{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,23]],"date-time":"2026-10-23T22:15:04Z","timestamp":1792793704048,"version":"4.5.0"},"reference-count":261,"publisher":"Frontiers Media SA","funder":[{"DOI":"10.13039\/501100004083","name":"Ministry of Science ICT and Future Planning","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100004083","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003725","name":"National Research Foundation of Korea","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100003725","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100005984","name":"Dr. Miriam and Sheldon G. Adelson Medical Research Foundation","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100005984","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003977","name":"Israel Science Foundation","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100003977","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["frontiersin.org"],"crossmark-restriction":true},"short-container-title":["Front. Neurosci."],"DOI":"10.3389\/fnins.2017.00185","type":"journal-article","created":{"date-parts":[[2017,4,5]],"date-time":"2017-04-05T23:39:32Z","timestamp":1491435572000},"update-policy":"https:\/\/doi.org\/10.3389\/crossmark-policy","source":"Crossref","is-referenced-by-count":337,"title":["Protein Quality Control by Molecular Chaperones in Neurodegeneration"],"prefix":"10.3389","volume":"11","author":[{"given":"Aaron","family":"Ciechanover","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yong Tae","family":"Kwon","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1965","published-online":{"date-parts":[[2017,4,6]]},"reference":[{"issue":"Pt 13","key":"B1","doi-asserted-by":"crossref","first-page":"2491","DOI":"10.1242\/jcs.114.13.2491","article-title":"A molecular chaperone complex at the lysosomal membrane is required for protein translocation","volume":"114","author":"Agarraberes","year":"2001","journal-title":"J. Cell Sci."},{"key":"B2","doi-asserted-by":"crossref","first-page":"825","DOI":"10.1083\/jcb.137.4.825","article-title":"An intralysosomal hsp70 is required for a selective pathway of lysosomal protein degradation","volume":"137","author":"Agarraberes","year":"1997","journal-title":"J. Cell Biol."},{"key":"B3","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1379\/1466-1268(2003)008<0225:BNEFOH>2.0.CO;2","article-title":"BAG-1\u2013a nucleotide exchange factor of Hsc70 with multiple cellular functions","volume":"8","author":"Alberti","year":"2003","journal-title":"Cell Stress Chaperones"},{"key":"B4","doi-asserted-by":"publisher","first-page":"26714","DOI":"10.1074\/jbc.M601603200","article-title":"CHIP protects from the neurotoxicity of expanded and wild-type ataxin-1 and promotes their ubiquitination and degradation","volume":"281","author":"Al-Ramahi","year":"2006","journal-title":"J. Biol. Chem."},{"key":"B5","doi-asserted-by":"publisher","first-page":"1175","DOI":"10.1038\/sj.onc.1210716","article-title":"The activity of hsp90\u03b1 promoter is regulated by NF-\u03b2 B transcription factors","volume":"27","author":"Ammirante","year":"2008","journal-title":"Oncogene"},{"key":"B6","doi-asserted-by":"publisher","first-page":"6212","DOI":"10.1073\/pnas.0601700103","article-title":"Impaired neurogenesis and cardiovascular development in mice lacking the E3 ubiquitin ligases UBR1 and UBR2 of the N-end rule pathway","volume":"103","author":"An","year":"2006","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"B7","doi-asserted-by":"publisher","first-page":"32","DOI":"10.4161\/pri.6.1.18272","article-title":"Misfolded PrP and a novel mechanism of proteasome inhibition","volume":"6","author":"Andre","year":"2012","journal-title":"Prion"},{"key":"B8","doi-asserted-by":"publisher","first-page":"1157","DOI":"10.1016\/j.jmb.2008.09.063","article-title":"Hsp104 targets multiple intermediates on the amyloid pathway and suppresses the seeding capacity of A\u03b2 fibrils and protofibrils","volume":"384","author":"Arimon","year":"2008","journal-title":"J. Mol. Biol."},{"key":"B9","doi-asserted-by":"publisher","first-page":"3522","DOI":"10.1091\/mbc.E12-02-0168","article-title":"BiP prevents rod opsin aggregation","volume":"23","author":"Athanasiou","year":"2012","journal-title":"Mol. Biol. Cell"},{"key":"B10","doi-asserted-by":"publisher","first-page":"1185","DOI":"10.1038\/nm1102-1185","article-title":"Pharmacological prevention of Parkinson disease in Drosophila","volume":"8","author":"Auluck","year":"2002","journal-title":"Nat. Med."},{"key":"B11","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1126\/science.3018930","article-title":"In vivo half-life of a protein is a function of its amino-terminal residue","volume":"234","author":"Bachmair","year":"1986","journal-title":"Science"},{"key":"B12","doi-asserted-by":"crossref","first-page":"4535","DOI":"10.1128\/MCB.19.6.4535","article-title":"Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions","volume":"19","author":"Ballinger","year":"1999","journal-title":"Mol. Cell. Biol."},{"key":"B13","doi-asserted-by":"publisher","first-page":"279","DOI":"10.1101\/lm.33500","article-title":"Varying intertrial interval reveals temporally defined memory deficits and enhancements in NTAN1-deficient mice","volume":"7","author":"Balogh","year":"2000","journal-title":"Learn. Mem."},{"key":"B14","doi-asserted-by":"publisher","first-page":"336","DOI":"10.1016\/S0006-8993(00)03268-6","article-title":"Facilitated stimulus-response associative learning and long-term memory in mice lacking the NTAN1 amidase of the N-end rule pathway","volume":"892","author":"Balogh","year":"2001","journal-title":"Brain Res."},{"key":"B15","doi-asserted-by":"publisher","first-page":"5747","DOI":"10.1128\/MCB.02070-07","article-title":"The chaperone-mediated autophagy receptor organizes in dynamic protein complexes at the lysosomal membrane","volume":"28","author":"Bandyopadhyay","year":"2008","journal-title":"Mol. Cell. Biol."},{"key":"B16","doi-asserted-by":"publisher","first-page":"213","DOI":"10.1016\/j.nbd.2006.06.017","article-title":"Induction of multiple heat shock proteins and neuroprotection in a primary culture model of familial amyotrophic lateral sclerosis","volume":"24","author":"Batulan","year":"2006","journal-title":"Neurobiol. Dis."},{"key":"B17","doi-asserted-by":"publisher","first-page":"256","DOI":"10.1038\/nbt.1608","article-title":"Harnessing chaperone-mediated autophagy for the selective degradation of mutant huntingtin protein","volume":"28","author":"Bauer","year":"2010","journal-title":"Nat. Biotechnol."},{"key":"B18","doi-asserted-by":"publisher","first-page":"887","DOI":"10.1016\/j.molcel.2006.08.017","article-title":"Chaperonin TRiC promotes the assembly of polyQ expansion proteins into nontoxic oligomers","volume":"23","author":"Behrends","year":"2006","journal-title":"Mol. Cell"},{"key":"B19","doi-asserted-by":"publisher","first-page":"470","DOI":"10.1038\/nature09371","article-title":"Role of a ribosome-associated E3 ubiquitin ligase in protein quality control","volume":"467","author":"Bengtson","year":"2010","journal-title":"Nature"},{"key":"B20","doi-asserted-by":"crossref","first-page":"9002","DOI":"10.1074\/jbc.272.14.9002","article-title":"Ubiquitin-dependent degradation of certain protein substrates in vitro requires the molecular chaperone Hsc70","volume":"272","author":"Bercovich","year":"1997","journal-title":"J. Biol. Chem."},{"key":"B21","doi-asserted-by":"publisher","first-page":"6926","DOI":"10.1523\/JNEUROSCI.0800-08.2008","article-title":"Autophagy induction and autophagosome clearance in neurons: relationship to autophagic pathology in Alzheimer's disease","volume":"28","author":"Boland","year":"2008","journal-title":"J. Neurosci."},{"key":"B22","doi-asserted-by":"publisher","first-page":"12","DOI":"10.1186\/alzrt36","article-title":"The culprit behind amyloid \u03b2 peptide related neurotoxicity in Alzheimer's disease: oligomer size or conformation?","volume":"2","author":"Broersen","year":"2010","journal-title":"Alzheimers. Res. Ther."},{"key":"B23","doi-asserted-by":"publisher","first-page":"161","DOI":"10.1016\/j.molcel.2013.02.009","article-title":"Neurodegeneration-associated protein fragments as short-lived substrates of the N-end rule pathway","volume":"50","author":"Brower","year":"2013","journal-title":"Mol. Cell"},{"key":"B24","doi-asserted-by":"publisher","first-page":"2956","DOI":"10.1002\/prot.23152","article-title":"Inhibition of \u03b1-synuclein aggregation by small heat shock proteins","volume":"79","author":"Bruinsma","year":"2011","journal-title":"Proteins"},{"key":"B25","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1096\/fasebj.10.1.8566529","article-title":"Supervising the fold: functional principles of molecular chaperones","volume":"10","author":"Buchner","year":"1996","journal-title":"FASEB J."},{"key":"B26","doi-asserted-by":"publisher","first-page":"007","DOI":"10.4172\/2161-0460.S10-007","article-title":"Chaperone-dependent Neurodegeneration: a Molecular Perspective on Therapeutic Intervention","volume":"2013","author":"Carman","year":"2013","journal-title":"J. Alzheimers Dis. Parkinson."},{"key":"B27","doi-asserted-by":"publisher","first-page":"83","DOI":"10.1016\/j.pneurobio.2011.09.009","article-title":"Alteration of protein folding and degradation in motor neuron diseases: implications and protective functions of small heat shock proteins","volume":"97","author":"Carra","year":"2012","journal-title":"Prog. Neurobiol."