Proteostasis collapse is a driver of cell aging and death
Open accessAbstract
Significance: Cells and organisms grow old and die. We develop a biophysical model of the mechanism. Young cells are kept healthy by the positive processes of protein synthesis, degradation, and chaperoning (the activity of keeping proteins properly folded). But, with age, negative processes increase: Oxidative damage accumulates randomly in the cell’s proteins, healthy synthesis and degradation slow down, and—like overfilled garbage cans—chaperone capacity is exceeded. The chaperones are distracted trying to fold irreversibly damaged proteins, leading to accumulating misfolded and aggregated proteins in the cell. The tipping point to death happens when the negative overwhelms the positive. The model makes several quantitative predictions of the life span of the worm Caenorhabditis elegans .
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
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?
Oxidative damage to proteins is associated with aging and is linked to protein misfolding.
“Much evidence suggests that oxidative damage to proteins is associated with aging and is linked to protein misfolding [216,217].”
From Nrf2 and Oxidative Stress: A General Overview of Mechanisms and Implications in Human Disease (2022) · cites this paper as [217]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
López-Otín, C., Blasco, M. A., Partridge, L., Serrano, M., & Kroemer, G. (2013) · Cell · doi:10.1016/j.cell.2013.05.039 · Cited by 14,982 · see citing works
Lindquist, S. L. (1986) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.55.070186.005443 · Cited by 4,611 · see citing works
Stadtman, E. R. (1992) · Science · doi:10.1126/science.1355616 · Cited by 2,701 · see citing works
Adapting Proteostasis for Disease Intervention
Balch, W. E., Morimoto, R. I., Dillin, A., & Kelly, J. W. (2008) · Science · doi:10.1126/science.1141448 · Cited by 2,495 · see citing works
Hoeijmakers, J. H. J. (2009) · New England Journal of Medicine · doi:10.1056/nejmra0804615 · Cited by 2,239 · see citing works
Understanding the odd science of aging
Kirkwood, T. B. L. (2005) · Cell · doi:10.1016/j.cell.2005.01.027 · Cited by 1,984 · see citing works
Regulation of aging and age-related disease by DAF-16 and heat-shock factor
Hsu, A.-L., Murphy, C. T., & Kenyon, C. (2003) · Science · doi:10.1126/science.1083701 · Cited by 1,513 · see citing works
Biological and Chemical Approaches to Diseases of Proteostasis Deficiency
Powers, E. T., Morimoto, R. I., Dillin, A., Kelly, J. W., & Balch, W. E. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.052308.114844 · Cited by 1,149 · see citing works
Stadtman, E. R. (2006) · Free Radical Research · doi:10.1080/10715760600918142 · Cited by 1,056 · see citing works
Mitonuclear protein imbalance as a conserved longevity mechanism
Houtkooper, R. H., Mouchiroud, L., Ryu, D., Moullan, N., Katsyuba, E., Knott, G., Williams, R. W., & Auwerx, J. (2013) · Nature · doi:10.1038/nature12188 · Cited by 1,035 · see citing works
Telomeres and telomerase: the path from maize, Tetrahymena and yeast to human cancer and aging
Blackburn, E. H., Greider, C. W., & Szostak, J. W. (2006) · Nature Medicine · doi:10.1038/nm1006-1133 · Cited by 992 · see citing works
Regulation of Longevity in Caenorhabditis elegans by Heat Shock Factor and Molecular Chaperones
Morley, J. F., & Morimoto, R. I. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e03-07-0532 · Cited by 725 · see citing works
Wright, S., & Pearl, R. (1928) · Journal of the American Statistical Association · doi:10.2307/2276751 · Cited by 676 · see citing works
Proteome-wide Analysis of Chaperonin-Dependent Protein Folding in Escherichia coli
