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

The Role of SUMOylation and Ubiquitination in Brain Ischaemia: Critical Concepts and Clinical Implications

Bernstock, J. D., Ye, D. G., Estevez, D., Chagoya, G., Wang, Y., Gessler, F. A., Hallenbeck, J. M., & Yang, W. (2019) · Current Issues in Molecular Biology · doi:10.21775/cimb.035.127 · Cited by 10

Programmed Trade-offs in Protein Folding Networks

Pechmann, S. (2020) · Structure · doi:10.1016/j.str.2020.09.009 · Cited by 11

Urea titration of a lipase from Pseudomonas sp. reveals four different conformational states, with a stable partially folded state explaining its high aggregation propensity

Qafary, M., Khajeh, K., Ramazzotti, M., Moosavi‐Movahedi, A. A., & Chiti, F. (2021) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2021.01.153 · Cited by 10

Acute Pharmacological Inhibition of Protein Kinase R-Like Endoplasmic Reticulum Kinase Signaling After Spinal Cord Injury Spares Oligodendrocytes and Improves Locomotor Recovery

Ohri, S. S., Andres, K. R., Howard, R. M., Brown, B. L., Forston, M. D., Hetman, M., & Whittemore, S. R. (2022) · Journal of Neurotrauma · doi:10.1089/neu.2022.0177 · Cited by 11

DNA methylation extends lifespan in the bumblebee Bombus terrestris

Renard, T., Martinet, B., Araujo, N. D. S., & Aron, S. (2023) · Proceedings of the Royal Society B Biological Sciences · doi:10.1098/rspb.2023.2093 · Cited by 11

Alzheimer’s-specific brain amyloid interactome: Neural-network analysis of intra-aggregate crosslinking identifies novel drug targets

Balasubramaniam, M., Ganne, A., Mainali, N., Pahal, S., Ayyadevara, S., & Reis, R. J. S. (2023) · iScience · doi:10.1016/j.isci.2023.108745 · Cited by 9

Ammonia stress-induced heat shock factor 1 enhances white spot syndrome virus infection by targeting the interferon-like system in shrimp

Wang, X., Zhang, H., Gao, J., & Wang, X. (2024) · mBio · doi:10.1128/mbio.03136-23 · Cited by 13

Dysfunction of Protein Quality Control in Parkinsonism–Dementia Complex of Guam

Verheijen, B. M., Oyanagi, K., & van Leeuwen, F. W. (2018) · Frontiers in Neurology · doi:10.3389/fneur.2018.00173 · Cited by 11

MED12 interacts with the heat‐shock transcription factor HSF1 and recruits CDK8 to promote the heat‐shock response in mammalian cells

Srivastava, P., Takii, R., Okada, M., Fujimoto, M., & Nakai, A. (2021) · FEBS Letters · doi:10.1002/1873-3468.14139 · Cited by 10

The CBP-1/p300 Lysine Acetyltransferase Regulates the Heat Shock Response in C. elegans

Barrett, L. N., & Westerheide, S. D. (2022) · Frontiers in Aging · doi:10.3389/fragi.2022.861761 · Cited by 12

Adaptive cellular response of the substantia nigra dopaminergic neurons upon age‐dependent iron accumulation

Kwon, K., Cho, H., Lee, S.-Y., Cho, E. J., Yu, W., Kok, C. Y. L., Je, H. S., Kim, J., Cho, H. J., & Kwon, T. (2022) · Aging Cell · doi:10.1111/acel.13694 · Cited by 9

An engineered, quantifiable in vitro model for analysing the effect of proteostasis-targeting drugs on tissue physical properties

Loaiza, S., Ferreira, S. A., Chinn, T. M., Kirby, A. C., Tsolaki, E., Dondi, C., Parzych, K., Strange, A. P., Bozec, L., Bertazzo, S., et al. (2018) · Biomaterials · doi:10.1016/j.biomaterials.2018.08.041 · Cited by 10