},{"key":"B28","doi-asserted-by":"publisher","first-page":"e02481","DOI":"10.7554\/eLife.02481","article-title":"Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation","volume":"3","author":"Carroni","year":"2014","journal-title":"Elife"},{"key":"B29","doi-asserted-by":"publisher","first-page":"917","DOI":"10.1038\/ncb3177","article-title":"Amino-terminal arginylation targets endoplasmic reticulum chaperone BiP for autophagy through p62 binding","volume":"17","author":"Cha-Molstad","year":"2015","journal-title":"Nat. Cell Biol."},{"issue":"Pt 2","key":"B30","doi-asserted-by":"crossref","first-page":"469","DOI":"10.1042\/bj2840469","article-title":"Human homologues of the bacterial heat-shock protein DnaJ are preferentially expressed in neurons","volume":"284","author":"Cheetham","year":"1992","journal-title":"Biochem. J."},{"key":"B31","doi-asserted-by":"crossref","first-page":"28","DOI":"10.1379\/1466-1268(1998)003<0028:SFAEOD>2.3.CO;2","article-title":"Structure, function and evolution of DnaJ: conservation and adaptation of chaperone function","volume":"3","author":"Cheetham","year":"1998","journal-title":"Cell Stress Chaperones"},{"key":"B32","doi-asserted-by":"publisher","first-page":"2464","DOI":"10.1523\/JNEUROSCI.0151-13.2014","article-title":"Hsp90 chaperone inhibitor 17-AAG attenuates A\u03b2-induced synaptic toxicity and memory impairment","volume":"34","author":"Chen","year":"2014","journal-title":"J. Neurosci."},{"key":"B33","doi-asserted-by":"crossref","first-page":"6797","DOI":"10.1016\/S0021-9258(18)68713-7","article-title":"Peptide sequences that target proteins for enhanced degradation during serum withdrawal","volume":"263","author":"Chiang","year":"1988","journal-title":"J. Biol. Chem."},{"key":"B34","doi-asserted-by":"crossref","first-page":"382","DOI":"10.1126\/science.2799391","article-title":"A role for a 70-kilodalton heat shock protein in lysosomal degradation of intracellular proteins","volume":"246","author":"Chiang","year":"1989","journal-title":"Science"},{"key":"B35","doi-asserted-by":"publisher","first-page":"1407","DOI":"10.1093\/hmg\/ddh162","article-title":"Mutant huntingtin directly increases susceptibility of mitochondria to the calcium-induced permeability transition and cytochrome c release","volume":"13","author":"Choo","year":"2004","journal-title":"Hum. Mol. Genet."},{"key":"B36","doi-asserted-by":"publisher","first-page":"245","DOI":"10.1016\/B978-0-12-800149-3.00005-6","article-title":"Genetics of Alzheimer's disease","volume":"87","author":"Chouraki","year":"2014","journal-title":"Adv. Genet."},{"key":"B37","doi-asserted-by":"publisher","first-page":"3400","DOI":"10.1016\/j.bmc.2013.01.056","article-title":"Intracellular protein degradation: from a vague idea through the lysosome and the ubiquitin-proteasome system and onto human diseases and drug targeting","volume":"21","author":"Ciechanover","year":"2013","journal-title":"Bioorg. Med. Chem."},{"key":"B38","doi-asserted-by":"publisher","first-page":"e147","DOI":"10.1038\/emm.2014.117","article-title":"Degradation of misfolded proteins in neurodegenerative diseases: therapeutic targets and strategies","volume":"47","author":"Ciechanover","year":"2015","journal-title":"Exp. Mol. Med."},{"key":"B39","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1101\/SQB.1995.060.01.053","article-title":"The ubiquitin-mediated proteolytic system: involvement of molecular chaperones, degradation of oncoproteins, and activation of transcriptional regulators","volume":"60","author":"Ciechanover","year":"1995","journal-title":"Cold Spring Harb. Symp. Quant. Biol."},{"key":"B40","doi-asserted-by":"publisher","first-page":"995","DOI":"10.1111\/j.1471-4159.2005.03253.x","article-title":"Celastrol protects against MPTP- and 3-nitropropionic acid-induced neurotoxicity","volume":"94","author":"Cleren","year":"2005","journal-title":"J. Neurochem."},{"key":"B41","doi-asserted-by":"publisher","first-page":"93","DOI":"10.1038\/35050618","article-title":"The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins","volume":"3","author":"Connell","year":"2001","journal-title":"Nat. Cell Biol."},{"key":"B42","doi-asserted-by":"publisher","first-page":"1401","DOI":"10.1016\/j.cell.2006.09.051","article-title":"Ubiquitin chains are remodeled at the proteasome by opposing ubiquitin ligase and deubiquitinating activities","volume":"127","author":"Crosas","year":"2006","journal-title":"Cell"},{"key":"B43","doi-asserted-by":"crossref","first-page":"501","DOI":"10.1126\/science.273.5274.501","article-title":"A receptor for the selective uptake and degradation of proteins by lysosomes","volume":"273","author":"Cuervo","year":"1996","journal-title":"Science"},{"key":"B44","doi-asserted-by":"publisher","first-page":"570","DOI":"10.1034\/j.1600-0854.2000.010707.x","article-title":"Regulation of lamp2a levels in the lysosomal membrane","volume":"1","author":"Cuervo","year":"2000","journal-title":"Traffic"},{"key":"B45","doi-asserted-by":"crossref","first-page":"5606","DOI":"10.1074\/jbc.272.9.5606","article-title":"A population of rat liver lysosomes responsible for the selective uptake and degradation of cytosolic proteins","volume":"272","author":"Cuervo","year":"1997","journal-title":"J. Biol. Chem."},{"issue":"5 Pt 1","key":"B46","doi-asserted-by":"crossref","first-page":"C1200","DOI":"10.1152\/ajpcell.1995.269.5.C1200","article-title":"Activation of a selective pathway of lysosomal proteolysis in rat liver by prolonged starvation","volume":"269","author":"Cuervo","year":"1995","journal-title":"Am. J. Physiol."},{"key":"B47","doi-asserted-by":"publisher","first-page":"1292","DOI":"10.1126\/science.1101738","article-title":"Impaired degradation of mutant \u03b1-synuclein by chaperone-mediated autophagy","volume":"305","author":"Cuervo","year":"2004","journal-title":"Science"},{"key":"B48","doi-asserted-by":"publisher","first-page":"368","DOI":"10.1016\/S0968-0004(02)02125-4","article-title":"Protein quality control: U-box-containing E3 ubiquitin ligases join the fold","volume":"27","author":"Cyr","year":"2002","journal-title":"Trends Biochem. Sci."},{"key":"B49","doi-asserted-by":"publisher","first-page":"655","DOI":"10.1016\/j.tibs.2003.10.007","article-title":"TPR proteins: the versatile helix","volume":"28","author":"D'Andrea","year":"2003","journal-title":"Trends Biochem. Sci."},{"key":"B50","doi-asserted-by":"publisher","first-page":"263","DOI":"10.1093\/cvr\/cvp255","article-title":"Stressing the ubiquitin-proteasome system","volume":"85","author":"Dantuma","year":"2010","journal-title":"Cardiovasc. Res."},{"key":"B51","doi-asserted-by":"publisher","first-page":"326","DOI":"10.1096\/fj.10-164624","article-title":"Heat-shock protein 70 modulates toxic extracellular \u03b1-synuclein oligomers and rescues trans-synaptic toxicity","volume":"25","author":"Danzer","year":"2011","journal-title":"FASEB J."},{"key":"B52","doi-asserted-by":"publisher","first-page":"14733","DOI":"10.1074\/jbc.M413024200","article-title":"Heat shock protein 70 inhibits \u03b1-synuclein fibril formation via preferential binding to prefibrillar species","volume":"280","author":"Dedmon","year":"2005","journal-title":"J. Biol. Chem."},{"key":"B53","doi-asserted-by":"publisher","first-page":"245","DOI":"10.1016\/j.neuron.2011.09.011","article-title":"Expanded GGGGCC hexanucleotide repeat in noncoding region of C9ORF72 causes chromosome 9p-linked FTD and ALS","volume":"72","author":"DeJesus-Hernandez","year":"2011","journal-title":"Neuron"},{"key":"B54","doi-asserted-by":"publisher","first-page":"1569","DOI":"10.1016\/S0960-9822(01)00487-0","article-title":"Cooperation of a ubiquitin domain protein and an E3 ubiquitin ligase during chaperone\/proteasome coupling","volume":"11","author":"Demand","year":"2001","journal-title":"Curr. Biol."},{"key":"B55","doi-asserted-by":"publisher","first-page":"778","DOI":"10.1016\/j.cell.2012.09.038","article-title":"Operational plasticity enables hsp104 to disaggregate diverse amyloid and nonamyloid clients","volume":"151","author":"DeSantis","year":"2012","journal-title":"Cell"},{"key":"B56","doi-asserted-by":"crossref","first-page":"305","DOI":"10.1016\/0968-0004(90)90019-8","article-title":"Peptide sequences that target cytosolic proteins for lysosomal proteolysis","volume":"15","author":"Dice","year":"1990","journal-title":"Trends Biochem. Sci."},{"key":"B57","doi-asserted-by":"publisher","first-page":"2839","DOI":"10.2174\/092986707782360079","article-title":"Anti-cancer therapeutic approaches based on intracellular and extracellular heat shock proteins","volume":"14","author":"Didelot","year":"2007","journal-title":"Curr. Med. Chem."},{"key":"B58","doi-asserted-by":"publisher","first-page":"3571","DOI":"10.1523\/JNEUROSCI.0037-07.2007","article-title":"Histone deacetylase 6 inhibition compensates for the transport deficit in Huntington's disease by increasing tubulin acetylation","volume":"27","author":"Dompierre","year":"2007","journal-title":"J. Neurosci."},{"key":"B59","doi-asserted-by":"crossref","first-page":"51","DOI":"10.4161\/pri.3.2.8587","article-title":"Molecular chaperones antagonize proteotoxicity by differentially modulating protein aggregation pathways","volume":"3","author":"Douglas","year":"2009","journal-title":"Prion"},{"key":"B60","doi-asserted-by":"publisher","first-page":"617","DOI":"10.1038\/nrm3660","article-title":"Protein rescue from aggregates by powerful molecular chaperone machines","volume":"14","author":"Doyle","year":"2013","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"B61","doi-asserted-by":"publisher","first-page":"40","DOI":"10.1016\/j.tibs.2008.09.010","article-title":"Hsp104 and ClpB: protein disaggregating machines","volume":"34","author":"Doyle","year":"2009","journal-title":"Trends Biochem. Sci."