{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,21]],"date-time":"2026-05-21T08:38:03Z","timestamp":1779352683109,"version":"3.51.4"},"reference-count":73,"publisher":"Public Library of Science (PLoS)","issue":"1","license":[{"start":{"date-parts":[[2018,1,18]],"date-time":"2018-01-18T00:00:00Z","timestamp":1516233600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"National Institution of Health","award":["RO1GM102115"],"award-info":[{"award-number":["RO1GM102115"]}]},{"DOI":"10.13039\/100006597","name":"Florida State University","doi-asserted-by":"crossref","award":["CRC planning Grant"],"award-info":[{"award-number":["CRC planning Grant"]}],"id":[{"id":"10.13039\/100006597","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":["www.plosone.org"],"crossmark-restriction":false},"short-container-title":["PLoS ONE"],"DOI":"10.1371\/journal.pone.0191490","type":"journal-article","created":{"date-parts":[[2018,1,18]],"date-time":"2018-01-18T18:53:13Z","timestamp":1516301593000},"page":"e0191490","update-policy":"https:\/\/doi.org\/10.1371\/journal.pone.corrections_policy","source":"Crossref","is-referenced-by-count":22,"title":["The absence of specific yeast heat-shock proteins leads to abnormal aggregation and compromised autophagic clearance of mutant Huntingtin proteins"],"prefix":"10.1371","volume":"13","author":[{"given":"Ryan","family":"Higgins","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Marie-Helene","family":"Kabbaj","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Alexa","family":"Hatcher","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6782-0570","authenticated-orcid":true,"given":"Yanchang","family":"Wang","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"340","published-online":{"date-parts":[[2018,1,18]]},"reference":[{"issue":"1","key":"ref1","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1038\/nrn1007","article-title":"Unfolding the role of protein misfolding in neurodegenerative diseases","volume":"4","author":"C Soto","year":"2003","journal-title":"Nat Rev Neurosci"},{"issue":"6","key":"ref2","doi-asserted-by":"crossref","first-page":"384","DOI":"10.1038\/nrm3810","article-title":"The amyloid state and its association with protein misfolding diseases","volume":"15","author":"TP Knowles","year":"2014","journal-title":"Nat Rev Mol Cell Biol"},{"key":"ref3","doi-asserted-by":"crossref","first-page":"97","DOI":"10.3389\/fonc.2015.00097","article-title":"Misfolding, Aggregation, and Disordered Segments in c-Abl and p53 in Human Cancer","volume":"5","author":"GA de Oliveira","year":"2015","journal-title":"Front Oncol"},{"issue":"7","key":"ref4","doi-asserted-by":"crossref","first-page":"439","DOI":"10.1016\/j.molmed.2015.04.005","article-title":"Type 2 diabetes as a protein misfolding disease","volume":"21","author":"A Mukherjee","year":"2015","journal-title":"Trends Mol Med"},{"issue":"7356","key":"ref5","doi-asserted-by":"crossref","first-page":"324","DOI":"10.1038\/nature10317","article-title":"Molecular chaperones in protein folding and proteostasis","volume":"475","author":"FU Hartl","year":"2011","journal-title":"Nature"},{"issue":"10","key":"ref6","doi-asserted-by":"crossref","first-page":"507","DOI":"10.1016\/j.tibs.2013.08.001","article-title":"Hsp70 chaperone dynamics and molecular mechanism","volume":"38","author":"MP Mayer","year":"2013","journal-title":"Trends Biochem Sci"},{"issue":"6","key":"ref7","doi-asserted-by":"crossref","first-page":"863","DOI":"10.1016\/j.molcel.2012.09.023","article-title":"Structure and dynamics of the ATP-bound open conformation of Hsp70 chaperones","volume":"48","author":"R Kityk","year":"2012","journal-title":"Mol Cell"},{"issue":"6959","key":"ref8","doi-asserted-by":"crossref","first-page":"737","DOI":"10.1038\/nature02046","article-title":"Global