{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,4]],"date-time":"2026-10-04T11:41:20Z","timestamp":1791114080899,"version":"4.1.0"},"reference-count":75,"publisher":"Elsevier BV","issue":"5","license":[{"start":{"date-parts":[[2011,7,1]],"date-time":"2011-07-01T00:00:00Z","timestamp":1309478400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Seminars in Cell &amp; Developmental Biology"],"published-print":{"date-parts":[[2011,7]]},"DOI":"10.1016\/j.semcdb.2011.03.011","type":"journal-article","created":{"date-parts":[[2011,4,8]],"date-time":"2011-04-08T16:21:29Z","timestamp":1302279689000},"page":"476-481","source":"Crossref","is-referenced-by-count":82,"title":["Amyloid in neurodegenerative diseases: Friend or foe?"],"prefix":"10.1016","volume":"22","author":[{"given":"Katie J.","family":"Wolfe","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Douglas M.","family":"Cyr","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.semcdb.2011.03.011_bib0005","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1146\/annurev.biochem.75.101304.123901","article-title":"Protein misfolding, functional amyloid, and human disease","volume":"75","author":"Chiti","year":"2006","journal-title":"Annu Rev Biochem"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0010","doi-asserted-by":"crossref","first-page":"101","DOI":"10.3109\/13506129.2010.526812","article-title":"Amyloid fibril protein nomenclature: 2010 recommendations from the nomenclature committee of the International Society of Amyloidosis","volume":"17","author":"Sipe","year":"2010","journal-title":"Amyloid"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0015","doi-asserted-by":"crossref","first-page":"891","DOI":"10.1038\/nrm1742","article-title":"Opinion: what is the role of protein aggregation in neurodegeneration?","volume":"6","author":"Ross","year":"2005","journal-title":"Nat Rev Mol Cell Biol"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0020","doi-asserted-by":"crossref","first-page":"535","DOI":"10.1038\/416535a","article-title":"Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo","volume":"416","author":"Walsh","year":"2002","journal-title":"Nature"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0025","doi-asserted-by":"crossref","first-page":"7206","DOI":"10.1073\/pnas.0802593105","article-title":"Chaperone-dependent amyloid assembly protects cells from prion toxicity","volume":"105","author":"Douglas","year":"2008","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0030","doi-asserted-by":"crossref","first-page":"134","DOI":"10.1016\/S0140-6736(97)02073-4","article-title":"Conformational disease","volume":"350","author":"Carrell","year":"1997","journal-title":"Lancet"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0035","doi-asserted-by":"crossref","first-page":"609","DOI":"10.1093\/hmg\/ddp527","article-title":"Expression analysis of novel striatal-enriched genes in Huntington disease","volume":"19","author":"Mazarei","year":"2010","journal-title":"Hum Mol Genet"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0040","doi-asserted-by":"crossref","first-page":"526","DOI":"10.1038\/ng1542","article-title":"A genomic screen in yeast implicates kynurenine 3-monooxygenase as a therapeutic target for Huntington disease","volume":"37","author":"Giorgini","year":"2005","journal-title":"Nat Genet"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0045","doi-asserted-by":"crossref","first-page":"1769","DOI":"10.1126\/science.1090389","article-title":"Yeast genes that enhance the toxicity of a mutant huntingtin fragment or alpha-synuclein","volume":"302","author":"Willingham","year":"2003","journal-title":"Science"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0050","doi-asserted-by":"crossref","first-page":"916","DOI":"10.1126\/science.1141448","article-title":"Adapting proteostasis for disease intervention","volume":"319","author":"Balch","year":"2008","journal-title":"Science"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0055","doi-asserted-by":"crossref","first-page":"1471","DOI":"10.1126\/science.1124514","article-title":"Progressive disruption of cellular protein folding in models of polyglutamine diseases","volume":"311","author":"Gidalevitz","year":"2006","journal-title":"Science"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0060","doi-asserted-by":"crossref","first-page":"2905","DOI":"10.1093\/hmg\/11.23.2905","article-title":"Aggregated polyglutamine peptides delivered to nuclei are toxic to mammalian cells","volume":"11","author":"Yang","year":"2002","journal-title":"Hum Mol Genet"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0065","doi-asserted-by":"crossref","first-page":"842","DOI":"10.1002\/1531-8249(199912)46:6<842::AID-ANA6>3.0.CO;2-O","article-title":"Huntington aggregates may not predict neuronal death in