},{"key":"B62","doi-asserted-by":"crossref","first-page":"299","DOI":"10.3233\/JPD-2011-11044","article-title":"Molecular chaperones in Parkinson's disease\u2013present and future","volume":"1","author":"Ebrahimi-Fakhari","year":"2011","journal-title":"J. Parkinsons. Dis."},{"key":"B63","doi-asserted-by":"publisher","first-page":"4143","DOI":"10.1016\/j.febslet.2008.11.015","article-title":"Degradation of misfolded protein in the cytoplasm is mediated by the ubiquitin ligase Ubr1","volume":"582","author":"Eisele","year":"2008","journal-title":"FEBS Lett."},{"key":"B64","doi-asserted-by":"publisher","first-page":"4","DOI":"10.1038\/cdd.2009.82","article-title":"Therapeutic strategies within the ubiquitin proteasome system","volume":"17","author":"Eldridge","year":"2010","journal-title":"Cell Death Differ."},{"key":"B65","doi-asserted-by":"publisher","first-page":"1168","DOI":"10.1111\/j.1471-4159.2009.06047.x","article-title":"BAG-1M is up-regulated in hippocampus of Alzheimer's disease patients and associates with tau and APP proteins","volume":"109","author":"Elliott","year":"2009","journal-title":"J. Neurochem."},{"key":"B66","doi-asserted-by":"publisher","first-page":"37276","DOI":"10.1074\/jbc.M706379200","article-title":"BAG-1 associates with Hsc70.Tau complex and regulates the proteasomal degradation of Tau protein","volume":"282","author":"Elliott","year":"2007","journal-title":"J. Biol. Chem."},{"key":"B67","doi-asserted-by":"publisher","first-page":"395","DOI":"10.1016\/j.tibs.2006.05.001","article-title":"Molecular chaperones: assisting assembly in addition to folding","volume":"31","author":"Ellis","year":"2006","journal-title":"Trends Biochem. Sci."},{"key":"B68","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1007\/978-0-387-39975-1_1","article-title":"Protein misassembly: macromolecular crowding and molecular chaperones","volume":"594","author":"Ellis","year":"2007","journal-title":"Adv. Exp. Med. Biol."},{"key":"B69","doi-asserted-by":"publisher","first-page":"485","DOI":"10.1515\/BC.2006.064","article-title":"Protein aggregation in crowded environments","volume":"387","author":"Ellis","year":"2006","journal-title":"Biol. Chem."},{"key":"B70","doi-asserted-by":"publisher","first-page":"664","DOI":"10.1016\/j.bbamcr.2008.07.014","article-title":"Autophagy: a lysosomal degradation pathway with a central role in health and disease","volume":"1793","author":"Eskelinen","year":"2009","journal-title":"Biochim. Biophys. Acta"},{"key":"B71","doi-asserted-by":"publisher","first-page":"33182","DOI":"10.1074\/jbc.M606192200","article-title":"Heat shock proteins 70 and 90 inhibit early stages of amyloid \u03b2-(1-42) aggregation in vitro","volume":"281","author":"Evans","year":"2006","journal-title":"J. Biol. Chem."},{"key":"B72","doi-asserted-by":"publisher","first-page":"1344","DOI":"10.1038\/ncb2343","article-title":"Hul5 HECT ubiquitin ligase plays a major role in the ubiquitylation and turnover of cytosolic misfolded proteins","volume":"13","author":"Fang","year":"2011","journal-title":"Nat. Cell Biol."},{"key":"B73","doi-asserted-by":"publisher","first-page":"2855","DOI":"10.1016\/j.neurobiolaging.2012.02.009","article-title":"Mutant FUS induces endoplasmic reticulum stress in amyotrophic lateral sclerosis and interacts with protein disulfide-isomerase","volume":"33","author":"Farg","year":"2012","journal-title":"Neurobiol. Aging"},{"key":"B74","doi-asserted-by":"publisher","first-page":"34592","DOI":"10.1074\/jbc.M604019200","article-title":"Triad3A regulates ubiquitination and proteasomal degradation of RIP1 following disruption of Hsp90 binding","volume":"281","author":"Fearns","year":"2006","journal-title":"J. Biol. Chem."},{"key":"B75","doi-asserted-by":"publisher","first-page":"591","DOI":"10.1007\/s12192-013-0413-3","article-title":"Proteomic data from human cell cultures refine mechanisms of chaperone-mediated protein homeostasis","volume":"18","author":"Finka","year":"2013","journal-title":"Cell Stress Chaperones"},{"issue":"Pt 1","key":"B76","doi-asserted-by":"publisher","first-page":"75","DOI":"10.1042\/BJ20030282","article-title":"Changes in the proteolytic activities of proteasomes and lysosomes in human fibroblasts produced by serum withdrawal, amino-acid deprivation and confluent conditions","volume":"375","author":"Fuertes","year":"2003","journal-title":"Biochem."},{"key":"B77","doi-asserted-by":"publisher","first-page":"26188","DOI":"10.1074\/jbc.M710521200","article-title":"Heat shock transcription factor 1-activating compounds suppress polyglutamine-induced neurodegeneration through induction of multiple molecular chaperones","volume":"283","author":"Fujikake","year":"2008","journal-title":"J. Biol. Chem."},{"key":"B78","doi-asserted-by":"publisher","first-page":"781","DOI":"10.1016\/j.molcel.2015.07.012","article-title":"Human Hsp70 Disaggregase Reverses Parkinson's-Linked \u03b1-Synuclein Amyloid Fibrils","volume":"59","author":"Gao","year":"2015","journal-title":"Mol. Cell"},{"key":"B79","doi-asserted-by":"publisher","first-page":"803","DOI":"10.1016\/j.cell.2005.01.016","article-title":"Degradation-mediated protein quality control in the nucleus","volume":"120","author":"Gardner","year":"2005","journal-title":"Cell"},{"key":"B80","doi-asserted-by":"publisher","first-page":"12208","DOI":"10.1074\/jbc.M111874200","article-title":"Binding of ATP to heat shock protein 90: evidence for an ATP-binding site in the C-terminal domain","volume":"277","author":"Garnier","year":"2002","journal-title":"J. Biol. Chem."},{"key":"B81","doi-asserted-by":"publisher","first-page":"2592","DOI":"10.4161\/cc.5.22.3448","article-title":"Heat shock proteins 27 and 70: anti-apoptotic proteins with tumorigenic properties","volume":"5","author":"Garrido","year":"2006","journal-title":"Cell Cycle"},{"key":"B82","doi-asserted-by":"publisher","first-page":"433","DOI":"10.1006\/bbrc.2001.5427","article-title":"Heat shock proteins: endogenous modulators of apoptotic cell death","volume":"286","author":"Garrido","year":"2001","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"B83","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1016\/S0092-8674(00)81223-4","article-title":"Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins","volume":"94","author":"Glover","year":"1998","journal-title":"Cell"},{"key":"B84","doi-asserted-by":"publisher","first-page":"492","DOI":"10.1038\/35081564","article-title":"\u03b1-synuclein and neurodegenerative diseases","volume":"2","author":"Goedert","year":"2001","journal-title":"Nat. Rev. Neurosci."},{"key":"B85","doi-asserted-by":"publisher","first-page":"5961","DOI":"10.1073\/pnas.0911991107","article-title":"Restoration of visual function in P23H rhodopsin transgenic rats by gene delivery of BiP\/Grp78","volume":"107","author":"Gorbatyuk","year":"2010","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"B86","doi-asserted-by":"publisher","first-page":"1327","DOI":"10.1038\/mt.2012.28","article-title":"Glucose regulated protein 78 diminishes \u03b1-synuclein neurotoxicity in a rat model of Parkinson disease","volume":"20","author":"Gorbatyuk","year":"2012","journal-title":"Mol. Ther."},{"key":"B87","doi-asserted-by":"crossref","first-page":"19702","DOI":"10.1074\/jbc.270.34.19702","article-title":"Amyloid \u03b2-protein inhibits ubiquitin-dependent protein degradation in vitro","volume":"270","author":"Gregori","year":"1995","journal-title":"J. Biol. Chem."},{"key":"B88","doi-asserted-by":"crossref","first-page":"28521","DOI":"10.1074\/jbc.271.45.28521","article-title":"A mouse amidase specific for N-terminal asparagine. The gene, the enzyme, and their function in the N-end rule pathway","volume":"271","author":"Grigoryev","year":"1996","journal-title":"J. Biol. Chem."},{"key":"B89","doi-asserted-by":"publisher","first-page":"25","DOI":"10.1016\/S0896-6273(03)00594-4","article-title":"Disruption of axonal transport by loss of huntingtin or expression of pathogenic polyQ proteins in Drosophila","volume":"40","author":"Gunawardena","year":"2003","journal-title":"Neuron"},{"key":"B90","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1016\/S0959-4388(98)80071-8","article-title":"Huntingtin: a single bait hooks many species","volume":"8","author":"Gusella","year":"1998","journal-title":"Curr. Opin. Neurobiol."},{"key":"B91","doi-asserted-by":"publisher","first-page":"26107","DOI":"10.1074\/jbc.M111.233163","article-title":"NF-\u03b3B essential modulator (NEMO) interaction with linear and lys-63 ubiquitin chains contributes to NF-\u03baB activation","volume":"286","author":"Hadian","year":"2011","journal-title":"J. Biol. Chem."},{"key":"B92","doi-asserted-by":"publisher","first-page":"355","DOI":"10.1016\/j.molcel.2010.01.001","article-title":"A DNAJB chaperone subfamily with HDAC-dependent activities suppresses toxic protein aggregation","volume":"37","author":"Hageman","year":"2010","journal-title":"Mol. Cell"},{"key":"B93","doi-asserted-by":"publisher","first-page":"819","DOI":"10.1016\/j.molcel.2013.08.016","article-title":"Proteasomes activate aggresome disassembly and clearance by producing unanchored ubiquitin chains","volume":"51","author":"Hao","year":"2013","journal-title":"Mol. Cell"},{"key":"B94","doi-asserted-by":"publisher","first-page":"324","DOI":"10.1038\/nature10317","article-title":"Molecular chaperones in protein folding and proteostasis","volume":"475","author":"Hartl","year":"2011","journal-title":"Nature"},{"key":"B95","doi-asserted-by":"publisher","first-page":"49071","DOI":"10.1074\/jbc.M208046200","article-title":"Phosphorylated \u03b1-synuclein is ubiquitinated in \u03b1-synucleinopathy lesions","volume":"277","author":"Hasegawa","year":"2002","journal-title":"J. Biol. Chem."