Adapting Proteostasis for Disease Intervention

Signal integration in the endoplasmic reticulum unfolded protein response

Ron, D., & Walter, P. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2199 · Cited by 6,308 · see citing works

THE MAMMALIAN UNFOLDED PROTEIN RESPONSE

Schröder, M., & Kaufman, R. J. (2005) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.011303.074134 · Cited by 3,035 · see citing works

Chemical Chaperones Reduce ER Stress and Restore Glucose Homeostasis in a Mouse Model of Type 2 Diabetes

Özcan, U., Yilmaz, E., Özcan, L., Furuhashi, M., Vaillancourt, E., Smith, R. O., Görgün, C. Z., & Hotamisligil, G. S. (2006) · Science · doi:10.1126/science.1128294 · Cited by 2,413 · see citing works

Regulation of the heat shock transcriptional response: cross talk between a family of heat shock factors, molecular chaperones, and negative regulatorsPreprint

Morimoto, R. I. (1998) · Genes & Development · doi:10.1101/gad.12.24.3788 · Cited by 1,898 · see citing works

Molecular Chaperones and Protein Quality Control

Bukau, B., Weissman, J. S., & Horwich, A. L. (2006) · Cell · doi:10.1016/j.cell.2006.04.014 · Cited by 1,556 · 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

A Selective Inhibitor of eIF2α Dephosphorylation Protects Cells from ER Stress

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Hsp90 as a capacitor of phenotypic variation

Queitsch, C., Sangster, T. A., & Lindquist, S. (2002) · Nature · doi:10.1038/nature749 · Cited by 1,372 · see citing works

The plasticity of aging: insights from long-lived mutants

Kenyon, C. (2005) · Cell · doi:10.1016/j.cell.2005.02.002 · Cited by 1,338 · see citing works

Chaperone Suppression of α-Synuclein Toxicity in a <i>Drosophila</i> Model for Parkinson's Disease

Auluck, P. K., Chan, H. Y. E., Trojanowski, J. Q., Lee, V. M.-Y., & Bonini, N. M. (2002) · Science · doi:10.1126/science.1067389 · Cited by 1,227 · see citing works

Opposing activities protect against age-onset proteotoxicity

Cohen, E., Bieschke, J., Perciavalle, R. M., Kelly, J. W., & Dillin, A. (2006) · Science · doi:10.1126/science.1124646 · Cited by 843 · see citing works

Heat Shock Factor 1 Is a Powerful Multifaceted Modifier of Carcinogenesis

Dai, C., Whitesell, L. J., Rogers, A. B., & Lindquist, S. L. (2007) · Cell · doi:10.1016/j.cell.2007.07.020 · Cited by 827 · see citing works

The threshold for polyglutamine-expansion protein aggregation and cellular toxicity is dynamic and influenced by aging in Caenorhabditis elegans

Morley, J. F., Brignull, H. R., Weyers, J. J., & Morimoto, R. I. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.152161099 · Cited by 811 · see citing works

Therapeutic approaches to protein-misfolding diseases

Cohen, F. E., & Kelly, J. W. (2003) · Nature · doi:10.1038/nature02265 · Cited by 792 · 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

Two neurons mediate diet-restriction-induced longevity in C. elegans

Bishop, N. A., & Guarente, L. (2007) · Nature · doi:10.1038/nature05904 · Cited by 643 · 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

Accelerated transport and maturation of lysosomal α–galactosidase A in Fabry lymphoblasts by an enzyme inhibitor

Fan, J., Ishii, S., Asano, N., & Suzuki, Y. (1999) · Nature Medicine · doi:10.1038/4801 · Cited by 616 · see citing works

Hsp90 Cochaperone Aha1 Downregulation Rescues Misfolding of CFTR in Cystic Fibrosis

Wang, X., Venable, J. D., LaPointe, P., Hutt, D. M., Koulov, A. V., Coppinger, J. A., Gürkan, C., Kellner, W. A., Matteson, J., Plutner, H., et al. (2006) · Cell · doi:10.1016/j.cell.2006.09.043 · Cited by 597 · see citing works