analysis of protein expression in yeast","volume":"425","author":"S Ghaemmaghami","year":"2003","journal-title":"Nature"},{"issue":"19","key":"ref9","doi-asserted-by":"crossref","first-page":"13155","DOI":"10.1074\/jbc.M113.530014","article-title":"Hierarchical functional specificity of cytosolic heat shock protein 70 (Hsp70) nucleotide exchange factors in yeast","volume":"289","author":"JL Abrams","year":"2014","journal-title":"J Biol Chem"},{"issue":"5","key":"ref10","doi-asserted-by":"crossref","first-page":"593","DOI":"10.1016\/S1097-2765(00)80158-6","article-title":"J proteins catalytically activate Hsp70 molecules to trap a wide range of peptide sequences","volume":"2","author":"B Misselwitz","year":"1998","journal-title":"Mol Cell"},{"key":"ref11","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1007\/978-3-319-11731-7_4","article-title":"Specification of Hsp70 function by Type I and Type II Hsp40","volume":"78","author":"DM Cyr","year":"2015","journal-title":"Subcell Biochem"},{"key":"ref12","doi-asserted-by":"crossref","first-page":"57","DOI":"10.3389\/fmolb.2015.00057","article-title":"Metazoan Hsp70-based protein disaggregases: emergence and mechanisms","volume":"2","author":"NB Nillegoda","year":"2015","journal-title":"Front Mol Biosci"},{"key":"ref13","article-title":"Coordinated Hsp110 and Hsp104 activities power protein disaggregation in Saccharomyces cerevisiae","author":"JM Kaimal","year":"2017","journal-title":"Mol Cell Biol"},{"issue":"6","key":"ref14","doi-asserted-by":"crossref","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":"MP Torrente","year":"2013","journal-title":"Prion"},{"issue":"21","key":"ref15","doi-asserted-by":"crossref","first-page":"4221","DOI":"10.1038\/emboj.2012.264","article-title":"Metazoan Hsp70 machines use Hsp110 to power protein disaggregation","volume":"31","author":"H Rampelt","year":"2012","journal-title":"EMBO J"},{"issue":"1","key":"ref16","doi-asserted-by":"crossref","first-page":"134","DOI":"10.1016\/j.cell.2013.06.003","article-title":"PolyQ proteins interfere with nuclear degradation of cytosolic proteins by sequestering the Sis1p chaperone","volume":"154","author":"SH Park","year":"2013","journal-title":"Cell"},{"issue":"1","key":"ref17","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":"H Olzscha","year":"2011","journal-title":"Cell"},{"issue":"1","key":"ref18","doi-asserted-by":"crossref","first-page":"436","DOI":"10.1046\/j.1471-4159.2000.0750436.x","article-title":"Impaired proteasome function in Alzheimer\u2019s disease","volume":"75","author":"JN Keller","year":"2000","journal-title":"J Neurochem"},{"issue":"5","key":"ref19","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":"JS Hwang","year":"2007","journal-title":"J Gerontol A Biol Sci Med Sci"},{"issue":"49","key":"ref20","doi-asserted-by":"crossref","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":"S Tydlacka","year":"2008","journal-title":"J Neurosci"},{"issue":"1","key":"ref21","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1016\/j.ygcen.2011.02.005","article-title":"The role of ubiquitin-proteasome system in ageing","volume":"172","author":"P Low","year":"2011","journal-title":"Gen Comp Endocrinol"},{"key":"ref22","doi-asserted-by":"crossref","first-page":"185","DOI":"10.3389\/fnins.2017.00185","article-title":"Protein Quality Control by Molecular Chaperones in Neurodegeneration","volume":"11","author":"A Ciechanover","year":"2017","journal-title":"Front Neurosci"},{"issue":"29","key":"ref23","doi-asserted-by":"crossref","first-page":"11045","DOI":"10.1073\/pnas.0604547103","article-title":"Flanking sequences profoundly alter polyglutamine toxicity in yeast","volume":"103","author":"ML