Integration of large-scale multi-omic datasets: A protein-centric view

Rendleman, J., Choi, H., & Vogel, C. (2018) · Current Opinion in Systems Biology · doi:10.1016/j.coisb.2018.09.001 · Cited by 10

High fructose diet induces early mortality via autophagy factors accumulation in the rostral ventrolateral medulla as ameliorated by pioglitazone

Lin, I.-C., Wu, C., Tain, Y., Chen, I., Hung, C., & Wu, K. L. H. (2019) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2019.03.014 · Cited by 10

Influence of Age on Skeletal Muscle Hypertrophy and Atrophy Signaling: Established Paradigms and Unexpected Links

Lee, E. H., & Neppl, R. L. (2021) · Genes · doi:10.3390/genes12050688 · Cited by 11

Proteome-Scale Mapping of Perturbed Proteostasis in Living CellsPreprint

Lam, I., Hallacli, E., & Khurana, V. (2019) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a034124 · Cited by 9

GR chaperone cycle mechanism revealed by cryo-EM: inactivation of GR by GR:Hsp90:Hsp70:Hop client-loading complex

Wang, R. Y.-R., Noddings, C. M., Kirschke, E., Myasnikov, A. G., Johnson, J. L., & Agard, D. A. (2020) · doi:10.1101/2020.11.05.370247 · Cited by 10

Proteolysis of Proteins

Raju, T. S. (2019) · Wiley eBooks · doi:10.1002/9781119053354.ch15 · Cited by 10

Dysregulation of neuroproteasomes by ApoE isoforms drives endogenous Tau aggregationPreprint

Paradise, V., Sabu, M., Bafia, J., Sharif, N., Nguyen, C., Konrad-Vicario, K., Mukim, R. D., Wang, X., Corjuc, B., Fu, J. M., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.11.29.518293 · Cited by 10

Mechanisms of RNA and Protein Quality Control and Their Roles in Cellular Senescence and Age-Related Diseases

Kang, D., Baek, Y., & Lee, J. (2022) · Cells · doi:10.3390/cells11244062 · Cited by 9

The NDR family of kinases: essential regulators of aging

Jonischkies, K., del Ángel, M., Demiray, Y. E., Zambrano, A. L., & Stork, O. (2024) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2024.1371086 · Cited by 9

Rejuvenation Strategy for Inducing and Enhancing Autoimmune Response to Eliminate Senescent Cells

Wang, X., Zhang, C., Su, J., Ren, S., Wang, X., Zhang, Y., Yuan, Z., He, X., Wu, X., Li, M., et al. (2025) · Aging and disease · doi:10.14336/ad.2024.0579 · Cited by 8

The neurotrophic factor MANF regulates autophagy and lysosome function to promote proteostasis in Caenorhabditis elegans

Taylor, S. K. B., Hartman, J. H., & Gupta, B. P. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2403906121 · Cited by 9

Proteostasis in cellular dormancy: lessons from yeast to oocytes

de Souza, S. R., Böke, E., & Zaffagnini, G. (2025) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2025.05.004 · Cited by 10

Chaperone nanomotors with chemotactic ability for the treatment of Parkinson’s disease

Wang, W., Xia, X., Zhang, Z., Zhu, Q., Chen, Y., Zhang, Y., Chen, L., Mao, C., & Wan, M. (2025) · Science Advances · doi:10.1126/sciadv.adw1061 · Cited by 9

Hyperactive 20 S proteasome enhances proteostasis and ERAD in C. elegans via degradation of intrinsically disordered proteins

Salcedo-Tacuma, D., Asad, N., Islam, M. Q., Anderson, R. T., & Smith, D. M. (2025) · Science Advances · doi:10.1126/sciadv.adx3014 · Cited by 12

Fatty acids impact sarcomere integrity through myristoylation and ER homeostasis

Tang, H., Cui, M., & Han, M. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109539 · Cited by 9

Molecular chaperones in DNA repair mechanisms: Role in genomic instability and proteostasis in cancer

Hasan, A., Rizvi, S. F., Parveen, S., & Mir, S. S. (2022) · Life Sciences · doi:10.1016/j.lfs.2022.120852 · Cited by 11

