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

Accumulation of “Old Proteins” and the Critical Need for MS‐based Protein Turnover Measurements in Aging and Longevity

Basisty, N., Holtz, A. N., & Schilling, B. (2019) · PROTEOMICS · doi:10.1002/pmic.201800403 · Cited by 29

Individualized management of genetic diversity in Niemann-Pick C1 through modulation of the Hsp70 chaperone system

Wang, C., Scott, S. M., Sun, S., Zhao, P., Hutt, D. M., Shao, H., Gestwicki, J. E., & Balch, W. E. (2019) · Human Molecular Genetics · doi:10.1093/hmg/ddz215 · Cited by 26

Crosstalk between the DNA damage response and cellular senescence drives aging and age-related diseases

Ahmad, A., Braden, A. A., Khan, S., Xiao, J., & Khan, M. M. (2024) · Seminars in Immunopathology · doi:10.1007/s00281-024-01016-7 · Cited by 31

Intersection of Sleep Disorders and Parkinson Disease: Unveiling the Bidirectional Relationship

Antelmi, E., Lanza, G., Mogavero, M. P., Mingolla, G. P., Plazzi, G., Ferini‐Strambi, L., Ferri, R., & Tinazzi, M. (2024) · Movement Disorders Clinical Practice · doi:10.1002/mdc3.14254 · Cited by 29

Glutamatergic nervous system degeneration in a C. elegans TauA152T tauopathy model involves pathways of excitotoxicity and Ca2+ dysregulation

Choudhary, B. C., Mandelkow�, E., Mandelkow, E.-M., & Pir, G. J. (2018) · Neurobiology of Disease · doi:10.1016/j.nbd.2018.06.005 · Cited by 26

Synaptic proteostasis in Parkinson's disease

Nachman, E., & Verstreken, P. (2021) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2021.09.001 · Cited by 27

The loss of cardiac SIRT3 decreases metabolic flexibility and proteostasis in an age-dependent manner

Li, P., Newhardt, M. F., Matsuzaki, S., Eyster, C. A., Pranay, A., Peelor, F. F., Batushansky, A., Kinter, C. S., Subramani, K., SUBRAHMANIAN, S. M., et al. (2022) · GeroScience · doi:10.1007/s11357-022-00695-0 · Cited by 27

Loss of regulation of protein synthesis and turnover underpins an attenuated stress response in senescent human mesenchymal stem cells

Llewellyn, J., Mallikarjun, V., Appleton, E., Osipova, M., Gilbert, H. T. J., Richardson, S. M., Hubbard, S. J., & Swift, J. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2210745120 · Cited by 30

Blue light receptor CRY1 regulates HSFA1d nuclear localization to promote plant thermotolerance

Gao, J., Zhang, R., Zheng, L., Song, L., Ji, M., Li, S., Wang, J., Yang, J., Kang, G., Zhang, P., et al. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.113117 · Cited by 26

Understanding and predicting protein misfolding and aggregation: Insights from proteomics

Pallarès, I., & Ventura, S. (2016) · PROTEOMICS · doi:10.1002/pmic.201500529 · Cited by 26

Cochaperones enable Hsp70 to use ATP energy to stabilize native proteins out of the folding equilibrium

Xu, H. (2018) · Scientific Reports · doi:10.1038/s41598-018-31641-w · Cited by 26

Amyloid-beta Degradation and Neuroprotection of Dauricine Mediated by Unfolded Protein Response in a Caenorhabditis elegans Model of Alzheimer’s disease

Pu, Z., Ma, S., Wang, L., Li, M., Shang, L., Luo, Y., & Chen, W. (2018) · Neuroscience · doi:10.1016/j.neuroscience.2018.09.022 · Cited by 26

Autophagy suppresses the pathogenic immune response to dietary antigens in cystic fibrosis

Villella, V. R., Esposito, S., Ferrari, E., Monzani, R., Tosco, A., Rossin, F., Castaldo, A., Silano, M., Marseglia, G. L., Romani, L. R., et al. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-1500-x · Cited by 26

