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 · see citing works

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 6,435 · see citing works

The Unfolded Protein Response: From Stress Pathway to Homeostatic Regulation

Walter, P., & Ron, D. (2011) · Science · doi:10.1126/science.1209038 · Cited by 5,893 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · 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

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 · see citing works

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 · see citing works

Mammalian autophagy: core molecular machinery and signaling regulation

Yang, Z., & Klionsky, D. J. (2010) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2009.11.014 · Cited by 1,956 · see citing works

Lewy bodies in grafted neurons in subjects with Parkinson's disease suggest host-to-graft disease propagation

Li, J.-Y., Englund, E., Holton, J. L., Soulet, D., Hagell, P., Lees, A. J., Lashley, T., Quinn, N. P., Rehncrona, S., Björklund, A., et al. (2008) · Nature Medicine · doi:10.1038/nm1746 · Cited by 1,845 · 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

Recognition and Processing of Ubiquitin-Protein Conjugates by the Proteasome

Finley, D. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.78.081507.101607 · Cited by 1,764 · see citing works

The HSP70 chaperone machinery: J proteins as drivers of functional specificity

Kampinga, H. H., & Craig, E. A. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2941 · Cited by 1,760 · see citing works

A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein

Chau, V., Tobias, J. W., Bachmair, A., Marriott, D., Ecker, D. J., Gonda, D. K., & Varshavsky, A. (1989) · Science · doi:10.1126/science.2538923 · Cited by 1,535 · see citing works

Molecular Chaperone Functions in Protein Folding and Proteostasis

Kim, Y., Hipp, M. S., Bracher, A., Hayer-Hartl, M. K., & Hartl, F. U. (2013) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060208-092442 · Cited by 1,468 · see citing works

Heat shock factors: integrators of cell stress, development and lifespan

Åkerfelt, M., Morimoto, R. I., & Sistonen, L. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2938 · Cited by 1,457 · see citing works

Inclusion body myopathy associated with Paget disease of bone and frontotemporal dementia is caused by mutant valosin-containing protein

Watts, G. D. J., Wymer, J., Kovach, M. J., Mehta, S. G., Mumm, S., Darvish, D., Pestronk, A., Whyte, M. P., & Kimonis, V. E. (2004) · Nature Genetics · doi:10.1038/ng1332 · Cited by 1,391 · see citing works

UBE3A/E6-AP mutations cause Angelman syndrome

Kishino, T., Lalande, M., & Wagstaff, J. E. (1997) · Nature Genetics · doi:10.1038/ng0197-70 · Cited by 1,304 · see citing works

Excess brain protein oxidation and enzyme dysfunction in normal aging and in Alzheimer disease.

Smith, C. D., Carney, J. M., Starke-Reed, P. E., Oliver, C. N., Stadtman, E. R., Floyd, R. A., & Markesbery, W. R. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.23.10540 · Cited by 1,296 · see citing works

Repression of Heat Shock Transcription Factor HSF1 Activation by HSP90 (HSP90 Complex) that Forms a Stress-Sensitive Complex with HSF1

Zou, J., Guo, Y., Guettouche, T., Smith, D. F., & Voellmy, R. W. (1998) · Cell · doi:10.1016/s0092-8674(00)81588-3 · Cited by 1,232 · 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

Lysosomal Proteolysis and Autophagy Require Presenilin 1 and Are Disrupted by Alzheimer-Related PS1 Mutations

Lee, J.-H., Yu, W. H., Kumar, A., Lee, S., Mohan, P. S., Peterhoff, C. M., Wolfe, D. M., Martinez-Vicente, M., Massey, A. C., Sovak, G., et al. (2010) · Cell · doi:10.1016/j.cell.2010.05.008 · Cited by 1,212 · see citing works

Mutations in UBQLN2 cause dominant X-linked juvenile and adult-onset ALS and ALS/dementia

Deng, H.-X., Chen, W., Hong, S.-T., Boycott, K. M., Gorrie, G. H., Siddique, N., Yang, Y., Fecto, F., Shi, Y., Zhai, H., et al. (2011) · Nature · doi:10.1038/nature10353 · Cited by 1,174 · 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

Autophagy Induction and Autophagosome Clearance in Neurons: Relationship to Autophagic Pathology in Alzheimer's Disease

Boland, B., Kumar, A., Lee, S., Platt, F. M., Wegiel, J., Yu, W. H., & Nixon, R. A. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.0800-08.2008 · Cited by 1,119 · see citing works

Aggregate-prone proteins with polyglutamine and polyalanine expansions are degraded by autophagy

Ravikumar, B. (2002) · Human Molecular Genetics · doi:10.1093/hmg/11.9.1107 · Cited by 1,099 · see citing works

The Cell Non-Autonomous Nature of Electron Transport Chain-Mediated Longevity

Durieux, J., Wolff, S., & Dillin, A. (2011) · Cell · doi:10.1016/j.cell.2010.12.016 · Cited by 1,059 · see citing works

The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins

Connell, P. M., Ballinger, C. A., Jiang, J., Wu, Y., Thompson, L. J., Höhfeld, J., & Patterson, C. (2000) · Nature Cell Biology · doi:10.1038/35050618 · Cited by 1,002 · see citing works

Role of Rpn11 Metalloprotease in Deubiquitination and Degradation by the 26 S Proteasome

Verma, R., Aravind, L., Oania, R. S., McDonald, W. H., Yates, J. R., Koonin, E. V., & Deshaies, R. J. (2002) · Science · doi:10.1126/science.1075898 · Cited by 994 · see citing works

The changing scene of amyotrophic lateral sclerosis

Robberecht, W., & Philips, T. (2013) · Nature Reviews Neuroscience · doi:10.1038/nrn3430 · Cited by 957 · see citing works

Enhancement of proteasome activity by a small-molecule inhibitor of USP14

Lee, B., Lee, M. J., Park, S., Oh, D., Elsasser, S., Chen, P., Gartner, C. A., Dimova, N. V., Hanna, J. W., Gygi, S. P., et al. (2010) · Nature · doi:10.1038/nature09299 · Cited by 943 · see citing works

Cargo recognition failure is responsible for inefficient autophagy in Huntington’s disease

Martinez-Vicente, M., Talloczy, Z., Wong, E., Tang, G., Koga, H., Kaushik, S., de Vries, R., Arias, E., Harris, S., Sulzer, D., et al. (2010) · Nature Neuroscience · doi:10.1038/nn.2528 · Cited by 885 · see citing works

Chaperone-mediated autophagy: a unique way to enter the lysosome world

Kaushik, S., & Cuervo, A. M. (2012) · Trends in Cell Biology · doi:10.1016/j.tcb.2012.05.006 · Cited by 850 · see citing works

Impaired Proteasome Function in Alzheimer's Disease

Keller, J. N., Hanni, K. B., & Markesbery, W. R. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0750436.x · Cited by 848 · 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

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

Yeast heat shock factor is an essential DNA-binding protein that exhibits temperature-dependent phosphorylation

Sorger, P. K., & Pelham, H. R. B. (1988) · Cell · doi:10.1016/s0092-8674(88)91219-6 · Cited by 832 · see citing works

Some like it hot: the structure and function of small heat-shock proteins

Haslbeck, M., Franzmann, T. M., Weinfurtner, D., & Büchner, J. (2005) · Nature Structural & Molecular Biology · doi:10.1038/nsmb993 · Cited by 830 · 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

α-Synuclein impairs macroautophagy: implications for Parkinson’s disease

Winslow, A. R., Chen, C.-W., Corrochano, S., Acevedo-Arozena, A., Gordon, D. E., Peden, A. A., Lichtenberg, M., Menzies, F. M., Ravikumar, B., Imarisio, S., et al. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201003122 · Cited by 825 · 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

Novel targets for Huntington's disease in an mTOR-independent autophagy pathway

Williams, A., Sarkar, S., Cuddon, P., Ttofi, E. K., Saiki, S., Siddiqi, F. H., Jahreiss, L., Fleming, A., Pask, D., Goldsmith, P., et al. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.79 · Cited by 800 · see citing works

Stress-activated cap’n’collar transcription factors in aging and human disease

Sykiotis, G. P., & Bohmann, D. (2010) · Science Signaling · doi:10.1126/scisignal.3112re3 · Cited by 776 · see citing works

A cryptic protease couples deubiquitination and degradation by the proteasome

Yao, T., & Cohen, R. E. (2002) · Nature · doi:10.1038/nature01071 · Cited by 727 · see citing works

Stress-Inducible Regulation of Heat Shock Factor 1 by the Deacetylase SIRT1

Westerheide, S. D., Anckar, J., Stevens, S. M., Sistonen, L., & Morimoto, R. I. (2009) · Science · doi:10.1126/science.1165946 · Cited by 722 · see citing works

Disturbance of endoplasmic reticulum proteostasis in neurodegenerative diseases

Hetz, C., & Mollereau, B. (2014) · Nature Reviews Neuroscience · doi:10.1038/nrn3689 · Cited by 684 · see citing works

Molecular chaperones as HSF1-specific transcriptional repressors.Preprint

Shi, Y.-H., Mosser, D., & Morimoto, R. (1998) · Genes & Development · doi:10.1101/gad.12.5.654 · Cited by 681 · see citing works

Amyloid-like Aggregates Sequester Numerous Metastable Proteins with Essential Cellular Functions