PHA-4/Foxa mediates diet-restriction-induced longevity of C. elegans

Panowski, S. H., Wolff, S., Aguilaniu, H., Durieux, J., & Dillin, A. G. (2007) · Nature · doi:10.1038/nature05837 · Cited by 538 · see citing works

Prevention of Transthyretin Amyloid Disease by Changing Protein Misfolding Energetics

Hammarström, P., Wiseman, R. L., Powers, E. T., & Kelly, J. W. (2003) · Science · doi:10.1126/science.1079589 · Cited by 526 · see citing works

Heat Shock Response Modulators as Therapeutic Tools for Diseases of Protein Conformation

Westerheide, S. D., & Morimoto, R. I. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.r500010200 · Cited by 481 · see citing works

Proteasome-dependent endoplasmic reticulum-associated protein degradation: An unconventional route to a familiar fate

Werner, E. D., Brodsky, J. L., & McCracken, A. A. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.24.13797 · Cited by 463 · see citing works

Celastrols as Inducers of the Heat Shock Response and Cytoprotection

Westerheide, S. D., Bosman, J. D., Mbadugha, B. N. A., Kawahara, T. L. A., Matsumoto, G., Kim, S., Gu, W., Devlin, J. P., Silverman, R. B., & Morimoto, R. I. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409267200 · Cited by 427 · see citing works

The chaperonin TRiC controls polyglutamine aggregation and toxicity through subunit-specific interactions

Tam, S. J., Geller, R., Spiess, C., & Frydman, J. (2006) · Nature Cell Biology · doi:10.1038/ncb1477 · Cited by 308 · see citing works

Chaperonin TRiC Promotes the Assembly of polyQ Expansion Proteins into Nontoxic Oligomers

Behrends, C., Langer, C. A., Boteva, R. N., Böttcher, U. M. K., Stemp, M. J., Schaffar, G., Rao, B. V., Giese, A., Kretzschmar, H. A., Siegers, K., et al. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.08.017 · Cited by 278 · see citing works

Cytosolic chaperonin prevents polyglutamine toxicity with altering the aggregation state

Kitamura, A., KUBOTA, H. Y., Pack, C., Matsumoto, G., Hirayama, S., Takahashi, Y., Kimurâ, H., Kinjo, M., Morimoto, R. I., & Nagata, K. (2006) · Nature Cell Biology · doi:10.1038/ncb1478 · Cited by 277 · see citing works

Evolutionary constraints on chaperone-mediated folding provide an antiviral approach refractory to development of drug resistancePreprint

Geller, R., Vignuzzi, M., Andino, R., & Frydman, J. (2007) · Genes & Development · doi:10.1101/gad.1505307 · Cited by 260 · see citing works

Metabolite-initiated protein misfolding may trigger Alzheimer's disease.

Zhang, Q.-H., Powers, E., Nieva, J., Huff, M. E., Dendle, M. T. A., Bieschke, J., Glabe, C., Eschenmoser, A., Wentworth, P., Lerner, R., et al. (2004) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.0400924101 · Cited by 192 · see citing works

An Adaptable Standard for Protein Export from the Endoplasmic Reticulum

Wiseman, R. L., Powers, E. T., Buxbaum, J. N., Kelly, J. W., & Balch, W. E. (2007) · Cell · doi:10.1016/j.cell.2007.10.025 · Cited by 155 · see citing works

Localization and Suppression of a Kinetic Defect in Cystic Fibrosis Transmembrane Conductance Regulator Folding

Qu, B.-H., Strickland, E., & Thomas, P. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.25.15739 · Cited by 145 · see citing works

Partial Restoration of Mutant Enzyme Homeostasis in Three Distinct Lysosomal Storage Disease Cell Lines by Altering Calcium Homeostasis

Mu, T., Fowler, D. M., & Kelly, J. W. (2008) · PLoS Biology · doi:10.1371/journal.pbio.0060026 · Cited by 125 · see citing works