Huntington's disease","volume":"46","author":"Kuemmerle","year":"1999","journal-title":"Ann Neurol"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0070","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1016\/S0092-8674(00)81782-1","article-title":"Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions","volume":"95","author":"Saudou","year":"1998","journal-title":"Cell"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0075","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1038\/nsmb1058","article-title":"Amyloid formation under physiological conditions proceeds via a native-like folding intermediate","volume":"13","author":"Jahn","year":"2006","journal-title":"Nat Struct Mol Biol"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0080","doi-asserted-by":"crossref","first-page":"3308","DOI":"10.1101\/gad.1673408","article-title":"Impaired ERAD and ER stress are early and specific events in polyglutamine toxicity","volume":"22","author":"Duennwald","year":"2008","journal-title":"Genes Dev"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0085","doi-asserted-by":"crossref","first-page":"1055","DOI":"10.1016\/0092-8674(93)90635-4","article-title":"Seeding \u201cone-dimensional crystallization\u201d of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie?","volume":"73","author":"Jarrett","year":"1993","journal-title":"Cell"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0090","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1126\/science.1079469","article-title":"Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis","volume":"300","author":"Kayed","year":"2003","journal-title":"Science"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0095","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1146\/annurev.neuro.23.1.217","article-title":"Glutamine repeats and neurodegeneration","volume":"23","author":"Zoghbi","year":"2000","journal-title":"Annu Rev Neurosci"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0100","doi-asserted-by":"crossref","first-page":"537","DOI":"10.1016\/S0092-8674(00)80513-9","article-title":"Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation","volume":"90","author":"Davies","year":"1997","journal-title":"Cell"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0105","doi-asserted-by":"crossref","first-page":"1990","DOI":"10.1126\/science.277.5334.1990","article-title":"Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain","volume":"277","author":"DiFiglia","year":"1997","journal-title":"Science"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0110","doi-asserted-by":"crossref","first-page":"14777","DOI":"10.1074\/jbc.M109.093708","article-title":"Mutant huntingtin fragments form oligomers in a polyglutamine length-dependent manner in vitro and in vivo","volume":"285","author":"Legleiter","year":"2010","journal-title":"J Biol Chem"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0115","doi-asserted-by":"crossref","first-page":"345","DOI":"10.1093\/hmg\/ddm311","article-title":"Soluble polyglutamine oligomers formed prior to inclusion body formation are cytotoxic","volume":"17","author":"Takahashi","year":"2008","journal-title":"Hum Mol Genet"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0120","doi-asserted-by":"crossref","first-page":"805","DOI":"10.1038\/nature02998","article-title":"Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death","volume":"431","author":"Arrasate","year":"2004","journal-title":"Nature"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0125","doi-asserted-by":"crossref","first-page":"1157","DOI":"10.1016\/j.cell.2009.11.014","article-title":"Reduced IGF-1 signaling delays age-associated proteotoxicity in mice","volume":"139","author":"Cohen","year":"2009","journal-title":"Cell"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0130","doi-asserted-by":"crossref","first-page":"556","DOI":"10.1038\/nm1234","article-title":"Amyloid beta protein immunotherapy neutralizes Abeta oligomers that disrupt synaptic plasticity in vivo","volume":"11","author":"Klyubin","year":"2005","journal-title":"Nat Med"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0135","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1038\/nrm2101","article-title":"Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide","volume":"8","author":"Haass","year":"2007","journal-title":"Nat Rev Mol Cell Biol"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0140","doi-asserted-by":"crossref","first-page":"572","DOI":"10.1002\/ana.410300410","article-title":"Physical basis of cognitive alterations in Alzheimer's disease: synapse loss is the major correlate of cognitive impairment","volume":"30","author":"Terry","year":"1991","journal-title":"Ann Neurol"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0145","doi-asserted-by":"crossref","first-page":"2183","DOI":"10.1101\/gad.1436506","article-title":"Polyglutamine