Olzscha, H., Schermann, S. M., Woerner, A. C., Pinkert, S., Hecht, M. H., Tartaglia, G. G., Vendruscolo, M., Hayer-Hartl, M. K., Hartl, F. U., & Vabulas, R. M. (2011) · Cell · doi:10.1016/j.cell.2010.11.050 · Cited by 679 · see citing works

Rapamycin alleviates toxicity of different aggregate-prone proteins

Berger, Z., Ravikumar, B., Menzies, F. M., Oroz, L. G., Underwood, B. R., Pangalos, M. N., Schmitt, I., Wullner, U., Evert, B. O., O'Kane, C. J., et al. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddi458 · Cited by 657 · see citing works

Proteostasis impairment in protein-misfolding and -aggregation diseases

Hipp, M. S., Park, S.-H., & Hartl, F. U. (2014) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.05.003 · Cited by 656 · see citing works

FOXO/4E-BP Signaling in Drosophila Muscles Regulates Organism-wide Proteostasis during Aging

Demontis, F., & Perrimon, N. (2010) · Cell · doi:10.1016/j.cell.2010.10.007 · Cited by 656 · see citing works

Proteasomal function is impaired in substantia nigra in Parkinson’s disease

McNaught, K. S. P., & Jenner, P. (2001) · Neuroscience Letters · doi:10.1016/s0304-3940(00)01701-8 · Cited by 653 · 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

Dopamine-modified α-synuclein blocks chaperone-mediated autophagy

Martínez‐Vicente, M., Tallóczy, Z., Kaushik, S., Massey, A. C., Mazzulli, J. R., Mosharov, E. V., Hodara, R., Fredenburg, R. A., Wu, D.-C., Follenzi, A., et al. (2008) · Journal of Clinical Investigation · doi:10.1172/jci32806 · Cited by 633 · see citing works

A Ribosome-Bound Quality Control Complex Triggers Degradation of Nascent Peptides and Signals Translation Stress

Brandman, O., Stewart-Ornstein, J., Wong, D., Larson, A. G., Williams, C. C., Li, G., Zhou, S., King, D., Shen, P. S., Weibezahn, J., et al. (2012) · Cell · doi:10.1016/j.cell.2012.10.044 · Cited by 631 · 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

Small molecules enhance autophagy and reduce toxicity in Huntington's disease models

Sarkar, S., Perlstein, E. O., Imarisio, S., Pineau, S., Cordenier, A., Maglathlin, R. L., Webster, J. A., Lewis, T. A., O’Kane, C. J., Schreiber, S. L., et al. (2007) · Nature Chemical Biology · doi:10.1038/nchembio883 · Cited by 596 · 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

Mutant small heat-shock protein 27 causes axonal Charcot-Marie-Tooth disease and distal hereditary motor neuropathy

Evgrafov, O. V., Mersiyanova, I., Irobi, J., Bosch, L. V. D., Dierick, I., Leung, C. L., Shchagina, O., Verpoorten, N., Impe, K. V., Fedotov, V. P., et al. (2004) · Nature Genetics · doi:10.1038/ng1354 · Cited by 581 · see citing works

The Sizes of Peptides Generated from Protein by Mammalian 26 and 20 S Proteasomes

Kisselev, A. F., Akopian, T. N., Woo, K. M., & Goldberg, A. L. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.6.3363 · Cited by 573 · see citing works

XBP-1 Is a Cell-Nonautonomous Regulator of Stress Resistance and Longevity

Taylor, R. C., & Dillin, A. G. (2013) · Cell · doi:10.1016/j.cell.2013.05.042 · Cited by 570 · see citing works

HSF1 is required for extra‐embryonic development, postnatal growth and protection during inflammatory responses in mice

Xiao, X., Zuo, X., Davis, A. A., McMillan, D. R., Curry, B. B., Richardson, J. A., & Benjamin, I. J. (1999) · The EMBO Journal · doi:10.1093/emboj/18.21.5943 · Cited by 542 · see citing works

Treatment with arimoclomol, a coinducer of heat shock proteins, delays disease progression in ALS mice

Kieran, D., Kalmár, B., Dick, J. R. T., Riddoch‐Contreras, J., Burnstock, G., & Greensmith, L. (2004) · Nature Medicine · doi:10.1038/nm1021 · Cited by 522 · see citing works

Global changes to the ubiquitin system in Huntington's disease

Bennett, E. J., Shaler, T. A., Woodman, B., Ryu, K.-Y., Zaitseva, T. S., Becker, C. H., Bates, G. P., Schulman, H., & Kopito, R. R. (2007) · Nature · doi:10.1038/nature06022 · Cited by 497 · see citing works

Prion-like propagation of mutant superoxide dismutase-1 misfolding in neuronal cells

Münch, C., O’Brien, J., & Bertolotti, A. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1017275108 · Cited by 475 · see citing works

Timing Requirements for Insulin/IGF-1 Signaling in C. elegans

Dillin, A., Crawford, D. K., & Kenyon, C. J. (2002) · Science · doi:10.1126/science.1074240 · Cited by 467 · see citing works

Advances in the genetics of Parkinson disease

Trinh, J., & Farrer, M. J. (2013) · Nature Reviews Neurology · doi:10.1038/nrneurol.2013.132 · Cited by 465 · see citing works

Activation of Human Heat Shock Genes Is Accompanied by Oligomerization, Modification, and Rapid Translocation of Heat Shock Transcription Factor HSF1

Baler, R., Dahl, G., & Voellmy, R. W. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.4.2486 · Cited by 460 · see citing works

Deciphering the mechanism underlying late-onset Alzheimer disease

Krstic, D., & Knuesel, I. (2013) · Nature Reviews Neurology · doi:10.1038/nrneurol.2012.236 · Cited by 457 · see citing works

Editing of ubiquitin conjugates by an isopeptidase in the 26S proteasome

Lam, Y. A., Xu, W., Demartino, G., & Cohen, R. E. (1997) · Nature · doi:10.1038/385737a0 · Cited by 455 · see citing works

Autosomal dominant congenital cataract associated with a missense mutation in the human alpha crystallin gene CRYAA

Litt, M. (1998) · Human Molecular Genetics · doi:10.1093/hmg/7.3.471 · Cited by 447 · see citing works

Geldanamycin activates a heat shock response and inhibits huntingtin aggregation in a cell culture model of Huntington's disease

Sittler, A. (2001) · Human Molecular Genetics · doi:10.1093/hmg/10.12.1307 · Cited by 442 · see citing works

Human αB-Crystallin Mutation Causes Oxido-Reductive Stress and Protein Aggregation Cardiomyopathy in Mice

Rajasekaran, N. S., Connell, P., Christians, E. S., Yan, L.-J., Taylor, R. P., Orosz, A., Zhang, X. Q., Stevenson, T. J., Peshock, R. M., Leopold, J. A., et al. (2007) · Cell · doi:10.1016/j.cell.2007.06.044 · Cited by 437 · see citing works

ARSACS, a spastic ataxia common in northeastern Québec, is caused by mutations in a new gene encoding an 11.5-kb ORF

Engert, J. C., Bérubé, P., Mercier, J., Doré, C., Lepage, P., Ge, B., Bouchard, J.-P., Mathieu, J., Melançon, S. B., Schalling, M., et al. (2000) · Nature Genetics · doi:10.1038/72769 · Cited by 434 · see citing works

Autophagy induction enhances TDP43 turnover and survival in neuronal ALS models

Barmada, S. J., Serio, A., Arjun, A., Bilican, B., Daub, A., Ando, D. M., Tsvetkov, A., Pleiss, M., Li, X., Peisach, D., et al. (2014) · Nature Chemical Biology · doi:10.1038/nchembio.1563 · Cited by 431 · see citing works

Analysis of the Role of Heat Shock Protein (Hsp) Molecular Chaperones in Polyglutamine Disease

Chai, Y., Koppenhafer, S. L., Bonini, N. M., & Paulson, H. L. (1999) · Journal of Neuroscience · doi:10.1523/jneurosci.19-23-10338.1999 · Cited by 421 · 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

Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates

Ren, P.-H., Lauckner, J. E., Kachirskaia, I., Heuser, J. E., Melki, R., & Kopito, R. R. (2009) · Nature Cell Biology · doi:10.1038/ncb1830 · Cited by 410 · see citing works

17-AAG, an Hsp90 inhibitor, ameliorates polyglutamine-mediated motor neuron degeneration

Waza, M., Adachi, H., Katsuno, M., Minamiyama, M., Sang, C., Tanaka, F., Inukai, A., Doyu, M., & Sobue, G. (2005) · Nature Medicine · doi:10.1038/nm1298 · Cited by 395 · see citing works

A Quantitative Chaperone Interaction Network Reveals the Architecture of Cellular Protein Homeostasis Pathways

Taipale, M., Tucker, G., Peng, J., Krykbaeva, I., Lin, Z., Larsen, B. G., Choi, H., Berger, B., Gingras, A., & Lindquist, S. L. (2014) · Cell · doi:10.1016/j.cell.2014.05.039 · Cited by 388 · 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

Cooperation of a ubiquitin domain protein and an E3 ubiquitin ligase during chaperone/proteasome coupling

Demand, J., Alberti, S., Patterson, C., & Höhfeld, J. (2001) · Current Biology · doi:10.1016/s0960-9822(01)00487-0 · Cited by 377 · see citing works

Hereditary Spastic Paraplegia SPG13 Is Associated with a Mutation in the Gene Encoding the Mitochondrial Chaperonin Hsp60

