The DOI matches its Crossref record; 183 of the 183 references it cites were found in a registry or an index.
The Biology of Proteostasis in Aging and Disease
Open accessAbstract
Loss of protein homeostasis (proteostasis) is a common feature of aging and disease that is characterized by the appearance of nonnative protein aggregates in various tissues. Protein aggregation is routinely suppressed by the proteostasis network (PN), a collection of macromolecular machines that operate in diverse ways to maintain proteome integrity across subcellular compartments and between tissues to ensure a healthy life span. Here, we review the composition, function, and organizational properties of the PN in the context of individual cells and entire organisms and discuss the mechanisms by which disruption of the PN, and related stress response pathways, contributes to the initiation and progression of disease. We explore emerging evidence that disease susceptibility arises from early changes in the composition and activity of the PN and propose that a more complete understanding of the temporal and spatial properties of the PN will enhance our ability to develop effective treatments for protein conformational diseases.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Aging affects all organ systems through common underlying mechanisms such as changes in the immune system, oxidative stress, and DNA damage and replication errors, as well as epigenetic changes and accumulation of abnormal proteins across multiple organ systems.35–38”
From Defining Optimal Brain Health in Adults: A Presidential Advisory From the American Heart Association/American Stroke Association (2017) · cites this paper as [38]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
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
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
Research works printed but not linked: 1
- Martinez-Vicente M, 2008, J. Clin. Investig., 118, 777
Cited by
Sorted by citations
Items 101–200 of 998
Sirtuins and FoxOs in osteoporosis and osteoarthritis
Almeida, M., & Porter, R. M. (2019) · Bone · doi:10.1016/j.bone.2019.01.018 · Cited by 131
Mediterranean diet and the hallmarks of ageing
Shannon, O. M., Ashor, A. W., Scialò, F., Saretzki, G. C., Martin-Ruiz, C. M., Lara, J., Matu, J., Griffiths, A., Robinson, N., Lionetti, L., et al. (2021) · European Journal of Clinical Nutrition · doi:10.1038/s41430-020-00841-x · Cited by 136
Protein Disaggregation in Multicellular Organisms
Nillegoda, N. B., Wentink, A. S., & Bukau, B. (2018) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2018.02.003 · Cited by 127
Berner, N., Reutter, K., & Wolf, D. H. (2018) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-062917-012749 · Cited by 132
Modulation of the proteostasis network promotes tumor resistance to oncogenic KRAS inhibitors
Lv, X., Lu, X., Cao, J., Luo, Q., Ding, Y., Peng, F., Pataer, A., Lu, D., Han, D., Malmberg, E., et al. (2023) · Science · doi:10.1126/science.abn4180 · Cited by 123
Acetylation-induced TDP-43 pathology is suppressed by an HSF1-dependent chaperone program
Wang, P., Wander, C. M., Yuan, C., Bereman, M. S., & Cohen, T. J. (2017) · Nature Communications · doi:10.1038/s41467-017-00088-4 · Cited by 123
Sleep Disturbance as a Potential Modifiable Risk Factor for Alzheimer’s Disease
Minakawa, E. N., Wada, K., & Nagai, Y. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20040803 · Cited by 122
Aging is associated with a systemic length-associated transcriptome imbalance
Stoeger, T., Grant, R. A., McQuattie‐Pimentel, A. C., Anekalla, K. R., Liu, S. S., Navarro, H. T., Singer, B. D., Abdala‐Valencia, H., Schwake, M., Tétreault, M., et al. (2022) · Nature Aging · doi:10.1038/s43587-022-00317-6 · Cited by 129
Self-citationRestricted access: spatial sequestration of damaged proteins during stress and aging
Hill, S. M., Hanzén, S., & Nyström, T. (2017) · EMBO Reports · doi:10.15252/embr.201643458 · Cited by 117
Biological basis and treatment of frailty and sarcopenia
Sato, R., Vatic, M., da Fonseca, G. W. P., Anker, S. D., & von Haehling, S. (2024) · Cardiovascular Research · doi:10.1093/cvr/cvae073 · Cited by 130
Immune aging in diabetes and its implications in wound healing