},{"key":"B96","doi-asserted-by":"publisher","DOI":"10.1101\/cshperspect.a024273","article-title":"\u03b1-Synuclein: experimental pathology","volume":"6","author":"Hasegawa","year":"2016","journal-title":"Cold Spring Harb. Perspect. Med"},{"key":"B97","doi-asserted-by":"publisher","first-page":"1106","DOI":"10.1073\/pnas.0910591107","article-title":"Cytoplasmic protein quality control degradation mediated by parallel actions of the E3 ubiquitin ligases Ubr1 and San1","volume":"107","author":"Heck","year":"2010","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"B98","doi-asserted-by":"publisher","first-page":"314","DOI":"10.1101\/lm.1504010","article-title":"The ubiquitin-proteasome pathway and synaptic plasticity","volume":"17","author":"Hegde","year":"2010","journal-title":"Learn. Mem."},{"key":"B99","doi-asserted-by":"publisher","first-page":"128","DOI":"10.1016\/j.bbagrm.2010.07.006","article-title":"Role of ubiquitin-proteasome-mediated proteolysis in nervous system disease","volume":"1809","author":"Hegde","year":"2011","journal-title":"Biochim. Biophys. Acta"},{"key":"B100","doi-asserted-by":"publisher","first-page":"425","DOI":"10.1146\/annurev.biochem.67.1.425","article-title":"The ubiquitin system","volume":"67","author":"Hershko","year":"1998","journal-title":"Annu. Rev. Biochem."},{"key":"B101","doi-asserted-by":"publisher","first-page":"233","DOI":"10.1038\/nrn3689","article-title":"Disturbance of endoplasmic reticulum proteostasis in neurodegenerative diseases","volume":"15","author":"Hetz","year":"2014","journal-title":"Nat. Rev. Neurosci."},{"key":"B102","doi-asserted-by":"publisher","first-page":"161","DOI":"10.1016\/j.jsb.2012.05.015","article-title":"Mapping the road to recovery: the ClpB\/Hsp104 molecular chaperone","volume":"179","author":"Hodson","year":"2012","journal-title":"J. Struct. Biol."},{"key":"B103","doi-asserted-by":"publisher","first-page":"160","DOI":"10.1038\/sj.emboj.7600016","article-title":"Identification of a redox-regulated chaperone network","volume":"23","author":"Hoffmann","year":"2004","journal-title":"EMBO J."},{"key":"B104","doi-asserted-by":"publisher","first-page":"712","DOI":"10.1017\/S0317167100015547","article-title":"Alzheimer's disease, cerebrovascular disease, and the \u03b2-amyloid cascade","volume":"39","author":"Honjo","year":"2012","journal-title":"Can. J. Neurol. Sci."},{"key":"B105","doi-asserted-by":"publisher","first-page":"444","DOI":"10.3109\/17482968.2011.594055","article-title":"Protein disulfide isomerase-immunopositive inclusions in patients with amyotrophic lateral sclerosis","volume":"12","author":"Honjo","year":"2011","journal-title":"Amyotroph. Lateral Scler."},{"key":"B106","doi-asserted-by":"publisher","first-page":"62","DOI":"10.1016\/j.tcm.2012.06.013","article-title":"Heat shock protein-inducing compounds as therapeutics to restore proteostasis in atrial fibrillation","volume":"22","author":"Hoogstra-Berends","year":"2012","journal-title":"Trends Cardiovasc. Med."},{"key":"B107","doi-asserted-by":"publisher","first-page":"394","DOI":"10.1046\/j.1471-4159.2003.01844.x","article-title":"Alzheimer's associated variant ubiquitin causes inhibition of the 26S proteasome and chaperone expression","volume":"86","author":"Hope","year":"2003","journal-title":"J. Neurochem."},{"key":"B108","doi-asserted-by":"crossref","first-page":"490","DOI":"10.1093\/gerona\/62.5.490","article-title":"Age-associated decrease in proteasome content and activities in human dermal fibroblasts: restoration of normal level of proteasome subunits reduces aging markers in fibroblasts from elderly persons","volume":"62","author":"Hwang","year":"2007","journal-title":"J. Gerontol. A Biol. Sci. Med. Sci."},{"key":"B109","doi-asserted-by":"crossref","first-page":"334","DOI":"10.1097\/00005072-199804000-00005","article-title":"Nigral and cortical Lewy bodies and dystrophic nigral neurites in Parkinson's disease and cortical Lewy body disease contain \u03b1-synuclein immunoreactivity","volume":"57","author":"Irizarry","year":"1998","journal-title":"J. Neuropathol. Exp. Neurol."},{"key":"B110","doi-asserted-by":"publisher","first-page":"5931","DOI":"10.1046\/j.1432-1033.2002.03317.x","article-title":"Mammalian HSP60 is quickly sorted into the mitochondria under conditions of dehydration","volume":"269","author":"Itoh","year":"2002","journal-title":"Eur. J. Biochem."},{"key":"B111","doi-asserted-by":"publisher","first-page":"170","DOI":"10.1016\/j.cell.2013.11.047","article-title":"Potentiated Hsp104 variants antagonize diverse proteotoxic misfolding events","volume":"156","author":"Jackrel","year":"2014","journal-title":"Cell"},{"key":"B112","doi-asserted-by":"publisher","first-page":"1175","DOI":"10.1242\/dmm.016113","article-title":"Potentiated Hsp104 variants suppress toxicity of diverse neurodegenerative disease-linked proteins","volume":"7","author":"Jackrel","year":"2014","journal-title":"Dis. Model. Mech."},{"key":"B113","doi-asserted-by":"publisher","first-page":"2009","DOI":"10.1093\/hmg\/9.13.2009","article-title":"Polyglutamine length-dependent interaction of Hsp40 and Hsp70 family chaperones with truncated N-terminal huntingtin: their role in suppression of aggregation and cellular toxicity","volume":"9","author":"Jana","year":"2000","journal-title":"Hum. Mol. Genet."},{"key":"B114","doi-asserted-by":"publisher","first-page":"796","DOI":"10.1007\/s12035-013-8562-z","article-title":"Potential effect of S-nitrosylated protein disulfide isomerase on mutant SOD1 aggregation and neuronal cell death in amyotrophic lateral sclerosis","volume":"49","author":"Jeon","year":"2014","journal-title":"Mol. Neurobiol."},{"key":"B115","doi-asserted-by":"publisher","first-page":"182","DOI":"10.1016\/j.neulet.2012.03.074","article-title":"GRP78 counteracts cell death and protein aggregation caused by mutant huntingtin proteins","volume":"516","author":"Jiang","year":"2012","journal-title":"Neurosci. Lett."},{"key":"B116","doi-asserted-by":"publisher","first-page":"40","DOI":"10.1016\/j.pharmthera.2013.08.003","article-title":"The role of heat shock proteins in Amyotrophic Lateral Sclerosis: the therapeutic potential of Arimoclomol","volume":"141","author":"Kalmar","year":"2014","journal-title":"Pharmacol. Ther."},{"key":"B117","doi-asserted-by":"publisher","first-page":"579","DOI":"10.1038\/nrm2941","article-title":"The HSP70 chaperone machinery: j proteins as drivers of functional specificity","volume":"11","author":"Kampinga","year":"2010","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"B118","doi-asserted-by":"publisher","first-page":"113","DOI":"10.1016\/B978-0-12-397863-9.00004-3","article-title":"Interactions of the proteasomal system with chaperones: protein triage and protein quality control","volume":"109","author":"Kastle","year":"2012","journal-title":"Prog. Mol. Biol. Transl. Sci."},{"key":"B119","doi-asserted-by":"publisher","first-page":"407","DOI":"10.1016\/j.tcb.2012.05.006","article-title":"Chaperone-mediated autophagy: a unique way to enter the lysosome world","volume":"22","author":"Kaushik","year":"2012","journal-title":"Trends Cell Biol."},{"key":"B120","doi-asserted-by":"publisher","first-page":"1837","DOI":"10.1126\/science.287.5459.1837","article-title":"Genetic suppression of polyglutamine toxicity in Drosophila","volume":"287","author":"Kazemi-Esfarjani","year":"2000","journal-title":"Science"},{"key":"B121","doi-asserted-by":"publisher","first-page":"149","DOI":"10.1016\/S0306-4522(00)00067-1","article-title":"Decreased levels of proteasome activity and proteasome expression in aging spinal cord","volume":"98","author":"Keller","year":"2000","journal-title":"Neuroscience"},{"key":"B122","doi-asserted-by":"publisher","first-page":"481","DOI":"10.1515\/BC.2010.058","article-title":"Chaperone-assisted degradation: multiple paths to destruction","volume":"391","author":"Kettern","year":"2010","journal-title":"Biol. Chem."},{"key":"B123","doi-asserted-by":"publisher","first-page":"e50547","DOI":"10.1371\/journal.pone.0050547","article-title":"Withaferin A induces proteasome inhibition, endoplasmic reticulum stress, the heat shock response and acquisition of thermotolerance","volume":"7","author":"Khan","year":"2012","journal-title":"PLoS ONE"},{"key":"B124","doi-asserted-by":"publisher","first-page":"402","DOI":"10.1038\/nm1021","article-title":"Treatment with arimoclomol, a coinducer of heat shock proteins, delays disease progression in ALS mice","volume":"10","author":"Kieran","year":"2004","journal-title":"Nat. Med."},{"key":"B125","doi-asserted-by":"publisher","first-page":"323","DOI":"10.1146\/annurev-biochem-060208-092442","article-title":"Molecular chaperone functions in protein folding and proteostasis","volume":"82","author":"Kim","year":"2013","journal-title":"Annu. Rev. Biochem."},{"key":"B126","doi-asserted-by":"publisher","first-page":"1163","DOI":"10.1038\/ncb1478","article-title":"Cytosolic chaperonin prevents polyglutamine toxicity with altering the aggregation state","volume":"8","author":"Kitamura","year":"2006","journal-title":"Nat. Cell Biol."},{"key":"B127","doi-asserted-by":"publisher","first-page":"76","DOI":"10.1016\/j.coi.2003.11.004","article-title":"Proteasome and peptidase function in MHC-class-I-mediated antigen presentation","volume":"16","author":"Kloetzel","year":"2004","journal-title":"Curr. Opin. Immunol."},{"key":"B128","doi-asserted-by":"publisher","first-page":"25497","DOI":"10.1074\/jbc.M400255200","article-title":"Hsp70 Reduces \u03b1-Synuclein Aggregation and Toxicity","volume":"279","author":"Klucken","year":"2004","journal-title":"J. Biol. Chem."