IRE-1 endoribonuclease activity declines early in C. elegans adulthood and is not rescued by reduced reproduction

De‐Souza, E. A., Cummins, N., & Taylor, R. C. (2022) · Frontiers in Aging · doi:10.3389/fragi.2022.1044556 · Cited by 9

Dissipative scaling of development and aging in multicellular organisms

Kriete, A. (2024) · Biosystems · doi:10.1016/j.biosystems.2024.105157 · Cited by 10

The expression system influences stability, maturation efficiency, and oligomeric properties of the potassium-chloride co-transporter KCC2

Kok, M., Hartnett, K. A., Happe, C. L., MacDonald, M. L., Aizenman, E., & Brodsky, J. L. (2024) · Neurochemistry International · doi:10.1016/j.neuint.2024.105695 · Cited by 9

Novel Modulators of Proteostasis: RNAi Screen of Chromosome I in a Heat Stress Paradigm in C. elegans

Kern, A., Spang, N., Huesmann, H., & Behl, C. (2018) · Cells · doi:10.3390/cells7060049 · Cited by 10

Assistance for Folding of Disease-Causing Plasma Membrane Proteins

Juarez-Navarro, K., Ayala‐García, V. M., Ruiz‐Baca, E., Meneses‐Morales, I., Rios-Banuelos, J. L., & López-Rodríguez, A. (2020) · Biomolecules · doi:10.3390/biom10050728 · Cited by 11

Acute Neural and Proteostasis Messenger Ribonucleic Acid Levels Predict Chronic Locomotor Recovery after Contusive Spinal Cord Injury

Ohri, S. S., Burke, D. A., Andres, K. R., Hetman, M., & Whittemore, S. R. (2020) · Journal of Neurotrauma · doi:10.1089/neu.2020.7258 · Cited by 9

Viruses as ‘Truffle Hounds’: Molecular Tools for Untangling Brain Cellular Pathology

Müller‐Schiffmann, A., Trossbach, S. V., Lingappa, V. R., & Korth, C. (2020) · Trends in Neurosciences · doi:10.1016/j.tins.2020.11.004 · Cited by 8

Hypoxia-inducible factor prolyl hydroxylase domain (PHD) inhibition after contusive spinal cord injury does not improve locomotor recovery

Wei, G. Z., Ohri, S. S., Khattar, N. K., Listerman, A. W., Doyle, C. H., Andres, K. R., Karuppagounder, S. S., Ratan, R. R., Whittemore, S. R., & Hetman, M. (2021) · PLoS ONE · doi:10.1371/journal.pone.0249591 · Cited by 9

Lysine245 plays a crucial role in stability and function of glycerol 3‐phosphate dehydrogenase (Gpd1) in Saccharomyces cerevisiae

Pallapati, A., Sirigiri, S. D., Jain, S., Ratnala, V., & Roy, I. (2021) · Journal of Cellular Biochemistry · doi:10.1002/jcb.30125 · Cited by 9

Insights into the Molecular Basis of Genome Stability and Pristine Proteostasis in Naked Mole-Rats

Narayan, V., McMahon, M. E., O’Brien, J. J., McAllister, F. E., & Buffenstein, R. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-65943-1_11 · Cited by 9

Carrying Excess Baggage Can Slowdown Life: Protein Clearance Machineries That Go Awry During Aging and the Relevance of Maintaining Them

Sarkar, A., & Nazir, A. (2021) · Molecular Neurobiology · doi:10.1007/s12035-021-02640-2 · Cited by 10

High-Throughput Analysis of Protein Turnover with Tandem Fluorescent Protein Timers

Fung, J. J., Juárez-Núñez, K. A., & Khmelinskii, A. (2022) · Methods in molecular biology · doi:10.1007/978-1-0716-1732-8_6 · Cited by 8

Understanding the mechanism of amylin aggregation: From identifying crucial segments to tracing dominant sequential events to modeling potential aggregation suppressors