Moura, J., Madureira, P., Leal, E. C., Fonseca, A. C., & Carvalho, E. (2019) · Clinical Immunology · doi:10.1016/j.clim.2019.02.002 · Cited by 122
Proteomic and transcriptomic profiling reveal different aspects of aging in the kidney
Takemon, Y., Chick, J. M., Gyuricza, I. G., Skelly, D. A., Devuyst, O., Gygi, S. P., Churchill, G. A., & Korstanje, R. (2021) · eLife · doi:10.7554/elife.62585 · Cited by 118
Pharmacoperones as Novel Therapeutics for Diverse Protein Conformational Diseases
Tao, Y., & Conn, P. M. (2018) · Physiological Reviews · doi:10.1152/physrev.00029.2016 · Cited by 118
E2F coregulates an essential HSF developmental program that is distinct from the heat-shock responsePreprint
Li, J., Chauve, L., Phelps, G., Brielmann, R. M., & Morimoto, R. I. (2016) · Genes & Development · doi:10.1101/gad.283317.116 · Cited by 116
Self-citationThe involvement of stress granules in aging and aging‐associated diseases
Cao, X., Jin, X., & Liu, B. (2020) · Aging Cell · doi:10.1111/acel.13136 · Cited by 118
Tundo, G. R., Sbardella, D., Santoro, A. M., Coletta, A., Oddone, F., Grasso, G., Milardi, D., Lacal, P. M., Marini, S., Purrello, R., et al. (2020) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2020.107579 · Cited by 120
A brain atlas of synapse protein lifetime across the mouse lifespan
Bulovaite, E., Qiu, Z., Kratschke, M., Zgraj, A., Fricker, D. G., Tuck, E. J., Gokhale, R., Koniaris, B., Jami, S. A., Merino-Serrais, P., et al. (2022) · Neuron · doi:10.1016/j.neuron.2022.09.009 · Cited by 111
Mouse Models to Disentangle the Hallmarks of Human Aging
Folgueras, A. R., Freitas-Rodríguez, S., Velasco, G., & López-Otín, C. (2018) · Circulation Research · doi:10.1161/circresaha.118.312204 · Cited by 113
Protein Misfolding and ER Stress in Huntington's Disease
Shacham, T., Sharma, N., & Lederkremer, G. Z. (2019) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2019.00020 · Cited by 115
Metabolic features and regulation in cell senescence
Kwon, S. M., Hong, S. M., Lee, Y.-K., Min, S., & Yoon, G. (2019) · BMB Reports · doi:10.5483/bmbrep.2019.52.1.291 · Cited by 111
“Protein synthesis and dysregulated proteostasis One of the most important alterations during normal aging is impaired proteasis (protein homeostasis) (81, 82).”
BackgroundRangaraju, S., Solis, G. M., Thompson, R. C., Gomez-Amaro, R. L., Kurian, L., Encalada, S. E., Niculescu, A. B., Salomon, D. R., & Petrascheck, M. (2015) · eLife · doi:10.7554/elife.08833 · Cited by 110
Protein Degradation and the Pathologic Basis of Disease
Hanna, J. W., Guerra-Moreno, Á., Ang, J., & Micoogullari, Y. (2018) · American Journal Of Pathology · doi:10.1016/j.ajpath.2018.09.004 · Cited by 115
Minguzzi, M., Cetrullo, S., D’Adamo, S., Silvestri, Y., Flamigni, F., & Borzı̀, R. M. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/3075293 · Cited by 113
Integrating the DNA damage and protein stress responses during cancer development and treatment
Gorgoulis, V. G., Pefani, D., Pateras, I. S., & Trougakos, I. P. (2018) · The Journal of Pathology · doi:10.1002/path.5097 · Cited by 108
Cellular Regulation of Amyloid Formation in Aging and Disease
Stroo, E., Koopman, M., Nollen, E. A. A., & Mata‐Cabana, A. (2017) · Frontiers in Neuroscience · doi:10.3389/fnins.2017.00064 · Cited by 119
Enhanced Degradation of Misfolded Proteins Promotes Tumorigenesis
Chen, L., Brewer, M. D., Guo, L., Wang, R., Jiang, P., & Yang, X. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.03.010 · Cited by 110
Molecular Chaperones: A Double-Edged Sword in Neurodegenerative Diseases
Tittelmeier, J., Nachman, E., & Nussbaum-Krammer, C. I. (2020) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.581374 · Cited by 114
The Role of Mitochondrial Calcium Homeostasis in Alzheimer’s and Related Diseases
Ryan, K. C., Ashkavand, Z., & Norman, K. R. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21239153 · Cited by 106
Oxidative stress, aging, antioxidant supplementation and their impact on human health: An overview
Martemucci, G., Portincasa, P., Ciaula, A. D., Mariano, M., Centonze, V., & D‘Alessandro, A. G. (2022) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2022.111707 · Cited by 112
Emerging Paradigm of Crosstalk between Autophagy and the Ubiquitin-Proteasome System.
