human lung fibroblasts

Ngassie, M. L. K., Drake, L. Y., Roos, B. B., Koenig-Kappes, A., Pabelick, C. M., Gosens, R., Brandsma, C., Burgess, J. K., & Prakash, Y. S. (2024) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00264.2023 · Cited by 21

The ubiquitin-conjugating enzyme UBE2D maintains a youthful proteome and ensures protein quality control during aging by sustaining proteasome activity

Hunt, L. C., Curley, M., Nyamkondiwa, K., Stephan, A., Jiao, J., Kavdia, K., Pagala, V., Peng, J., & Demontis, F. (2025) · PLoS Biology · doi:10.1371/journal.pbio.3002998 · Cited by 20

The glymphatic system

Ghanizada, H., & Nedergaard, M. (2025) · Handbook of clinical neurology · doi:10.1016/b978-0-443-19104-6.00006-1 · Cited by 22

Recombinant production and purification of the human protein Tau

Ferrari, L., & Rüdiger, S. (2018) · Protein Engineering Design and Selection · doi:10.1093/protein/gzz010 · Cited by 17

A Drosophila model of neuronal ceroid lipofuscinosis CLN4 reveals a hypermorphic gain of function mechanism

Imler, E., Pyon, J. S., Kindelay, S. M., Torvund, M., Zhang, Y.-Q., Chandra, S. S., & Zinsmaier, K. E. (2019) · eLife · doi:10.7554/elife.46607 · Cited by 17

Acceleration of ageing via disturbing mTOR‐regulated proteostasis by a new ageing‐associated gene PC4

Chen, L., Liao, F., Wu, J., Wang, Z., Jiang, Z., Zhang, C., Luo, P., Ma, L., Gong, Q., Wang, Y., et al. (2021) · Aging Cell · doi:10.1111/acel.13370 · Cited by 17

Targeting Chaperone/Co-Chaperone Interactions with Small Molecules: A Novel Approach to Tackle Neurodegenerative Diseases

Wang, L., Bergkvist, L., Kumar, R., Winblad, B. G., & Pavlov, P. F. (2021) · Cells · doi:10.3390/cells10102596 · Cited by 21

Accelerated Cardiac Aging in Patients With Congenital Heart Disease

Iacobazzi, D., Alvino, V. V., Caputo, M., & Madeddu, P. R. (2022) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2022.892861 · Cited by 19

Capturing the conversion of the pathogenic alpha-1-antitrypsin fold by ATF6 enhanced proteostasis

Sun, S., Wang, C., Zhao, P., Kline, G. M., Grandjean, J. M. D., Jiang, X. J., Labaudinière, R. F., Wiseman, R. L., Kelly, J. W., & Balch, W. E. (2023) · Cell chemical biology · doi:10.1016/j.chembiol.2022.12.004 · Cited by 21

Chp1 is a dedicated chaperone at the ribosome that safeguards eEF1A biogenesis

Minoia, M., Quintana-Cordero, J., Jetzinger, K., Kotan, I., Turnbull, K. J., Ciccarelli, M., Masser, A. E., Liebers, D., Gouarin, E., Czech, M., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-45645-w · Cited by 18

Adding intrinsically disordered proteins to biological ageing clocks

Dormann, D., & Lemke, E. A. (2024) · Nature Cell Biology · doi:10.1038/s41556-024-01423-w · Cited by 23

Cellular senescence: from homeostasis to pathological implications and therapeutic strategies

Li, C., Yuan, Y., Jia, Y., Zhou, Q., Wang, Q., & Jiang, X. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1534263 · Cited by 21

Possible Function of Molecular Chaperones in Diseases Caused by Propagating Amyloid Aggregates

Lazarev, V. F., Mikhaylova, E. R., Guzhova, I. V., & Margulis, B. A. (2017) · Frontiers in Neuroscience · doi:10.3389/fnins.2017.00277 · Cited by 19

Deletion of Long Isoform of Eukaryotic Elongation Factor 1Bδ Leads to Audiogenic Seizures and Aversive Stimulus-Induced Long-Lasting Activity Suppression in Mice

Kaitsuka, T., Kiyonari, H., Shiraishi, A., Tomizawa, K., & Matsushita, M. (2018) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2018.00358 · Cited by 19

Advanced proteomics approaches to unravel protein homeostasis

Grandi, P., & Bantscheff, M. (2019) · Drug Discovery Today Technologies · doi:10.1016/j.ddtec.2019.02.001 · Cited by 19

