The metazoan protein disaggregase and amyloid depolymerase system

References

• Lindquist SL, Kelly JW. Chemical and biological approaches for adapting proteostasis to ameliorate protein misfolding and aggregation diseases: progress and prognosis. Cold Spring Harb Perspect Biol 2011; 3:3; http://dx.doi.org/10.1101/cshperspect.a004507; PMID: 21900404
   PubMed Web of Science ®Google Scholar
• Sarkar M, Smith AE, Pielak GJ. Impact of reconstituted cytosol on protein stability. Proc Natl Acad Sci U S A 2013; 110:19342 - 7; http://dx.doi.org/10.1073/pnas.1312678110; PMID: 24218610
   PubMed Web of Science ®Google Scholar
• Uversky VN, M Cooper E, Bower KS, Li J, Fink AL. Accelerated alpha-synuclein fibrillation in crowded milieu. FEBS Lett 2002; 515:99 - 103; http://dx.doi.org/10.1016/S0014-5793(02)02446-8; PMID: 11943202
   PubMed Web of Science ®Google Scholar
• van den Berg B, Ellis RJ, Dobson CM. Effects of macromolecular crowding on protein folding and aggregation. EMBO J 1999; 18:6927 - 33; http://dx.doi.org/10.1093/emboj/18.24.6927; PMID: 10601015
   PubMed Web of Science ®Google Scholar
• Kim YE, Hipp MS, Bracher A, Hayer-Hartl M, Hartl FU. Molecular chaperone functions in protein folding and proteostasis. Annu Rev Biochem 2013; 82:323 - 55; http://dx.doi.org/10.1146/annurev-biochem-060208-092442; PMID: 23746257
   PubMed Web of Science ®Google Scholar
• Wong E, Cuervo AM. Integration of clearance mechanisms: the proteasome and autophagy. Cold Spring Harb Perspect Biol 2010; 2:a006734; http://dx.doi.org/10.1101/cshperspect.a006734; PMID: 21068151
   PubMed Web of Science ®Google Scholar
• Maday S, Holzbaur EL. Autophagosome assembly and cargo capture in the distal axon. Autophagy 2012; 8:858 - 60; http://dx.doi.org/10.4161/auto.20055; PMID: 22617438
   PubMed Web of Science ®Google Scholar
• Maday S, Wallace KE, Holzbaur EL. Autophagosomes initiate distally and mature during transport toward the cell soma in primary neurons. J Cell Biol 2012; 196:407 - 17; http://dx.doi.org/10.1083/jcb.201106120; PMID: 22331844
   PubMed Web of Science ®Google Scholar
• Coelho M, Dereli A, Haese A, Kühn S, Malinovska L, DeSantis ME, Shorter J, Alberti S, Gross T, Tolić-Nørrelykke IM. Fission yeast does not age under favorable conditions, but does so after stress. Curr Biol 2013; 23:1844 - 52; http://dx.doi.org/10.1016/j.cub.2013.07.084; PMID: 24035542
   PubMed Web of Science ®Google Scholar
• Cushman M, Johnson BS, King OD, Gitler AD, Shorter J. Prion-like disorders: blurring the divide between transmissibility and infectivity. J Cell Sci 2010; 123:1191 - 201; http://dx.doi.org/10.1242/jcs.051672; PMID: 20356930
   PubMed Web of Science ®Google Scholar
• Jackrel ME, Shorter J. Shock and awe: unleashing the heat shock response to treat Huntington disease. J Clin Invest 2011; 121:2972 - 5; http://dx.doi.org/10.1172/JCI59190; PMID: 21785212
   PubMed Web of Science ®Google Scholar
• Glover JR, Lindquist S. Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins. Cell 1998; 94:73 - 82; http://dx.doi.org/10.1016/S0092-8674(00)81223-4; PMID: 9674429