Ghosh, R., Ghosh, S., & Das, A. (2022) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2022.140866 · Cited by 9

An integrative review of nonobvious puzzles of cellular and molecular cardiooncology

Uruski, P., Matuszewska, J., Leśniewska, A., Rychlewski, D., Niklas, A. A., Mikuła‐Pietrasik, J., Tykarski, A., & Książek, K. (2023) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-023-00451-y · Cited by 9

An Overview of the Molecular and Cellular Biomarkers of Aging

Solovev, I. A., Shaposhnikov, M. V., & Moskalev, A. (2019) · Healthy ageing and longevity · doi:10.1007/978-3-030-24970-0_6 · Cited by 9

DMSO-mediated curing of several yeast prion variants involves Hsp104 expression and protein solubilization, and is decreased in several autophagy related gene (atg) mutants

Dorweiler, J. E., Obaoye, J. O., Oddo, M. J., Shilati, F. M., Scheidemantle, G. M., Coleman, T. J., Reilly, J. A., Smith, G. R., & Manogaran, A. L. (2020) · PLoS ONE · doi:10.1371/journal.pone.0229796 · Cited by 9

Manipulating the aggregation activity of human prion-like proteins

Cascarina, S. M., Paul, K. R., & Ross, E. D. (2017) · Prion · doi:10.1080/19336896.2017.1356560 · Cited by 9

Manganese disrupts the maturation and degradation of axonal autophagosome leading to hippocampal synaptic toxicity in mice via the activation of LRRK2 on phosphorylation of Rab10

Ma, Z., Liu, K., Zhang, R.-F., Xie, Z., Liu, W., & Xu, B. (2024) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2024.170021 · Cited by 8

Sensory quiescence induces a cell-non-autonomous integrated stress response curbed by condensate formation of the ATF4 and XRP1 effectors

Shekhar, S., Tracy, C., Lidsky, P. V., Andino, R., Wert, K. J., & Krämer, H. (2025) · Nature Communications · doi:10.1038/s41467-024-55576-1 · Cited by 10

Proteomic and phosphoproteomic signatures of aging mouse liver

Mohallem, R., Schaser, A. J., & Aryal, U. K. (2025) · GeroScience · doi:10.1007/s11357-025-01601-0 · Cited by 7

Interplay Between Aging and Glial Cell Dysfunction: Implications for CNS Health

García‐Domínguez, M. (2025) · Life · doi:10.3390/life15101498 · Cited by 12

The Ambiguous Role of HMGB1 Across the Hallmarks of Aging: A Narrative Review

Ning, M., Liang, Y., Zhang, L., Wang, F., & He, L. (2025) · Clinical Interventions in Aging · doi:10.2147/cia.s550572 · Cited by 8

Suboptimal codon pairs trigger ribosome collisions and cellular quality control responses in tRNA modification mutants

Wu, J., Eggers, C., Sin, O., Koziej, L., Mancilla, H., Mollet, F., Schöler, H. R., Drexler, H. C. A., Ranff, T., Fufezan, C., et al. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf1311 · Cited by 8

Exercise and the hallmarks of cardiovascular aging

Zhong, D., Fernández‐Garcia, B., Gokulnath, P., Lin, K., Li, G., Kroemer, G., López-Otín, C., & Xiao, J. (2026) · Ageing Research Reviews · doi:10.1016/j.arr.2026.103030 · Cited by 8

Epigenetic reprogramming for ocular aging and disease: Mechanisms, biomarkers, and the road to the clinic

Lee, J., Han, M., Wang, K., Butler, L. R., & Sinclair, D. A. (2026) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2026.101442 · Cited by 7

Early-life exposure to polystyrene nanoplastics at ambient doses induces neurotoxicity via mTOR-mediated autophagy-lysosomal dysfunction and proteostasis imbalance

Yang, G., Peng, Y., Li, J., Yang, S., Li, M., Zheng, X., Chen, X., Wan, J., Zhu, Z., Zhang, L., et al. (2026) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2026.141318 · Cited by 8