Nam, T., Han, J. H., Devkota, S., & Lee, H. (2017) · Europe PMC (PubMed Central) · doi:10.14348/molcells.2017.0226 · Cited by 114
Mitochondria orchestrate proteostatic and metabolic stress responses
Andréasson, C., Ott, M., & Büttner, S. (2019) · EMBO Reports · doi:10.15252/embr.201947865 · Cited by 96
Modest Declines in Proteome Quality Impair Hematopoietic Stem Cell Self-Renewal
Jose, L. H. S., Sunshine, M. J., Dillingham, C. H., Chua, B. A., Krutá, M., Hong, Y., Hatters, D. M., & Signer, R. A. J. (2020) · Cell Reports · doi:10.1016/j.celrep.2019.12.003 · Cited by 106
Tsai, P.-L., Zhao, C., TURNER, E. M. C., & Schlieker, C. D. (2016) · eLife · doi:10.7554/elife.16011 · Cited by 102
Freer, R., Sormanni, P., Vecchi, G., Ciryam, P., Dobson, C. M., & Vendruscolo, M. (2016) · Science Advances · doi:10.1126/sciadv.1600947 · Cited by 101
Schneider, C. V., Hamesch, K., Groß, A., Mandorfer, M., Moeller, L. S., Pereira, V. M., Pons, M., Kuca, P., Reichert, M., Benini, F., et al. (2020) · Gastroenterology · doi:10.1053/j.gastro.2020.04.058 · Cited by 99
Shin, W. H., Park, J. H., & Chung, K. C. (2020) · BMB Reports · doi:10.5483/bmbrep.2020.53.1.283 · Cited by 101
Cell-Nonautonomous Regulation of Proteostasis in Aging and DiseasePreprint
Morimoto, R. I. (2019) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a034074 · Cited by 98
Self-citationProtein aggregation and ER stress
Ogen‐Shtern, N., David, T. B., & Lederkremer, G. Z. (2016) · Brain Research · doi:10.1016/j.brainres.2016.03.044 · Cited by 98
Integrated stress response stimulates FGF21 expression: Systemic enhancer of longevity
Salminen, A., Kaarniranta, K., & Kauppinen, A. (2017) · Cellular Signalling · doi:10.1016/j.cellsig.2017.08.009 · Cited by 100
P‐glycoprotein: a role in the export of amyloid‐β in Alzheimer's disease?
Chai, A. B., Leung, G. K. F., Callaghan, R., & Gelissen, I. C. (2019) · FEBS Journal · doi:10.1111/febs.15148 · Cited by 100
Rai, M., Coleman, Z., Curley, M., Nityanandam, A., Platt, A., Robles‐Murguia, M., Jiao, J., Finkelstein, D., Wang, Y., Xu, B., et al. (2021) · Cell Metabolism · doi:10.1016/j.cmet.2021.03.005 · Cited by 95
Oxidative Stress-Induced Cellular Senescence: Is Labile Iron the Connecting Link?