   PubMed Web of Science ®Google Scholar
• Parsell DA, Kowal AS, Singer MA, Lindquist S. Protein disaggregation mediated by heat-shock protein Hsp104. Nature 1994; 372:475 - 8; http://dx.doi.org/10.1038/372475a0; PMID: 7984243
   PubMed Web of Science ®Google Scholar
• Sanchez Y, Lindquist SL. HSP104 required for induced thermotolerance. Science 1990; 248:1112 - 5; http://dx.doi.org/10.1126/science.2188365; PMID: 2188365
   PubMed Web of Science ®Google Scholar
• Pelham HR. Speculations on the functions of the major heat shock and glucose-regulated proteins. Cell 1986; 46:959 - 61; http://dx.doi.org/10.1016/0092-8674(86)90693-8; PMID: 2944601
   PubMed Web of Science ®Google Scholar
• Vogel JL, Parsell DA, Lindquist S. Heat-shock proteins Hsp104 and Hsp70 reactivate mRNA splicing after heat inactivation. Curr Biol 1995; 5:306 - 17; http://dx.doi.org/10.1016/S0960-9822(95)00061-3; PMID: 7780741
   PubMed Web of Science ®Google Scholar
• Vashist S, Cushman M, Shorter J. Applying Hsp104 to protein-misfolding disorders. Biochem Cell Biol 2010; 88:1 - 13; http://dx.doi.org/10.1139/O09-121; PMID: 20130674
   PubMed Web of Science ®Google Scholar
• DeSantis ME, Shorter J. The elusive middle domain of Hsp104 and ClpB: location and function. Biochim Biophys Acta 2012; 1823:29 - 39; http://dx.doi.org/10.1016/j.bbamcr.2011.07.014; PMID: 21843558
   PubMed Web of Science ®Google Scholar
• Saibil H. Chaperone machines for protein folding, unfolding and disaggregation. Nat Rev Mol Cell Biol 2013; 14:630 - 42; http://dx.doi.org/10.1038/nrm3658; PMID: 24026055
   PubMed Web of Science ®Google Scholar
• Desantis ME, Sweeny EA, Snead D, Leung EH, Go MS, Gupta K, Wendler P, Shorter J. Conserved distal loop residues in the Hsp104 and ClpB middle domain contact nucleotide-binding domain 2 and enable Hsp70-dependent protein disaggregation. J Biol Chem 2014; 289:848 - 67; http://dx.doi.org/10.1074/jbc.M113.520759; PMID: 24280225
   PubMed Web of Science ®Google Scholar
• Doyle SM, Genest O, Wickner S. Protein rescue from aggregates by powerful molecular chaperone machines. Nat Rev Mol Cell Biol 2013; 14:617 - 29; http://dx.doi.org/10.1038/nrm3660; PMID: 24061228
   PubMed Web of Science ®Google Scholar
• Wendler P, Shorter J, Plisson C, Cashikar AG, Lindquist S, Saibil HR. Atypical AAA+ subunit packing creates an expanded cavity for disaggregation by the protein-remodeling factor Hsp104. Cell 2007; 131:1366 - 77; http://dx.doi.org/10.1016/j.cell.2007.10.047; PMID: 18160044
   PubMed Web of Science ®Google Scholar
• Shorter J, Lindquist S. Navigating the ClpB channel to solution. Nat Struct Mol Biol 2005; 12:4 - 6; http://dx.doi.org/10.1038/nsmb0105-4; PMID: 15689967
   PubMed Web of Science ®Google Scholar
• Wendler P, Shorter J, Snead D, Plisson C, Clare DK, Lindquist S, Saibil HR. Motor mechanism for protein threading through Hsp104. Mol Cell 2009; 34:81 - 92; http://dx.doi.org/10.1016/j.molcel.2009.02.026; PMID: 19362537
   PubMed Web of Science ®Google Scholar