Kerner, M. J., Naylor, D. J., Ishihama, Y., Maier, T., Chang, H.-C., Stines, A. P., Georgopoulos, C. P., Frishman, D., Hayer-Hartl, M. K., Mann, M., et al. (2005) · Cell · doi:10.1016/j.cell.2005.05.028 · Cited by 659 · see citing works
Collapse of proteostasis represents an early molecular event in <i>Caenorhabditis elegans</i> aging
Ben-Zvi, A., Miller, E. A., & Morimoto, R. I. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0902882106 · Cited by 649 · see citing works
Progressive disruption of cellular protein folding in models of polyglutamine diseases
Gidalevitz, T., Ben-Zvi, A., Ho, K. H., Brignull, H. R., & Morimoto, R. I. (2006) · Science · doi:10.1126/science.1124514 · Cited by 643 · see citing works
Widespread protein aggregation as an inherent part of aging in C. elegans
David, D. C., Ollikainen, N., Trinidad, J. C., Cary, M. P., Burlingame, A. L., & Kenyon, C. (2010) · PLoS Biology · doi:10.1371/journal.pbio.1000450 · Cited by 627 · see citing works
Increased cell-to-cell variation in gene expression in ageing mouse heart
Bahar, R., Hartmann, C. H., Rodriguez, K. A., Denny, A. D., Busuttil, R. A., Dollé, M. E. T., Calder, R. B., Chisholm, G. B., Pollock, B. H., Klein, C. A., et al. (2006) · Nature · doi:10.1038/nature04844 · Cited by 603 · see citing works
Widespread Proteome Remodeling and Aggregation in Aging C. elegans
Walther, D. M., Kasturi, P., Zheng, M., Pinkert, S., Vecchi, G., Ciryam, P., Morimoto, R. I., Dobson, C. M., Vendruscolo, M., Mann, M., et al. (2015) · Cell · doi:10.1016/j.cell.2015.03.032 · Cited by 569 · see citing works
Bernardes de Jesus, B., Vera, E., Schneeberger, K., Tejera, A. M., Ayuso, E., Bosch, F., & Blasco, M. A. (2012) · EMBO Molecular Medicine · doi:10.1002/emmm.201200245 · Cited by 548 · see citing works
Aging as an event of proteostasis collapse
Taylor, R. C., & Dillin, A. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a004440 · Cited by 538 · see citing works
Distinct Modes of Regulation by Chromatin Encoded through Nucleosome Positioning Signals
Field, Y., Kaplan, N., Fondufe‐Mittendorf, Y. N., Moore, I. K., Sharon, E., Lubling, Y., Widom, J., & Segal, E. (2008) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1000216 · Cited by 455 · see citing works
Hip, a novel cochaperone involved in the eukaryotic hsc70/hsp40 reaction cycle
Höfeld, J., Minami, Y., & Hartl, F. U. (1995) · Cell · doi:10.1016/0092-8674(95)90099-3 · Cited by 440 · see citing works
Elevated histone expression promotes life span extension
Feser, J., Truong, D., Das, C., Carson, J. J., Kieft, J., Harkness, T., & Tyler, J. K. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.08.015 · Cited by 435 · see citing works
The Stability Effects of Protein Mutations Appear to be Universally Distributed
Tokuriki, N., Stricher, F., Schymkowitz, J. W. H., Serrano, L. G., & Tawfik, D. S. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.03.069 · Cited by 415 · see citing works
RPN-6 determines C. elegans longevity under proteotoxic stress conditions
Vilchez, D., Morantte, I., Liu, Z., Douglas, P. M., Merkwirth, C., Rodrigues, A. P. C., Manning, G., & Dillin, A. (2012) · Nature · doi:10.1038/nature11315 · Cited by 413 · see citing works
GrpE‐like regulation of the Hsc70 chaperone by the anti‐apoptotic protein BAG‐1
Höhfeld, J., & Jentsch, S. (1997) · The EMBO Journal · doi:10.1093/emboj/16.20.6209 · Cited by 395 · see citing works
Repression of the Heat Shock Response Is a Programmed Event at the Onset of Reproduction
Labbadia, J. P., & Morimoto, R. I. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.06.027 · Cited by 330 · see citing works