Regulation of the 20S Proteasome by a Novel Family of Inhibitory Proteins

Olshina, M. A., Arkind, G., Deshmukh, F. K., Fainer, I., Taranavsky, M., Hayat, D., Ben‐Dor, S., Ben‐Nissan, G., & Sharon, M. (2020) · Antioxidants and Redox Signaling · doi:10.1089/ars.2019.7816 · Cited by 26

Peptidylprolylisomerases, Protein Folders, or Scaffolders? The Example of FKBP51 and FKBP52

Rein, T. (2020) · BioEssays · doi:10.1002/bies.201900250 · Cited by 25

Hsf1 and the molecular chaperone Hsp90 support a ‘rewiring stress response’ leading to an adaptive cell size increase in chronic stress

Maiti, S., Bhattacharya, K., Wider, D., Hany, D., Panasenko, O. O., Bernasconi, L., Hulo, N., & Picard, D. (2023) · eLife · doi:10.7554/elife.88658 · Cited by 31

The Indirubin Derivative 6-Bromoindirubin-3′-Oxime Activates Proteostatic Modules, Reprograms Cellular Bioenergetic Pathways, and Exerts Antiaging Effects

Tsakiri, E. N., Gaboriaud‐Kolar, N., Iliaki, K. K., Tchoumtchoua, J., Papanagnou, E., Chatzigeorgiou, S., Tallas, K. D., Mikros, E., Halabalaki, M., Skaltsounis, A., et al. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2016.6910 · Cited by 25

CUL4-DDB1-CRBN E3 Ubiquitin Ligase Regulates Proteostasis of ClC-2 Chloride Channels: Implication for Aldosteronism and Leukodystrophy

Fu, S.-J., Hu, M., Peng, Y.-J., Fang, H.-Y., Hsiao, C.-T., Chen, T., Jeng, C., & Tang, C. (2020) · Cells · doi:10.3390/cells9061332 · Cited by 25

The proteostasis guardian HSF1 directs the transcription of its paralog and interactor HSF2 during proteasome dysfunction

Santopolo, S., Riccio, A., Rossi, A., & Santoro, M. G. (2020) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03568-x · Cited by 25

Influence of Subcellular Localization and Functional State on Protein Turnover

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

HSF-1: Guardian of the Proteome Through Integration of Longevity Signals to the Proteostatic Network

Lázaro‐Peña, M. I., Ward, Z. C., Yang, S., Strohm, A. O., Merrill, A. K., Soto, C. A., & Samuelson, A. V. (2022) · Frontiers in Aging · doi:10.3389/fragi.2022.861686 · Cited by 27

Emerging links between endoplasmic reticulum stress responses and acute kidney injury

Porter, A. W., Brodsky, J. L., & Buck, T. M. (2022) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00370.2022 · Cited by 25

Translation is an emerging constraint on protein homeostasis in ageing

Llewellyn, J., Hubbard, S. J., & Swift, J. (2024) · Trends in Cell Biology · doi:10.1016/j.tcb.2024.02.001 · Cited by 26

Derailed Proteostasis as a Determinant of Cardiac Aging

Wiersma, M., Henning, R. H., & Brundel, B. J. J. M. (2016) · Canadian Journal of Cardiology · doi:10.1016/j.cjca.2016.03.005 · Cited by 26

A Novel Microtubule-Binding Drug Attenuates and Reverses Protein Aggregation in Animal Models of Alzheimer’s Disease

Kakraba, S., Ayyadevara, S., Penthala, N. R., Balasubramaniam, M., Ganne, A., Liu, L., Alla, R., Bommagani, S., Barger, S. W., Griffin, W. S. T., et al. (2019) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2019.00310 · Cited by 23

Role of Body-Fluid Biomarkers in Alzheimer’s Disease Diagnosis

Nguyen, T. T., Ta, Q. T. H., Nguyen, T. K. O., Nguyen, T. K. O., & Giau, V. V. (2020) · Diagnostics · doi:10.3390/diagnostics10050326 · Cited by 25