• Lum R, Niggemann M, Glover JR. Peptide and protein binding in the axial channel of Hsp104. Insights into the mechanism of protein unfolding. J Biol Chem 2008; 283:30139 - 50; http://dx.doi.org/10.1074/jbc.M804849200; PMID: 18755692
   PubMed Web of Science ®Google Scholar
• Lum R, Tkach JM, Vierling E, Glover JR. Evidence for an unfolding/threading mechanism for protein disaggregation by Saccharomyces cerevisiae Hsp104. J Biol Chem 2004; 279:29139 - 46; http://dx.doi.org/10.1074/jbc.M403777200; PMID: 15128736
   PubMed Web of Science ®Google Scholar
• DeSantis ME, Leung EH, Sweeny EA, Jackrel ME, Cushman-Nick M, Neuhaus-Follini A, Vashist S, Sochor MA, Knight MN, Shorter J. Operational plasticity enables hsp104 to disaggregate diverse amyloid and nonamyloid clients. Cell 2012; 151:778 - 93; http://dx.doi.org/10.1016/j.cell.2012.09.038; PMID: 23141537
   PubMed Web of Science ®Google Scholar
• DeSantis ME, Shorter J. Hsp104 drives “protein-only” positive selection of Sup35 prion strains encoding strong [PSI(+)]. Chem Biol 2012; 19:1400 - 10; http://dx.doi.org/10.1016/j.chembiol.2012.09.013; PMID: 23177195
   PubMed Web of Science ®Google Scholar
• DiSalvo S, Derdowski A, Pezza JA, Serio TR. Dominant prion mutants induce curing through pathways that promote chaperone-mediated disaggregation. Nat Struct Mol Biol 2011; 18:486 - 92; http://dx.doi.org/10.1038/nsmb.2031; PMID: 21423195
   PubMed Web of Science ®Google Scholar
• Lo Bianco C, Shorter J, Régulier E, Lashuel H, Iwatsubo T, Lindquist S, Aebischer P. Hsp104 antagonizes alpha-synuclein aggregation and reduces dopaminergic degeneration in a rat model of Parkinson disease. J Clin Invest 2008; 118:3087 - 97; http://dx.doi.org/10.1172/JCI35781; PMID: 18704197
   PubMed Web of Science ®Google Scholar
• Shorter J, Lindquist S. Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers. Science 2004; 304:1793 - 7; http://dx.doi.org/10.1126/science.1098007; PMID: 15155912
   PubMed Web of Science ®Google Scholar
• Sweeny EA, Shorter J. Prion proteostasis: Hsp104 meets its supporting cast. Prion 2008; 2:135 - 40; http://dx.doi.org/10.4161/pri.2.4.7952; PMID: 19242125
   PubMed Web of Science ®Google Scholar
• Shorter J, Lindquist S. Destruction or potentiation of different prions catalyzed by similar Hsp104 remodeling activities. Mol Cell 2006; 23:425 - 38; http://dx.doi.org/10.1016/j.molcel.2006.05.042; PMID: 16885031
   PubMed Web of Science ®Google Scholar
• Doyle SM, Shorter J, Zolkiewski M, Hoskins JR, Lindquist S, Wickner S. Asymmetric deceleration of ClpB or Hsp104 ATPase activity unleashes protein-remodeling activity. Nat Struct Mol Biol 2007; 14:114 - 22; http://dx.doi.org/10.1038/nsmb1198; PMID: 17259993
   PubMed Web of Science ®Google Scholar
• Duennwald ML, Echeverria A, Shorter J. Small heat shock proteins potentiate amyloid dissolution by protein disaggregases from yeast and humans. PLoS Biol 2012; 10:e1001346; http://dx.doi.org/10.1371/journal.pbio.1001346; PMID: 22723742
   PubMed Web of Science ®Google Scholar
• Shorter J, Lindquist S. Hsp104, Hsp70 and Hsp40 interplay regulates formation, growth and elimination of Sup35 prions. EMBO J 2008; 27:2712 - 24; http://dx.doi.org/10.1038/emboj.2008.194; PMID: 18833196