Aging-Related Molecular Pathways in Chronic Cholestatic Conditions

Pinto, C., Ninfole, E., Benedetti, A., Maroni, L., & Marzioni, M. (2020) · Frontiers in Medicine · doi:10.3389/fmed.2019.00332 · Cited by 18

Adaptability of the ubiquitin-proteasome system to proteolytic and folding stressors

Work, J. J., & Brandman, O. (2020) · The Journal of Cell Biology · doi:10.1083/jcb.201912041 · Cited by 19

Targeting DNA topoisomerases or checkpoint kinases results in an overload of chaperone systems, triggering aggregation of a metastable subproteome

Huiting, W., Dekker, S. L., van der Lienden, J. C., Mergener, R., Musskopf, M. K., Furtado, G. V., Gerrits, E., Coit, D., Oghbaie, M., Stefano, L. H. D., et al. (2022) · eLife · doi:10.7554/elife.70726 · Cited by 20

Influence of anaerobic and aerobic exercise on age-related pathways in skeletal muscle

Navas‐Enamorado, I., Bernier, M., Brea‐Calvo, G., & de Cabo, R. (2017) · Ageing Research Reviews · doi:10.1016/j.arr.2017.04.005 · Cited by 21

Putative novel CSF biomarkers of Alzheimer’s disease based on the novel concept of generic protein misfolding and proteotoxicity: the PRAMA cohort

Bigi, A., Fani, G., Bessi, V., Napolitano, L., Bagnoli, S., Ingannato, A., Neri, L., Cascella, R., Matteini, P., Sorbi, S., et al. (2024) · Translational Neurodegeneration · doi:10.1186/s40035-024-00405-0 · Cited by 18

HSF-1 promotes longevity through ubiquilin-1-dependent mitochondrial network remodelling

Erinjeri, A. P., Wang, X., Williams, R., Chiozzi, R. Z., Thalassinos, K., & Labbadia, J. P. (2024) · Nature Communications · doi:10.1038/s41467-024-54136-x · Cited by 20

Dog Aging: A Comprehensive Review of Molecular, Cellular, and Physiological Processes

Guelfi, G., Capaccia, C., Tedeschi, M., Bufalari, A., Leonardi, L., Cenci-Goga, B. T., & Maranesi, M. (2024) · Cells · doi:10.3390/cells13242101 · Cited by 22

Targeting EDEM protects against ER stress and improves development and survival in C. elegans

Ghenea, S., Chiritoiu‐Butnaru, M., Tăcutu, R., Miranda‐Vizuete, A., & Petrescu, S. M. (2022) · PLoS Genetics · doi:10.1371/journal.pgen.1010069 · Cited by 19

The Long-Term Culture of Human Fibroblasts Reveals a Spectroscopic Signature of Senescence

Magalhães, S., Almeida, I., Pereira, C. D., Rebelo, S., Goodfellow, B. J., & Nunes, A. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23105830 · Cited by 21

Cell Non-autonomous Proteostasis Regulation in Aging and Disease

Ferreira, J. V., Soares, A. D. R., & Pereira, P. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2022.878296 · Cited by 19

The Proteostasis Network: A Global Therapeutic Target for Neuroprotection after Spinal Cord Injury

Whittemore, S. R., Ohri, S. S., Forston, M. D., Wei, G. Z., & Hetman, M. (2022) · Cells · doi:10.3390/cells11213339 · Cited by 18

Contribution of Extracellular Vesicles and Molecular Chaperones in Age-Related Neurodegenerative Disorders of the CNS

Noori, L., Filip, K., Nazmara, Z., Mahakizadeh, S., Hassanzadeh, G., Bavisotto, C. C., Bucchieri, F., Marino, A., Cappello, F., Wnuk, M., et al. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24020927 · Cited by 18

Thermodynamic Bounds on the Ultra- and Infra-affinity of Hsp70 for Its Substrates

Nguyen, B., Hartich, D., Seifert, U., & Rios, P. D. L. (2017) · Biophysical Journal · doi:10.1016/j.bpj.2017.06.010 · Cited by 18

Hsp83 loss suppresses proteasomal activity resulting in an upregulation of caspase-dependent compensatory autophagy

Choutka, C., DeVorkin, L., Go, N. E., Hou, Y. C., Moradian, A., Morin, G. B., & Gorski, S. M. (2017) · Autophagy · doi:10.1080/15548627.2017.1339004 · Cited by 19