Duennwald","year":"2006","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"4","key":"ref24","doi-asserted-by":"crossref","first-page":"1589","DOI":"10.1073\/pnas.97.4.1589","article-title":"Aggregation of huntingtin in yeast varies with the length of the polyglutamine expansion and the expression of chaperone proteins","volume":"97","author":"S Krobitsch","year":"2000","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"2","key":"ref25","doi-asserted-by":"crossref","first-page":"451","DOI":"10.1096\/fj.08-117614","article-title":"Abnormal proteins can form aggresome in yeast: aggresome-targeting signals and components of the machinery","volume":"23","author":"Y Wang","year":"2009","journal-title":"FASEB J"},{"issue":"13","key":"ref26","doi-asserted-by":"crossref","first-page":"2025","DOI":"10.1091\/mbc.E16-01-0026","article-title":"Ubiquilin\/Dsk2 promotes inclusion body formation and vacuole (lysosome)-mediated disposal of mutated huntingtin","volume":"27","author":"KH Chuang","year":"2016","journal-title":"Mol Biol Cell"},{"key":"ref27","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.11792","article-title":"Spatial sequestration and detoxification of Huntingtin by the ribosome quality control complex","volume":"5","author":"J Yang","year":"2016","journal-title":"Elife"},{"issue":"7","key":"ref28","doi-asserted-by":"crossref","first-page":"e41450","DOI":"10.1371\/journal.pone.0041450","article-title":"Temporal separation of aggregation and ubiquitination during early inclusion formation in transgenic mice carrying the Huntington\u2019s disease mutation","volume":"7","author":"B Gong","year":"2012","journal-title":"PLoS One"},{"issue":"50","key":"ref29","doi-asserted-by":"crossref","first-page":"41262","DOI":"10.1074\/jbc.M503614200","article-title":"The yeast Hsp110 Sse1 functionally interacts with the Hsp70 chaperones Ssa and Ssb","volume":"280","author":"L Shaner","year":"2005","journal-title":"J Biol Chem"},{"issue":"11","key":"ref30","doi-asserted-by":"crossref","first-page":"2519","DOI":"10.1038\/sj.emboj.7601138","article-title":"Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s","volume":"25","author":"Z Dragovic","year":"2006","journal-title":"EMBO J"},{"key":"ref31","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.18065","article-title":"Control of the structural landscape and neuronal proteotoxicity of mutant Huntingtin by domains flanking the polyQ tract","volume":"5","author":"K Shen","year":"2016","journal-title":"Elife"},{"key":"ref32","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1196\/annals.1391.018","article-title":"New tricks for an old dog: the evolving world of Hsp70","volume":"1113","author":"KA Morano","year":"2007","journal-title":"Ann N Y Acad Sci"},{"key":"ref33","doi-asserted-by":"crossref","first-page":"10","DOI":"10.3389\/fmolb.2015.00010","article-title":"The nucleotide exchange factors of Hsp70 molecular chaperones","volume":"2","author":"A Bracher","year":"2015","journal-title":"Front Mol Biosci"},{"key":"ref34","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1038\/msb.2009.26","article-title":"An atlas of chaperone-protein interactions in Saccharomyces cerevisiae: implications to protein folding pathways in the cell","volume":"5","author":"Y Gong","year":"2009","journal-title":"Mol Syst Biol"},{"issue":"18","key":"ref35","doi-asserted-by":"crossref","first-page":"2948","DOI":"10.1016\/j.jmb.2015.04.010","article-title":"Mutations in the Yeast Hsp70, Ssa1, at P417 Alter ATP Cycling, Interdomain Coupling, and Specific Chaperone Functions","volume":"427","author":"PG Needham","year":"2015","journal-title":"J Mol Biol"},{"issue":"13","key":"ref36","doi-asserted-by":"crossref","first-page":"4677","DOI":"10.1128\/MCB.22.13.4677-4689.2002","article-title":"Nucleotide exchange