   PubMed Web of Science ®Google Scholar
• Cashikar AG, Duennwald M, Lindquist SL. A chaperone pathway in protein disaggregation. Hsp26 alters the nature of protein aggregates to facilitate reactivation by Hsp104. J Biol Chem 2005; 280:23869 - 75; http://dx.doi.org/10.1074/jbc.M502854200; PMID: 15845535
   PubMed Web of Science ®Google Scholar
• Haslbeck M, Miess A, Stromer T, Walter S, Buchner J. Disassembling protein aggregates in the yeast cytosol. The cooperation of Hsp26 with Ssa1 and Hsp104. J Biol Chem 2005; 280:23861 - 8; http://dx.doi.org/10.1074/jbc.M502697200; PMID: 15843375
   PubMed Web of Science ®Google Scholar
• Newby GA, Lindquist S. Blessings in disguise: biological benefits of prion-like mechanisms. Trends Cell Biol 2013; 23:251 - 9; http://dx.doi.org/10.1016/j.tcb.2013.01.007; PMID: 23485338
   PubMed Web of Science ®Google Scholar
• True HL, Berlin I, Lindquist SL. Epigenetic regulation of translation reveals hidden genetic variation to produce complex traits. Nature 2004; 431:184 - 7; http://dx.doi.org/10.1038/nature02885; PMID: 15311209
   PubMed Web of Science ®Google Scholar
• True HL, Lindquist SL. A yeast prion provides a mechanism for genetic variation and phenotypic diversity. Nature 2000; 407:477 - 83; http://dx.doi.org/10.1038/35035005; PMID: 11028992
   PubMed Web of Science ®Google Scholar
• Halfmann R, Jarosz DF, Jones SK, Chang A, Lancaster AK, Lindquist S. Prions are a common mechanism for phenotypic inheritance in wild yeasts. Nature 2012; 482:363 - 8; http://dx.doi.org/10.1038/nature10875; PMID: 22337056
   PubMed Web of Science ®Google Scholar
• Alberti S, Halfmann R, King O, Kapila A, Lindquist S. A systematic survey identifies prions and illuminates sequence features of prionogenic proteins. Cell 2009; 137:146 - 58; http://dx.doi.org/10.1016/j.cell.2009.02.044; PMID: 19345193
   PubMed Web of Science ®Google Scholar
• Chernoff YO, Lindquist SL, Ono B, Inge-Vechtomov SG, Liebman SW. Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+]. [psi+] Science 1995; 268:880 - 4; http://dx.doi.org/10.1126/science.7754373; PMID: 7754373
   PubMed Web of Science ®Google Scholar
• Liebman SW, Chernoff YO. Prions in yeast. Genetics 2012; 191:1041 - 72; http://dx.doi.org/10.1534/genetics.111.137760; PMID: 22879407
   PubMed Web of Science ®Google Scholar
• Paushkin SV, Kushnirov VV, Smirnov VN, Ter-Avanesyan MD. Propagation of the yeast prion-like [psi+] determinant is mediated by oligomerization of the SUP35-encoded polypeptide chain release factor. EMBO J 1996; 15:3127 - 34; PMID: 8670813
   PubMed Web of Science ®Google Scholar
• Shorter J. Hsp104: a weapon to combat diverse neurodegenerative disorders. Neurosignals 2008; 16:63 - 74; http://dx.doi.org/10.1159/000109760; PMID: 18097161
   PubMed Web of Science ®Google Scholar
• Murdock DG, Boone BE, Esposito LA, Wallace DC. Up-regulation of nuclear and mitochondrial genes in the skeletal muscle of mice lacking the heart/muscle isoform of the adenine nucleotide translocator. J Biol Chem 1999; 274:14429 - 33; http://dx.doi.org/10.1074/jbc.274.20.14429; PMID: 10318868