Hansen, J. J., Dürr, A., Cournu‐Rebeix, I., Georgopoulos, C. P., Ang, D., Nielsen, M. N., Davoine, C.-S., Brice, A., Fontaine, B., Gregersen, N., et al. (2002) · The American Journal of Human Genetics · doi:10.1086/339935 · Cited by 373 · see citing works

Huntington's disease: underlying molecular mechanisms and emerging concepts

Labbadia, J. P., & Morimoto, R. I. (2013) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2013.05.003 · Cited by 368 · see citing works

Regulation of the Cellular Heat Shock Response in Caenorhabditis elegans by Thermosensory Neurons

Prahlad, V., Cornelius, T., & Morimoto, R. I. (2008) · Science · doi:10.1126/science.1156093 · Cited by 359 · see citing works

PolyQ Proteins Interfere with Nuclear Degradation of Cytosolic Proteins by Sequestering the Sis1p Chaperone

Park, S.-H., Kukushkin, Y., Gupta, R., Chen, T., Konagai, A., Hipp, M. S., Hayer-Hartl, M. K., & Hartl, F. U. (2013) · Cell · doi:10.1016/j.cell.2013.06.003 · Cited by 358 · see citing works

Deubiquitinating Enzyme Ubp6 Functions Noncatalytically to Delay Proteasomal Degradation

Hanna, J. W., Hathaway, N. A., Tone, Y., Crosas, B., Elsasser, S., Kirkpatrick, D. S., Leggett, D., Gygi, S. P., King, R. W., & Finley, D. J. (2006) · Cell · doi:10.1016/j.cell.2006.07.038 · Cited by 354 · see citing works

The gene for Machado–Joseph disease maps to human chromosome 14q

Takiyama, Y., Nishizawa, M., Tanaka, H., Kawashima, S., Sakamoto, H., Karube, Y., Shimazaki, H., Soutome, M., Endo, K., Ohta, S., et al. (1993) · Nature Genetics · doi:10.1038/ng0793-300 · Cited by 345 · see citing works

Autophagy and Lipid Metabolism Coordinately Modulate Life Span in Germline-less C. elegans

Lapierre, L. R., Gelino, S., Meléndez, A., & Hansen, M. (2011) · Current Biology · doi:10.1016/j.cub.2011.07.042 · Cited by 343 · see citing works

Widespread Regulation of Translation by Elongation Pausing in Heat Shock

Shalgi, R., Hurt, J. A., Krykbaeva, I., Taipale, M., Lindquist, S. L., & Burge, C. B. (2013) · Molecular Cell · doi:10.1016/j.molcel.2012.11.028 · Cited by 334 · see citing works

Progressive decrease in chaperone protein levels in a mouse model of Huntington's disease and induction of stress proteins as a therapeutic approach

Hay, D. (2004) · Human Molecular Genetics · doi:10.1093/hmg/ddh144 · Cited by 329 · see citing works

Proteasome assembly defect due to a proteasome subunit beta type 8 (PSMB8) mutation causes the autoinflammatory disorder, Nakajo-Nishimura syndrome

Arima, K., Kinoshita, A., Mishima, H., Kanazawa, N., Kaneko, T., Mizushima, T., Ichinose, K., Nakamura, H., Tsujino, A., Kawakami, A., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1106015108 · Cited by 326 · see citing works

Inhibition of the ubiquitin-proteasome system in Alzheimer's disease

Lam, Y. A., Pickart, C. M., Alban, A., Landon, M., Jamieson, C. J., Ramage, R., Mayer, R. J., & Layfield, R. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.170173897 · Cited by 325 · see citing works

TorsinA and heat shock proteins act as molecular chaperones: suppression of α‐synuclein aggregation

McLean, P. J., Kawamata, H., Shariff, S., Hewett, J. W., Sharma, N., Ueda, K., Breakefield, X. O., & Hyman, B. T. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.01190.x · Cited by 324 · see citing works

A Deleterious Mutation in DNAJC6 Encoding the Neuronal-Specific Clathrin-Uncoating Co-Chaperone Auxilin, Is Associated with Juvenile Parkinsonism

Edvardson, S., Cinnamon, Y., Ta‐Shma, A., Shaag, A., Yim, Y.-I., Zenvirt, S., Jalas, C., Lesage, S., Brice, A., Taraboulos, A., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0036458 · Cited by 318 · see citing works

Metazoan Hsp70 machines use Hsp110 to power protein disaggregation

Rampelt, H., Kirstein, J., Nillegoda, N. B., Chi, K., Scholz, S., Morimoto, R. I., & Bukau, B. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.264 · Cited by 316 · see citing works

DNAJC13 mutations in Parkinson disease

Vilariño‐Güell, C., Rajput, A. H., Milnerwood, A. J., Shah, B., Szu‐Tu, C., Trinh, J., Yu, I. S., Encarnacion, M. J., Munsie, L. N., Tapia, L., et al. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt570 · Cited by 313 · see citing works

Multiple functions of Drosophila heat shock transcription factor in vivo

Jedlicka, P., Mortin, M. A., & Wu, C. (1997) · The EMBO Journal · doi:10.1093/emboj/16.9.2452 · Cited by 306 · see citing works

Decreased levels of proteasome activity and proteasome expression in aging spinal cord

Keller, J. N., Huang, F. F., & Markesbery, W. R. (2000) · Neuroscience · doi:10.1016/s0306-4522(00)00067-1 · Cited by 297 · 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

Genetic Evidence Linking Age-Dependent Attenuation of the 26S Proteasome with the Aging Process

Tonoki, A., Kuranaga, E., Tomioka, T., Hamazaki, J., Murata, S., Tanaka, K., & Miura, M. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01227-08 · Cited by 288 · see citing works

Inefficient degradation of truncated polyglutamine proteins by the proteasome

Holmberg, C. I., Staniszewski, K. E., Mensah, K., Matouschek, A. T., & Morimoto, R. I. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600426 · Cited by 286 · see citing works

Pharmacological prevention of Parkinson disease in Drosophila

Auluck, P. K., & Bonini, N. M. (2002) · Nature Medicine · doi:10.1038/nm1102-1185 · Cited by 280 · see citing works

High Threshold for Induction of the Stress Response in Motor Neurons Is Associated with Failure to Activate HSF1

Batulan, Z., Shinder, G. A., Minotti, S., He, B. P., Doroudchi, M. M., Nalbantoglu, J. N., Strong, M. J., & Durham, H. D. (2003) · Journal of Neuroscience · doi:10.1523/jneurosci.23-13-05789.2003 · Cited by 269 · see citing works

A small-molecule scaffold induces autophagy in primary neurons and protects against toxicity in a Huntington disease model

Tsvetkov, A. S., Miller, J., Arrasate, M., Wong, J. S., Pleiss, M. A., & Finkbeiner, S. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1004498107 · Cited by 266 · see citing works

Autophagy induction reduces mutant ataxin-3 levels and toxicity in a mouse model of spinocerebellar ataxia type 3

Menzies, F. M., Hübener‐Schmid, J., Renna, M., von Bonin, M., Rieß, O., & Rubinsztein, D. C. (2009) · Brain · doi:10.1093/brain/awp292 · Cited by 260 · see citing works

Nuclear factor erythroid 2-related factor 2 protects against beta amyloid

Kanninen, K. M., Malm, T., Jyrkkänen, H.-K., Goldsteins, G., Keksa-Goldsteine, V., Tanila, H., Yamamoto, M. P., Ylä‐Herttuala, S., Levonen, A., & Koıstınaho, J. (2008) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2008.07.010 · Cited by 256 · see citing works

Systems Analyses Reveal Two Chaperone Networks with Distinct Functions in Eukaryotic Cells

Albanèse, V., Yam, A. Y.-W., Baughman, J. M., Parnot, C., & Frydman, J. (2006) · Cell · doi:10.1016/j.cell.2005.11.039 · Cited by 254 · see citing works

Mutations in SIL1 cause Marinesco-Sjögren syndrome, a cerebellar ataxia with cataract and myopathy

Senderek, J., Krieger, M., Stendel, C., Bergmann, C., Moser, M., Breitbach‐Faller, N., Rudnik‐Schöneborn, S., Blaschek, A., Wolf, N. I., Harting, I., et al. (2005) · Nature Genetics · doi:10.1038/ng1678 · Cited by 252 · see citing works

Protein rescue from aggregates by powerful molecular chaperone machines

Doyle, S. M., Genest, O., & Wickner, S. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3660 · Cited by 250 · see citing works

Diversity in the origins of proteostasis networks — a driver for protein function in evolution

Powers, E. T., & Balch, W. E. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3542 · Cited by 247 · see citing works

The gene disrupted in Marinesco-Sjögren syndrome encodes SIL1, an HSPA5 cochaperone

Anttonen, A., Mahjneh, I., Hämäläinen, R. H., Lagier‐Tourenne, C., Kopra, O., Waris, L., Anttonen, M., Joensuu, T. H., Kalimo, H., Paetau, A. E., et al. (2005) · Nature Genetics · doi:10.1038/ng1677 · Cited by 242 · see citing works

Mutations in SQSTM1 encoding p62 in amyotrophic lateral sclerosis: genetics and neuropathology

Teyssou, E., Takeda, T., Lebon, V., Boillée, S., Doukouré, B., Bataillon, G., Sazdovitch, V., Cazeneuve, C., Meininger, V., LeGuern, E., et al. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1090-0 · Cited by 241 · see citing works