Filling the Gaps in the Aβ Cascade Hypothesis of Alzheimers Disease

Golde, T. E., Dickson, D. W., & Hutton, M. L. (2006) · Current Alzheimer Research · doi:10.2174/156720506779025189 · Cited by 115 · see citing works

Dissection of the Dislocation Pathway for Type I Membrane Proteins with a New Small Molecule Inhibitor, Eeyarestatin

Fiebiger, E., Hirsch, C., Vyas, J. M., Gordon, E. J., Ploegh, H. L., & Tortorella, D. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e03-07-0506 · Cited by 104 · see citing works

Defective Trafficking of Nephrin Missense Mutants Rescued by a Chemical Chaperone

Liu, X., Doné, S. C., Yan, K., et al. (2004) · Journal of the American Society of Nephrology · doi:10.1097/01.asn.0000129826.28932.fd · Cited by 93 · see citing works

The Effect of Aging on the Chaperone Concentrations in the Hepatic, Endoplasmic Reticulum of Male Rats: The Possible Role of Protein Misfolding Due to the Loss of Chaperones in the Decline in Physiological Function Seen With Age

Erickson, R. R., Dunning, L. M., & Holtzman, J. L. (2006) · The Journals of Gerontology Series A · doi:10.1093/gerona/61.5.435 · Cited by 83 · see citing works

Effect of aging on the chaperone-like function of human α-crystallin assessed by three methods

DERHAM, K. B., & Harding, J. J. (1997) · Biochemical Journal · doi:10.1042/bj3280763 · Cited by 51 · see citing works

Autophagic Defects in Aging: Looking for an “Emergency Exit"?

Massey, A. C., Kiffin, R., & Cuervo, A. M. (2006) · Cell Cycle · doi:10.4161/cc.5.12.2865 · Cited by 41 · see citing works

Single-cell transcriptomic analysis of Alzheimer’s disease

Mathys, H., Davila-Velderrain, J., Peng, Z., Gao, F., Mohammadi, S., Young, J. Z., Menon, M., He, L., Abdurrob, F., Jiang, X., et al. (2019) · Nature · doi:10.1038/s41586-019-1195-2 · Cited by 2,568 · see citing works

Mechanisms, regulation and functions of the unfolded protein response

Hetz, C., Zhang, K., & Kaufman, R. J. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0250-z · Cited by 2,666 · see citing works

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 · see citing works

HSP90 at the hub of protein homeostasis: emerging mechanistic insights

Taipale, M., Jarosz, D. F., & Lindquist, S. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2918 · Cited by 1,818 · see citing works

Disease Tolerance as a Defense Strategy

Medzhitov, R., Schneider, D. S., & Soares, M. P. (2012) · Science · doi:10.1126/science.1214935 · Cited by 1,718 · see citing works

The proteostasis network and its decline in ageing

Hipp, M. S., Kasturi, P., & Hartl, F. U. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0101-y · Cited by 1,642 · see citing works

Self-propagation of pathogenic protein aggregates in neurodegenerative diseases

Jucker, M., & Walker, L. C. (2013) · Nature · doi:10.1038/nature12481 · Cited by 1,663 · see citing works

Huntington disease

Bates, G. P., Dorsey, R., Gusella, J. F., Hayden, M. R., Kay, C., Leavitt, B. R., Nance, M., Ross, C. A., Scahill, R. I., Wetzel, R., et al. (2015) · Nature Reviews Disease Primers · doi:10.1038/nrdp.2015.5 · Cited by 1,641 · 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

Misfolded proteins partition between two distinct quality control compartments

Kaganovich, D., Kopito, R., & Frydman, J. (2008) · Nature · doi:10.1038/nature07195 · Cited by 932 · see citing works

Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging

Morimoto, R. I. (2008) · Genes &amp; Development · doi:10.1101/gad.1657108 · Cited by 872 · see citing works

α-Synuclein propagates from mouse brain to grafted dopaminergic neurons and seeds aggregation in cultured human cells