Identification of proteins interacting with the mitochondrial small heat shock protein Hsp22 of Drosophila melanogaster: Implication in mitochondrial homeostasis

Dabbaghizadeh, A., Morrow, G., Amer, Y. O., Chatelain, É. H., Pichaud, N., & Tanguay, R. M. (2018) · PLoS ONE · doi:10.1371/journal.pone.0193771 · Cited by 18

AGGRESCAN3D: Toward the Prediction of the Aggregation Propensities of Protein Structures

Pujols, J., Peña‐Díaz, S., & Ventura, S. (2018) · Methods in molecular biology · doi:10.1007/978-1-4939-7756-7_21 · Cited by 18

Structural and functional insights on the roles of molecular chaperones in the mistargeting and aggregation phenotypes associated with primary hyperoxaluria type I

Fernández-Higuero, J. Á., Betancor-Fernández, I., Mesa‐Torres, N., Muga, A., SALIDO, E. C., & Pey, A. L. (2018) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2018.09.003 · Cited by 16

Mass Spectrometry-Based Proteomics to Define Intracellular Collagen Interactomes

Doan, N., DiChiara, A. S., Rosario, A. M. D., Schiavoni, R. P., & Shoulders, M. D. (2019) · Methods in molecular biology · doi:10.1007/978-1-4939-9095-5_7 · Cited by 18

Free-energy analysis of the hydration and cosolvent effects on the β-sheet aggregation through all-atom molecular dynamics simulation

Masutani, K., Yamamori, Y., Kim, K., & Matubayasi, N. (2019) · The Journal of Chemical Physics · doi:10.1063/1.5088395 · Cited by 18

Sorting out how Msp1 maintains mitochondrial membrane proteostasis

Fresenius, H. L., & Wohlever, M. L. (2019) · Mitochondrion · doi:10.1016/j.mito.2019.07.011 · Cited by 17

Proteostasis in Cerebral Small Vessel Disease

Haffner, C. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.01142 · Cited by 17

Stem cell aging: The upcoming era of proteins and metabolites

Schüler, S. C., Gebert, N., & Ori‬‬, A. (2020) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2020.111288 · Cited by 18

FoxO1 Is a Novel Regulator of 20S Proteasome Subunits Expression and Activity

Καπετάνου, Μ., Nespital, T., Tain, L. S., Pahl, A., Partridge, L., & Gonos, E. S. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.625715 · Cited by 19

Chronic temperature stress inhibits reproduction and disrupts endocytosis via chaperone titration in Caenorhabditis elegans

Plagens, R. N., Mossiah, I., Guisbert, K. S. K., & Guisbert, E. (2021) · BMC Biology · doi:10.1186/s12915-021-01008-1 · Cited by 19

An Expanded Polyproline Domain Maintains Mutant Huntingtin Soluble in vivo and During Aging

Pigazzini, M. L., Lawrenz, M., Margineanu, A., Schierle, G. S. K., & Kirstein, J. (2021) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2021.721749 · Cited by 20

Role of misfolding in rare enzymatic deficits and use of pharmacological chaperones as therapeutic approach

Pampalone, G., Grottelli, S., Gatticchi, L., Lombardi, E. M., Bellezza, I., & Cellini, B. (2021) · Frontiers in Bioscience-Landmark · doi:10.52586/5056 · Cited by 18

Targeting Estrogen Signaling in the Radiation-induced Neurodegeneration: A Possible Role of Phytoestrogens

Mitra, S., Dash, R., Sohel, M., Chowdhury, A., Munni, Y. A., Ali, M. C., Hannan, M. A., Islam, T., & Moon, I. S. (2022) · Current Neuropharmacology · doi:10.2174/1570159x20666220310115004 · Cited by 19

IRE1α–XBP1 safeguards hematopoietic stem and progenitor cells by restricting pro-leukemogenic gene programs

Barton, B. M., Son, F., Verma, A., Bal, S. K., Tang, Q., Wang, R., Umphred-Wilson, K., Khan, R., Trichka, J., Dong, H., et al. (2025) · Nature Immunology · doi:10.1038/s41590-024-02063-w · Cited by 18

Addressing osteoblast senescence: Molecular pathways and the frontier of anti‐ageing treatments

Zhang, Z., Liu, P., Song, Y., Ma, L., Xu, Y., Lei, J., Tong, B., Zhu, D., Liang, H., Wang, H., et al. (2025) · Clinical and Translational Medicine · doi:10.1002/ctm2.70417 · Cited by 20

Microglia in Brain Aging and Age-Related Diseases: Friends or Foes?