Accelerated neurodegeneration through chaperone-mediated oligomerization of tau
Blair, L. J., Nordhues, B. A., Hill, S. E., Scaglione, K. M., O’Leary, J. C., Fontaine, S. N., Breydo, L., Zhang, B., Li, P., Wang, L., et al. (2013) · Journal of Clinical Investigation · doi:10.1172/jci69003 · Cited by 322 · see citing works
Proteasome inhibition by lipofuscin/ceroid during postmitotic aging of fibroblasts
Sitte, N., Huber, M., Grune, T., Ladhoff, A., Doecke, W., Zglinicki, T. V., & Davies, K. J. A. (2000) · The FASEB Journal · doi:10.1096/fj.14.11.1490 · Cited by 318 · see citing works
Morrow, G., Samson, M., Michaud, S., & Tanguay, R. M. (2004) · The FASEB Journal · doi:10.1096/fj.03-0860fje · Cited by 317 · see citing works
Polyglutamine protein aggregates are dynamic
Kim, S., Nollen, E. A. A., Kitagawa, K., Bindokas, V. P., & Morimoto, R. I. (2002) · Nature Cell Biology · doi:10.1038/ncb863 · Cited by 296 · see citing works
Voorhies, W. A. V., & Ward, S. F. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.20.11399 · Cited by 282 · see citing works
Protein damage and death by radiation in <i>Escherichia coli</i> and <i>Deinococcus radiodurans</i>
Krisko, A., & Radman, M. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1009312107 · Cited by 243 · see citing works
Yokoyama, K., Fukumoto, K., Murakami, T., Harada, S.-I., Hosono, R., Wadhwa, R., Mitsui, Y., & Ohkuma, S. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)02470-5 · Cited by 229 · see citing works
Kowald, A., & Kirkwood, T. B. L. (1996) · Mutation Research/DNAging · doi:10.1016/s0921-8734(96)90005-3 · Cited by 221 · see citing works
Protein biogenesis machinery is a driver of replicative aging in yeast
Janssens, G. E., Meinema, A. C., González, J., Wolters, J. C., Schmidt, A., Guryev, V., Bischoff, R., Wit, E. C., Veenhoff, L. M., & Heinemann, M. (2015) · eLife · doi:10.7554/elife.08527 · Cited by 193 · see citing works
Mechanisms of life span determination in Caenorhabditis elegans☆
Vanfleteren, J. R., & Braeckman, B. P. (1999) · Neurobiology of Aging · doi:10.1016/s0197-4580(99)00087-1 · Cited by 181 · see citing works
The temporal scaling of Caenorhabditis elegans ageing
Stroustrup, N., Anthony, W., Nash, Z. M., Gowda, V., Gomez, A., López-Moyado, I. F., Apfeld, J., & Fontana, W. (2016) · Nature · doi:10.1038/nature16550 · Cited by 181 · see citing works
Bimston, D. N., Song, J., Winchester, D., Takayama, S.-I. J., Reed, J. C., & Morimoto, R. I. (1998) · The EMBO Journal · doi:10.1093/emboj/17.23.6871 · Cited by 180 · see citing works
Adachi, H., Fujiwara, Y., & Ishii, N. (1998) · The Journals of Gerontology Series A · doi:10.1093/gerona/53a.4.b240 · Cited by 178 · see citing works
Chondrogianni, N., Georgila, K., Kourtis, N., Tavernarakis, N., & Gonos, E. S. (2014) · The FASEB Journal · doi:10.1096/fj.14-252189 · Cited by 174 · see citing works
Heat shock proteins as potential targets for protective strategies in neurodegeneration
Kampinga, H. H., & Bergink, S. (2016) · The Lancet Neurology · doi:10.1016/s1474-4422(16)00099-5 · Cited by 172 · see citing works
Aging and molecular chaperones
Sőti, C. (2003) · Experimental Gerontology · doi:10.1016/s0531-5565(03)00185-2 · Cited by 167 · see citing works
Protein aggregation can inhibit clathrin-mediated endocytosis by chaperone competition
Yu, A., Shibata, Y., Shah, B., Calamini, B., Lo, D. C., & Morimoto, R. I. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1321811111 · Cited by 149 · see citing works
Bershtein, S., Mu, W., Serohijos, A. W. R., Zhou, J., & Shakhnovich, E. I. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.11.004 · Cited by 147 · see citing works
How Do Thermophilic Proteins and Proteomes Withstand High Temperature?