Nousis, L., Kanavaros, P., & Barbouti, A. (2023) · Antioxidants · doi:10.3390/antiox12061250 · Cited by 103
Cellular senescence is associated with reorganization of the microtubule cytoskeleton
Moujaber, O., Fishbein, F., Omran, N., Liang, Y., Colmegna, I., Presley, J. F., & Stochaj, U. (2018) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-018-2999-1 · Cited by 101
Alternative systems for misfolded protein clearance: life beyond the proteasome
Johnston, H. E., & Samant, R. S. (2020) · FEBS Journal · doi:10.1111/febs.15617 · Cited by 93
Xiong, S., Chng, W. J., & Zhou, J. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-03756-3 · Cited by 99
Molecular mechanism of ATF6 in unfolded protein response and its role in disease
Lei, Y., Yu, H., Ding, S., Liu, H., Liu, C., & Fu, R. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e25937 · Cited by 102
Modulation of Amyloid States by Molecular ChaperonesPreprint
Wentink, A. S., Nussbaum-Krammer, C. I., & Bukau, B. (2019) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a033969 · Cited by 93
Autophagy and Immune Senescence
Zhang, H., Puleston, D. J., & Simon, A. K. (2016) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2016.06.001 · Cited by 95
Jiang, T., Shi, Y., Cui, X.-W., Pan, Y., Lin, Y., Feng, X., Ding, Z., Yang, C., Tan, Y., Dong, L., et al. (2022) · Gastroenterology · doi:10.1053/j.gastro.2022.11.025 · Cited by 93
NAD+ boosting reduces age-associated amyloidosis and restores mitochondrial homeostasis in muscle
Romani, M., Sorrentino, V., Oh, C.-M., Li, H., de Lima, T. I., Zhang, H., Shong, M., & Auwerx, J. (2021) · Cell Reports · doi:10.1016/j.celrep.2020.108660 · Cited by 92
Protein homeostasis of a metastable subproteome associated with Alzheimer’s disease
Kundra, R., Ciryam, P., Morimoto, R. I., Dobson, C. M., & Vendruscolo, M. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1618417114 · Cited by 93
Self-citationPiette, B. L., Alerasool, N., Lin, Z., Lacoste, J., Lam, M. H. Y., Qian, W. W., Tran, S., Larsen, B. G., Campos, E. I., Peng, J., et al. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.04.012 · Cited by 94
Quality Control of Membraneless Organelles
Alberti, S., & Carra, S. (2018) · Journal of Molecular Biology · doi:10.1016/j.jmb.2018.05.013 · Cited by 92
The role of hydrogen sulfide in aging and age-related pathologies
Perridon, B. W., Leuvenink, H. G. D., Hillebrands, J., van Goor, H., & Bos, E. M. (2016) · Aging · doi:10.18632/aging.101026 · Cited by 90
Lellahi, S. M., Rosenlund, I. A., Hedberg, A., Kiær, L. T., Mikkola, I., Knutsen, E., & Perander, M. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.004473 · Cited by 91
Targeting the proteostasis network in Huntington’s disease
Soares, T. R., Reis, S., Pinho, B. R., Duchen, M. R., & Oliveira, J. M. A. (2018) · Ageing Research Reviews · doi:10.1016/j.arr.2018.11.006 · Cited by 93
Regulation of Hsf1 and the Heat Shock Response
Pincus, D. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-40204-4_3 · Cited by 91
Biological ageing with HIV infection: evaluating the geroscience hypothesis
Montano, M. A., Oursler, K. K., Xu, K., Sun, Y. V., & Marconi, V. C. (2022) · The Lancet Healthy Longevity · doi:10.1016/s2666-7568(21)00278-6 · Cited by 94
Dynamics, flexibility, and allostery in molecular chaperonins
Skjærven, L., Cuéllar, J., Martı́nez, A., & Valpuesta, J. (2015) · FEBS Letters · doi:10.1016/j.febslet.2015.06.019 · Cited by 89
Quality control of glycoprotein folding and ERAD: the role of N-glycan handling, EDEM1 and OS-9
Roth, J., & Zuber, C. (2016) · Histochemistry and Cell Biology · doi:10.1007/s00418-016-1513-9 · Cited by 92