Ishikawa, K., Fujikawa, R., Okita, K., Kimura, F., Watanabe, T., Katsurabayashi, S., & Iwasaki, K. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms262311494 · Cited by 18

Crystal and solution structures of human protein-disulfide isomerase-like protein of the testis (PDILT) provide insight into its chaperone activity

Li, H., Yang, K. S., Wang, W., Niu, Y., Li, J., Dong, Y., Liu, Y., Wang, C.-C., Wang, L., & Liang, H. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.797290 · Cited by 17

A unique chaperoning mechanism in class A JDPs recognizes and stabilizes mutant p53

Zoltsman, G., Dang, T. L., Kuchersky, M., Faust, O., Silva, M. S., Ilani, T., Wentink, A. S., Bukau, B., & Rosenzweig, R. (2024) · Molecular Cell · doi:10.1016/j.molcel.2024.02.018 · Cited by 18

The hexosamine biosynthetic pathway rescues lysosomal dysfunction in Parkinson’s disease patient iPSC derived midbrain neurons

Wani, W. Y., Zunke, F., Belur, N. R., & Mazzulli, J. R. (2024) · Nature Communications · doi:10.1038/s41467-024-49256-3 · Cited by 17

Regulation of physiological and pathological condensates by molecular chaperones

Akaree, N., Secco, V., Levy‐Adam, F., Younis, A., Carra, S., & Shalgi, R. (2025) · FEBS Journal · doi:10.1111/febs.17390 · Cited by 17

Impaired capacity to restore proteostasis in the aged brain after ischemia: Implications for translational brain ischemia research

Wang, Z., & Yang, W. (2018) · Neurochemistry International · doi:10.1016/j.neuint.2018.12.018 · Cited by 17

Combining molecular dynamics simulations and experimental analyses in protein misfolding

Wille, H., Dorosh, L., Amidian, S., Schmitt‐Ulms, G., & Stepanova, M. (2019) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2019.10.001 · Cited by 17

Mapping the gene network landscape of Alzheimer’s disease through integrating genomics and transcriptomics

Rosenthal, S. B., Wang, H., Shi, D., Liu, C., Abagyan, R. A., McEvoy, L. K., & Chen, C. (2022) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1009903 · Cited by 18

Multiple functionalities of molecular chaperones revealed through systematic mapping of their interaction networks

Rizzolo, K., & Houry, W. A. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.tm118.002805 · Cited by 17

Targeting mitochondrial autophagy for anti-aging

Shan, W., Liu, Y., Tang, R., Li, L., Yang, H., & Lin, L. (2025) · Cell Death Discovery · doi:10.1038/s41420-025-02913-y · Cited by 19

Slowed Protein Turnover in Aging Drosophila Reflects a Shift in Cellular Priorities

Vincow, E. S., Thomas, R. E., Merrihew, G. E., MacCoss, M. J., & Pallanck, L. J. (2021) · The Journals of Gerontology Series A · doi:10.1093/gerona/glab015 · Cited by 17

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

Temporal differences of neurodevelopment processes between species

Iwata, R. (2021) · Neuroscience Research · doi:10.1016/j.neures.2021.08.004 · Cited by 14

HSF1 and Its Role in Huntington’s Disease Pathology

Kim, H., & Gómez‐Pastor, R. (2022) · Advances in experimental medicine and biology · doi:10.1007/5584_2022_742 · Cited by 21

Cellular liquid–liquid phase separation: Concept, functions, regulations, and detections

Che, X., Wu, J., Liu, H., Su, J., & Chen, X. (2023) · Journal of Cellular Physiology · doi:10.1002/jcp.30980 · Cited by 16

The Metabolostasis Network and the Cellular Depository of Aggregation‐Prone Metabolites

Levkovich, S. A., Gazit, E., & Bar‐Yosef, D. L. (2023) · Angewandte Chemie International Edition · doi:10.1002/anie.202217622 · Cited by 16

Proteostasis in T cell aging

Gressler, A. E., Leng, H., Zinecker, H., & Simon, A. K. (2023) · Seminars in Immunology · doi:10.1016/j.smim.2023.101838 · Cited by 15

Proteostasis defects: Medicinal challenges of imperfect aging & neurodegeneration