Sawle, L., & Ghosh, K. (2011) · Biophysical Journal · doi:10.1016/j.bpj.2011.05.059 · Cited by 142 · see citing works
Proteasome inhibition by lipofuscin/ceroid during postmitotic aging of fibroblasts
Sitte, N., Huber, M., Grune, T., et al. (2000) · The FASEB Journal · doi:10.1096/fj.99-0843com · Cited by 142 · see citing works
Temperature dependence of protein folding kinetics in living cells
Guo, M., Xu, Y., & Gruebele, M. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1201797109 · Cited by 132 · see citing works
HSP90 Shapes the Consequences of Human Genetic Variation
Karras, G. I., Yi, S. S., Sahni, N., Fischer, M., Xie, J., Vidal, M., D’Andrea, A. D., Whitesell, L. J., & Lindquist, S. L. (2017) · Cell · doi:10.1016/j.cell.2017.01.023 · Cited by 129 · see citing works
Deep proteome analysis identifies age-related processes in C. elegans
Narayan, V., Ly, T., Pourkarimi, E., Murillo, A. B., Gartner, A., Lamond, A. I., & Kenyon, C. (2016) · Cell Systems · doi:10.1016/j.cels.2016.06.011 · Cited by 127 · see citing works
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 125 · see citing works
Exogenous Hsp70 delays senescence and improves cognitive function in aging mice
Bobkova, N. V., Evgen’ev, M., Garbuz, D. G., Kulikov, A. M., Morozov, A., Samokhin, A., Velmeshev, D., Medvinskaya, N., Nesterova, I., Pollock, A., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1516131112 · Cited by 118 · see citing works
Rangaraju, 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 111 · see citing works
Shemesh, N., Shai, N., & Ben‐Zvi, A. (2013) · Aging Cell · doi:10.1111/acel.12110 · Cited by 110 · see citing works
Computing protein stabilities from their chain lengths
Ghosh, K., & Dill, K. A. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0903995106 · Cited by 109 · see citing works
Self-citationThermosensitivity of growth is determined by chaperone-mediated proteome reallocation
Chen, K., Gao, Y., Mih, N., O’Brien, E. J., Yang, L., & Palsson, B. Ø. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1705524114 · Cited by 90 · see citing works
Modelling the Role of the Hsp70/Hsp90 System in the Maintenance of Protein Homeostasis
Proctor, C. J., & Lorimer, I. A. J. (2011) · PLoS ONE · doi:10.1371/journal.pone.0022038 · Cited by 87 · see citing works
Defense against Protein Carbonylation by DnaK/DnaJ and Proteases of the Heat Shock Regulon
Fredriksson, Å., Ballesteros, M., Dukan, S., & Nyström, T. (2005) · Journal of Bacteriology · doi:10.1128/jb.187.12.4207-4213.2005 · Cited by 81 · see citing works
General Mechanism of Two-State Protein Folding Kinetics
Rollins, G. C., & Dill, K. A. (2014) · Journal of the American Chemical Society · doi:10.1021/ja5049434 · Cited by 81 · see citing works
Self-citationYasuda, K., Adachi, H., Fujiwara, Y., & Ishii, N. (1999) · The Journals of Gerontology Series A · doi:10.1093/gerona/54.2.b47 · Cited by 78 · see citing works
Highly Charged Proteins: The Achilles' Heel of Aging Proteomes
de Graff, A. M. R., Hazoglou, M. J., & Dill, K. A. (2015) · Structure · doi:10.1016/j.str.2015.11.006 · Cited by 75 · see citing works
Self-citationModelling the actions of chaperones and their role in ageing
Proctor, C. J., Sőti, C., Boys, R. J., Gillespie, C. S., Shanley, D. P., Wilkinson, D. J., & Kirkwood, T. B. L. (2004) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2004.09.031 · Cited by 73 · see citing works
Corruption and Spread of Pathogenic Proteins in Neurodegenerative Diseases
Walker, L. C., & LeVine, H. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.r112.399378 · Cited by 72 · see citing works
FoldEco: A Model for Proteostasis in E. coli
Powers, E. T., Powers, D. L., & Gierasch, L. M. (2012) · Cell Reports · doi:10.1016/j.celrep.2012.02.011 · Cited by 71 · see citing works
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 69 · see citing works
Self-citationProtein damage, radiation sensitivity and aging
Radman, M. (2016) · DNA repair · doi:10.1016/j.dnarep.2016.05.025 · Cited by 68 · see citing works
Phenotypic and Genetic Consequences of Protein Damage
Kriško, A., & Radman, M. (2013) · PLoS Genetics · doi:10.1371/journal.pgen.1003810 · Cited by 63 · see citing works
Autophagy links lipid metabolism to longevity inC. elegans
Lapierre, L. R., Meléndez, A., & Hansen, M. (2012) · Autophagy · doi:10.4161/auto.8.1.18722 · Cited by 60 · see citing works
Petrov, D., & Žagrović, B. (2011) · Journal of the American Chemical Society · doi:10.1021/ja110577e · Cited by 59 · see citing works
Chakrabarti, S., Hyeon, C., Ye, X., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1712962114 · Cited by 47 · see citing works
Depuydt, G., Shanmugam, N., Rasulova, M., Dhondt, I., & Braeckman, B. P. (2016) · The Journals of Gerontology Series A · doi:10.1093/gerona/glv221 · Cited by 46 · see citing works
Role of Proteome Physical Chemistry in Cell Behavior
Ghosh, K., de Graff, A. M. R., Sawle, L., & Dill, K. A. (2016) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.6b04886 · Cited by 38 · see citing works
Self-citationHow Do Chaperones Protect a Cell's Proteins from Oxidative Damage?