Mutation of DNAJC19, a human homologue of yeast inner mitochondrial membrane co-chaperones, causes DCMA syndrome, a novel autosomal recessive Barth syndrome-like condition

Davey, K., Parboosingh, J. S., McLeod, D. R., Chan, A., Casey, R., Ferreira, P., Snyder, F. F., Bridge, P. J., & Bernier, F. P. (2005) · Journal of Medical Genetics · doi:10.1136/jmg.2005.036657 · Cited by 239 · see citing works

Pharmacological induction of heat-shock proteins alleviates polyglutamine-mediated motor neuron disease

Katsuno, M., Sang, C., Adachi, H., Minamiyama, M., Waza, M., Tanaka, F., Doyu, M., & Sobue, G. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506249102 · Cited by 236 · see citing works

Amyloid β-Protein Inhibits Ubiquitin-dependent Protein Degradation in Vitro

Gregori, L. L., Fuchs, C., Figueiredo‐Pereira, M. E., Nostrand, W. E. V., & Goldgaber, D. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.34.19702 · Cited by 232 · see citing works

DNA damage in germ cells induces an innate immune response that triggers systemic stress resistance

Ermolaeva, M. A., Segref, A., Dakhovnik, A., Ou, H.-L., Schneider, J. I., Utermöhlen, O., Hoppe, T., & Schumacher, B. (2013) · Nature · doi:10.1038/nature12452 · Cited by 221 · see citing works

Small-molecule proteostasis regulators for protein conformational diseases

Calamini, B., Silva, M. C., Madoux, F., Hutt, D. M., Khanna, S., Chalfant, M. A., Saldanha, S. A., Hodder, P., Tait, B. D., Garza, D., et al. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.763 · Cited by 220 · see citing works

Stress-induced heat shock protein 70 expression in adrenal cortex: an adrenocorticotropic hormone-sensitive, age-dependent response.

Blake, M. J., Udelsman, R., Feulner, G. J., Norton, D. D., & Holbrook, N. J. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.21.9873 · Cited by 219 · see citing works

Interaction of intracellular β amyloid peptide with chaperone proteins

Fonte, V. G., Kapulkin, W. J., Taft, A. S., Fluet, A., Friedman, D., & Link, C. D. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.152313999 · Cited by 211 · see citing works

Evaluating and responding to mitochondrial dysfunction: the mitochondrial unfolded-protein response and beyond

Haynes, C. M., Fiorese, C. J., & Lin, Y. (2013) · Trends in Cell Biology · doi:10.1016/j.tcb.2013.02.002 · Cited by 209 · see citing works

Mutant SOD1 alters the motor neuronal transcriptome: implications for familial ALS

Kirby, J., Halligan, E. P., Baptista, M. J., Allen, S., Heath, P. R., Holden, H. M., Barber, S. C., Loynes, C. A., Wood-Allum, C. A., Lunec, J., et al. (2005) · Brain · doi:10.1093/brain/awh503 · Cited by 200 · see citing works

Heat Shock Transcription Factor 1-activating Compounds Suppress Polyglutamine-induced Neurodegeneration through Induction of Multiple Molecular Chaperones

Fujikake, N., Nagai, Y., Popiel, H. A., Okamoto, Y., Yamaguchi, M., & Toda, T. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m710521200 · Cited by 199 · see citing works

Regulation of Organismal Proteostasis by Transcellular Chaperone Signaling

van Oosten‐Hawle, P., Porter, R. S., & Morimoto, R. I. (2013) · Cell · doi:10.1016/j.cell.2013.05.015 · Cited by 197 · see citing works

Neural transplants in patients with Huntington's disease undergo disease-like neuronal degeneration

Cicchetti, F., Saporta, S., Hauser, R. A., Parent, M., Saint‐Pierre, M., Sanberg, P. R., Li, X., Parker, J. R., Chu, Y., Mufson, E. J., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0904239106 · Cited by 196 · see citing works

Widespread Inhibition of Posttranscriptional Splicing Shapes the Cellular Transcriptome following Heat Shock

Shalgi, R., Hurt, J. A., Lindquist, S. L., & Burge, C. B. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.04.044 · Cited by 192 · see citing works

Modulation of Heat Shock Transcription Factor 1 as a Therapeutic Target for Small Molecule Intervention in Neurodegenerative Disease

Neef, D. W., Turski, M. L., & Thiele, D. J. (2010) · PLoS Biology · doi:10.1371/journal.pbio.1000291 · Cited by 190 · see citing works

Ribosome-associated chaperones as key players in proteostasis

Preißler, S., & Deuerling, E. (2012) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2012.03.002 · Cited by 189 · see citing works

Transneuronal propagation of mutant huntingtin contributes to non–cell autonomous pathology in neurons

Pecho‐Vrieseling, E., Rieker, C., Fuchs, S., Bleckmann, D., Esposito, M. S., Botta, P., Goldstein, C., Bernhard, M., Galimberti, I., Müller, M. M., et al. (2014) · Nature Neuroscience · doi:10.1038/nn.3761 · Cited by 185 · see citing works

Proteostasis of polyglutamine varies among neurons and predicts neurodegeneration

Tsvetkov, A. S., Arrasate, M., Barmada, S., Ando, D. M., Sharma, P., Shaby, B. A., & Finkbeiner, S. (2013) · Nature Chemical Biology · doi:10.1038/nchembio.1308 · Cited by 178 · 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

Small heat-shock protein 22 mutated in autosomal dominant Charcot-Marie-Tooth disease type 2L

Tang, B., Zhao, G., Luo, W., Xia, K., Cai, F., Pan, Q., Zhang, R.-X., Zhang, F.-F., Liu, X., Chen, B., et al. (2004) · Human Genetics · doi:10.1007/s00439-004-1218-3 · Cited by 174 · see citing works

Exome sequencing reveals DNAJB6 mutations in dominantly‐inherited myopathy

Harms, M. B., Sommerville, R. B., Allred, P., Bell, S., Ma, D., Cooper, P. R., Lopate, G., Pestronk, A., Weihl, C. C., & Baloh, R. H. (2011) · Annals of Neurology · doi:10.1002/ana.22683 · Cited by 173 · see citing works

Altered chromatin architecture underlies progressive impairment of the heat shock response in mouse models of Huntington disease

Labbadia, J. P., Cunliffe, H. E., Weiss, A., Katsyuba, E., Sathasivam, K., Seredenina, T. S., Woodman, B., Moussaoui, S. M., Frentzel, S., Luthi‐Carter, R., et al. (2011) · Journal of Clinical Investigation · doi:10.1172/jci57413 · Cited by 171 · see citing works

Indirect inhibition of 26S proteasome activity in a cellular model of Huntington’s disease

Hipp, M. S., Patel, C. N., Bersuker, K., Riley, B. E., Kaiser, S. E., Shaler, T. A., Brandeis, M., & Kopito, R. R. (2012) · The Journal of Cell Biology · doi:10.1083/jcb.201110093 · Cited by 168 · see citing works

A Direct Regulatory Interaction between Chaperonin TRiC and Stress-Responsive Transcription Factor HSF1

Neef, D. W., Jaeger, A. M., Gómez‐Pastor, R., Willmund, F., Frydman, J., & Thiele, D. J. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.09.056 · Cited by 163 · see citing works

Structural properties and neuronal toxicity of amyotrophic lateral sclerosis–associated Cu/Zn superoxide dismutase 1 aggregates

Matsumoto, G., Stojanovic, A., Holmberg, C. I., Kim, S., & Morimoto, R. I. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200504050 · Cited by 162 · see citing works

VAPB interacts with and modulates the activity of ATF6

Gkogkas, C. G., Middleton, S., Kremer, A., Wardrope, C., Hannah, M. J., Gillingwater, T. H., & Skehel, P. (2008) · Human Molecular Genetics · doi:10.1093/hmg/ddn040 · Cited by 161 · see citing works

Functional alterations of the ubiquitin-proteasome system in motor neurons of a mouse model of familial amyotrophic lateral sclerosis†

Cheroni, C., Marino, M., Tortarolo, M., Veglianese, P., Biasi, S. D., Fontana, E., Vitellaro‐Zuccarello, L., Maynard, C. J., Dantuma, N. P., & Bendotti, C. (2008) · Human Molecular Genetics · doi:10.1093/hmg/ddn319 · Cited by 159 · see citing works

Interplay of Acetyltransferase EP300 and the Proteasome System in Regulating Heat Shock Transcription Factor 1

Raychaudhuri, S., Loew, C., Körner, R., Pinkert, S., Theis, M., Hayer-Hartl, M. K., Buchholz, F., & Hartl, F. U. (2014) · Cell · doi:10.1016/j.cell.2014.01.055 · Cited by 149 · 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

Quality Control Autophagy Degrades Soluble ERAD-Resistant Conformers of the Misfolded Membrane Protein GnRHR

Houck, S. A., Ren, H. Y., Madden, V. J., Bonner, J. N., Conlin, M. P., Janovick, J. A., Conn, P. M., & Cyr, D. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.02.025 · Cited by 147 · see citing works

Sorting out the trash: the spatial nature of eukaryotic protein quality control

Sontag, E. M., Vonk, W. I. M., & Frydman, J. (2014) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2013.12.006 · Cited by 146 · see citing works

Neuronal circuitry regulates the response of Caenorhabditis elegans to misfolded proteins