   PubMed Web of Science ®Google Scholar
• Ozelius LJ, Page CE, Klein C, Hewett JW, Mineta M, Leung J, Shalish C, Bressman SB, de Leon D, Brin MF, et al. The TOR1A (DYT1) gene family and its role in early onset torsion dystonia. Genomics 1999; 62:377 - 84; http://dx.doi.org/10.1006/geno.1999.6039; PMID: 10644435
   PubMed Web of Science ®Google Scholar
• Périer F, Radeke CM, Raab-Graham KF, Vandenberg CA. Expression of a putative ATPase suppresses the growth defect of a yeast potassium transport mutant: identification of a mammalian member of the Clp/HSP104 family. Gene 1995; 152:157 - 63; http://dx.doi.org/10.1016/0378-1119(94)00697-Q; PMID: 7835694
   PubMed Web of Science ®Google Scholar
• Cushman-Nick M, Bonini NM, Shorter J. Hsp104 suppresses polyglutamine-induced degeneration post onset in a drosophila MJD/SCA3 model. PLoS Genet 2013; 9:e1003781; http://dx.doi.org/10.1371/journal.pgen.1003781; PMID: 24039611
   PubMed Web of Science ®Google Scholar
• Dandoy-Dron F, Bogdanova A, Beringue V, Bailly Y, Tovey MG, Laude H, Dron M. Infection by ME7 prion is not modified in transgenic mice expressing the yeast chaperone Hsp104 in neurons. Neurosci Lett 2006; 405:181 - 5; http://dx.doi.org/10.1016/j.neulet.2006.05.066; PMID: 16884849
   PubMed Web of Science ®Google Scholar
• Perrin V, Régulier E, Abbas-Terki T, Hassig R, Brouillet E, Aebischer P, Luthi-Carter R, Déglon N. Neuroprotection by Hsp104 and Hsp27 in lentiviral-based rat models of Huntington’s disease. Mol Ther 2007; 15:903 - 11; http://dx.doi.org/10.1038/mt.sj.6300141; PMID: 17375066
   PubMed Web of Science ®Google Scholar
• Satyal SH, Schmidt E, Kitagawa K, Sondheimer N, Lindquist S, Kramer JM, Morimoto RI. Polyglutamine aggregates alter protein folding homeostasis in Caenorhabditis elegans.. Proc Natl Acad Sci U S A 2000; 97:5750 - 5; http://dx.doi.org/10.1073/pnas.100107297; PMID: 10811890
   PubMed Web of Science ®Google Scholar
• Vacher C, Garcia-Oroz L, Rubinsztein DC. Overexpression of yeast hsp104 reduces polyglutamine aggregation and prolongs survival of a transgenic mouse model of Huntington’s disease. Hum Mol Genet 2005; 14:3425 - 33; http://dx.doi.org/10.1093/hmg/ddi372; PMID: 16204350
   PubMed Web of Science ®Google Scholar
• Shorter J. The mammalian disaggregase machinery: Hsp110 synergizes with Hsp70 and Hsp40 to catalyze protein disaggregation and reactivation in a cell-free system. PLoS One 2011; 6:e26319; http://dx.doi.org/10.1371/journal.pone.0026319; PMID: 22022600
   PubMed Web of Science ®Google Scholar
• Easton DP, Kaneko Y, Subjeck JR. The hsp110 and Grp1 70 stress proteins: newly recognized relatives of the Hsp70s. Cell Stress Chaperones 2000; 5:276 - 90; http://dx.doi.org/10.1379/1466-1268(2000)005<0276:THAGSP>2.0.CO;2; PMID: 11048651
   PubMed Web of Science ®Google Scholar
• Oh HJ, Chen X, Subjeck JR. Hsp110 protects heat-denatured proteins and confers cellular thermoresistance. J Biol Chem 1997; 272:31636 - 40; http://dx.doi.org/10.1074/jbc.272.50.31636; PMID: 9395504