Fluc‐EGFP reporter mice reveal differential alterations of neuronal proteostasis in aging and disease

Blumenstock, S., Schulz‐Trieglaff, E. K., Bolender, A., Voelkl, K., Lapios, P., Lindner, J., Hipp, M. S., Hartl, F. U., Klein, R., & Dudanova, I. (2021) · The EMBO Journal · doi:10.15252/embj.2020107260 · Cited by 24

PKM2 aggregation drives metabolism reprograming during aging process

Bie, J., Li, R., Li, Y., Chen, S., Chen, Z., Zhang, T., Tang, Z., Su, L., Zhu, L., Wang, J., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-50242-y · Cited by 25

Targeting immunosenescence for improved tumor immunotherapy

Liu, Z., Zuo, L., Zhou, Z., Liu, S., Ba, Y., Zuo, A., Ren, Y., Zhang, C., Chen, Y., Ma, H., et al. (2024) · MedComm · doi:10.1002/mco2.777 · Cited by 24

Endometrial Aging and Reproductive Decline: The Central Role of Mitochondrial Dysfunction

Kobayashi, H., Nishio, M., Umetani, M., Shigetomi, H., Imanaka, S., & Hashimoto, H. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26115060 · Cited by 28

TORC 1‐mediated sensing of chaperone activity alters glucose metabolism and extends lifespan

Perić, M., Lovrić, A., Šarić, A., Musa, M., Dib, P. B., Rudan, M., Nikolić, A., Sobočanec, S., Mikecin, A., Dennerlein, S., et al. (2017) · Aging Cell · doi:10.1111/acel.12623 · Cited by 24

N-Acyldopamine induces aggresome formation without proteasome inhibition and enhances protein aggregation via p62/SQSTM1 expression

Matsumoto, G., Inobe, T., Amano, T., Murai, K., Nukina, N., & Mori, N. (2018) · Scientific Reports · doi:10.1038/s41598-018-27872-6 · Cited by 24

Multiple system‐level feedback loops control life‐and‐death decisions in endoplasmic reticulum stress

Kapuy, O., Márton, M., Bánhegyi, G., & Vinod, P. K. U. (2019) · FEBS Letters · doi:10.1002/1873-3468.13689 · Cited by 24

Sex differences in changes of protein synthesis with rapamycin treatment are minimized when metformin is added to rapamycin

Wolff, C. A., Lawrence, M. M., Porter, H. L., Zhang, Q., Reid, J. J., Laurin, J. L., Musci, R. V., Linden, M. A., Peelor, F. F., Wren, J. D., et al. (2020) · GeroScience · doi:10.1007/s11357-020-00243-8 · Cited by 23

Dynamic mRNP Remodeling in Response to Internal and External Stimuli

Zarnack, K., Balasubramanian, S., Gantier, M. P., Kunetsky, V., Kracht, M., Schmitz, M. L., & Sträßer, K. (2020) · Biomolecules · doi:10.3390/biom10091310 · Cited by 24

The molecular chaperone GRP170 protects against ER stress and acute kidney injury in mice

Porter, A. W., Nguyen, D. N., Clayton, D. R., Ruiz, W. G., Mutchler, S. M., Ray, E. C., Marciszyn, A. L., Nkashama, L. J., Subramanya, A. R., Gingras, S., et al. (2022) · JCI Insight · doi:10.1172/jci.insight.151869 · Cited by 24

C. elegans as an Animal Model to Study the Intersection of DNA Repair, Aging and Neurodegeneration

Naranjo-Galindo, F. J., Ai, R., Fang, E. F., Nilsen, H. L., & SenGupta, T. (2022) · Frontiers in Aging · doi:10.3389/fragi.2022.916118 · Cited by 29

Modulation of protease expression by the transcription factor Ptx1/PITX regulates protein quality control during aging

Jiao, J., Curley, M., Graça, F. A., Robles‐Murguia, M., Shirinifard, A., Finkelstein, D., Xu, B., Fan, Y., & Demontis, F. (2023) · Cell Reports · doi:10.1016/j.celrep.2022.111970 · Cited by 24