Prahlad, V., & Morimoto, R. I. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1106557108 · Cited by 143 · see citing works

Dissecting the role of the mitochondrial chaperone mortalin in Parkinson's disease: functional impact of disease-related variants on mitochondrial homeostasis

Burbulla, L. F., Schelling, C., Kato, H., Rapaport, D., Woitalla, D., Schiesling, C., Schulte, C., Sharma, M., Illig, T., Bauer, P., et al. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq370 · Cited by 137 · see citing works

Mutant Huntingtin reduces HSP70 expression through the sequestration of NF‐Y transcription factor

Yamanaka, T., Miyazaki, H., Oyama, F., Kurosawa, M., Washizu, C., Doi, H., & Nukina, N. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.23 · Cited by 126 · see citing works

Identification of a Tissue-Selective Heat Shock Response Regulatory Network

Guisbert, E., Czyż, D. M., Richter, K., McMullen, P. D., & Morimoto, R. I. (2013) · PLoS Genetics · doi:10.1371/journal.pgen.1003466 · Cited by 123 · see citing works

Activation of Human Heat Shock Genes Is Accompanied by Oligomerization, Modification, and Rapid Translocation of Heat Shock Transcription Factor HSF1

Baler, R., Dahl, G., & Voellmy, R. W. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.4.2486-2496.1993 · Cited by 117 · see citing works

EGF signalling activates the ubiquitin proteasome system to modulate C. elegans lifespan

Liu, G., Rogers, J. V., Murphy, C. T., & Rongo, C. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.195 · Cited by 110 · see citing works

Germline stem cell arrest inhibits the collapse of somatic proteostasis early in Caenorhabditis elegans adulthood

Shemesh, N., Shai, N., & Ben‐Zvi, A. (2013) · Aging Cell · doi:10.1111/acel.12110 · Cited by 110 · see citing works

Chronic Treatment with 17-DMAG Improves Balance and Coordination in A New Mouse Model of Machado-Joseph Disease

Silva‐Fernandes, A., Duarte‐Silva, S., Neves‐Carvalho, A., Amorim, M. F., Soares‐Cunha, C., Oliveira, P., Thirstrup, K., Teixeira‐Castro, A., & Maciel, P. (2014) · Neurotherapeutics · doi:10.1007/s13311-013-0255-9 · Cited by 107 · see citing works

A photoconvertible reporter of the ubiquitin-proteasome system in vivo

Hamer, G., Matilainen, O., & Holmberg, C. I. (2010) · Nature Methods · doi:10.1038/nmeth.1460 · Cited by 105 · see citing works

Impaired Mitochondrial Dynamics and Nrf2 Signaling Contribute to Compromised Responses to Oxidative Stress in Striatal Cells Expressing Full-Length Mutant Huntingtin

Jin, Y. N., Yu, Y. V., Gundemir, S., Jo, C., Cui, M., Tieu, K., & Johnson, G. V. W. (2013) · PLoS ONE · doi:10.1371/journal.pone.0057932 · Cited by 102 · 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

Differential regulation of proteasome functionality in reproductive vs. somatic tissues of Drosophila during aging or oxidative stress

Tsakiri, E. N., Sykiotis, G. P., Papassideri, I. S., Gorgoulis, V. G., Bohmann, D., & Trougakos, I. P. (2013) · The FASEB Journal · doi:10.1096/fj.12-221408 · Cited by 92 · see citing works

Organismal proteostasis: role of cell-nonautonomous regulation and transcellular chaperone signalingPreprint

van Oosten‐Hawle, P., & Morimoto, R. I. (2014) · Genes & Development · doi:10.1101/gad.241125.114 · Cited by 91 · see citing works

Modulation of the Maladaptive Stress Response to Manage Diseases of Protein Folding

Roth, D., Hutt, D. M., Tong, J., Bouchecareilh, M., Wang, N., Seeley, T., Dekkers, J. F., Beekman, J. M., Garza, D., Drew, L., et al. (2014) · PLoS Biology · doi:10.1371/journal.pbio.1001998 · Cited by 89 · see citing works

Parkin Directly Modulates 26S Proteasome Activity

Um, J. W., Im, E., Lee, H. J., Min, B., Yoo, L., Yoo, J., Lübbert, H., Stichel-Gunkel, C. C., Cho, H.-S., Yoon, J. B., et al. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.2862-09.2010 · Cited by 81 · see citing works

The Induction Levels of Heat Shock Protein 70 Differentiate the Vulnerabilities to Mutant Huntingtin among Neuronal Subtypes

Tagawa, K., Marubuchi, S., Qi, M., Enokido, Y., Tamura, T., Inagaki, R., Murata, M., Kanazawa, I., Wanker, E. E., & Okazawa, H. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.4522-06.2007 · Cited by 79 · see citing works

Temporal requirements of insulin/IGF‐1 signaling for proteotoxicity protection

Cohen, E., Du, D., Joyce, D., Kapernick, E. A., Volovik, Y., Kelly, J. W., & Dillin, A. G. (2009) · Aging Cell · doi:10.1111/j.1474-9726.2009.00541.x · Cited by 75 · see citing works

A rare recessive distal hereditary motor neuropathy with HSJ1 chaperone mutation

Blumen, S. C., Astord, S., Robín, V., Vignaud, L., Nawel, T., Cieslik, A., Achiron, A., Carasso, R. L., Gurevich, M., Braverman, I., et al. (2011) · Annals of Neurology · doi:10.1002/ana.22684 · Cited by 74 · see citing works

Impaired Heat Shock Response in Cells Expressing Full-Length Polyglutamine-Expanded Huntingtin

Chafekar, S. M., & Duennwald, M. L. (2012) · PLoS ONE · doi:10.1371/journal.pone.0037929 · Cited by 74 · see citing works

Neuronal expression of TATA box-binding protein containing expanded polyglutamine in knock-in mice reduces chaperone protein response by impairing the function of nuclear factor-Y transcription factor

Huang, S., Ling, J. J., Yang, S., Li, X., & Li, S. (2011) · Brain · doi:10.1093/brain/awr146 · Cited by 63 · see citing works

Heat shock factor functions at the convergence of the stress response and developmental pathways in Caenorhabditis elegans

Walker, G. A., Thompson, F., Brawley, A., Scanlon, T., & Devaney, E. (2003) · The FASEB Journal · doi:10.1096/fj.03-0164fje · Cited by 62 · see citing works

Temporal requirements of heat shock factor‐1 for longevity assurance

Volovik, Y., Maman, M., Dubnikov, T., Bejerano‐Sagie, M., Joyce, D., Kapernick, E. A., Cohen, E., & Dillin, A. G. (2012) · Aging Cell · doi:10.1111/j.1474-9726.2012.00811.x · Cited by 59 · see citing works

Spreading of a Prion Domain from Cell-to-Cell by Vesicular Transport in Caenorhabditis elegans

Nussbaum-Krammer, C. I., Park, K.-W., Li, L., Melki, R., & Morimoto, R. I. (2013) · PLoS Genetics · doi:10.1371/journal.pgen.1003351 · Cited by 58 · see citing works

Cytosolic proteins lose solubility as amyloid deposits in a transgenic mouse model of Alzheimer-type amyloidosis

Xu, G. M., Stevens, S. M., Moore, B. D., McClung, S. H., & Borchelt, D. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt121 · Cited by 53 · see citing works

Dexamethasone induces heat shock response and slows down disease progression in mouse and fly models of Huntington's disease.

Maheshwari, M., Bhutani, S., Das, A., Mukherjee, R., Sharma, A., Kino, Y., Nukina, N., & Jana, N. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddt667 · Cited by 51 · see citing works

Association studies indicate that protein disulfide isomerase is a risk factor in amyotrophic lateral sclerosis

Kwok, C. T., Morris, A. G., Frampton, J., Smith, B. N., Shaw, C. E., & de Belleroche, J. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.01.001 · Cited by 50 · see citing works

Polyglutamine Expanded Huntingtin Dramatically Alters the Genome-Wide Binding of HSF1

Riva, L., Koeva, M., Yildirim, F., Pirhaji, L., Dinesh, D., Mazor, T., Duennwald, M. L., & Fraenkel, E. (2012) · Journal of Huntington s Disease · doi:10.3233/jhd-2012-120020 · Cited by 49 · see citing works

Impaired ATF6α processing, decreased Rheb and neuronal cell cycle re-entry in Huntington's disease

Fernández-Fernández, M. R., Ferrer, I., & Lucas, J. J. (2010) · Neurobiology of Disease · doi:10.1016/j.nbd.2010.08.014 · Cited by 45 · see citing works

Absence of lipofuscin in motor neurons of SOD1-linked ALS mice

Bandyopadhyay, U., Nagy, M., Fenton, W. A., & Horwich, A. L. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1409314111 · Cited by 41 · see citing works

Genetic Variations in HSPA8 Gene Associated with Coronary Heart Disease Risk in a Chinese Population

He, M., Guo, H., Yang, X., Zhou, L., Zhang, X., Cheng, L., Zeng, H., Hu, F. B., Tanguay, R. M., & Wu, T. (2010) · PLoS ONE · doi:10.1371/journal.pone.0009684 · Cited by 39 · see citing works

Contesting the dogma of an age-related heat shock response impairment: implications for cardiac-specific age-related disorders

Carnemolla, A., Labbadia, J. P., Lazell, H., Neueder, A., Moussaoui, S. M., & Bates, G. P. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu073 · Cited by 38 · see citing works