},{"key":"B129","doi-asserted-by":"publisher","first-page":"175","DOI":"10.1016\/j.molcel.2007.04.001","article-title":"Disease-associated prion protein oligomers inhibit the 26S proteasome","volume":"26","author":"Kristiansen","year":"2007","journal-title":"Mol. Cell"},{"key":"B130","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1016\/S0014-5793(97)01180-0","article-title":"Small heat shock proteins inhibit in vitro A \u03b2(1-42) amyloidogenesis","volume":"416","author":"Kudva","year":"1997","journal-title":"FEBS Lett."},{"key":"B131","doi-asserted-by":"crossref","first-page":"345","DOI":"10.1007\/BF00687787","article-title":"Lewy bodies are ubiquitinated. A light and electron microscopic immunocytochemical study","volume":"75","author":"Kuzuhara","year":"1988","journal-title":"Acta Neuropathol."},{"key":"B132","doi-asserted-by":"publisher","first-page":"4135","DOI":"10.1128\/MCB.20.11.4135-4148.2000","article-title":"Altered activity, social behavior, and spatial memory in mice lacking the NTAN1p amidase and the asparagine branch of the N-end rule pathway","volume":"20","author":"Kwon","year":"2000","journal-title":"Mol. Cell. Biol."},{"key":"B133","doi-asserted-by":"publisher","first-page":"96","DOI":"10.1126\/science.1069531","article-title":"An essential role of N-terminal arginylation in cardiovascular development","volume":"297","author":"Kwon","year":"2002","journal-title":"Science"},{"key":"B134","doi-asserted-by":"crossref","first-page":"182","DOI":"10.1128\/MCB.19.1.182","article-title":"Alternative splicing results in differential expression, activity, and localization of the two forms of arginyl-tRNA-protein transferase, a component of the N-end rule pathway","volume":"19","author":"Kwon","year":"1999a","journal-title":"Mol. Cell. Biol."},{"key":"B135","doi-asserted-by":"crossref","first-page":"18135","DOI":"10.1074\/jbc.274.25.18135","article-title":"Bivalent inhibitor of the N-end rule pathway","volume":"274","author":"Kwon","year":"1999b","journal-title":"J. Biol. Chem."},{"issue":"Pt 4","key":"B136","doi-asserted-by":"publisher","first-page":"1180","DOI":"10.1093\/brain\/aws022","article-title":"Suppression of protein aggregation by chaperone modification of high molecular weight complexes","volume":"135","author":"Labbadia","year":"2012","journal-title":"Brain"},{"key":"B137","doi-asserted-by":"publisher","first-page":"1986","DOI":"10.4161\/cc.8.13.8892","article-title":"NBR1 and p62 as cargo receptors for selective autophagy of ubiquitinated targets","volume":"8","author":"Lamark","year":"2009","journal-title":"Cell Cycle"},{"key":"B138","doi-asserted-by":"publisher","first-page":"1543","DOI":"10.1100\/tsw.2010.152","article-title":"Heat shock proteins: cell protection through protein triage","volume":"10","author":"Lanneau","year":"2010","journal-title":"ScientificWorldJournal"},{"key":"B139","doi-asserted-by":"publisher","first-page":"179","DOI":"10.1038\/nature09299","article-title":"Enhancement of proteasome activity by a small-molecule inhibitor of USP14","volume":"467","author":"Lee","year":"2010","journal-title":"Nature"},{"key":"B140","doi-asserted-by":"publisher","first-page":"8513","DOI":"10.1073\/pnas.1217988110","article-title":"Heat shock protein (Hsp) 70 is an activator of the Hsp104 motor","volume":"110","author":"Lee","year":"2013","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"B141","doi-asserted-by":"publisher","first-page":"100","DOI":"10.1073\/pnas.0708465105","article-title":"Synthetic heterovalent inhibitors targeting recognition E3 components of the N-end rule pathway","volume":"105","author":"Lee","year":"2008","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"B142","doi-asserted-by":"publisher","first-page":"15030","DOI":"10.1073\/pnas.0507533102","article-title":"RGS4 and RGS5 are in vivo substrates of the N-end rule pathway","volume":"102","author":"Lee","year":"2005","journal-title":"Proc. Natl. Acad. Sci. USA."},{"key":"B143","doi-asserted-by":"publisher","first-page":"339","DOI":"10.1016\/j.neures.2011.05.008","article-title":"Protein aggregate spreading in neurodegenerative diseases: problems and perspectives","volume":"70","author":"Lee","year":"2011","journal-title":"Neurosci. Res."},{"key":"B144","doi-asserted-by":"publisher","first-page":"12924","DOI":"10.1074\/jbc.M306390200","article-title":"Proteasomal inhibition by \u03b1-synuclein filaments and oligomers","volume":"279","author":"Lindersson","year":"2004","journal-title":"J. Biol. Chem."},{"key":"B145","doi-asserted-by":"publisher","first-page":"103","DOI":"10.1101\/sqb.2009.74.043","article-title":"Protein folding sculpting evolutionary change","volume":"74","author":"Lindquist","year":"2009","journal-title":"Cold Spring Harb. Symp. Quant. Biol."},{"key":"B146","doi-asserted-by":"crossref","first-page":"5301","DOI":"10.1073\/pnas.93.11.5301","article-title":"Heat-shock protein 104 expression is sufficient for thermotolerance in yeast","volume":"93","author":"Lindquist","year":"1996","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"B147","doi-asserted-by":"publisher","first-page":"2857","DOI":"10.1074\/jbc.M112.387589","article-title":"Disruption of ionic interactions between the nucleotide binding domain 1 (NBD1) and middle (M) domain in Hsp100 disaggregase unleashes toxic hyperactivity and partial independence from Hsp70","volume":"288","author":"Lipinska","year":"2013","journal-title":"J. Biol. Chem."},{"key":"B148","doi-asserted-by":"publisher","first-page":"875","DOI":"10.1111\/j.1471-4159.2005.03054.x","article-title":"Elevation of the Hsp70 chaperone does not effect toxicity in mouse models of familial amyotrophic lateral sclerosis","volume":"93","author":"Liu","year":"2005","journal-title":"J. Neurochem."},{"key":"B149","doi-asserted-by":"publisher","first-page":"3087","DOI":"10.1172\/JCI35781","article-title":"Hsp104 antagonizes \u03b1-synuclein aggregation and reduces dopaminergic degeneration in a rat model of Parkinson disease","volume":"118","author":"Lo Bianco","year":"2008","journal-title":"J. Clin. Invest."},{"key":"B150","doi-asserted-by":"publisher","first-page":"2919","DOI":"10.1016\/j.jmb.2015.04.013","article-title":"The mechanism and function of Group II Chaperonins","volume":"427","author":"Lopez","year":"2015","journal-title":"J. Mol. Biol."},{"key":"B151","doi-asserted-by":"publisher","first-page":"39","DOI":"10.1016\/j.ygcen.2011.02.005","article-title":"The role of ubiquitin-proteasome system in ageing","volume":"172","author":"Low","year":"2011","journal-title":"Gen. Comp. Endocrinol."},{"key":"B152","doi-asserted-by":"publisher","first-page":"12614","DOI":"10.1021\/bi801475r","article-title":"Interactions between Hsp70 and the hydrophobic core of \u03b1-synuclein inhibit fibril assembly","volume":"47","author":"Luk","year":"2008","journal-title":"Biochemistry"},{"key":"B153","doi-asserted-by":"publisher","first-page":"9511","DOI":"10.1073\/pnas.0701055104","article-title":"Roles of heat-shock protein 90 in maintaining and facilitating the neurodegenerative phenotype in tauopathies","volume":"104","author":"Luo","year":"2007","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"B154","doi-asserted-by":"publisher","first-page":"31066","DOI":"10.1074\/jbc.M114.595124","article-title":"Interaction of the molecular chaperone DNAJB6 with growing amyloid-\u03b2 42 (A\u03b242) aggregates leads to sub-stoichiometric inhibition of amyloid formation","volume":"289","author":"Mansson","year":"2014","journal-title":"J. Biol. Chem."},{"key":"B155","doi-asserted-by":"publisher","first-page":"5805","DOI":"10.1073\/pnas.0507436103","article-title":"Consequences of the selective blockage of chaperone-mediated autophagy","volume":"103","author":"Massey","year":"2006","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"B156","doi-asserted-by":"publisher","first-page":"477","DOI":"10.1016\/j.molcel.2010.07.001","article-title":"K11-linked polyubiquitination in cell cycle control revealed by a K11 linkage-specific antibody","volume":"39","author":"Matsumoto","year":"2010","journal-title":"Mol. Cell"},{"key":"B157","doi-asserted-by":"crossref","first-page":"303","DOI":"10.1379\/1466-1268(2003)008<0303:CALBTC>2.0.CO;2","article-title":"CHIP: a link between the chaperone and proteasome systems","volume":"8","author":"McDonough","year":"2003","journal-title":"Cell Stress Chaperones"},{"key":"B158","doi-asserted-by":"publisher","first-page":"846","DOI":"10.1046\/j.1471-4159.2002.01190.x","article-title":"TorsinA and heat shock proteins act as molecular chaperones: suppression of \u03b1-synuclein aggregation","volume":"83","author":"McLean","year":"2002","journal-title":"J. Neurochem."},{"key":"B159","doi-asserted-by":"publisher","first-page":"665","DOI":"10.1016\/j.bbrc.2004.07.021","article-title":"Geldanamycin induces Hsp70 and prevents \u03b1-synuclein aggregation and toxicity in vitro","volume":"321","author":"McLean","year":"2004","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"B160","doi-asserted-by":"publisher","first-page":"701","DOI":"10.1093\/nar\/gkr744","article-title":"Ubiquitin ligase UBR3 regulates cellular levels of the essential DNA repair protein APE1 and is required for genome stability","volume":"40","author":"Meisenberg","year":"2012","journal-title":"Nucleic Acids Res."},{"key":"B161","doi-asserted-by":"crossref","first-page":"9267","DOI":"10.1523\/JNEUROSCI.22-21-09267.2002","article-title":"Purification of polyglutamine aggregates and identification of elongation factor-1\u03b1 and heat shock protein 84 as aggregate-interacting proteins","volume":"22","author":"Mitsui","year":"2002","journal-title":"J. Neurosci."},{"key":"B162","doi-asserted-by":"publisher","first-page":"6934","DOI":"10.1093\/emboj\/18.24.6934","article-title":"Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB","volume":"18","author":"Mogk","year":"1999","journal-title":"EMBO J."