Circadian regulation of macromolecular complex turnover and proteome renewal

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Thermosensation and longevity

Xiao, R., Liu, J., & Xu, X. Z. S. (2015) · Journal of Comparative Physiology A · doi:10.1007/s00359-015-1021-8 · Cited by 24

Molecular chaperone HSP70 prevents formation of inclusion bodies of the 25-kDa C-terminal fragment of TDP-43 by preventing aggregate accumulation

Kitamura, A., Iwasaki, N., & Kinjo, M. (2018) · Cell Stress and Chaperones · doi:10.1007/s12192-018-0930-1 · Cited by 24

JNK modifies neuronal metabolism to promote proteostasis and longevity

Wang, L., Davis, S. S., Jensen, M. B., Rodriguez‐Fernandez, I. A., Apaydin, C., Juhász, G., Gibson, B. W., Schilling, B., Ramanathan, A., Ghaemmaghami, S., et al. (2019) · Aging Cell · doi:10.1111/acel.12849 · Cited by 24

Supersaturated proteins are enriched at synapses and underlie cell and tissue vulnerability in Alzheimer's disease

Freer, R., Sormanni, P., Ciryam, P., Rammner, B., Rizzoli, S. O., Dobson, C. M., & Vendruscolo, M. (2019) · Heliyon · doi:10.1016/j.heliyon.2019.e02589 · Cited by 24

Water Loss in Aging Erythrocytes Provides a Clue to a General Mechanism of Cellular Senescence

Minton, A. P. (2020) · Biophysical Journal · doi:10.1016/j.bpj.2020.10.004 · Cited by 23

Arrayed CRISPR reveals genetic regulators of tau aggregation, autophagy and mitochondria in Alzheimer’s disease model

Duan, L., Hu, M., Tamm, J. A., Grinberg, Y. Y., Shen, F., Chai, Y., Xi, H. S., Gibilisco, L., Ravikumar, B., Gautam, V., et al. (2021) · Scientific Reports · doi:10.1038/s41598-021-82658-7 · Cited by 26

A Comprehensive Enumeration of the Human Proteostasis Network. 2. Components of the Autophagy-Lysosome PathwayPreprint

coordination, O., Elsasser, S., Elia, L. P., Morimoto, R. I., Powers, E. T., Elsasser, S., Finley, D. J., Costa, B., Budron, M., Tokuno, Z., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.03.22.533675 · Cited by 32

Does death drive the scaling of life?

Glazier, D. S. (2024) · Biological reviews/Biological reviews of the Cambridge Philosophical Society · doi:10.1111/brv.13153 · Cited by 24

Potential common pathogenesis of several neurodegenerative diseases

Fan, T., Peng, J., Liang, H., Chen, W., Wang, J., & Xu, R. (2025) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-24-01054 · Cited by 29

The role of ER-associated degradation and ER-phagy in health and disease

Jeon, Y. J., & Ronai, Z. A. (2026) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02501-7 · Cited by 28

Defective Gating and Proteostasis of Human ClC-1 Chloride Channel: Molecular Pathophysiology of Myotonia Congenita

Jeng, C., Fu, S.-J., You, C.-Y., Peng, Y.-J., Hsiao, C.-T., Chen, T., & Tang, C. (2020) · Frontiers in Neurology · doi:10.3389/fneur.2020.00076 · Cited by 22

Kinetic analysis reveals that independent nucleation events determine the progression of polyglutamine aggregation in C. elegans

Sinnige, T., Meisl, G., Michaels, T. C. T., Vendruscolo, M., Knowles, T. P. J., & Morimoto, R. I. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2021888118 · Cited by 24

Multivalent protein–protein interactions are pivotal regulators of eukaryotic Hsp70 complexes

Johnson, O. T., & Gestwicki, J. E. (2022) · Cell Stress and Chaperones · doi:10.1007/s12192-022-01281-1 · Cited by 23