Regeneration in starved planarians depends on TRiC/CCT subunits modulating the unfolded protein response

Gutiérrez‐Gutiérrez, Ó., Felix, D. A., Salvetti, A., Amro, E. M., Thems, A., Pietsch, S., Koeberle, A., Rudolph, K. L., & González‐Estévez, C. (2021) · EMBO Reports · doi:10.15252/embr.202152905 · Cited by 9

Oxidized low-density lipoprotein causes ribosome reduction and inhibition of protein synthesis in retinal pigment epithelial cells

Giorgianni, F., & Beranová-Giorgianni, Š. (2022) · Biochemistry and Biophysics Reports · doi:10.1016/j.bbrep.2022.101345 · Cited by 8

Astrocytic deletion of protein kinase R‐like ER kinase ( PERK ) does not affect learning and memory in aged mice but worsens outcome from experimental stroke

Lahiri, A., Walton, J. C., Zhang, N., Billington, N., DeVries, A. C., & Meares, G. P. (2023) · Journal of Neuroscience Research · doi:10.1002/jnr.25224 · Cited by 10

Neutrophil-Mediated Progression of Mild Cognitive Impairment to Dementia

Cho, K. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241914795 · Cited by 9

PLK2-mediated phosphorylation of SQSTM1 S349 promotes aggregation of polyubiquitinated proteins upon proteasomal dysfunction

Chen, Y.-D., Lin, X., Ruan, Z.-L., Li, M., Yi, X.-M., Zhang, X., Li, S., & Shu, H. (2024) · Autophagy · doi:10.1080/15548627.2024.2361574 · Cited by 8

Disruption of tRNA biogenesis enhances proteostatic resilience, improves later-life health, and promotes longevity

Malik, Y., Kulaberoglu, Y., Anver, S., Javidnia, S., Borland, G., Diazgranados, R. R., Cranwell, S., Medelbekova, D., Svermova, T., Thomson, J., et al. (2024) · PLoS Biology · doi:10.1371/journal.pbio.3002853 · Cited by 7

CHIP and aging: a key regulator of proteostasis and cellular senescence

Pandey, S. N., Agrawal, N., Moglad, E. H. O., Priya, G. P., Srivastava, M., Chennakesavulu, K., Mohanty, B., Arya, R., Kazmi, I. A., Alzarea, S. I., et al. (2025) · Biogerontology · doi:10.1007/s10522-025-10247-6 · Cited by 8

Early Stage Discovery and Validation of Pharmacological Chaperones for the Correction of Protein Misfolding Diseases

Aubi, O., Knappskog, P. M., & Martı́nez, A. (2018) · Methods in molecular biology · doi:10.1007/978-1-4939-8820-4_18 · Cited by 8

Chaperonins: Nanocarriers with Biotechnological Applications

Pipaón, S., Gragera, M., Bueno-Carrasco, M. T., Diego, J. G.-B., Cantero, M., Cuéllar, J., Fernández-Fernández, M. R., & Valpuesta, J. (2021) · Nanomaterials · doi:10.3390/nano11020503 · Cited by 8

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

Endoplasmic Reticulum Homeostasis and Stress Responses in Caenorhabditis elegans

Lee, S.-K. (2021) · Progress in molecular and subcellular biology · doi:10.1007/978-3-030-67696-4_13 · Cited by 8

Unzipping the Secrets of Amyloid Disassembly by the Human Disaggregase

Franco, A., Velasco‐Carneros, L., Alvarez, N., Orozco, N., Moro, F., Prado, A., & Muga, A. (2021) · Cells · doi:10.3390/cells10102745 · Cited by 8

Hsp40 Affinity to Identify Proteins Destabilized by Cellular Toxicant Exposure

Quanrud, G. M., Montoya, M. R., Mei, L., Awad, M. R., & Genereux, J. C. (2021) · Analytical Chemistry · doi:10.1021/acs.analchem.1c04230 · Cited by 8

Deletion of SERF2 in mice delays embryonic development and alters amyloid deposit structure in the brain