neurodegenerative diseases and regulation of transcription: assembling the puzzle","volume":"20","author":"Riley","year":"2006","journal-title":"Genes Dev"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0150","doi-asserted-by":"crossref","first-page":"2423","DOI":"10.1126\/science.1056784","article-title":"Interference by huntingtin and atrophin-1 with cbp-mediated transcription leading to cellular toxicity","volume":"291","author":"Nucifora","year":"2001","journal-title":"Science"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0155","doi-asserted-by":"crossref","first-page":"1552","DOI":"10.1126\/science.292.5521.1552","article-title":"Impairment of the ubiquitin-proteasome system by protein aggregation","volume":"292","author":"Bence","year":"2001","journal-title":"Science"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0160","doi-asserted-by":"crossref","first-page":"5153","DOI":"10.1523\/JNEUROSCI.0783-09.2009","article-title":"Cross-seeding fibrillation of Q\/N-rich proteins offers new pathomechanism of polyglutamine diseases","volume":"29","author":"Furukawa","year":"2009","journal-title":"J Neurosci"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0165","doi-asserted-by":"crossref","first-page":"11051","DOI":"10.1073\/pnas.0604548103","article-title":"A network of protein interactions determines polyglutamine toxicity","volume":"103","author":"Duennwald","year":"2006","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0170","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1016\/j.cell.2010.11.050","article-title":"Amyloid-like aggregates sequester numerous metastable proteins with essential cellular functions","volume":"144","author":"Olzscha","year":"2011","journal-title":"Cell"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0175","doi-asserted-by":"crossref","first-page":"1121","DOI":"10.1016\/j.cell.2010.11.042","article-title":"Essential role of coiled coils for aggregation and activity of Q\/N-rich prions and PolyQ proteins","volume":"143","author":"Fiumara","year":"2010","journal-title":"Cell"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0180","doi-asserted-by":"crossref","first-page":"136","DOI":"10.1126\/science.6801762","article-title":"Novel proteinaceous infectious particles cause scrapie","volume":"216","author":"Prusiner","year":"1982","journal-title":"Science"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0185","doi-asserted-by":"crossref","first-page":"435","DOI":"10.1038\/nrg1616","article-title":"Prions as adaptive conduits of memory and inheritance","volume":"6","author":"Shorter","year":"2005","journal-title":"Nat Rev Genet"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0190","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1016\/S1097-2765(00)80412-8","article-title":"Rnq1: an epigenetic modifier of protein function in yeast","volume":"5","author":"Sondheimer","year":"2000","journal-title":"Mol Cell"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0195","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1016\/S0092-8674(01)00427-5","article-title":"Prions affect the appearance of other prions: the story of [PIN(+)]","volume":"106","author":"Derkatch","year":"2001","journal-title":"Cell"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0200","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1007\/s00294-007-0127-0","article-title":"Propagation of the [PIN+] prion by fragments of Rnq1 fused to GFP","volume":"51","author":"Vitrenko","year":"2007","journal-title":"Curr Genet"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0205","doi-asserted-by":"crossref","first-page":"997","DOI":"10.1083\/jcb.200112104","article-title":"Huntington toxicity in yeast model depends on polyglutamine aggregation mediated by a prion-like protein Rnq1","volume":"157","author":"Meriin","year":"2002","journal-title":"J Cell Biol"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0210","doi-asserted-by":"crossref","DOI":"10.1091\/mbc.E09-02-0170","article-title":"Reciprocal efficiency of RNQ1 and polyglutamine detoxification in the cytosol and nucleus","author":"Douglas","year":"2009","journal-title":"Mol Biol Cell"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0215","doi-asserted-by":"crossref","first-page":"9679","DOI":"10.1073\/pnas.0812083106","article-title":"Distinct conformations of in vitro and in vivo amyloids of huntingtin-exon1 show different cytotoxicity","volume":"106","author":"Nekooki-Machida","year":"2009","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0220","doi-asserted-by":"crossref","DOI":"10.1074\/jbc.M110.192013","article-title":"A compact {beta} model of huntingtin toxicity","author":"Zhang","year":"2011","journal-title":"J Biol