Expanded polyglutamine domain possesses nuclear export activity which modulates subcellular localization and toxicity of polyQ disease protein via exportin-1

Chan, W. M., Tsoi, H., Wu, C. C., Wong, C. H., Cheng, T. C., Li, H., Lau, K., Shaw, P. C., Perrimon, N., & Chan, H. Y. E. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr049 · Cited by 37 · see citing works

Analysis of Chaperone mRNA Expression in the Adult Mouse Brain by Meta Analysis of the Allen Brain Atlas

Tebbenkamp, A. T. N., & Borchelt, D. (2010) · PLoS ONE · doi:10.1371/journal.pone.0013675 · Cited by 36 · see citing works

Post-eclosion decline in ‘knock-down’ thermal resistance and reduced effect of heat hardening in Drosophila melanogaster

Pappas, C., Hyde, D., Bowler, K., Loeschcke, V., & Sørensen, J. G. (2006) · Comparative Biochemistry and Physiology Part A Molecular & Integrative Physiology · doi:10.1016/j.cbpa.2006.11.010 · Cited by 33 · see citing works

Recent technical developments in the study of ER-associated degradation

Nakatsukasa, K., Kamura, T., & Brodsky, J. L. (2014) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2014.04.008 · Cited by 32 · see citing works

The Novel Hydroxylamine Derivative NG-094 Suppresses Polyglutamine Protein Toxicity in Caenorhabditis elegans

Haldimann, P., Muriset, M., Vı́gh, L., & Goloubinoff, P. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.234773 · Cited by 30 · see citing works

Ribosome-associated chaperones act as proteostasis sentinels

Kirstein, J., & Morimoto, R. I. (2013) · Cell Cycle · doi:10.4161/cc.25703 · Cited by 6 · see citing works

The integrated stress response

Pakos‐Zebrucka, K., Koryga, I., Mnich, K., Ljujic, M., Samali, A., & Gorman, A. M. (2016) · The EMBO Reports · doi:10.15252/embr.201642195 · Cited by 2,659 · see citing works

Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade

Chiti, F., & Dobson, C. M. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-045115 · Cited by 2,629 · 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

The Cellular Phase of Alzheimer’s Disease

De Strooper, B., & Karran, E. (2016) · Cell · doi:10.1016/j.cell.2015.12.056 · Cited by 1,990 · 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

The integrated stress response: From mechanism to disease

Costa-Mattioli, M., & Walter, P. (2020) · Science · doi:10.1126/science.aat5314 · Cited by 1,617 · see citing works

The glymphatic pathway in neurological disorders.

Rasmussen, M. K., Mestre, H., & Nedergaard, M. (2018) · The Lancet Neurology · doi:10.1016/s1474-4422(18)30318-1 · Cited by 1,560 · see citing works

In vivo aspects of protein folding and quality control

Balchin, D., Hayer-Hartl, M. K., & Hartl, F. U. (2016) · Science · doi:10.1126/science.aac4354 · Cited by 1,432 · see citing works

Autophagy in healthy aging and disease

Aman, Y., Schmauck-Medina, T., Hansen, M., Morimoto, R. I., Simon, A. K., Bjedov, I., Palikaras, K., Simonsen, A., Johansen, T., Tavernarakis, N., et al. (2021) · Nature Aging · doi:10.1038/s43587-021-00098-4 · Cited by 1,313 · see citing works

Biomolecular condensates at the nexus of cellular stress, protein aggregation disease and ageing

Alberti, S., & Hyman, A. A. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-00326-6 · Cited by 1,135 · see citing works

Proteasomal and Autophagic Degradation Systems

Đikić, I. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-044908 · Cited by 1,165 · see citing works

Proteostasis and aging

Kaushik, S., & Cuervo, A. M. (2015) · Nature Medicine · doi:10.1038/nm.4001 · Cited by 899 · see citing works

Pathways of cellular proteostasis in aging and disease

Klaips, C. L., Jayaraj, G. G., & Hartl, F. U. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201709072 · Cited by 803 · see citing works

Metabolic Control of Longevity

López-Otín, C., Galluzzi, L., Freije, J. M. P., Madeo, F., & Kroemer, G. (2016) · Cell · doi:10.1016/j.cell.2016.07.031 · Cited by 753 · see citing works

Mitochondrial metabolism promotes adaptation to proteotoxic stress

Tsvetkov, P., Detappe, A., Cai, K., Keys, H. R., Brune, Z., Ying, W., Thiru, P., Reidy, M., Kugener, G., Rossen, J., et al. (2019) · Nature Chemical Biology · doi:10.1038/s41589-019-0291-9 · Cited by 645 · see citing works

Fluid transport in the brain

Rasmussen, M. K., Mestre, H., & Nedergaard, M. (2021) · Physiological Reviews · doi:10.1152/physrev.00031.2020 · Cited by 622 · see citing works

Selective vulnerability in neurodegenerative diseases

Fu, H., Hardy, J., & Duff, K. E. (2018) · Nature Neuroscience · doi:10.1038/s41593-018-0221-2 · Cited by 585 · see citing works

Systemic immunoglobulin light chain amyloidosis

Merlini, G., Dispenzieri, A. A., Sanchorawala, V., Schönland, S. O., Palladini, G. O., Hawkins, P. N., & Gertz, M. A. (2018) · Nature Reviews Disease Primers · doi:10.1038/s41572-018-0034-3 · Cited by 557 · see citing works

Protein Misfolding Diseases

Hartl, F. U. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-044518 · Cited by 519 · see citing works

Oxidative Stress and Advanced Lipoxidation and Glycation End Products (ALEs and AGEs) in Aging and Age-Related Diseases

Moldogazieva, N. T., Mokhosoev, I. M., Melnikova, T. I., Porozov, Y. B., & Terentiev, A. A. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/3085756 · Cited by 504 · see citing works

Propagation and spread of pathogenic protein assemblies in neurodegenerative diseases

Jucker, M., & Walker, L. C. (2018) · Nature Neuroscience · doi:10.1038/s41593-018-0238-6 · Cited by 450 · see citing works

Healthy Effects of Plant Polyphenols: Molecular Mechanisms

Leri, M., Scuto, M. C., Ontario, M. L., Calabrese, V., Calabrese, E. J., Bucciantini, M., & Stefani, M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21041250 · Cited by 440 · see citing works

Aging Hallmarks and the Role of Oxidative Stress

Maldonado, E., Morales-Pison, S., Urbina, F., & Solari, A. (2023) · Antioxidants · doi:10.3390/antiox12030651 · Cited by 421 · see citing works

Defining Optimal Brain Health in Adults: A Presidential Advisory From the American Heart Association/American Stroke Association

Gorelick, P. B., Furie, K. L., Iadecola, C., Smith, E. E., Waddy, S. P., Lloyd-Jones, D. M., Bae, H.-J., Bauman, M. A., Dichgans, M., Duncan, P. W., et al. (2017) · Stroke · doi:10.1161/str.0000000000000148 · Cited by 411 · see citing works

The amyloid cascade hypothesis: are we poised for success or failure?

Karran, E., & De Strooper, B. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13632 · Cited by 402 · see citing works

Inflammation, epigenetics, and metabolism converge to cell senescence and ageing: the regulation and intervention

Zhu, X., Chen, Z., Shen, W., Huang, G., Sedivy, J. M., Wang, H., & Ju, Z. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00646-9 · Cited by 410 · see citing works

Biomarkers of aging

Bao, H., Cao, J., Chen, M., Min, C., Chen, W., Chen, X., Chen, Y., Chen, Y., Chen, Y., Chen, Z., et al. (2023) · Science China Life Sciences · doi:10.1007/s11427-023-2305-0 · Cited by 389 · see citing works

The Hsp70/Hsp90 Chaperone Machinery in Neurodegenerative Diseases

Lackie, R. E., Maciejewski, A., Ostapchenko, V. G., Marques-Lopes, J., Choy, W., Duennwald, M. L., Prado, V. F., & Prado, M. A. M. (2017) · Frontiers in Neuroscience · doi:10.3389/fnins.2017.00254 · Cited by 375 · see citing works

The Biology of Aging and Cancer: A Brief Overview of Shared and Divergent Molecular Hallmarks

Aunan, J. R., Cho, W. C. S., & Søreide, K. (2017) · Aging and Disease · doi:10.14336/ad.2017.0103 · Cited by 374 · see citing works

Happily (n)ever after: Aging in the context of oxidative stress, proteostasis loss and cellular senescence

Höhn, A., Weber, D., Jung, T., Ott, C., Hugo, M., Kochlik, B., Kehm, R., König, J., Grune, T., & Castro, J. P. (2016) · Redox Biology · doi:10.1016/j.redox.2016.12.001 · Cited by 368 · see citing works

A common mechanism of proteasome impairment by neurodegenerative disease-associated oligomers

Thibaudeau, T. A., Anderson, R. T., & Smith, D. M. (2018) · Nature Communications · doi:10.1038/s41467-018-03509-0 · Cited by 362 · see citing works

Selective autophagy as a potential therapeutic target for neurodegenerative disorders

Scrivo, A., Bourdenx, M., Pampliega, O., & Cuervo, A. M. (2018) · The Lancet Neurology · doi:10.1016/s1474-4422(18)30238-2 · Cited by 355 · see citing works