Hansen, C., Angot, E., Bergström, A.-L., Steiner, J. A., Pieri, L., Paul, G., Outeiro, T. F., Melki, R., Kallunki, P., Fog, K., et al. (2011) · Journal of Clinical Investigation · doi:10.1172/jci43366 · Cited by 842 · see citing works

Stem cell aging: mechanisms, regulators and therapeutic opportunities

Oh, J., Lee, Y. D., & Wagers, A. J. (2014) · Nature Medicine · doi:10.1038/nm.3651 · Cited by 796 · 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

A chaperome subnetwork safeguards proteostasis in aging and neurodegenerative disease

Brehme, M., Voisine, C., Rolland, T., Wachi, S., Soper, J. H., Zhu, Y., Orton, K., Villella, A., Garza, D., Vidal, M., et al. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.09.042 · Cited by 584 · 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

Oral treatment targeting the unfolded protein response prevents neurodegeneration and clinical disease in prion-infected mice

Moreno, J. A., Halliday, M., Molloy, C., Radford, H., Verity, N., Axten, J. M., Ortori, C. A., Willis, A. E., Fischer, P. M., Barrett, D. A., et al. (2013) · Science Translational Medicine · doi:10.1126/scitranslmed.3006767 · Cited by 589 · see citing works

Lysosome activation clears aggregates and enhances quiescent neural stem cell activation during aging

Leeman, D. S., Hebestreit, K., Ruetz, T., Webb, A. E., McKay, A., Pollina, E. A., Dulken, B. W., Zhao, X., Yeo, R. W., Ho, T. T., et al. (2018) · Science · doi:10.1126/science.aag3048 · Cited by 528 · 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

Mitohormesis: Promoting Health and Lifespan by Increased Levels of Reactive Oxygen Species (ROS)

Ristow, M., & Schmeisser, K. (2014) · Dose-Response · doi:10.2203/dose-response.13-035.ristow · Cited by 534 · see citing works

Protein quality control during aging involves recruitment of the macroautophagy pathway by BAG3

Gamerdinger, M., Hajieva, P., Kaya, A. M., Wolfrum, U., Hartl, F. U., & Behl, C. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.29 · Cited by 522 · see citing works

The aging lung: Physiology, disease, and immunity

Schneider, J. L., Rowe, J. H., Garcia-de-Alba, C., Kim, C. F., Sharpe, A. H., & Haigis, M. C. (2021) · Cell · doi:10.1016/j.cell.2021.03.005 · Cited by 500 · see citing works

The CamSol method of rational design of protein mutants with enhanced solubility

Sormanni, P., Aprile, F. A., & Vendruscolo, M. (2015) · Journal of Molecular Biology · doi:10.1016/j.jmb.2014.09.026 · Cited by 494 · see citing works

Protein Homeostasis and Aging: the importance of exquisite quality control

Koga, H., Kaushik, S., & Cuervo, A. M. (2011) · Ageing research reviews · doi:10.1016/j.arr.2010.02.001 · Cited by 476 · see citing works

Tight Regulation of Unstructured Proteins: From Transcript Synthesis to Protein Degradation

Gsponer, J., Futschik, M. E., Teichmann, S. A., & Babu, M. M. (2008) · Science · doi:10.1126/science.1163581 · Cited by 466 · see citing works

Increased proteasome activity in human embryonic stem cells is regulated by PSMD11

Vilchez, D., Boyer, L., Morantte, I., Lutz, M., Merkwirth, C., Joyce, D., Spencer, B., Page, L., Masliah, E., Berggren, W. T., et al. (2012) · Nature · doi:10.1038/nature11468 · Cited by 388 · see citing works

Neurodegenerative Diseases: Expanding the Prion Concept

Walker, L. C., & Jucker, M. (2015) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-071714-033828 · Cited by 361 · see citing works

Aging and Immune Function: Molecular Mechanisms to Interventions

Ponnappan, S., & Ponnappan, U. (2011) · Antioxidants &amp; Redox Signaling · doi:10.1089/ars.2010.3228 · Cited by 339 · see citing works