   PubMed Web of Science ®Google Scholar
• Raviol H, Sadlish H, Rodriguez F, Mayer MP, Bukau B. Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor. EMBO J 2006; 25:2510 - 8; http://dx.doi.org/10.1038/sj.emboj.7601139; PMID: 16688211
   PubMed Web of Science ®Google Scholar
• Dragovic Z, Broadley SA, Shomura Y, Bracher A, Hartl FU. Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s. EMBO J 2006; 25:2519 - 28; http://dx.doi.org/10.1038/sj.emboj.7601138; PMID: 16688212
   PubMed Web of Science ®Google Scholar
• Polier S, Dragovic Z, Hartl FU, Bracher A. Structural basis for the cooperation of Hsp70 and Hsp110 chaperones in protein folding. Cell 2008; 133:1068 - 79; http://dx.doi.org/10.1016/j.cell.2008.05.022; PMID: 18555782
   PubMed Web of Science ®Google Scholar
• Mattoo RU, Sharma SK, Priya S, Finka A, Goloubinoff P. Hsp110 is a bona fide chaperone using ATP to unfold stable misfolded polypeptides and reciprocally collaborate with Hsp70 to solubilize protein aggregates. J Biol Chem 2013; 288:21399 - 411; http://dx.doi.org/10.1074/jbc.M113.479253; PMID: 23737532
   PubMed Web of Science ®Google Scholar
• Polier S, Hartl FU, Bracher A. Interaction of the Hsp110 molecular chaperones from S. cerevisiae with substrate protein. J Mol Biol 2010; 401:696 - 707; http://dx.doi.org/10.1016/j.jmb.2010.07.004; PMID: 20624400
   PubMed Web of Science ®Google Scholar
• Shaner L, Sousa R, Morano KA. Characterization of Hsp70 binding and nucleotide exchange by the yeast Hsp110 chaperone Sse1. Biochemistry 2006; 45:15075 - 84; http://dx.doi.org/10.1021/bi061279k; PMID: 17154545
   PubMed Web of Science ®Google Scholar
• Fan Q, Park KW, Du Z, Morano KA, Li L. The role of Sse1 in the de novo formation and variant determination of the [PSI+] prion. Genetics 2007; 177:1583 - 93; http://dx.doi.org/10.1534/genetics.107.077982; PMID: 18039878
   PubMed Web of Science ®Google Scholar
• Moran C, Kinsella GK, Zhang ZR, Perrett S, Jones GW. Mutational analysis of Sse1 (Hsp110) suggests an integral role for this chaperone in yeast prion propagation in vivo. G3 (Bethesda) 2013; 3:1409 - 18; http://dx.doi.org/10.1534/g3.113.007112; PMID: 23797105
   PubMed Web of Science ®Google Scholar
• Sadlish H, Rampelt H, Shorter J, Wegrzyn RD, Andréasson C, Lindquist S, Bukau B. Hsp110 chaperones regulate prion formation and propagation in S. cerevisiae by two discrete activities. PLoS One 2008; 3:e1763; http://dx.doi.org/10.1371/journal.pone.0001763; PMID: 18335038
   PubMed Web of Science ®Google Scholar
• Escusa-Toret S, Vonk WI, Frydman J. Spatial sequestration of misfolded proteins by a dynamic chaperone pathway enhances cellular fitness during stress. Nat Cell Biol 2013; 15:1231 - 43; http://dx.doi.org/10.1038/ncb2838; PMID: 24036477
   PubMed Web of Science ®Google Scholar
• Spokoini R, Moldavski O, Nahmias Y, England JL, Schuldiner M, Kaganovich D. Confinement to organelle-associated inclusion structures mediates asymmetric inheritance of aggregated protein in budding yeast. Cell Rep 2012; 2:738 - 47; http://dx.doi.org/10.1016/j.celrep.2012.08.024; PMID: 23022486