},{"key":"B163","doi-asserted-by":"publisher","first-page":"41","DOI":"10.1007\/s12035-012-8246-0","article-title":"Protein homeostasis, aging and Alzheimer's disease","volume":"46","author":"Morawe","year":"2012","journal-title":"Mol. Neurobiol."},{"key":"B164","doi-asserted-by":"publisher","first-page":"482","DOI":"10.1016\/j.semcdb.2011.04.002","article-title":"Misfolded protein aggregates: mechanisms, structures and potential for disease transmission","volume":"22","author":"Moreno-Gonzalez","year":"2011","journal-title":"Semin. Cell Dev. Biol."},{"key":"B165","doi-asserted-by":"publisher","first-page":"8107","DOI":"10.1021\/bi0493766","article-title":"Saccharomyces cerevisiae Hsp104 enhances the chaperone capacity of human cells and inhibits heat stress-induced proapoptotic signaling","volume":"43","author":"Mosser","year":"2004","journal-title":"Biochemistry"},{"key":"B166","doi-asserted-by":"publisher","first-page":"247","DOI":"10.1038\/nature14884","article-title":"Crucial HSP70 co\u2013chaperone complex unlocks metazoan protein disaggregation","volume":"524","author":"Nillegoda","year":"2015","journal-title":"Nature"},{"key":"B167","doi-asserted-by":"publisher","first-page":"e1000291","DOI":"10.1371\/journal.pbio.1000291","article-title":"Modulation of heat shock transcription factor 1 as a therapeutic target for small molecule intervention in neurodegenerative disease","volume":"8","author":"Neef","year":"2010","journal-title":"PLoS Biol."},{"key":"B168","doi-asserted-by":"publisher","first-page":"646","DOI":"10.3390\/biom4030646","article-title":"Protein quality control in the nucleus","volume":"4","author":"Nielsen","year":"2014","journal-title":"Biomolecules"},{"key":"B169","doi-asserted-by":"publisher","first-page":"4133","DOI":"10.1038\/sj.onc.1209461","article-title":"17-AAG, an Hsp90 inhibitor, causes kinetochore defects: a novel mechanism by which 17-AAG inhibits cell proliferation","volume":"25","author":"Niikura","year":"2006","journal-title":"Oncogene"},{"key":"B170","doi-asserted-by":"publisher","first-page":"2102","DOI":"10.1091\/mbc.E10-02-0098","article-title":"Ubr1 and Ubr2 function in a quality control pathway for degradation of unfolded cytosolic proteins","volume":"21","author":"Nillegoda","year":"2010","journal-title":"Mol. Biol. Cell"},{"key":"B171","doi-asserted-by":"publisher","first-page":"6403","DOI":"10.1073\/pnas.0307697101","article-title":"Genome-wide RNA interference screen identifies previously undescribed regulators of polyglutamine aggregation","volume":"101","author":"Nollen","year":"2004","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"B172","doi-asserted-by":"publisher","first-page":"e73944","DOI":"10.1371\/journal.pone.0073944","article-title":"Molecular chaperone mediated late-stage neuroprotection in the SOD1(G93A) mouse model of amyotrophic lateral sclerosis","volume":"8","author":"Novoselov","year":"2013","journal-title":"PLoS ONE"},{"key":"B173","doi-asserted-by":"publisher","first-page":"6896","DOI":"10.1074\/jbc.M206867200","article-title":"Tetratricopeptide repeat motif-mediated Hsc70-mSTI1 interaction. Molecular characterization of the critical contacts for successful binding and specificity","volume":"278","author":"Odunuga","year":"2003","journal-title":"J. Biol. Chem."},{"key":"B174","doi-asserted-by":"publisher","first-page":"1590","DOI":"10.1073\/pnas.0710531105","article-title":"Genomic evidence for independent origins of \u03b2-like globin genes in monotremes and therian mammals","volume":"105","author":"Opazo","year":"2008","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"B175","doi-asserted-by":"publisher","first-page":"e1867","DOI":"10.1371\/journal.pone.0001867","article-title":"Formation of toxic oligomeric \u03b1-synuclein species in living cells","volume":"3","author":"Outeiro","year":"2008","journal-title":"PLoS ONE"},{"key":"B176","doi-asserted-by":"publisher","first-page":"17","DOI":"10.1186\/1742-2094-7-17","article-title":"Reduction of \u03b2-amyloid pathology by celastrol in a transgenic mouse model of Alzheimer's disease","volume":"7","author":"Paris","year":"2010","journal-title":"J. Neuroinflammation"},{"key":"B177","doi-asserted-by":"publisher","first-page":"475","DOI":"10.1038\/372475a0","article-title":"Protein disaggregation mediated by heat-shock protein Hsp104","volume":"372","author":"Parsell","year":"1994","journal-title":"Nature"},{"key":"B178","doi-asserted-by":"publisher","first-page":"256","DOI":"10.1016\/j.molbrainres.2004.10.028","article-title":"Hsp27 and Hsp70 administered in combination have a potent protective effect against FALS-associated SOD1-mutant-induced cell death in mammalian neuronal cells","volume":"134","author":"Patel","year":"2005","journal-title":"Brain Res. Mol. Brain Res."},{"key":"B179","doi-asserted-by":"publisher","first-page":"917","DOI":"10.1111\/j.1365-2958.2007.05718.x","article-title":"Chaperoning Anfinsen: the steric foldases","volume":"64","author":"Pauwels","year":"2007","journal-title":"Mol. Microbiol."},{"key":"B180","doi-asserted-by":"publisher","first-page":"271","DOI":"10.1146\/annurev.biochem.75.103004.142738","article-title":"Structure and mechanism of the Hsp90 molecular chaperone machinery","volume":"75","author":"Pearl","year":"2006","journal-title":"Annu. Rev. Biochem."},{"key":"B181","doi-asserted-by":"publisher","first-page":"921","DOI":"10.1038\/nbt849","article-title":"A proteomics approach to understanding protein ubiquitination","volume":"21","author":"Peng","year":"2003","journal-title":"Nat. Biotechnol."},{"key":"B182","doi-asserted-by":"publisher","first-page":"903","DOI":"10.1038\/mt.sj.6300141","article-title":"Neuroprotection by Hsp104 and Hsp27 in lentiviral-based rat models of Huntington's disease","volume":"15","author":"Perrin","year":"2007","journal-title":"Mol. Ther."},{"key":"B183","doi-asserted-by":"publisher","first-page":"1640","DOI":"10.1007\/PL00012491","article-title":"Heat-shock protein 90, a chaperone for folding and regulation","volume":"59","author":"Picard","year":"2002","journal-title":"Cell. Mol. Life Sci."},{"key":"B184","doi-asserted-by":"publisher","first-page":"503","DOI":"10.1146\/annurev.biochem.70.1.503","article-title":"Mechanisms underlying ubiquitination","volume":"70","author":"Pickart","year":"2001","journal-title":"Annu. Rev. Biochem."},{"key":"B185","doi-asserted-by":"publisher","first-page":"1068","DOI":"10.1016\/j.cell.2008.05.022","article-title":"Structural basis for the cooperation of Hsp70 and Hsp110 chaperones in protein folding","volume":"133","author":"Polier","year":"2008","journal-title":"Cell"},{"key":"B186","doi-asserted-by":"publisher","first-page":"2117","DOI":"10.1091\/mbc.E10-02-0111","article-title":"A nucleus-based quality control mechanism for cytosolic proteins","volume":"21","author":"Prasad","year":"2010","journal-title":"Mol. Biol. Cell"},{"key":"B187","doi-asserted-by":"publisher","first-page":"849","DOI":"10.1124\/jpet.109.158436","article-title":"Brain-permeable small-molecule inhibitors of Hsp90 prevent \u03b1-synuclein oligomer formation and rescue \u03b1-synuclein-induced toxicity","volume":"332","author":"Putcha","year":"2010","journal-title":"J. Pharmacol. Exp. Ther."},{"key":"B188","doi-asserted-by":"publisher","first-page":"551","DOI":"10.1038\/nature04600","article-title":"CHIP-mediated stress recovery by sequential ubiquitination of substrates and Hsp70","volume":"440","author":"Qian","year":"2006","journal-title":"Nature"},{"key":"B189","doi-asserted-by":"crossref","first-page":"17078","DOI":"10.1074\/jbc.270.29.17078","article-title":"Independence of the chaperone activity of protein disulfide isomerase from its thioredoxin-like active site","volume":"270","author":"Quan","year":"1995","journal-title":"J. Biol. Chem."},{"key":"B190","doi-asserted-by":"publisher","first-page":"483","DOI":"10.1016\/j.neuroscience.2008.01.058","article-title":"Expression of the small heat shock protein family in the mouse CNS: differential anatomical and biochemical compartmentalization","volume":"153","author":"Quraishe","year":"2008","journal-title":"Neuroscience"},{"key":"B191","doi-asserted-by":"publisher","first-page":"301","DOI":"10.3727\/000000007783464687","article-title":"Huntington's disease: pathological mechanisms and therapeutic strategies","volume":"16","author":"Ramaswamy","year":"2007","journal-title":"Cell Transplant."},{"key":"B192","doi-asserted-by":"publisher","first-page":"4221","DOI":"10.1038\/emboj.2012.264","article-title":"Metazoan Hsp70 machines use Hsp110 to power protein disaggregation","volume":"31","author":"Rampelt","year":"2012","journal-title":"EMBO J."},{"key":"B193","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1017\/S1462399400002015","article-title":"Chaperonins are cell-signalling proteins: the unfolding biology of molecular chaperones","volume":"2","author":"Ranford","year":"2000","journal-title":"Expert Rev. Mol. Med."},{"key":"B194","doi-asserted-by":"publisher","first-page":"16101","DOI":"10.1073\/pnas.1000916107","article-title":"Dynamics of heat shock protein 90 C-terminal dimerization is an important part of its conformational cycle","volume":"107","author":"Ratzke","year":"2010","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"B195","doi-asserted-by":"publisher","first-page":"195","DOI":"10.1007\/978-1-59745-157-4_13","article-title":"Clearance of mutant aggregate-prone proteins by autophagy","volume":"445","author":"Ravikumar","year":"2008","journal-title":"Methods Mol. Biol."