Physical limits of cells and proteomes

Dill, K. A., Ghosh, K., & Schmit, J. D. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1114477108 · Cited by 298 · see citing works

Amyloid-Beta Protein Clearance and Degradation (ABCD) Pathways and their Role in Alzheimer’s Disease

Baranello, R., Bharani, K., Padmaraju, V., Chopra, N., Lahiri, D., Greig, N., Pappolla, M., & Sambamurti, K. (2015) · Current Alzheimer Research · doi:10.2174/1567205012666141218140953 · Cited by 331 · 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

Spatial sequestration of misfolded proteins by a dynamic chaperone pathway enhances cellular fitness during stress

Escusa-Toret, S., Vonk, W. I. M., & Frydman, J. (2013) · Nature Cell Biology · doi:10.1038/ncb2838 · Cited by 321 · see citing works

Mechanisms that Regulate Stem Cell Aging and Life Span

Signer, R. A. J., & Morrison, S. J. (2013) · Cell Stem Cell · doi:10.1016/j.stem.2013.01.001 · Cited by 320 · see citing works

Network Organization of the Huntingtin Proteomic Interactome in Mammalian Brain

Shirasaki, D. I., Greiner, E. R., Al-Ramahi, I., Gray, M., Boontheung, P., Geschwind, D. H., Botas, J., Coppola, G., Horvath, S., Loo, J. A., et al. (2012) · Neuron · doi:10.1016/j.neuron.2012.05.024 · Cited by 297 · see citing works

Widespread aggregation and neurodegenerative diseases are associated with supersaturated proteins

Ciryam, P., Tartaglia, G. G., Morimoto, R. I., Dobson, C. M., & Vendruscolo, M. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.09.043 · Cited by 270 · see citing works

Aging Hallmarks: The Benefits of Physical Exercise

Rebelo-Marques, A., De Sousa Lages, A., Andrade, R., Ribeiro, C. F., Mota-Pinto, A., Carrilho, F., & Espregueira-Mendes, J. (2018) · Frontiers in Endocrinology · doi:10.3389/fendo.2018.00258 · Cited by 246 · see citing works

Firefly luciferase mutants as sensors of proteome stress

Gupta, R., Kasturi, P., Bracher, A., Loew, C., Zheng, M., Villella, A., Garza, D., Hartl, F. U., & Raychaudhuri, S. (2011) · Nature Methods · doi:10.1038/nmeth.1697 · Cited by 219 · see citing works

The role of calcium and mitochondrial oxidant stress in the loss of substantia nigra pars compacta dopaminergic neurons in Parkinson's disease

Surmeier, D. J., Guzman, J. N., Sanchez-Padilla, J., & Schumacker, P. T. (2011) · Neuroscience · doi:10.1016/j.neuroscience.2011.08.045 · Cited by 236 · see citing works

Emerging roles of <scp>ER</scp> stress in the etiology and pathogenesis of Alzheimer's disease

Gerakis, Y., & Hetz, C. (2018) · The FEBS Journal · doi:10.1111/febs.14332 · Cited by 226 · see citing works

Proteostasis in cardiac health and disease

Henning, R. H., & Brundel, B. J. J. M. (2017) · Nature Reviews Cardiology · doi:10.1038/nrcardio.2017.89 · Cited by 193 · see citing works

Proteostasis collapse is a driver of cell aging and death

Santra, M., Dill, K. A., & de Graff, A. M. R. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1906592116 · Cited by 175 · see citing works

Protein Homeostasis and the Phenotypic Manifestation of Genetic Diversity: Principles and Mechanisms

Jarosz, D. F., Taipale, M., & Lindquist, S. (2010) · Annual Review of Genetics · doi:10.1146/annurev.genet.40.110405.090412 · Cited by 179 · see citing works

Proteomic analysis of age-dependent changes in protein solubility identifies genes that modulate lifespan

Reis‐Rodrigues, P., Czerwieniec, G., Peters, T. W., Evani, U. S., Alavez, S., Gaman, E. A., Vantipalli, M., Mooney, S. D., Gibson, B. W., Lithgow, G. J., et al. (2012) · Aging Cell · doi:10.1111/j.1474-9726.2011.00765.x · Cited by 174 · see citing works