Chem"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0225","doi-asserted-by":"crossref","first-page":"7841","DOI":"10.1073\/pnas.140202897","article-title":"Hsp70 and hsp40 chaperones can inhibit self-assembly of polyglutamine proteins into amyloid-like fibrils","volume":"97","author":"Muchowski","year":"2000","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0230","doi-asserted-by":"crossref","first-page":"22809","DOI":"10.1074\/jbc.M500390200","article-title":"Modulation of prion-dependent polyglutamine aggregation and toxicity by chaperone proteins in the yeast model","volume":"280","author":"Gokhale","year":"2005","journal-title":"J Biol Chem"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0235","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":"10.1016\/j.semcdb.2011.03.011_bib0240","doi-asserted-by":"crossref","first-page":"176","DOI":"10.1016\/0968-0004(94)90281-X","article-title":"DnaJ-like proteins: molecular chaperones and specific regulators of Hsp70","volume":"19","author":"Cyr","year":"1994","journal-title":"Trends Biochem Sci"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0245","doi-asserted-by":"crossref","first-page":"761","DOI":"10.1091\/mbc.E03-03-0146","article-title":"Exchangeable chaperone modules contribute to specification of type I and type II Hsp40 cellular function","volume":"15","author":"Fan","year":"2004","journal-title":"Mol Biol Cell"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0250","doi-asserted-by":"crossref","first-page":"11073","DOI":"10.1073\/pnas.0900746106","article-title":"Identification of a consensus motif in substrates bound by a Type I Hsp40","volume":"106","author":"Kota","year":"2009","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0255","doi-asserted-by":"crossref","first-page":"38183","DOI":"10.1074\/jbc.M110.160218","article-title":"Hsp70 and Hsp40 functionally interact with soluble mutant huntingtin oligomers in a classic ATP-dependent reaction cycle","volume":"285","author":"Lotz","year":"2010","journal-title":"J Biol Chem"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0260","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1038\/70532","article-title":"Suppression of polyglutamine-mediated neurodegeneration in Drosophila by the molecular chaperone HSP70","volume":"23","author":"Warrick","year":"1999","journal-title":"Nat Genet"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0265","doi-asserted-by":"crossref","first-page":"3628","DOI":"10.1074\/jbc.M807369200","article-title":"The type I Hsp40 Ydj1 utilizes a farnesyl moiety and zinc finger-like region to suppress prion toxicity","volume":"284","author":"Summers","year":"2009","journal-title":"J Biol Chem"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0270","doi-asserted-by":"crossref","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":"10.1016\/j.semcdb.2011.03.011_bib0275","doi-asserted-by":"crossref","first-page":"10338","DOI":"10.1523\/JNEUROSCI.19-23-10338.1999","article-title":"Analysis of the role of heat shock protein (Hsp) molecular chaperones in polyglutamine disease","volume":"19","author":"Chai","year":"1999","journal-title":"J Neurosci"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0280","doi-asserted-by":"crossref","first-page":"880","DOI":"10.1126\/science.7754373","article-title":"Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+]","volume":"268","author":"Chernoff","year":"1995","journal-title":"Science"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0285","doi-asserted-by":"crossref","first-page":"23869","DOI":"10.1074\/jbc.M502854200","article-title":"A chaperone pathway in protein disaggregation. Hsp26 alters the nature of protein aggregates to facilitate reactivation by Hsp104","volume":"280","author":"Cashikar","year":"2005","journal-title":"J Biol Chem"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0290","doi-asserted-by":"crossref","first-page":"5750","DOI":"10.1073\/pnas.100107297","article-title":"Polyglutamine aggregates alter protein folding homeostasis in Caenorhabditis elegans","volume":"97","author":"Satyal","year":"2000","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0295","doi-asserted-by":"crossref","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":"10.1016\/j.semcdb.2011.03.011_bib0300","doi-asserted-by":"crossref","first-page":"1172","DOI":"10.1091\/mbc.E02-09-0593","article-title":"Specificity of class II Hsp40 Sis1 in maintenance of yeast prion [RNQ+]","volume":"14","author":"Lopez","year":"2003","journal-title":"Mol Biol Cell"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0305","doi-asserted-by":"crossref","first-page":"2898","DOI":"10.1073\/pnas.97.6.2898","article-title":"Effects of heat shock, heat shock protein 40 (HDJ-2), and proteasome inhibition on protein aggregation in cellular models of Huntington's disease","volume":"97","author":"Wyttenbach","year":"2000","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0310","doi-asserted-by":"crossref","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 USA"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0315","doi-asserted-by":"crossref","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":"10.1016\/j.semcdb.2011.03.011_bib0320","doi-asserted-by":"crossref","first-page":"1279","DOI":"10.1038\/nsmb.1700","article-title":"The chaperonin TRiC blocks a huntingtin sequence element that promotes the conformational switch to aggregation","volume":"16","author":"Tam","year":"2009","journal-title":"Nat Struct Mol Biol"},{"issue":"Suppl. 