},{"key":"B196","doi-asserted-by":"crossref","first-page":"347","DOI":"10.1016\/0197-4580(94)90030-2","article-title":"No global neocortical nerve cell loss in brains from patients with senile dementia of Alzheimer's type","volume":"15","author":"Regeur","year":"1994","journal-title":"Neurobiol. Aging"},{"key":"B197","doi-asserted-by":"publisher","first-page":"1167","DOI":"10.1016\/j.jmb.2004.05.054","article-title":"Interaction of the molecular chaperone \u03b1B-crystallin with \u03b1-synuclein: effects on amyloid fibril formation and chaperone activity","volume":"340","author":"Rekas","year":"2004","journal-title":"J. Mol. Biol."},{"key":"B198","doi-asserted-by":"publisher","first-page":"6290","DOI":"10.1111\/j.1742-4658.2007.06144.x","article-title":"Monitoring the prevention of amyloid fibril formation by \u03b1-crystallin. Temperature dependence and the nature of the aggregating species","volume":"274","author":"Rekas","year":"2007","journal-title":"FEBS J."},{"key":"B199","doi-asserted-by":"publisher","first-page":"248","DOI":"10.1038\/nrn3430","article-title":"The changing scene of amyotrophic lateral sclerosis","volume":"14","author":"Robberecht","year":"2013","journal-title":"Nat. Rev. Neurosci."},{"key":"B200","doi-asserted-by":"publisher","first-page":"227","DOI":"10.1016\/j.molcel.2014.05.025","article-title":"Cytosolic quality control of mislocalized proteins requires RNF126 recruitment to Bag6","volume":"55","author":"Rodrigo-Brenni","year":"2014","journal-title":"Mol. Cell"},{"key":"B201","doi-asserted-by":"publisher","first-page":"40","DOI":"10.1186\/1750-1172-5-40","article-title":"Huntington's disease: a clinical review","volume":"5","author":"Roos","year":"2010","journal-title":"Orphanet J. Rare Dis."},{"key":"B202","doi-asserted-by":"publisher","first-page":"59","DOI":"10.1038\/362059a0","article-title":"Mutations in Cu\/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis","volume":"362","author":"Rosen","year":"1993","journal-title":"Nature"},{"key":"B203","doi-asserted-by":"publisher","first-page":"93","DOI":"10.1016\/j.molcel.2010.12.004","article-title":"Disorder targets misorder in nuclear quality control degradation: a disordered ubiquitin ligase directly recognizes its misfolded substrates","volume":"41","author":"Rosenbaum","year":"2011","journal-title":"Mol. Cell"},{"key":"B204","doi-asserted-by":"publisher","first-page":"S10","DOI":"10.1038\/nm1066","article-title":"Protein aggregation and neurodegenerative disease","volume":"10","author":"Ross","year":"2004","journal-title":"Nat. Med."},{"key":"B205","doi-asserted-by":"publisher","first-page":"1501","DOI":"10.1093\/emboj\/16.7.1501","article-title":"Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries","volume":"16","author":"Rudiger","year":"1997","journal-title":"EMBO J."},{"key":"B206","doi-asserted-by":"publisher","first-page":"1218","DOI":"10.1002\/(SICI)1522-2683(20000401)21:61218::AID-ELPS12183.0.CO;2-H","article-title":"Heat shock proteins in human cancer","volume":"21","author":"Sarto","year":"2000","journal-title":"Electrophoresis"},{"key":"B207","doi-asserted-by":"publisher","first-page":"273","DOI":"10.1007\/s002800050817","article-title":"The benzoquinone ansamycin 17-allylamino-17-demethoxygeldanamycin binds to HSP90 and shares important biologic activities with geldanamycin","volume":"42","author":"Schulte","year":"1998","journal-title":"Cancer Chemother. Pharmacol."},{"key":"B208","doi-asserted-by":"publisher","first-page":"1347","DOI":"10.1038\/nsmb.2442","article-title":"Hsp70 proteins bind Hsp100 regulatory M domains to activate AAA+ disaggregase at aggregate surfaces","volume":"19","author":"Seyffer","year":"2012","journal-title":"Nat. Struct. Mol. Biol."},{"key":"B209","doi-asserted-by":"publisher","first-page":"1681","DOI":"10.1016\/j.bpj.2011.07.056","article-title":"Binding of the molecular chaperone \u03b1B-crystallin to A\u03b2 amyloid fibrils inhibits fibril elongation","volume":"101","author":"Shammas","year":"2011","journal-title":"Biophys. J."},{"key":"B210","doi-asserted-by":"publisher","first-page":"837","DOI":"10.1038\/nm1782","article-title":"Amyloid-\u03b2 protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory","volume":"14","author":"Shankar","year":"2008","journal-title":"Nat. Med."},{"key":"B211","doi-asserted-by":"publisher","first-page":"1819","DOI":"10.1038\/nn.4160","article-title":"Cell type- and brain region-resolved mouse brain proteome","volume":"18","author":"Sharma","year":"2015","journal-title":"Nat. Neurosci."},{"key":"B212","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/S0197-0186(02)00196-1","article-title":"Neurodegenerative disorders of protein aggregation","volume":"43","author":"Shastry","year":"2003","journal-title":"Neurochem. Int."},{"key":"B213","doi-asserted-by":"publisher","first-page":"39962","DOI":"10.1074\/jbc.M505524200","article-title":"Geldanamycin induces heat shock protein 70 and protects against MPTP-induced dopaminergic neurotoxicity in mice","volume":"280","author":"Shen","year":"2005","journal-title":"J. Biol. Chem."},{"key":"B214","doi-asserted-by":"publisher","first-page":"e26319","DOI":"10.1371\/journal.pone.0026319","article-title":"The mammalian disaggregase machinery: Hsp110 synergizes with Hsp70 and Hsp40 to catalyze protein disaggregation and reactivation in a cell-free system","volume":"6","author":"Shorter","year":"2011","journal-title":"PLoS ONE"},{"key":"B215","doi-asserted-by":"publisher","first-page":"1793","DOI":"10.1126\/science.1098007","article-title":"Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers","volume":"304","author":"Shorter","year":"2004","journal-title":"Science"},{"key":"B216","doi-asserted-by":"publisher","first-page":"11753","DOI":"10.1074\/jbc.M208641200","article-title":"Aggregated and monomeric \u03b1-synuclein bind to the S6' proteasomal protein and inhibit proteasomal function","volume":"278","author":"Snyder","year":"2003","journal-title":"J. Biol. Chem."},{"key":"B217","doi-asserted-by":"crossref","first-page":"6469","DOI":"10.1073\/pnas.95.11.6469","article-title":"\u03b1-Synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with lewy bodies","volume":"95","author":"Spillantini","year":"1998","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"B218","doi-asserted-by":"publisher","first-page":"121","DOI":"10.1016\/j.chembiol.2009.01.012","article-title":"Multivalency-assisted control of intracellular signaling pathways: application for ubiquitin- dependent N-end rule pathway","volume":"16","author":"Sriram","year":"2009","journal-title":"Chem. Biol."},{"key":"B219","doi-asserted-by":"publisher","first-page":"735","DOI":"10.1038\/nrm3217","article-title":"The N-end rule pathway: emerging functions and molecular principles of substrate recognition","volume":"12","author":"Sriram","year":"2011","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"B220","doi-asserted-by":"publisher","first-page":"1164","DOI":"10.1038\/nsmb1010-1164","article-title":"The molecular principles of N-end rule recognition","volume":"17","author":"Sriram","year":"2010","journal-title":"Nat. Struct. Mol. Biol."},{"key":"B221","doi-asserted-by":"publisher","first-page":"152","DOI":"10.1006\/bbrc.1999.1167","article-title":"The molecular chaperone \u03b1B-crystallin enhances amyloid \u03b2 neurotoxicity","volume":"262","author":"Stege","year":"1999","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"B222","doi-asserted-by":"publisher","first-page":"495","DOI":"10.1038\/ncb2979","article-title":"Cargo recognition and trafficking in selective autophagy","volume":"16","author":"Stolz","year":"2014","journal-title":"Nat. Cell Biol."},{"key":"B223","doi-asserted-by":"publisher","first-page":"230","DOI":"10.1016\/j.tibs.2008.12.009","article-title":"Polypeptide transfer from Hsp40 to Hsp70 molecular chaperones","volume":"34","author":"Summers","year":"2009","journal-title":"Trends Biochem. Sci."},{"key":"B224","doi-asserted-by":"publisher","first-page":"2613","DOI":"10.1111\/j.1742-4658.2005.04708.x","article-title":"The small heat shock proteins and their role in human disease","volume":"272","author":"Sun","year":"2005","journal-title":"FEBS J."},{"key":"B225","doi-asserted-by":"publisher","first-page":"1426","DOI":"10.1016\/j.ajpath.2012.06.033","article-title":"The synaptic accumulation of hyperphosphorylated tau oligomers in Alzheimer disease is associated with dysfunction of the ubiquitin-proteasome system","volume":"181","author":"Tai","year":"2012","journal-title":"Am. J. Pathol."},{"key":"B226","doi-asserted-by":"publisher","first-page":"515","DOI":"10.1038\/nrm2918","article-title":"HSP90 at the hub of protein homeostasis: emerging mechanistic insights","volume":"11","author":"Taipale","year":"2010","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"B227","doi-asserted-by":"publisher","first-page":"4887","DOI":"10.1093\/emboj\/16.16.4887","article-title":"BAG-1 modulates the chaperone activity of Hsp70\/Hsc70","volume":"16","author":"Takayama","year":"1997","journal-title":"EMBO J."},{"key":"B228","doi-asserted-by":"publisher","first-page":"520","DOI":"10.1016\/j.tibs.2007.08.010","article-title":"The mammalian N-end rule pathway: new insights into its components and physiological roles","volume":"32","author":"Tasaki","year":"2007","journal-title":"Trends Biochem. Sci."},{"key":"B229","doi-asserted-by":"publisher","first-page":"7120","DOI":"10.1128\/MCB.25.16.7120-7136.2005","article-title":"A family of mammalian E3 ubiquitin ligases that contain the UBR box motif and recognize N-degrons","volume":"25","author":"Tasaki","year":"2005","journal-title":"Mol. Cell. Biol."