Nicotine is a selective pharmacological chaperone of acetylcholine receptor number and stoichiometry. Implications for drug discovery

Lester, H. A., Xiao, C., Srinivasan, R., Son, C. D., Miwa, J., Pantoja, R., Banghart, M. R., Dougherty, D. A., Goate, A. M., & Wang, J. C. (2009) · The AAPS Journal · doi:10.1208/s12248-009-9090-7 · Cited by 163 · see citing works

Protein Homeostasis and Aging: Taking Care of Proteins From the Cradle to the Grave

Morimoto, R. I., & Cuervo, A. M. (2009) · The Journals of Gerontology Series A: Biological Sciences and Medical Sciences · doi:10.1093/gerona/gln071 · Cited by 151 · see citing works

HSP72 Is a Mitochondrial Stress Sensor Critical for Parkin Action, Oxidative Metabolism, and Insulin Sensitivity in Skeletal Muscle

Drew, B. G., Ribas, V., Le, J. A., Henstridge, D. C., Phun, J., Zhou, Z., Soleymani, T., Daraei, P., Sitz, D., Vergnes, L., et al. (2014) · Diabetes · doi:10.2337/db13-0665 · Cited by 145 · see citing works

DAMPs, ageing, and cancer: The ‘DAMP Hypothesis’

Huang, J., Xie, Y., Sun, X., Zeh, H. J., Kang, R., Lotze, M. T., & Tang, D. (2015) · Ageing Research Reviews · doi:10.1016/j.arr.2014.10.004 · Cited by 144 · see citing works

Endoplasmic Reticulum Stress in Motor Neurons of the Spinal Cord in Sporadic Amyotrophic Lateral Sclerosis

Sasaki, S. (2010) · Journal of Neuropathology &amp; Experimental Neurology · doi:10.1097/nen.0b013e3181d44992 · Cited by 121 · see citing works

Hsp90: A New Player in DNA Repair?

Pennisi, R., Ascenzi, P., & Di Masi, A. (2015) · Biomolecules · doi:10.3390/biom5042589 · Cited by 112 · see citing works

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 · see citing works

Human iPSC-derived neuronal model of Tau-A152T frontotemporal dementia reveals tau-mediated mechanisms of neuronal vulnerability

Silva, M. C., Cheng, C., Mair, W., Almeida, S., Fong, H., Biswas, M. H. U., Zhang, Z., Huang, Y., Temple, S., Coppola, G., et al. (2016) · Stem Cell Reports · doi:10.1016/j.stemcr.2016.08.001 · Cited by 103 · see citing works

Proteostasis and longevity: when does aging really begin?

Labbadia, J., & Morimoto, R. I. (2014) · F1000Prime Reports · doi:10.12703/p6-07 · Cited by 100 · see citing works

Declining signal dependence of <scp>N</scp> rf2‐ <scp>M</scp> af <scp>S</scp> ‐regulated gene expression correlates with aging phenotypes

Rahman, M. M., Sykiotis, G. P., Nishimura, M., Bodmer, R., & Bohmann, D. (2013) · Aging Cell · doi:10.1111/acel.12078 · Cited by 100 · see citing works

Changes in the detergent‐insoluble brain proteome linked to amyloid and tau in Alzheimer's Disease progression

Hales, C. M., Dammer, E. B., Deng, Q., Duong, D. M., Gearing, M., Troncoso, J. C., Thambisetty, M., Lah, J. J., Shulman, J. M., Levey, A. I., et al. (2016) · PROTEOMICS · doi:10.1002/pmic.201600057 · Cited by 99 · see citing works

Proteasome activation delays aging in vitro and in vivo

Chondrogianni, N., Sakellari, M., Lefaki, M., Papaevgeniou, N., & Gonos, E. S. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.03.031 · Cited by 94 · see citing works

Chemoselective small molecules that covalently modify one lysine in a non-enzyme protein in plasma

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

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