Protein Folding and Mechanisms of Proteostasis

Díaz‐Villanueva, J. F., Díaz-Molina, R. J., & García‐González, V. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms160817193 · Cited by 341 · 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

Skin Aging, Cellular Senescence and Natural Polyphenols

Csekes, E., & Račková, L. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222312641 · Cited by 334 · see citing works

Molecular and biological hallmarks of ageing

Aunan, J. R., Watson, M. M., Hagland, H. R., & Søreide, K. (2016) · British journal of surgery · doi:10.1002/bjs.10053 · Cited by 322 · see citing works

The Unfolded Protein Response: Detecting and Responding to Fluctuations in the Protein-Folding Capacity of the Endoplasmic ReticulumPreprint

Karagöz, G. E., Acosta‐Alvear, D., & Walter, P. (2019) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a033886 · Cited by 302 · see citing works

Propagation of Protein Aggregation in Neurodegenerative Diseases

Vaquer‐Alicea, J., & Diamond, M. I. (2019) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-045049 · Cited by 308 · see citing works

ROS and RNS signalling: adaptive redox switches through oxidative/nitrosative protein modifications

Moldogazieva, N. T., Mokhosoev, I. M., Feldman, N. B., & Lutsenko, S. V. (2018) · Free Radical Research · doi:10.1080/10715762.2018.1457217 · Cited by 291 · see citing works

Cellular Senescence in Neurodegenerative Diseases

Martínez‐Cué, C., & Rueda, N. (2020) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2020.00016 · Cited by 285 · see citing works

Autophagy and the hallmarks of aging

Kaushik, S., Tasset, I., Arias, E., Pampliega, O., Wong, E., Martinez-Vicente, M., & Cuervo, A. M. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2021.101468 · Cited by 285 · see citing works

Principles of Protein Stability and Their Application in Computational Design

Goldenzweig, A., & Fleishman, S. J. (2018) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-062917-012102 · Cited by 283 · see citing works

Mechanisms and Functions of Spatial Protein Quality Control

Sontag, E. M., Samant, R. S., & Frydman, J. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060815-014616 · Cited by 269 · see citing works

Rethinking HSF1 in Stress, Development, and Organismal Health

Li, J., Labbadia, J. P., & Morimoto, R. I. (2017) · Trends in Cell Biology · doi:10.1016/j.tcb.2017.08.002 · Cited by 265 · see citing works

A tau homeostasis signature is linked with the cellular and regional vulnerability of excitatory neurons to tau pathology

Fu, H., Possenti, A., Freer, R., Nakano, Y., Villegas, N. C. H., Tang, M., Cauhy, P. M., Lassus, B., Chen, S., Fowler, S. L., et al. (2018) · Nature Neuroscience · doi:10.1038/s41593-018-0298-7 · Cited by 252 · see citing works

Large-scale investigation of the reasons why potentially important genes are ignored

Stoeger, T., Gerlach, M., Morimoto, R. I., & Nunes Amaral, L. A. (2018) · PLOS Biology · doi:10.1371/journal.pbio.2006643 · Cited by 261 · see citing works

Obesity May Accelerate the Aging Process

Salvestrini, V., Sell, C., & Lorenzini, A. (2019) · Frontiers in Endocrinology · doi:10.3389/fendo.2019.00266 · Cited by 260 · see citing works

Ubiquilins Chaperone and Triage Mitochondrial Membrane Proteins for Degradation

Itakura, E., Zavodszky, E., Shao, S., Wohlever, M. L., Keenan, R. J., & Hegde, R. S. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.05.020 · Cited by 255 · see citing works

The Mitochondrial Unfolded Protein Response Is Mediated Cell-Non-autonomously by Retromer-Dependent Wnt Signaling

Zhang, Q., Wu, X., Chen, P., Liu, L., Xin, N., Tian, Y., & Dillin, A. G. (2018) · Cell · doi:10.1016/j.cell.2018.06.029 · Cited by 255 · see citing works

Functional Modules of the Proteostasis NetworkPreprint

Jayaraj, G. G., Hipp, M. S., & Hartl, F. U. (2019) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a033951 · Cited by 249 · see citing works

Shaping proteostasis at the cellular, tissue, and organismal level

Sala, A. J., Bott, L. C., & Morimoto, R. I. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201612111 · Cited by 246 · see citing works

Dynamic control of Hsf1 during heat shock by a chaperone switch and phosphorylation

Zheng, X., Krakowiak, J., Patel, N., Ali Beyzavi, B., Ezike, J., Khalil, A. S., & Pincus, D. (2016) · eLife · doi:10.7554/elife.18638 · Cited by 245 · see citing works

Alzheimer’s Disease: From Firing Instability to Homeostasis Network Collapse

Frère, S. G. A., & Slutsky, I. (2018) · Neuron · doi:10.1016/j.neuron.2017.11.028 · Cited by 230 · see citing works

Mammalian prions and their wider relevance in neurodegenerative diseases

Collinge, J. (2016) · Nature · doi:10.1038/nature20415 · Cited by 231 · see citing works

Walking the tightrope: proteostasis and neurodegenerative disease

Yerbury, J. J., Ooi, L., Dillin, A. G., Saunders, D. N., Hatters, D. M., Beart, P. M., Cashman, N. R., Wilson, M. R., & Ecroyd, H. W. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13575 · Cited by 243 · see citing works

Multiplexed Proteome Dynamics Profiling Reveals Mechanisms Controlling Protein Homeostasis

Savitski, M. M., Zinn, N., Faelth-Savitski, M., Poeckel, D., Gade, S., Becher, I., Muelbaier, M., Wagner, A. J., Strohmer, K., Werner, T., et al. (2018) · Cell · doi:10.1016/j.cell.2018.02.030 · Cited by 217 · see citing works

Structure of Hsp90–Hsp70–Hop–GR reveals the Hsp90 client-loading mechanism

Wang, R. Y.-R., Noddings, C. M., Kirschke, E., Myasnikov, A. G., Johnson, J. L., & Agard, D. A. (2022) · Nature · doi:10.1038/s41586-021-04252-1 · Cited by 213 · see citing works

IRE1 signaling exacerbates Alzheimer’s disease pathogenesis

Duran-Aniotz, C. A., Cornejo, V. H., Espinoza, S., Ardiles, Á. O., Medinas, D. B., Salazar, C., Foley, A., Gajardo, I., Thielen, P., Iwawaki, T., et al. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1694-x · Cited by 210 · see citing works

HSF1: Guardian of Proteostasis in Cancer

Dai, C., & Sampson, S. B. (2015) · Trends in Cell Biology · doi:10.1016/j.tcb.2015.10.011 · Cited by 213 · see citing works

Modelling the molecular mechanisms of aging

Auley, M. T. M., Guimera, A. M., Hodgson, D., Mcdonald, N., Mooney, K. M., Morgan, A. E., & Proctor, C. J. (2017) · Bioscience Reports · doi:10.1042/bsr20160177 · Cited by 212 · see citing works

Survival assays using Caenorhabditis elegans

Park, H. H., Jung, Y., & Lee, S. (2017) · Molecules and Cells · doi:10.14348/molcells.2017.0017 · Cited by 204 · see citing works

Exosome‐like nanoparticles from Mulberry bark prevent DSS‐induced colitis via the AhR/COPS8 pathway

Sriwastva, M. K., Deng, Z., Wang, B., Teng, Y., Kumar, A., Sundaram, K., Mu, J., Lei, C., Dryden, G. W., Xu, F., et al. (2022) · EMBO Reports · doi:10.15252/embr.202153365 · Cited by 200 · see citing works

Proteostasis Failure in Neurodegenerative Diseases: Focus on Oxidative Stress

Höhn, A., Tramutola, A., & Cascella, R. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/5497046 · Cited by 197 · see citing works

The Role of the Multifunctional BAG3 Protein in Cellular Protein Quality Control and in Disease

Stürner, E., & Behl, C. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00177 · Cited by 194 · 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

Pharmacologic ATF6 activation confers global protection in widespread disease models by reprograming cellular proteostasis

Blackwood, E. A., Azizi, K., Thuerauf, D. J., Paxman, R. J., Plate, L., Kelly, J. W., Wiseman, R. L., & Glembotski, C. C. (2019) · Nature Communications · doi:10.1038/s41467-018-08129-2 · Cited by 191 · see citing works

Sirtuins at the crossroads of stemness, aging, and cancer

O'Callaghan, C., & Vassilopoulos, A. (2017) · Aging Cell · doi:10.1111/acel.12685 · Cited by 187 · see citing works

Effects of in vivo conditions on amyloid aggregation

Owen, M. C., Gnutt, D., Gao, M., Wärmländer, S. K. T. S., Jarvet, J., Gräslund, A., Winter, R., Ebbinghaus, S., & Strodel, B. (2019) · Chemical Society Reviews · doi:10.1039/c8cs00034d · Cited by 179 · see citing works

Axonal Degeneration during Aging and Its Functional Role in Neurodegenerative Disorders

Salvadores, N., Sanhueza, M., Manque, P., & Court, F. A. (2017) · Frontiers in Neuroscience · doi:10.3389/fnins.2017.00451 · Cited by 182 · see citing works

Gene expression hallmarks of cellular ageing

Frenk, S., & Houseley, J. M. (2018) · Biogerontology · doi:10.1007/s10522-018-9750-z · Cited by 180 · see citing works