   PubMed Web of Science ®Google Scholar
• Kaganovich D, Kopito R, Frydman J. Misfolded proteins partition between two distinct quality control compartments. Nature 2008; 454:1088 - 95; http://dx.doi.org/10.1038/nature07195; PMID: 18756251
   PubMed Web of Science ®Google Scholar
• Rampelt H, Kirstein-Miles J, Nillegoda NB, Chi K, Scholz SR, Morimoto RI, Bukau B. Metazoan Hsp70 machines use Hsp110 to power protein disaggregation. EMBO J 2012; 31:4221 - 35; http://dx.doi.org/10.1038/emboj.2012.264; PMID: 22990239
   PubMed Web of Science ®Google Scholar
• Cherkasov V, Hofmann S, Druffel-Augustin S, Mogk A, Tyedmers J, Stoecklin G, Bukau B. Coordination of Translational Control and Protein Homeostasis during Severe Heat Stress. Curr Biol 2013; 23:2452 - 62; http://dx.doi.org/10.1016/j.cub.2013.09.058; PMID: 24291094
   PubMed Web of Science ®Google Scholar
• Goeckeler JL, Stephens A, Lee P, Caplan AJ, Brodsky JL. Overexpression of yeast Hsp110 homolog Sse1p suppresses ydj1-151 thermosensitivity and restores Hsp90-dependent activity. Mol Biol Cell 2002; 13:2760 - 70; http://dx.doi.org/10.1091/mbc.02-04-0051; PMID: 12181344
   PubMed Web of Science ®Google Scholar
• Hrizo SL, Gusarova V, Habiel DM, Goeckeler JL, Fisher EA, Brodsky JL. The Hsp110 molecular chaperone stabilizes apolipoprotein B from endoplasmic reticulum-associated degradation (ERAD). J Biol Chem 2007; 282:32665 - 75; http://dx.doi.org/10.1074/jbc.M705216200; PMID: 17823116
   PubMed Web of Science ®Google Scholar
• Ben-Zvi A, De Los Rios P, Dietler G, Goloubinoff P. Active solubilization and refolding of stable protein aggregates by cooperative unfolding action of individual hsp70 chaperones. J Biol Chem 2004; 279:37298 - 303; http://dx.doi.org/10.1074/jbc.M405627200; PMID: 15201275
   PubMed Web of Science ®Google Scholar
• De Los Rios P, Ben-Zvi A, Slutsky O, Azem A, Goloubinoff P. Hsp70 chaperones accelerate protein translocation and the unfolding of stable protein aggregates by entropic pulling. Proc Natl Acad Sci U S A 2006; 103:6166 - 71; http://dx.doi.org/10.1073/pnas.0510496103; PMID: 16606842
   PubMed Web of Science ®Google Scholar
• Goloubinoff P, De Los Rios P. The mechanism of Hsp70 chaperones: (entropic) pulling the models together. Trends Biochem Sci 2007; 32:372 - 80; http://dx.doi.org/10.1016/j.tibs.2007.06.008; PMID: 17629485
   PubMed Web of Science ®Google Scholar
• Schuermann JP, Jiang J, Cuellar J, Llorca O, Wang L, Gimenez LE, Jin S, Taylor AB, Demeler B, Morano KA, et al. Structure of the Hsp110:Hsc70 nucleotide exchange machine. Mol Cell 2008; 31:232 - 43; http://dx.doi.org/10.1016/j.molcel.2008.05.006; PMID: 18550409
   PubMed Web of Science ®Google Scholar
• Goeckeler JL, Petruso AP, Aguirre J, Clement CC, Chiosis G, Brodsky JL. The yeast Hsp110, Sse1p, exhibits high-affinity peptide binding. FEBS Lett 2008; 582:2393 - 6; http://dx.doi.org/10.1016/j.febslet.2008.05.047; PMID: 18539149
   PubMed Web of Science ®Google Scholar