factor for the yeast Hsp70 molecular chaperone Ssa1p","volume":"22","author":"M Kabani","year":"2002","journal-title":"Mol Cell Biol"},{"issue":"10","key":"ref37","doi-asserted-by":"crossref","first-page":"2435","DOI":"10.1093\/emboj\/20.10.2435","article-title":"The role of Sis1 in the maintenance of the [RNQ+] prion","volume":"20","author":"N Sondheimer","year":"2001","journal-title":"EMBO J"},{"issue":"6","key":"ref38","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":"AB Meriin","year":"2002","journal-title":"J Cell Biol"},{"issue":"1","key":"ref39","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":"JR Glover","year":"1998","journal-title":"Cell"},{"issue":"6505","key":"ref40","doi-asserted-by":"crossref","first-page":"475","DOI":"10.1038\/372475a0","article-title":"Protein disaggregation mediated by heat-shock protein Hsp104","volume":"372","author":"DA Parsell","year":"1994","journal-title":"Nature"},{"issue":"1","key":"ref41","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1083\/jcb.201505104","article-title":"Prion aggregate structure in yeast cells is determined by the Hsp104-Hsp110 disaggregase machinery","volume":"211","author":"J O\u2032Driscoll","year":"2015","journal-title":"J Cell Biol"},{"issue":"1","key":"ref42","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1111\/j.1600-0854.2007.00666.x","article-title":"Nucleocytoplasmic trafficking of the molecular chaperone Hsp104 in unstressed and heat-shocked cells","volume":"9","author":"JM Tkach","year":"2008","journal-title":"Traffic"},{"key":"ref43","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1016\/j.micres.2017.03.009","article-title":"Differential stress response of Saccharomyces hybrids revealed by monitoring Hsp104 aggregation and disaggregation","volume":"200","author":"C Kempf","year":"2017","journal-title":"Microbiol Res"},{"issue":"5","key":"ref44","doi-asserted-by":"crossref","first-page":"663","DOI":"10.4161\/auto.6.5.12336","article-title":"Clearance of mutant huntingtin","volume":"6","author":"XJ Li","year":"2010","journal-title":"Autophagy"},{"issue":"13","key":"ref45","doi-asserted-by":"crossref","first-page":"2076","DOI":"10.1091\/mbc.E13-01-0010","article-title":"Ubiquitin conjugation triggers misfolded protein sequestration into quality control foci when Hsp70 chaperone levels are limiting","volume":"24","author":"A Shiber","year":"2013","journal-title":"Mol Biol Cell"},{"issue":"Pt 9","key":"ref46","doi-asserted-by":"crossref","first-page":"1980","DOI":"10.1242\/jcs.141838","article-title":"The requirement for Cdc48\/p97 in nuclear protein quality control degradation depends on the substrate and correlates with substrate insolubility","volume":"127","author":"PS Gallagher","year":"2014","journal-title":"J Cell Sci"},{"key":"ref47","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1146\/annurev-biochem-051910-094049","article-title":"The ubiquitin system, an immense realm","volume":"81","author":"A Varshavsky","year":"2012","journal-title":"Annual review of biochemistry"},{"issue":"5","key":"ref48","doi-asserted-by":"crossref","first-page":"739","DOI":"10.1016\/j.cell.2005.03.024","article-title":"Folding and quality control of the VHL tumor suppressor proceed through distinct chaperone pathways","volume":"121","author":"AJ McClellan","year":"2005","journal-title":"Cell"},{"issue":"3","key":"ref49","doi-asserted-by":"crossref","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":"JW Heck","year":"2010","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"13","key":"ref50","doi-asserted-by":"crossref","first-page":"2117","DOI":"10.1091\/mbc.E10-02-0111","article-title":"A nucleus-based quality control mechanism for cytosolic proteins","volume":"21","author":"R Prasad","year":"2010","journal-title":"Mol