Santra, M., Dill, K. A., & de Graff, A. M. R. (2018) · Cell Systems · doi:10.1016/j.cels.2018.05.001 · Cited by 37 · see citing works
Self-citationFredriksson, Å., Ballesteros, M., Dukan, S., & Nyström, T. (2005) · Molecular Microbiology · doi:10.1111/j.1365-2958.2005.04947.x · Cited by 35 · see citing works
Temperature Dependence of the Folding and Unfolding Kinetics of the GCN4 Leucine Zipper via 13Cα-NMR
Holtzer, M. E., Bretthorst, G. L., d’Avignon, D. A., Angeletti, R. H., Mints, L., & Holtzer, A. M. (2001) · Biophysical Journal · doi:10.1016/s0006-3495(01)76073-0 · Cited by 30 · see citing works
Signatures of Conformational Stability and Oxidation Resistance in Proteomes of Pathogenic Bacteria
Vidovic, A., Supek, F., Nikolic, A., & Kriško, A. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.04.057 · Cited by 21 · see citing works
Shpigel, N., Shemesh, N., Kishner, M., & Ben‐Zvi, A. (2019) · Aging Cell · doi:10.1111/acel.12891 · Cited by 18 · see citing works
Sun, L., Edelmann, F. T., Kaiser, C. J. O., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0033980 · Cited by 17 · see citing works
Structural Basis of Protein Oxidation Resistance: A Lysozyme Study
Girod, M., Enjalbert, Q., Brunet, C., Antoine, R., Lemoine, J., Lukač, I., Radman, M., Kriško, A., & Dugourd, P. (2014) · PLoS ONE · doi:10.1371/journal.pone.0101642 · Cited by 12 · see citing works
McAuley, J., Taylor, R., Simonds, A. K., et al. (2017) · BMJ Case Reports · doi:10.1136/bcr-2016-218484 · Cited by 11 · see citing works
Suda, H., Satõ, K., & Yanase, S. (2012) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2012.07.007 · Cited by 7 · see citing works
Suda, H., Satõ, K., & Shimizu, Y. (2011) · Experimental Gerontology · doi:10.1016/j.exger.2011.02.009 · Cited by 5 · see citing works
Senescent cells and the dynamics of agingPreprint
Karin, O., Agrawal, A., Porat, Z., Krizhanovsky, V., & Alon, U. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/470500 · Cited by 4 · see citing works
Redox Pioneer: Professor Vadim N. Gladyshev
Hatfield, D. L. (2016) · Antioxidants and Redox Signaling · doi:10.1089/ars.2015.6625 · Cited by 4 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Nrf2 and Oxidative Stress: A General Overview of Mechanisms and Implications in Human Disease
Ngo, V., & Duennwald, M. L. (2022) · Antioxidants · doi:10.3390/antiox11122345 · Cited by 1,130 · see citing works
Chang, Y.-H., & Dubnau, J. (2023) · Nature Communications · doi:10.1038/s41467-023-36649-z · Cited by 49 · see citing works
- Authors
- Santra, M., Dill, K. A., & de Graff, A. M. R.
- Affiliations
- Stony Brook School (US)
- Stony Brook University (US)
- Laufer Center for Physical and Quantitative Biology, Stony Brook University, Stony Brook, NY 11794-5252;
- Corresponding author
- Dill, Ken A.
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2019-10-16
- Volume
- 116
- Issue
- 44
- Pages
- 22173-22178
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC6825304
- OpenAlex
- W2981013456
- Cited by
- 175
- References
- 85
- Citations by year
- 2026: 17 · 2025: 27 · 2024: 21 · 2023: 34 · 2022: 35 · 2021: 24 · 2020: 16 · 2019: 1
- FWCI
- 6.91
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion, cc-by-nc-nd)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- eScholarship (California Digital Library) (submittedVersion, cc-by-nc-nd)
- Funders
- NSF | BIO | Division of Biological Infrastructure (PHY1205881)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Aging › Genetics, Aging, and Longevity in Model Organisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Keywords
- proteostasis, cellular aging, cell death, protein folding, molecular chaperones, protein misfolding, protein aggregation, oxidative damage, protein synthesis, protein degradation, biophysical model, lifespan, Caenorhabditis elegans, aging
- MeSH terms
- Proteostasis, Animals, DNA Damage, Models, Biological, Time Factors, Cellular Senescence, Cell Death, Caenorhabditis elegans, Oxidative Stress, Molecular Chaperones
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