Dietary Polyphenols: A Multifactorial Strategy to Target Alzheimer’s Disease
Dhakal, S., Kushairi, N., Phan, C., Adhikari, B., Sabaratnam, V., & Macreadie, I. G. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20205090 · Cited by 92
Ciryam, P., Kundra, R., Freer, R., Morimoto, R. I., Dobson, C. M., & Vendruscolo, M. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1516604113 · Cited by 85
Self-citationWu, J. J., Cai, A., Greenslade, J. E., Higgins, N. R., Fan, C., Le, N. T. T., Tatman, M., Whiteley, A. M., Prado, M. A., Dieriks, B. V., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1917371117 · Cited by 86
ER stress causes widespread protein aggregation and prion formation
Hamdan, N., Kritsiligkou, P., & Grant, C. M. (2017) · Journal of Cell Biology · doi:10.1083/jcb.201612165 · Cited by 85
HSF1 stress response pathway regulates autophagy receptor SQSTM1/p62-associated proteostasis
Watanabe, Y., Tsujimura, A., Taguchi, K., & Tanaka, M. (2016) · Autophagy · doi:10.1080/15548627.2016.1248018 · Cited by 87
TDP-43 Promotes Neurodegeneration by Impairing Chromatin Remodeling
Berson, A., Sartoris, A., Nativio, R., Deerlin, V. M. V., Toledo, J. B., Porta, S., Liu, S., Chung, C., Garcia, B. A., Lee, V. M. ‐., et al. (2017) · Current Biology · doi:10.1016/j.cub.2017.10.024 · Cited by 90
mTORC1 signaling activates NRF1 to increase cellular proteasome levels
Zhang, Y., & Manning, B. D. (2015) · Cell Cycle · doi:10.1080/15384101.2015.1044188 · Cited by 85
Differentiation Drives Widespread Rewiring of the Neural Stem Cell Chaperone Network
Vonk, W. I. M., Rainbolt, T. K., Dolan, P. T., Webb, A. E., Brunet, A., & Frydman, J. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.03.009 · Cited by 84
Compromising the 19S proteasome complex protects cells from reduced flux through the proteasome
Tsvetkov, P., Mendillo, M. L., Zhao, J., Carette, J. E., Merrill, P. H., Cikes, D., Varadarajan, M., van Diemen, F. R., Penninger, J. M., Goldberg, A. L., et al. (2015) · eLife · doi:10.7554/elife.08467 · Cited by 83
Proteostasis Disturbances and Inflammation in Neurodegenerative Diseases
Sonninen, T.-M., Goldsteins, G., Laham-Karam, N., Koıstınaho, J., & Lehtonen, Š. (2020) · Cells · doi:10.3390/cells9102183 · Cited by 89
Chimeric efferocytic receptors improve apoptotic cell clearance and alleviate inflammation
Morioka, S., Kajioka, D., Yamaoka, Y., Ellison, R. M., Tufan, T., Werkman, I. L., Tanaka, S., Barron, B. J., Ito, S., Kucenas, S., et al. (2022) · Cell · doi:10.1016/j.cell.2022.11.029 · Cited by 85
Successes and challenges in simulating the folding of large proteins
Gershenson, A., Gosavi, S., Faccioli, P., & Wintrode, P. L. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.rev119.006794 · Cited by 86
Transcriptional reprogramming at the intersection of the heat shock response and proteostasis
Pessa, J. C., Joutsen, J., & Sistonen, L. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.11.024 · Cited by 85
The HSF1–PARP13–PARP1 complex facilitates DNA repair and promotes mammary tumorigenesis
Fujimoto, M., Takii, R., Takaki, E., Katiyar, A., Nakato, R., Shirahige, K., & Nakai, A. (2017) · Nature Communications · doi:10.1038/s41467-017-01807-7 · Cited by 82
MitoStores: chaperone‐controlled protein granules store mitochondrial precursors in the cytosol
Krämer, L., Dalheimer, N., Räschle, M., Štorchová, Z., Pielage, J., Boos, F., & Herrmann, J. M. (2023) · The EMBO Journal · doi:10.15252/embj.2022112309 · Cited by 81
Brosh, R. M., Bellani, M. A., Liu, Y., & Seidman, M. M. (2016) · Ageing Research Reviews · doi:10.1016/j.arr.2016.05.005 · Cited by 84
Amyloid β Modification: A Key to the Sporadic Alzheimer's Disease?