Age-related macular degeneration: A two-level model hypothesis

Rozing, M. P., Durhuus, J. A., Nielsen, M. K., Subhi, Y., Kirkwood, T. B. L., Westendorp, R. G., & Sørensen, T. L. (2019) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2019.100825 · Cited by 183 · see citing works

ZFAND1 Recruits p97 and the 26S Proteasome to Promote the Clearance of Arsenite-Induced Stress Granules

Turakhiya, A., MEYER, S. R., Marincola, G., Böhm, S., Vanselow, J. T., Schlösser, A., Hofmann, K., & Buchberger, A. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.04.021 · Cited by 174 · see citing works

Ribosome collisions trigger cis-acting feedback inhibition of translation initiation

Juszkiewicz, S., Slodkowicz, G., Lin, Z., Freire-Pritchett, P., Peak‐Chew, S., & Hegde, R. S. (2020) · eLife · doi:10.7554/elife.60038 · Cited by 170 · see citing works

Mechanism of ribosome stalling during translation of a poly(A) tail

Chandrasekaran, V., Juszkiewicz, S., Choi, J., Puglisi, J. D., Brown, A., Shao, S., Ramakrishnan, V., & Hegde, R. S. (2019) · Nature Structural & Molecular Biology · doi:10.1038/s41594-019-0331-x · Cited by 173 · see citing works

Disassembly of Tau fibrils by the human Hsp70 disaggregation machinery generates small seeding-competent species

Nachman, E., Wentink, A. S., Madiona, K., Bousset, L., Katsinelos, T., Allinson, K. S. J., Kampinga, H. H., McEwan, W. A., Jahn, T. R., Melki, R., et al. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.013478 · Cited by 169 · see citing works

The Amyloid Phenomenon and Its Significance in Biology and MedicinePreprint

Dobson, C. M., Knowles, T. P. J., & Vendruscolo, M. (2019) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a033878 · Cited by 166 · see citing works

Protein synthesis and quality control in aging

Anisimova, A. S., Alexandrov, A. I., Makarova, N. E., Gladyshev, V. N., & Dmitriev, S. E. (2018) · Aging · doi:10.18632/aging.101721 · Cited by 172 · see citing works

Autophagy in the presynaptic compartment in health and disease

Vijayan, V., & Verstreken, P. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201611113 · Cited by 167 · see citing works

Integrated proteomics and network analysis identifies protein hubs and network alterations in Alzheimer’s disease

Zhang, Q., Ma, C., Gearing, M., Wang, P. G., Chin, L.-S., & Li, L. (2018) · Acta Neuropathologica Communications · doi:10.1186/s40478-018-0524-2 · Cited by 165 · see citing works

Hsp70 displaces small heat shock proteins from aggregates to initiate protein refolding

Żwirowski, S., Klosowska, A. A., Obuchowski, I., Nillegoda, N. B., Piróg, A., Ziętkiewicz, S., Bukau, B., Mogk, A., & Liberek, K. (2017) · The EMBO Journal · doi:10.15252/embj.201593378 · Cited by 166 · see citing works

Mitochondrial Stress Restores the Heat Shock Response and Prevents Proteostasis Collapse during Aging

Labbadia, J. P., Brielmann, R. M., Neto, M. F., Lin, Y.-F., Haynes, C. M., & Morimoto, R. I. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.10.038 · Cited by 165 · see citing works

Proteome Turnover in the Spotlight: Approaches, Applications, and Perspectives

Ross, A. B., Langer, J. D., & Jovanović, M. (2020) · Molecular & Cellular Proteomics · doi:10.1074/mcp.r120.002190 · Cited by 151 · see citing works

Cellular proteostasis: degradation of misfolded proteins by lysosomes

Jackson, M. P., & Hewitt, E. W. (2016) · Essays in Biochemistry · doi:10.1042/ebc20160005 · Cited by 155 · see citing works

A Futile Battle? Protein Quality Control and the Stress of Aging

Higuchi‐Sanabria, R., Frankino, P. A., Paul, J. W., Tronnes, S. U., & Dillin, A. G. (2018) · Developmental Cell · doi:10.1016/j.devcel.2017.12.020 · Cited by 149 · see citing works

Granulostasis: Protein Quality Control of RNP Granules

Alberti, S., Matějů, D., Mediani, L., & Carra, S. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00084 · Cited by 147 · see citing works

Adapting to stress — chaperome networks in cancer

Joshi, S., Wang, T., Araujo, T. L. S., Sharma, S., Brodsky, J. L., & Chiosis, G. (2018) · Nature reviews. Cancer · doi:10.1038/s41568-018-0020-9 · Cited by 144 · see citing works

Proteome-wide observation of the phenomenon of life on the edge of solubility

Vecchi, G., Sormanni, P., Mannini, B., Vandelli, A., Tartaglia, G. G., Dobson, C. M., Hartl, F. U., & Vendruscolo, M. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1910444117 · Cited by 143 · see citing works

Cellular proteostasis decline in human senescence

Sabath, N., Levy‐Adam, F., Younis, A., Rozales, K., Meller, A., Hadar, S., Soueid‐Baumgarten, S., & Shalgi, R. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2018138117 · Cited by 148 · see citing works

The Hsp70-Hsp90 co-chaperone Hop/Stip1 shifts the proteostatic balance from folding towards degradation

Bhattacharya, K., Weidenauer, L., Luengo, T. M., Pieters, E. C., Echeverría, P. C., Bernasconi, L., Wider, D., Sadian, Y., Koopman, M. B., Villemin, M., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-19783-w · Cited by 140 · see citing works

The AAA+ ATPase/ubiquitin ligase mysterin stabilizes cytoplasmic lipid droplets

Sugihara, M., Morito, D., Ainuki, S., Hirano, Y., Ogino, K., Kitamura, A., Hirata, H., & Nagata, K. (2019) · The Journal of Cell Biology · doi:10.1083/jcb.201712120 · Cited by 140 · see citing works

Chaperoning Endoplasmic Reticulum–Associated Degradation (ERAD) and Protein Conformational DiseasesPreprint

Needham, P. G., Guerriero, C. J., & Brodsky, J. L. (2019) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a033928 · Cited by 139 · see citing works

The Role of Co-chaperones in Synaptic Proteostasis and Neurodegenerative Disease

Gorenberg, E. L., & Chandra, S. S. (2017) · Frontiers in Neuroscience · doi:10.3389/fnins.2017.00248 · Cited by 138 · see citing works

Impaired proteostasis during skeletal muscle aging

Fernando, R., Drescher, C., Nowotny, K., Grune, T., & Castro, J. P. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.08.037 · Cited by 134 · see citing works

Beyond the cell factory: Homeostatic regulation of and by the UPR ER

Metcalf, M. G., Higuchi‐Sanabria, R., Garcia, G., Tsui, C. K., & Dillin, A. G. (2020) · Science Advances · doi:10.1126/sciadv.abb9614 · Cited by 131 · see citing works

Increased fidelity of protein synthesis extends lifespan

Martinez-Miguel, V. E., Lujan, C., Espie-Caullet, T., Martínez‐Martínez, D., Moore, S., Backes, C., Gonzalez, S., Galimov, E. R., Brown, A. E., Halić, M., et al. (2021) · Cell Metabolism · doi:10.1016/j.cmet.2021.08.017 · Cited by 134 · see citing works

UBE2O is a quality control factor for orphans of multiprotein complexes

Yanagitani, K., Juszkiewicz, S., & Hegde, R. S. (2017) · Science · doi:10.1126/science.aan0178 · Cited by 132 · see citing works

Experimental Milestones in the Discovery of Molecular Chaperones as Polypeptide Unfolding Enzymes

Finka, A., Mattoo, R. U. H., & Goloubinoff, P. (2016) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060815-014124 · Cited by 132 · see citing works

The heat-shock, or HSF1-mediated proteotoxic stress, response in cancer: from proteomic stability to oncogenesis

Dai, C. (2017) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2016.0525 · Cited by 130 · see citing works

Parkinson's disease: convergence on synaptic homeostasis

Soukup, S., Vanhauwaert, R., & Verstreken, P. (2018) · The EMBO Journal · doi:10.15252/embj.201898960 · Cited by 129 · see citing works

Aging causes decreased resistance to multiple stresses and a failure to activate specific stress response pathways

Dues, D. J., Andrews, E. K., Schaar, C. E., Bergsma, A. L., Senchuk, M. M., & Raamsdonk, J. M. V. (2016) · Aging · doi:10.18632/aging.100939 · Cited by 131 · see citing works

Proteostasis impairment in protein-misfolding and -aggregation diseases

Hipp, M. S., Park, S.-H., & Hartl, F. U. (2014) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.05.003 · Cited by 656 · see citing works

Shaping proteostasis at the cellular, tissue, and organismal level

Sala, A. J., Bott, L. C., & Morimoto, R. I. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201612111 · Cited by 246 · see citing works

S3–02–01: Proteostasis: monitoring the health of the proteome in biology, aging and disease

Morimoto, R. I. (2013) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2013.04.218 · Cited by 2 · see citing works

Proteostasis and the Aging Proteome in Health and Disease

Morimoto, R. I., & Cuervo, A. M. (2014) · The Journals of Gerontology Series A: Biological Sciences and Medical Sciences · doi:10.1093/gerona/glu049 · Cited by 277 · see citing works

Functional Modules of the Proteostasis NetworkPreprint

Jayaraj, G. G., Hipp, M. S., & Hartl, F. U. (2019) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a033951 · Cited by 249 · see citing works