• Eisenberg D, Jucker M. The amyloid state of proteins in human diseases. Cell 2012; 148:1188 - 203; http://dx.doi.org/10.1016/j.cell.2012.02.022; PMID: 22424229
   PubMed Web of Science ®Google Scholar
• Shorter J. Emergence and natural selection of drug-resistant prions. Mol Biosyst 2010; 6:1115 - 30; http://dx.doi.org/10.1039/c004550k; PMID: 20422111
   PubMed Web of Science ®Google Scholar
• Carulla N, Caddy GL, Hall DR, Zurdo J, Gairí M, Feliz M, Giralt E, Robinson CV, Dobson CM. Molecular recycling within amyloid fibrils. Nature 2005; 436:554 - 8; http://dx.doi.org/10.1038/nature03986; PMID: 16049488
   PubMed Web of Science ®Google Scholar
• Carulla N, Zhou M, Giralt E, Robinson CV, Dobson CM. Structure and intermolecular dynamics of aggregates populated during amyloid fibril formation studied by hydrogen/deuterium exchange. Acc Chem Res 2010; 43:1072 - 9; http://dx.doi.org/10.1021/ar9002784; PMID: 20557067
   PubMed Web of Science ®Google Scholar
• Kuo Y, Ren S, Lao U, Edgar BA, Wang T. Suppression of polyglutamine protein toxicity by co-expression of a heat-shock protein 40 and a heat-shock protein 110. Cell Death Dis 2013; 4:e833; http://dx.doi.org/10.1038/cddis.2013.351; PMID: 24091676
   PubMed Web of Science ®Google Scholar
• Blum ES, Schwendeman AR, Shaham S. PolyQ disease: misfiring of a developmental cell death program?. Trends Cell Biol 2013; 23:168 - 74; http://dx.doi.org/10.1016/j.tcb.2012.11.003; PMID: 23228508
   PubMed Web of Science ®Google Scholar
• Song Y, Nagy M, Ni W, Tyagi NK, Fenton WA, López-Giráldez F, Overton JD, Horwich AL, Brady ST. Molecular chaperone Hsp110 rescues a vesicle transport defect produced by an ALS-associated mutant SOD1 protein in squid axoplasm. Proc Natl Acad Sci U S A 2013; 110:5428 - 33; http://dx.doi.org/10.1073/pnas.1303279110; PMID: 23509252
   PubMed Web of Science ®Google Scholar
• Calamini B, Silva MC, Madoux F, Hutt DM, Khanna S, Chalfant MA, Saldanha SA, Hodder P, Tait BD, Garza D, et al. Small-molecule proteostasis regulators for protein conformational diseases. Nat Chem Biol 2012; 8:185 - 96; http://dx.doi.org/10.1038/nchembio.763; PMID: 22198733
   PubMed Web of Science ®Google Scholar
• Labbadia J, Cunliffe H, Weiss A, Katsyuba E, Sathasivam K, Seredenina T, Woodman B, Moussaoui S, Frentzel S, Luthi-Carter R, et al. Altered chromatin architecture underlies progressive impairment of the heat shock response in mouse models of Huntington disease. J Clin Invest 2011; 121:3306 - 19; http://dx.doi.org/10.1172/JCI57413; PMID: 21785217
   PubMed Web of Science ®Google Scholar
• Wang AM, Miyata Y, Klinedinst S, Peng HM, Chua JP, Komiyama T, Li X, Morishima Y, Merry DE, Pratt WB, et al. Activation of Hsp70 reduces neurotoxicity by promoting polyglutamine protein degradation. Nat Chem Biol 2013; 9:112 - 8; http://dx.doi.org/10.1038/nchembio.1140; PMID: 23222885
   PubMed Web of Science ®Google Scholar
• Zorn JA, Wells JA. Turning enzymes ON with small molecules. Nat Chem Biol 2010; 6:179 - 88; http://dx.doi.org/10.1038/nchembio.318; PMID: 20154666
   PubMed Web of Science ®Google Scholar