Proteostasis and Ribostasis Impairment as Common Cell Death Mechanisms in Neurodegenerative Diseases

Lim, S. M., Nahm, M., & Kim, S. H. (2023) · Journal of Clinical Neurology · doi:10.3988/jcn.2022.0379 · Cited by 24

Small heat shock proteins mediate cell-autonomous and -nonautonomous protection in a Drosophila model for environmental-stress-induced degeneration

Kawasaki, F., Koonce, N. L., Guo, L., Fatima, S., Qiu, C., Moon, M. T., Zheng, Y., & Ordway, R. W. (2016) · Disease Models & Mechanisms · doi:10.1242/dmm.026385 · Cited by 23

Scavengers of reactive γ-ketoaldehydes extend Caenorhabditis elegans lifespan and healthspan through protein-level interactions with SIR-2.1 and ETS-7

Nguyen, T., Caito, S. W., Zackert, W. E., West, J. D., Shijun, Z., Aschner, M., Fessel, J. P., & Roberts, L. J. (2016) · Aging · doi:10.18632/aging.101011 · Cited by 23

Differential adiponectin signalling couples ER stress with lipid metabolism to modulate ageing in C. elegans

Kyriakakis, E., Charmpilas, N., & Tavernarakis, N. (2017) · Scientific Reports · doi:10.1038/s41598-017-05276-2 · Cited by 21

Luminescence resonance energy transfer between genetically encoded donor and acceptor for protein-protein interaction studies in the molecular chaperone HSP70/HSP90 complexes

Bhattacharya, K., Bernasconi, L., & Picard, D. (2018) · Scientific Reports · doi:10.1038/s41598-018-21210-6 · Cited by 23

Proteostasis in the Male and Female Germline: A New Outlook on the Maintenance of Reproductive Health

Cafe, S. L., Nixon, B., Ecroyd, H. W., Martin, J. H., Skerrett-Byrne, D. A., & Bromfield, E. G. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.660626 · Cited by 23

Involvement of NRF2 and AMPK signaling in aging and progeria: a digest

Petsouki, E., Gerakopoulos, V., Gianniou, D. D., Heiß, E. H., & Trougakos, I. P. (2025) · Redox Biology · doi:10.1016/j.redox.2025.103782 · Cited by 22

Sequence features governing aggregation or degradation of prion-like proteins

Cascarina, S. M., Paul, K. R., Machihara, S., & Ross, E. D. (2018) · PLoS Genetics · doi:10.1371/journal.pgen.1007517 · Cited by 22

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

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

Expression of Amyloidogenic Transthyretin Drives Hepatic Proteostasis Remodeling in an Induced Pluripotent Stem Cell Model of Systemic Amyloid Disease

Giadone, R. M., Liberti, D. C., Matte, T. M., Rosarda, J. D., Torres-Arancivia, C., Ghosh, S., Diedrich, J. K., Pankow, S., Skvir, N. J., Jean, J., et al. (2020) · Stem Cell Reports · doi:10.1016/j.stemcr.2020.07.003 · Cited by 22

Oligodendrocyte‐specific deletion of Xbp1 exacerbates the endoplasmic reticulum stress response and restricts locomotor recovery after thoracic spinal cord injury

Ohri, S. S., Howard, R. M., Liu, Y., Andres, K. R., Shepard, C. T., Hetman, M., & Whittemore, S. R. (2020) · Glia · doi:10.1002/glia.23907 · Cited by 22

Interplay between symmetric arginine dimethylation and ubiquitylation regulates TDP1 proteostasis for the repair of topoisomerase I-DNA adducts

Bhattacharjee, S., Rehman, I., Basu, S., Nandy, S., Richardson, J. M., & Das, B. B. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.110940 · Cited by 23

Developmental disruption and restoration of brain synaptome architecture in the murine Pax6 neurodevelopmental disease model

Tomás‐Roca, L., Qiu, Z., Fransén, E. A., Gokhale, R., Bulovaite, E., Price, D. J., Komiyama, N. H., & Grant, S. G. N. (2022) · Nature Communications · doi:10.1038/s41467-022-34131-w · Cited by 27