Biol Cell"},{"issue":"15","key":"ref51","doi-asserted-by":"crossref","first-page":"5975","DOI":"10.1073\/pnas.1216778110","article-title":"Hsp70 nucleotide exchange factor Fes1 is essential for ubiquitin-dependent degradation of misfolded cytosolic proteins","volume":"110","author":"NK Gowda","year":"2013","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"8","key":"ref52","doi-asserted-by":"crossref","first-page":"1210","DOI":"10.1091\/mbc.E15-10-0697","article-title":"Cytosolic splice isoform of Hsp70 nucleotide exchange factor Fes1 is required for the degradation of misfolded proteins in yeast","volume":"27","author":"NK Gowda","year":"2016","journal-title":"Mol Biol Cell"},{"issue":"3","key":"ref53","doi-asserted-by":"crossref","first-page":"1135","DOI":"10.1016\/j.celrep.2014.09.042","article-title":"A chaperome subnetwork safeguards proteostasis in aging and neurodegenerative disease","volume":"9","author":"M Brehme","year":"2014","journal-title":"Cell Rep"},{"issue":"23","key":"ref54","doi-asserted-by":"crossref","first-page":"3588","DOI":"10.1091\/mbc.E13-06-0315","article-title":"The Hsp70\/90 cochaperone, Sti1, suppresses proteotoxicity by regulating spatial quality control of amyloid-like proteins","volume":"24","author":"KJ Wolfe","year":"2013","journal-title":"Mol Biol Cell"},{"issue":"33","key":"ref55","doi-asserted-by":"crossref","first-page":"23633","DOI":"10.1074\/jbc.C113.481945","article-title":"Heat shock response activation exacerbates inclusion body formation in a cellular model of Huntington disease","volume":"288","author":"K Bersuker","year":"2013","journal-title":"J Biol Chem"},{"key":"ref56","doi-asserted-by":"crossref","first-page":"e00710","DOI":"10.7554\/eLife.00710","article-title":"TRiC\u2019s tricks inhibit huntingtin aggregation","volume":"2","author":"SH Shahmoradian","year":"2013","journal-title":"Elife"},{"issue":"10","key":"ref57","doi-asserted-by":"crossref","first-page":"e46834","DOI":"10.1371\/journal.pone.0046834","article-title":"The role of chaperone-mediated autophagy in huntingtin degradation","volume":"7","author":"L Qi","year":"2012","journal-title":"PLoS One"},{"issue":"9 Pt A","key":"ref58","doi-asserted-by":"crossref","first-page":"1714","DOI":"10.1016\/j.jmb.2016.02.004","article-title":"Mechanisms of Selective Autophagy","volume":"428","author":"G Zaffagnini","year":"2016","journal-title":"J Mol Biol"},{"issue":"12","key":"ref59","doi-asserted-by":"crossref","first-page":"1546","DOI":"10.4161\/auto.7.12.18424","article-title":"GFP-Atg8 protease protection as a tool to monitor autophagosome biogenesis","volume":"7","author":"U Nair","year":"2011","journal-title":"Autophagy"},{"issue":"5766","key":"ref60","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":"T Gidalevitz","year":"2006","journal-title":"Science"},{"issue":"5","key":"ref61","doi-asserted-by":"crossref","first-page":"719","DOI":"10.1083\/jcb.201005144","article-title":"Protein homeostasis and aging in neurodegeneration","volume":"190","author":"PM Douglas","year":"2010","journal-title":"J Cell Biol"},{"issue":"15","key":"ref62","doi-asserted-by":"crossref","first-page":"5706","DOI":"10.1073\/pnas.1402215111","article-title":"Differential ubiquitination and degradation of huntingtin fragments modulated by ubiquitin-protein ligase E3A","volume":"111","author":"KP Bhat","year":"2014","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"3","key":"ref63","doi-asserted-by":"crossref","first-page":"549","DOI":"10.1016\/j.cell.2014.05.048","article-title":"Autophagic clearance of polyQ proteins mediated by ubiquitin-Atg8 adaptors of the conserved CUET protein family","volume":"158","author":"K Lu","year":"2014","journal-title":"Cell"},{"issue":"7208","key":"ref64","doi-asserted-by":"crossref","first-page":"1088","DOI":"10.1038\/nature07195","article-title":"Misfolded