Barykin, E. P., Mitkevich, V. A., Kozin, S. A., & Makarov, A. А. (2017) · Frontiers in Genetics · doi:10.3389/fgene.2017.00058 · Cited by 84
Proteasome Inhibitors: Harnessing Proteostasis to Combat Disease
Sherman, D. J., & Li, J. (2020) · Molecules · doi:10.3390/molecules25030671 · Cited by 77
Structural visualization of the tubulin folding pathway directed by human chaperonin TRiC/CCT
Gestaut, D. R., Zhao, Y., Park, J., Ma, B., Leitner, A., Collier, M., Pintilie, G. D., Roh, S., Chiu, W., & Frydman, J. (2022) · Cell · doi:10.1016/j.cell.2022.11.014 · Cited by 76
Fluid Flow and Mass Transport in Brain Tissue
Ray, L., & Heys, J. J. (2019) · Fluids · doi:10.3390/fluids4040196 · Cited by 78
Kitamura, A., Nakayama, Y., Shibasaki, A., Taki, A., Yuno, S., Takeda, K., Yahara, M., Tanabe, N., & Kinjo, M. (2016) · Scientific Reports · doi:10.1038/srep19230 · Cited by 77
Aging, Cellular Senescence, and Glaucoma
Zhang, Y., Huang, S., Xie, B., & Zhong, Y. (2023) · Aging and Disease · doi:10.14336/ad.2023.0631 · Cited by 80
Swovick, K., Firsanov, D., Welle, K. A., Hryhorenko, J. R., Wise, J. P., George, C., Sformo, T. L., Seluanov, A., Gorbunova, V., & Ghaemmaghami, S. (2021) · Molecular & Cellular Proteomics · doi:10.1074/mcp.ra120.002301 · Cited by 73
Bhattacharya, K., & Picard, D. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-03962-z · Cited by 74
Aging of the eye: Lessons from cataracts and age-related macular degeneration
Cvekl, A., & Vijg, J. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102407 · Cited by 77
Systematic study of the dynamics and half-lives of newly synthesized proteins in human cells
Chen, W., Smeekens, J. M., & Wu, R. (2015) · Chemical Science · doi:10.1039/c5sc03826j · Cited by 75
Understanding Pre‐Eclampsia Using Alzheimer's Etiology: An Intriguing Viewpoint
Cheng, S., Nakashima, A., & Sharma, S. (2015) · American Journal of Reproductive Immunology · doi:10.1111/aji.12446 · Cited by 72
González‐Freire, M., Moaddel, R., Sun, K., Fabbri, E., Zhang, P., Khadeer, M., Salem, N., Ferrucci, L., & Semba, R. D. (2018) · The Journals of Gerontology Series A · doi:10.1093/gerona/gly100 · Cited by 75
Magnesium and the Hallmarks of Aging
Dominguez, L. J., Veronese, N., & Barbagallo, M. (2024) · Nutrients · doi:10.3390/nu16040496 · Cited by 78
Yang, Y., Ma, F., Liu, Z., Su, Q., Liu, Y., Liu, Z., & Li, Y. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.005166 · Cited by 75
Azkanaz, M., López, A. R., de Boer, B., Huiting, W., Angrand, P., Vellenga, E., Kampinga, H. H., Bergink, S., Martens, J. H. A., Schuringa, J. J., et al. (2019) · eLife · doi:10.7554/elife.45205 · Cited by 72
Proteotoxic Stress and Cell Death in Cancer Cells
Brancolini, C., & Iuliano, L. (2020) · Cancers · doi:10.3390/cancers12092385 · Cited by 73
Peng, W., Zhou, R., Sun, Z., Long, J.-W., & Gong, Y.-Q. (2022) · Aging and Disease · doi:10.14336/ad.2021.0928 · Cited by 73
Chaperone-client interactions: Non-specificity engenders multifunctionality
Koldewey, P., Horowitz, S. A., & Bardwell, J. C. A. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.r117.796862 · Cited by 69