},{"key":"B230","doi-asserted-by":"publisher","first-page":"1884","DOI":"10.1074\/jbc.M803641200","article-title":"The substrate recognition domains of the N-end rule pathway","volume":"284","author":"Tasaki","year":"2009","journal-title":"J. Biol. Chem."},{"key":"B231","doi-asserted-by":"publisher","first-page":"19958","DOI":"10.1074\/jbc.M113.477984","article-title":"Prefoldin protects neuronal cells from polyglutamine toxicity by preventing aggregation formation","volume":"288","author":"Tashiro","year":"2013","journal-title":"J. Biol. Chem."},{"key":"B232","doi-asserted-by":"publisher","first-page":"1991","DOI":"10.1126\/science.1067122","article-title":"Toxic proteins in neurodegenerative disease","volume":"296","author":"Taylor","year":"2002","journal-title":"Science"},{"key":"B233","doi-asserted-by":"publisher","first-page":"457","DOI":"10.4161\/pri.27531","article-title":"The metazoan protein disaggregase and amyloid depolymerase system: Hsp110, Hsp70, Hsp40, and small heat shock proteins","volume":"7","author":"Torrente","year":"2013","journal-title":"Prion"},{"key":"B234","doi-asserted-by":"publisher","first-page":"963","DOI":"10.1016\/j.cell.2008.04.039","article-title":"The amyotrophic lateral sclerosis 8 protein VAPB is cleaved, secreted, and acts as a ligand for Eph receptors","volume":"133","author":"Tsuda","year":"2008","journal-title":"Cell"},{"key":"B235","doi-asserted-by":"crossref","first-page":"216","DOI":"10.2174\/138920110790909632","article-title":"Heat shock proteins; an overview","volume":"11","author":"Tutar","year":"2010","journal-title":"Curr. Pharm. Biotechnol."},{"key":"B236","doi-asserted-by":"publisher","first-page":"13285","DOI":"10.1523\/JNEUROSCI.4393-08.2008","article-title":"Differential activities of the ubiquitin-proteasome system in neurons versus glia may account for the preferential accumulation of misfolded proteins in neurons","volume":"28","author":"Tydlacka","year":"2008","journal-title":"J. Neurosci."},{"key":"B237","doi-asserted-by":"publisher","first-page":"S12","DOI":"10.1186\/1471-2091-8-S1-S12","article-title":"Role of the ubiquitin proteasome system in Alzheimer's disease","volume":"8","author":"Upadhya","year":"2007","journal-title":"BMC Biochem."},{"key":"B238","doi-asserted-by":"publisher","first-page":"3425","DOI":"10.1093\/hmg\/ddi372","article-title":"Overexpression of yeast hsp104 reduces polyglutamine aggregation and prolongs survival of a transgenic mouse model of Huntington's disease","volume":"14","author":"Vacher","year":"2005","journal-title":"Hum. Mol. Genet."},{"key":"B239","doi-asserted-by":"publisher","first-page":"9","DOI":"10.1242\/dmm.013474","article-title":"Mechanisms of protein-folding diseases at a glance","volume":"7","author":"Valastyan","year":"2014","journal-title":"Dis. Model. Mech."},{"key":"B240","doi-asserted-by":"publisher","first-page":"1298","DOI":"10.1002\/pro.666","article-title":"The N-end rule pathway and regulation by proteolysis","volume":"20","author":"Varshavsky","year":"2011","journal-title":"Protein Sci."},{"key":"B241","doi-asserted-by":"publisher","first-page":"944","DOI":"10.1038\/nrm2546","article-title":"One step at a time: endoplasmic reticulum-associated degradation","volume":"9","author":"Vembar","year":"2008","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"B242","doi-asserted-by":"publisher","first-page":"4677","DOI":"10.1093\/hmg\/ddq398","article-title":"HSPB7 is the most potent polyQ aggregation suppressor within the HSPB family of molecular chaperones","volume":"19","author":"Vos","year":"2010","journal-title":"Hum. Mol. Genet."},{"key":"B243","doi-asserted-by":"publisher","first-page":"9104","DOI":"10.1523\/JNEUROSCI.2250-09.2009","article-title":"Loss of Hsp70 exacerbates pathogenesis but not levels of fibrillar aggregates in a mouse model of Huntington's disease","volume":"29","author":"Wacker","year":"2009","journal-title":"J. Neurosci."},{"key":"B245","doi-asserted-by":"publisher","first-page":"e81170","DOI":"10.1371\/journal.pone.0081170","article-title":"ALS-associated TDP-43 induces endoplasmic reticulum stress, which drives cytoplasmic TDP-43 accumulation and stress granule formation","volume":"8","author":"Walker","year":"2013","journal-title":"PLoS ONE"},{"key":"B246","first-page":"255","article-title":"The ubiquitin-proteasome system and its role in inflammatory and autoimmune diseases","volume":"3","author":"Wang","year":"2006","journal-title":"Cell. Mol. Immunol."},{"key":"B247","doi-asserted-by":"publisher","first-page":"739","DOI":"10.1515\/BC.2005.086","article-title":"Novel insights into the mechanism of chaperone-assisted protein disaggregation","volume":"386","author":"Weibezahn","year":"2005","journal-title":"Biol. Chem."},{"key":"B248","doi-asserted-by":"publisher","first-page":"761","DOI":"10.1038\/nrc1716","article-title":"HSP90 and the chaperoning of cancer","volume":"5","author":"Whitesell","year":"2005","journal-title":"Nat. Rev. Cancer"},{"issue":"Pt 1","key":"B249","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1042\/bj2750165","article-title":"Proteins containing peptide sequences related to Lys-Phe-Glu-Arg-Gln are selectively depleted in liver and heart, but not skeletal muscle, of fasted rats","volume":"275","author":"Wing","year":"1991","journal-title":"Biochem. J."},{"key":"B250","doi-asserted-by":"publisher","first-page":"152","DOI":"10.1016\/j.jsb.2012.05.002","article-title":"Chaperone networks in protein disaggregation and prion propagation","volume":"179","author":"Winkler","year":"2012","journal-title":"J. Struct. Biol."},{"key":"B251","doi-asserted-by":"publisher","first-page":"S1","DOI":"10.1007\/s10654-011-9581-6","article-title":"Epidemiology and etiology of Parkinson's disease: a review of the evidence","volume":"26","author":"Wirdefeldt","year":"2011","journal-title":"Eur. J. Epidemiol."},{"key":"B252","doi-asserted-by":"publisher","first-page":"552","DOI":"10.1007\/s12035-012-8325-2","article-title":"Molecular chaperones, \u03b1-synuclein, and neurodegeneration","volume":"47","author":"Witt","year":"2013","journal-title":"Mol. Neurobiol."},{"key":"B253","doi-asserted-by":"publisher","first-page":"499","DOI":"10.1016\/j.jmb.2012.01.004","article-title":"Roles of extracellular chaperones in amyloidosis","volume":"421","author":"Wyatt","year":"2012","journal-title":"J. Mol. Biol."},{"key":"B254","doi-asserted-by":"publisher","first-page":"69","DOI":"10.1385\/JMN:23:1-2:069","article-title":"Role of heat shock proteins during polyglutamine neurodegeneration: mechanisms and hypothesis","volume":"23","author":"Wyttenbach","year":"2004","journal-title":"J. Mol. Neurosci."},{"key":"B255","doi-asserted-by":"publisher","first-page":"308","DOI":"10.1093\/jmcb\/mjq030","article-title":"Structure, assembly and homeostatic regulation of the 26S proteasome","volume":"2","author":"Xie","year":"2010","journal-title":"J. Mol. Cell Biol."},{"key":"B256","doi-asserted-by":"publisher","first-page":"2424","DOI":"10.1016\/j.yexcr.2010.06.003","article-title":"Hsp105 reduces the protein aggregation and cytotoxicity by expanded-polyglutamine proteins through the induction of Hsp70","volume":"316","author":"Yamagishi","year":"2010","journal-title":"Exp. Cell Res."},{"key":"B257","doi-asserted-by":"publisher","first-page":"607","DOI":"10.3109\/00207454.2015.1050098","article-title":"Polymorphisms in protein disulfide isomerase are associated with sporadic amyotrophic lateral sclerosis in the Chinese Han population","volume":"126","author":"Yang","year":"2016","journal-title":"Int. J. Neurosci."},{"key":"B258","doi-asserted-by":"publisher","first-page":"251","DOI":"10.1007\/s12192-012-0371-1","article-title":"The small heat shock proteins \u03b1B-crystallin and Hsp27 suppress SOD1 aggregation in vitro","volume":"18","author":"Yerbury","year":"2013","journal-title":"Cell Stress Chaperones"},{"key":"B259","doi-asserted-by":"publisher","first-page":"1421","DOI":"10.1007\/s00109-007-0251-9","article-title":"Celastrol inhibits polyglutamine aggregation and toxicity though induction of the heat shock response","volume":"85","author":"Zhang","year":"2007","journal-title":"J. Mol. Med."},{"key":"B260","doi-asserted-by":"publisher","first-page":"39155","DOI":"10.1074\/jbc.M405456200","article-title":"Analysis of \u03b1-synuclein-associated proteins by quantitative proteomics","volume":"279","author":"Zhou","year":"2004","journal-title":"J. Biol. Chem."},{"key":"B261","doi-asserted-by":"publisher","first-page":"7022","DOI":"10.1074\/jbc.M507893200","article-title":"Hsp70 chaperone machine remodels protein aggregates at the initial step of Hsp70-Hsp100-dependent disaggregation","volume":"281","author":"Zietkiewicz","year":"2006","journal-title":"J. Biol. Chem."},{"key":"B262","doi-asserted-by":"publisher","first-page":"499","DOI":"10.1007\/s12192-016-0678-4","article-title":"Plasmodium falciparum Hsp70-z, an Hsp110 homologue, exhibits independent chaperone activity and interacts with Hsp70-1 in a nucleotide-dependent fashion","volume":"21","author":"Zininga","year":"2016","journal-title":"Cell Stress Chaperones"}],"container-title":["Frontiers in Neuroscience"],"original-title":[],"link":[{"URL":"http:\/\/journal.frontiersin.org\/article\/10.3389\/fnins.2017.00185\/full","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,7,27]],"date-time":"2022-07-27T03:26:18Z","timestamp":1658892378000},"score":1,"resource":{"primary":{"URL":"http:\/\/journal.frontiersin.org\/article\/10.3389\/fnins.2017.00185\/full"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2017,4,6]]},"references-count":261,"URL":"https:\/\/doi.org\/10.3389\/fnins.2017.00185","relation":{},"ISSN":["1662-453X"],"issn-type":[{"value":"1662-453X","type":"electronic"}],"subject":[],"published":{"date-parts":[[2017,4,6]]}}}