proteins partition between two distinct quality control compartments","volume":"454","author":"D Kaganovich","year":"2008","journal-title":"Nature"},{"issue":"1","key":"ref65","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1016\/j.cell.2017.08.009","article-title":"In Situ Architecture and Cellular Interactions of PolyQ Inclusions","volume":"171","author":"FJB Bauerlein","year":"2017","journal-title":"Cell"},{"issue":"Pt 18","key":"ref66","doi-asserted-by":"crossref","first-page":"4173","DOI":"10.1242\/jcs.126102","article-title":"14-3-3 protein targets misfolded chaperone-associated proteins to aggresomes","volume":"126","author":"Z Xu","year":"2013","journal-title":"J Cell Sci"},{"key":"ref67","doi-asserted-by":"crossref","first-page":"2753","DOI":"10.1038\/ncomms3753","article-title":"Soluble forms of polyQ-expanded huntingtin rather than large aggregates cause endoplasmic reticulum stress","volume":"4","author":"J Leitman","year":"2013","journal-title":"Nat Commun"},{"issue":"4","key":"ref68","doi-asserted-by":"crossref","first-page":"285","DOI":"10.4161\/pri.18071","article-title":"Polyglutamine misfolding in yeast: toxic and protective aggregation","volume":"5","author":"ML Duennwald","year":"2011","journal-title":"Prion"},{"issue":"19","key":"ref69","doi-asserted-by":"crossref","first-page":"5424","DOI":"10.1073\/pnas.1604885113","article-title":"Extended survival of misfolded G85R SOD1-linked ALS mice by transgenic expression of chaperone Hsp110","volume":"113","author":"M Nagy","year":"2016","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"19","key":"ref70","doi-asserted-by":"crossref","first-page":"4626","DOI":"10.1128\/MCB.01493-09","article-title":"Loss of Hsp110 leads to age-dependent tau hyperphosphorylation and early accumulation of insoluble amyloid beta","volume":"30","author":"B Eroglu","year":"2010","journal-title":"Mol Cell Biol"},{"issue":"10","key":"ref71","doi-asserted-by":"crossref","first-page":"953","DOI":"10.1002\/(SICI)1097-0061(199807)14:10<953::AID-YEA293>3.0.CO;2-U","article-title":"Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae","volume":"14","author":"MS Longtine","year":"1998","journal-title":"Yeast"},{"issue":"2","key":"ref72","doi-asserted-by":"crossref","first-page":"477","DOI":"10.1091\/mbc.E02-07-0413","article-title":"Chemical genetic analysis of Apg1 reveals a non-kinase role in the induction of autophagy","volume":"14","author":"H Abeliovich","year":"2003","journal-title":"Mol Biol Cell"},{"issue":"8","key":"ref73","doi-asserted-by":"crossref","first-page":"2002","DOI":"10.1523\/JNEUROSCI.4474-04.2005","article-title":"Parkin mediates nonclassical, proteasomal-independent ubiquitination of synphilin-1: implications for Lewy body formation","volume":"25","author":"KL Lim","year":"2005","journal-title":"J Neurosci"}],"container-title":["PLOS ONE"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/dx.plos.org\/10.1371\/journal.pone.0191490","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2020,5,9]],"date-time":"2020-05-09T06:02:02Z","timestamp":1589004122000},"score":1,"resource":{"primary":{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.pone.0191490"}},"subtitle":[],"editor":[{"given":"Jeffrey L","family":"Brodsky","sequence":"first","affiliation":[],"role":[{"role":"editor","vocabulary":"crossref"}]}],"short-title":[],"issued":{"date-parts":[[2018,1,18]]},"references-count":73,"journal-issue":{"issue":"1","published-online":{"date-parts":[[2018,1,18]]}},"URL":"https:\/\/doi.org\/10.1371\/journal.pone.0191490","relation":{},"ISSN":["1932-6203"],"issn-type":[{"value":"1932-6203","type":"electronic"}],"subject":[],"published":{"date-parts":[[2018,1,18]]}}}