Stroo, E., Janssen, L., Sin, O., Hogewerf, W., Koster, M. H., Harkema, L., Youssef, S. A., Beschörner, N., Wolters, A. H. G., Bakker, B., et al. (2023) · Life Science Alliance · doi:10.26508/lsa.202201730 · Cited by 9

Workshop on Synergies Between Alzheimer’s Research and Clinical Gerontology and Geriatrics: Current Status and Future Directions

Brinkley, T. E., Berger, M., Callahan, K. E., Fieo, R. A., Jennings, L. A., Morris, J. K., Wilkins, H., & Kritchevsky, S. B. (2018) · The Journals of Gerontology Series A · doi:10.1093/gerona/gly041 · Cited by 8

Alterations in Organismal Physiology, Impaired Stress Resistance, and Accelerated Aging inDrosophilaFlies Adapted to Multigenerational Proteome Instability

Manola, M. S., Tsakiri, E. N., & Trougakos, I. P. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/7823285 · Cited by 7

Theoretical and computational advances in protein misfolding

Biswas, P. (2019) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2019.08.010 · Cited by 8

Protein homeostasis and disease

Pey, A. L. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-819132-3.00002-6 · Cited by 9

Studying heat shock proteins through single-molecule mechanical manipulation

Choudhary, D., Mediani, L., Carra, S., & Cecconi, C. (2020) · Cell Stress and Chaperones · doi:10.1007/s12192-020-01096-y · Cited by 8

Tempus fugit: How time flies during development

Iwata, R., & Vanderhaeghen, P. (2020) · Science · doi:10.1126/science.abe0953 · Cited by 10

Loss of an extensive ciliary connectome induces proteostasis and cell fate switching in a severe motile ciliopathyPreprint

Brody, S. L., Pan, J., Huang, T., Xu, J., Xu, H., Koenitizer, J., Brennan, S. K., Nanjundappa, R., Saba, T. G., Berical, A. C., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.03.20.585965 · Cited by 8

Clearance of protein aggregates during cell divisionPreprint

Du, S., Wang, Y., Chen, B., Xie, S., Chan, K. Y., Hay, D. C., & Chew, T. G. (2024) · eLife · doi:10.7554/elife.96675.4 · Cited by 9

E3 ligase recruitment by UBQLN2 protects substrates from proteasomal degradationPreprint

Scheutzow, A., Thanthirige, S., Siffer, G., Sorkin, A. D., & Wohlever, M. L. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.07.04.602059 · Cited by 6

Comprehensive degron mapping in human transcription factors

Larsen, F. B., Voutsinos, V., Jonsson, N., Johansson, K. E., Ethelberg, F. D., Henrichs, I. K., Lindorff‐Larsen, K., & Hartmann‐Petersen, R. (2026) · Science Advances · doi:10.1101/2025.05.16.654404 · Cited by 8

G-quadruplex DNA and RNA in cellular senescence

Escarcega, R. D., Marshall, P. R., & Tsvetkov, A. S. (2024) · Frontiers in Aging · doi:10.3389/fragi.2024.1491389 · Cited by 9

HLH ‐30/ TFEB Rewires the Chaperone Network to Promote Proteostasis Upon Perturbations to the Coenzyme A and Iron–Sulfur Cluster Biosynthesis Pathways

Shalash, R., Solomon, D. M., Levi‐Ferber, M., von Chrzanowski, H., Atrash, M. K., Nakar, B., Avivi, M. Y., Hauschner, H., Swisa, A., Meléndez, A., et al. (2025) · Aging Cell · doi:10.1111/acel.70038 · Cited by 9

Thermodynamic stability modulates chaperone-mediated disaggregation of α-synuclein fibrils

Fricke, C., Kunka, A., Norrild, R. K., Wang, S., Dang, T. L., Folke, J., Shahnawaz, M., Soto, C. A., Aznar, S., Wentink, A. S., et al. (2025) · Chemical Science · doi:10.1039/d5sc04927j · Cited by 7

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Advances in Research on Down Syndrome

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