Kumar, P., Choudhary, A., Kinger, S., Jagtap, Y. A., Dubey, A. R., Gutti, R. K., Chitkara, D., Suresh, A. K., & Mishra, A. (2023) · Translational Medicine of Aging · doi:10.1016/j.tma.2023.09.001 · Cited by 16

Modulating Stress Proteins in Response to Therapeutic Interventions for Parkinson’s Disease

Silvestro, S., Raffaele, I., & Mazzon, E. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242216233 · Cited by 19

Protein Misfolding in Pregnancy: Current Insights, Potential Mechanisms, and Implications for the Pathogenesis of Preeclampsia

Fagla, B. M., & Buhimschi, I. A. (2024) · Molecules · doi:10.3390/molecules29030610 · Cited by 17

Unraveling the Connection: Pain and Endoplasmic Reticulum Stress

Kawanaka, R., Jin, H., & Aoe, T. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25094995 · Cited by 18

P-hydroxybenzaldehyde protects Caenorhabditis elegans from oxidative stress and β-amyloid toxicity

Yu, X., Tao, J., Xiao, T., & Duan, X. (2024) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2024.1414956 · Cited by 16

Locked in a vicious cycle: the connection between genomic instability and a loss of protein homeostasis

Huiting, W., & Bergink, S. (2020) · Genome Instability & Disease · doi:10.1007/s42764-020-00027-6 · Cited by 17

The amino acid substitution affects cellular response to mistranslation

Berg, M. D., Zhu, Y., Ruiz, B. Y., Loll‐Krippleber, R., Isaacson, J., Luis, B.-J. S., Genereaux, J. L., Boone, C. M., Villén, J., Brown, G. W., et al. (2021) · G3 Genes Genomes Genetics · doi:10.1093/g3journal/jkab218 · Cited by 18

Hidden information on protein function in censuses of proteome foldedness

Cox, D., Ang, C.-S., Nillegoda, N. B., Reid, G. E., & Hatters, D. M. (2022) · Nature Communications · doi:10.1038/s41467-022-29661-2 · Cited by 16

Systemic immunoglobulin light chain amyloidosis

(2018) · Nature Reviews Disease Primers · doi:10.1038/s41572-018-0040-5 · Cited by 16

Targeting immunoproteasome in neurodegeneration: A glance to the future

Tundo, G. R., Cascio, P., Milardi, D., Santoro, A. M., Graziani, G., Lacal, P. M., Bocedi, A., Oddone, F., Parravano, M., Coletta, A., et al. (2022) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2022.108329 · Cited by 19

Proteostasis network deregulation signatures as biomarkers for pharmacological disease intervention

Brehme, M., Sverchkova, A., & Voisine, C. (2019) · Current Opinion in Systems Biology · doi:10.1016/j.coisb.2019.03.008 · Cited by 16

Regular Exercise Participation Contributes to Better Proteostasis, Inflammatory Profile, and Vasoactive Profile in Patients With Hypertension

Teixeira, M., Gouveia, M., Duarte, A., Ferreira, M., Simões, M. I., Conceição, M., Silva, G., Magalhães, S., Ferreira, R. M., Nunes, A., et al. (2019) · American Journal of Hypertension · doi:10.1093/ajh/hpz160 · Cited by 16

Cystic fibrosis transmembrane conductance regulator (CFTR) and autophagy: hereditary defects in cystic fibrosis versus gluten-mediated inhibition in celiac disease

Maiuri, L., Raia, V., Piacentini, M., Tosco, A., Villella, V. R., & Kroemer, G. (2019) · Oncotarget · doi:10.18632/oncotarget.27037 · Cited by 16

HUWE1 Amplifies Ubiquitin Modifications to Broadly Stimulate Clearance of Proteins and AggregatesPreprint

Zhou, M., Fang, R., Colson, L., Donovan, K. A., Hunkeler, M., Song, Y., Zhang, C. M., Chen, S.-Y., Lee, D. H., Bradshaw, G. A., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.05.30.542866 · Cited by 16

Apigenin enhancing oxidative resistance and proteostasis to extend lifespan via PTEN-mediated AKT signalling pathway

Sun, Z., Li, L., & Zhang, L. (2025) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2025.167670 · Cited by 16

Viral Evolution Shaped by Host Proteostasis Networks

Yoon, J., Patrick, J. E., Ogbunugafor, C. B., & Shoulders, M. D. (2023) · Annual Review of Virology · doi:10.1146/annurev-virology-100220-112120 · Cited by 13

Protein aggregation: A detrimental symptom or an adaptation mechanism?

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