Logic Gate Activated Lysosome Targeting DNA Nanodevice for Controlled Proteins Degradation

Shang, Y., Zhu, L., Xiao, Y., Du, S., Ji, R., Li, B., Chen, J., Deng, S., & Ren, K. (2023) · Advanced Functional Materials · doi:10.1002/adfm.202311722 · Cited by 22

Impaired protein stability and nuclear localization of NOBOX variants associated with premature ovarian insufficiency

Ferrari, I., Bouilly, J., Beau, I., Guizzardi, F., Ferlin, A., Pollazzon, M., Salerno, M., Binart, N., Persani, L., & Rossetti, R. (2016) · Human Molecular Genetics · doi:10.1093/hmg/ddw342 · Cited by 22

Structural and Functional Recovery of Sensory Cilia in C. elegans IFT Mutants upon Aging

Cornils, A., Maurya, A. K., Tereshko, L., Kennedy, J. E., Brear, A. G., Prahlad, V., Blacque, O. E., & Sengupta, P. (2016) · PLoS Genetics · doi:10.1371/journal.pgen.1006325 · Cited by 23

The chaperonin CCT promotes the formation of fibrillar aggregates of γ-tubulin

Pouchucq, L., Lobos-Ruiz, P., Araya, G., Valpuesta, J., & Monasterio, O. (2018) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2018.01.007 · Cited by 22

Structural insights into pro-aggregation effects of C. elegans CRAM-1 and its human ortholog SERF2

Balasubramaniam, M., Ayyadevara, S., & Reis, R. J. S. (2018) · Scientific Reports · doi:10.1038/s41598-018-33143-1 · Cited by 24

A one-pot analysis approach to simplify measurements of protein stability and folding kinetics

Liu, Y., Chen, H.-Y., Chueh, P. J., & Liu, P.-F. (2018) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2018.12.006 · Cited by 22

A metastable subproteome underlies inclusion formation in muscle proteinopathies

Ciryam, P., Antalek, M. D., Cid, F., Tartaglia, G. G., Dobson, C. M., Güttsches, A., Eggers, B., Vorgerd, M., Marcus, K., Kley, R. A., et al. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0853-9 · Cited by 21

Proteostasis regulators as potential rescuers of PMM2 activity

Vilas, A., Yuste‐Checa, P., Gallego, D., Desviat, L. R., Ugarte, M., Pérez‐Cerdá, C., Gámez, A., & Pérez, B. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2020.165777 · Cited by 22

Cell-Nonautonomous Mechanisms Underlying Cellular and Organismal Aging

Medkour, Y., Svistkova, V., & Titorenko, V. I. (2015) · International review of cytology · doi:10.1016/bs.ircmb.2015.09.003 · Cited by 21

DNA repair deficiencies and neurodegeneration

Ropert, B., Gallrein, C., & Schumacher, B. (2024) · DNA repair · doi:10.1016/j.dnarep.2024.103679 · Cited by 21

Molecular insights into the interaction of Hsp90 with allosteric inhibitors targeting the C-terminal domain

Vasantha Kumar, M. V., Noor, R. E., Davis, R. E., Zhang, Z., Sipavicius, E., Keramisanou, D., Blagg, B. S. J., & Gelis, I. (2018) · MedChemComm · doi:10.1039/c8md00151k · Cited by 21

Brain Protein Synthesis Rates in the UM-HET3 Mouse Following Treatment With Rapamycin or Rapamycin With Metformin

Reid, J. J., Linden, M. A., Peelor, F. F., Miller, R. A., Hamilton, K. L., & Miller, B. F. (2019) · The Journals of Gerontology Series A · doi:10.1093/gerona/glz069 · Cited by 22

Looking into Endoplasmic Reticulum Stress: The Key to Drug-Resistance of Multiple Myeloma?

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ECPAS/Ecm29-mediated 26S proteasome disassembly is an adaptive response to glucose starvation

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