4","key":"10.1016\/j.semcdb.2011.03.011_bib0325","doi-asserted-by":"crossref","first-page":"16412","DOI":"10.1073\/pnas.182426899","article-title":"Molecular chaperones as modulators of polyglutamine protein aggregation and toxicity","volume":"99","author":"Sakahira","year":"2002","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0330","doi-asserted-by":"crossref","first-page":"42938","DOI":"10.1074\/jbc.M101968200","article-title":"CHIP is a U-box-dependent E3 ubiquitin ligase: identification of Hsc70 as a target for ubiquitylation","volume":"276","author":"Jiang","year":"2001","journal-title":"J Biol Chem"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0335","doi-asserted-by":"crossref","first-page":"22267","DOI":"10.1074\/jbc.M700513200","article-title":"Chaperone functions of the E3 ubiquitin ligase CHIP","volume":"282","author":"Rosser","year":"2007","journal-title":"J Biol Chem"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0340","doi-asserted-by":"crossref","first-page":"11635","DOI":"10.1074\/jbc.M412042200","article-title":"Co-chaperone CHIP associates with expanded polyglutamine protein and promotes their degradation by proteasomes","volume":"280","author":"Jana","year":"2005","journal-title":"J Biol Chem"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0345","doi-asserted-by":"crossref","first-page":"9152","DOI":"10.1523\/JNEUROSCI.3001-05.2005","article-title":"CHIP suppresses polyglutamine aggregation and toxicity in vitro and in vivo","volume":"25","author":"Miller","year":"2005","journal-title":"J Neurosci"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0350","doi-asserted-by":"crossref","first-page":"463","DOI":"10.1016\/S1534-5807(04)00099-1","article-title":"Development by self-digestion: molecular mechanisms and biological functions of autophagy","volume":"6","author":"Levine","year":"2004","journal-title":"Dev Cell"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0355","doi-asserted-by":"crossref","first-page":"885","DOI":"10.1038\/nature04724","article-title":"Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice","volume":"441","author":"Hara","year":"2006","journal-title":"Nature"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0360","doi-asserted-by":"crossref","first-page":"1107","DOI":"10.1093\/hmg\/11.9.1107","article-title":"Aggregate-prone proteins with polyglutamine and polyalanine expansions are degraded by autophagy","volume":"11","author":"Ravikumar","year":"2002","journal-title":"Hum Mol Genet"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0365","doi-asserted-by":"crossref","first-page":"60","DOI":"10.1016\/j.cell.2009.03.018","article-title":"Acetylation targets mutant huntingtin to autophagosomes for degradation","volume":"137","author":"Jeong","year":"2009","journal-title":"Cell"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0370","doi-asserted-by":"crossref","first-page":"2197","DOI":"10.1093\/hmg\/9.14.2197","article-title":"CREB-binding protein sequestration by expanded polyglutamine","volume":"9","author":"McCampbell","year":"2000","journal-title":"Hum Mol Genet"},{"key":"10.1016\/j.semcdb.2011.03.011_bib0375","doi-asserted-by":"crossref","first-page":"140","DOI":"10.1038\/nchembio.283","article-title":"A causative link between the structure of aberrant protein oligomers and their toxicity","volume":"6","author":"Campioni","year":"2010","journal-title":"Nat Chem Biol"}],"container-title":["Seminars in Cell &amp; Developmental Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1084952111000607?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1084952111000607?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2019,6,9]],"date-time":"2019-06-09T17:41:28Z","timestamp":1560102088000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1084952111000607"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2011,7]]},"references-count":75,"journal-issue":{"issue":"5","published-print":{"date-parts":[[2011,7]]}},"alternative-id":["S1084952111000607"],"URL":"https:\/\/doi.org\/10.1016\/j.semcdb.2011.03.011","relation":{},"ISSN":["1084-9521"],"issn-type":[{"value":"1084-9521","type":"print"}],"subject":[],"published":{"date-parts":[[2011,7]]}}}