Levada, K. V., Güldiken, N., Zhang, X., Vella, G., Mo, F., James, L. P., Haybaeck, J., Kessler, S. M., Kiemer, A. K., Ott, T., et al. (2018) · Journal of Hepatology · doi:10.1016/j.jhep.2018.01.003 · Cited by 71
Kinetic and structural comparison of a protein’s cotranslational folding and refolding pathways
Samelson, A. J., Bolin, E. R., Costello, S. M., Sharma, A. K., O’Brien, E. P., & Marqusee, S. (2018) · Science Advances · doi:10.1126/sciadv.aas9098 · Cited by 70
Bar‐Yosef, D. L., Sade, D., Shaham‐Niv, S., Zaguri, D., Gartner, M., Basavalingappa, V., Raveh, A., Pichinuk, E., Engel, H., Iwasaki, K., et al. (2019) · Nature Communications · doi:10.1038/s41467-018-07966-5 · Cited by 67
J-domain protein chaperone circuits in proteostasis and disease
Zhang, R., Malinverni, D., Cyr, D., Rios, P. D. L., & Nillegoda, N. B. (2022) · Trends in Cell Biology · doi:10.1016/j.tcb.2022.05.004 · Cited by 69
Bacterial proteostasis balances energy and chaperone utilization efficiently
Santra, M., Farrell, D. W., & Dill, K. A. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1620646114 · Cited by 68
Dickey, A. S., Sanchez, D. N., Arreola, M., Sampat, K. R., Fan, W., Arbez, N., Akimov, S., Kanegan, M. J. V., Ohnishi, K., Gilmore-Hall, S. K., et al. (2017) · Science Translational Medicine · doi:10.1126/scitranslmed.aal2332 · Cited by 70
Metadata
- Authors
- Labbadia, J., & Morimoto, R. I.
- Affiliations
- Department of Molecular Biosciences, Rice Institute for Biomedical Research, Northwestern University, Evanston, Illinois 60208;
- Northwestern University (US)
- Corresponding author
- Morimoto, Richard I
- ORCID
- Morimoto, Richard I
- Venue
- Annual Review of Biochemistry
- Publisher
- Annual Reviews
- Published
- 2015-06-02
- Volume
- 84
- Issue
- 1
- Pages
- 435-464
- ISSN
- 0066-4154 (ISSN-L)
- 1545-4509
- PMC
- PMC4539002
- OpenAlex
- W2152231829
- Cited by
- 1,472
- References
- 182
- Citations by year
- 2026: 142 · 2025: 127 · 2024: 150 · 2023: 152 · 2022: 140 · 2021: 148 · 2020: 143 · 2019: 139 · 2018: 136 · 2017: 106 · 2016: 69 · 2015: 19
- FWCI
- 10.55
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Annual Review of Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- UCL Discovery (University College London) (submittedVersion)
- Funders
- Ellison Medical Foundation
- National Institutes of Health (5p50mh094267-05)
- National Institute on Aging (R37AG026647, R01AG026647)
- National Institute of Mental Health (P50-MH094267)
- National Institute of General Medical Sciences (P50GM081892, R01GM038109, R37GM038109)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Aging › Genetics, Aging, and Longevity in Model Organisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- proteostasis, proteostasis network, aging, protein aggregation, stress response pathways, protein conformational diseases, disease susceptibility, lifespan
- MeSH terms
- Aging, Animals, Humans, Proteins, Neurodegenerative Diseases, Metabolic Networks and Pathways, Proteolysis, Endoplasmic Reticulum Stress
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review