{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,8]],"date-time":"2026-10-08T04:44:34Z","timestamp":1791434674876,"version":"4.3.3"},"reference-count":201,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2019,1,1]],"date-time":"2019-01-01T00:00:00Z","timestamp":1546300800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2019,1,1]],"date-time":"2019-01-01T00:00:00Z","timestamp":1546300800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2018,11,28]],"date-time":"2018-11-28T00:00:00Z","timestamp":1543363200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"FCT \u2013 Funda\u00e7\u00e3o para a Ci\u00eancia e a Tecnologia, Portugal","award":["P2020-PTDC\/NEU-NMC\/0412\/2014"],"award-info":[{"award-number":["P2020-PTDC\/NEU-NMC\/0412\/2014"]}]},{"name":"FCT \u2013 Funda\u00e7\u00e3o para a Ci\u00eancia e a Tecnologia, Portugal","award":["3599-PPCDT"],"award-info":[{"award-number":["3599-PPCDT"]}]},{"name":"FCT \u2013 Funda\u00e7\u00e3o para a Ci\u00eancia e a Tecnologia, Portugal","award":["UID\/QUI\/50006\/2013"],"award-info":[{"award-number":["UID\/QUI\/50006\/2013"]}]},{"DOI":"10.13039\/501100000780","name":"European Union","doi-asserted-by":"crossref","award":["POCI-01-0145-FEDER-016577"],"award-info":[{"award-number":["POCI-01-0145-FEDER-016577"]}],"id":[{"id":"10.13039\/501100000780","id-type":"DOI","asserted-by":"crossref"}]},{"name":"BBSRC, UK","award":["BB\/P018726\/1"],"award-info":[{"award-number":["BB\/P018726\/1"]}]},{"name":"Michael J Fox Foundation","award":["12159.01"],"award-info":[{"award-number":["12159.01"]}]},{"name":"Kephalos Foundation"}],"content-domain":{"domain":["clinicalkey.com","clinicalkey.com.au","clinicalkey.es","clinicalkey.fr","clinicalkey.jp","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Ageing Research Reviews"],"published-print":{"date-parts":[[2019,1]]},"DOI":"10.1016\/j.arr.2018.11.006","type":"journal-article","created":{"date-parts":[[2018,11,28]],"date-time":"2018-11-28T04:46:15Z","timestamp":1543380375000},"page":"92-103","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":88,"special_numbering":"C","title":["Targeting the proteostasis network in Huntington\u2019s disease"],"prefix":"10.1016","volume":"49","author":[{"given":"T\u00e2nia R.","family":"Soares","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sara D.","family":"Reis","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1627-6795","authenticated-orcid":false,"given":"Br\u00edgida R.","family":"Pinho","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michael R.","family":"Duchen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6040-5355","authenticated-orcid":false,"given":"Jorge M.A.","family":"Oliveira","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.arr.2018.11.006_bib0005","doi-asserted-by":"crossref","first-page":"1089","DOI":"10.1146\/annurev-biochem-060809-095203","article-title":"Regulation of HSF1 function in the heat stress response: implications in aging and disease","volume":"80","author":"Anckar","year":"2011","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.arr.2018.11.006_bib0010","doi-asserted-by":"crossref","first-page":"374","DOI":"10.1038\/nchembio.1230","article-title":"Chemical modulation of chaperone-mediated autophagy by retinoic acid derivatives","volume":"9","author":"Anguiano","year":"2013","journal-title":"Nat. Chem. Biol."},{"key":"10.1016\/j.arr.2018.11.006_bib0015","doi-asserted-by":"crossref","first-page":"28","DOI":"10.1016\/j.tibs.2016.09.008","article-title":"Emerging mechanisms in initiating and terminating autophagy","volume":"42","author":"Antonioli","year":"2017","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.arr.2018.11.006_bib0020","doi-asserted-by":"crossref","first-page":"19238","DOI":"10.1074\/jbc.M117.782300","article-title":"Post-translational modifications clustering within proteolytic domains decrease mutant huntingtin toxicity","volume":"292","author":"Arbez","year":"2017","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.arr.2018.11.006_bib0025","doi-asserted-by":"crossref","first-page":"523","DOI":"10.1038\/nn.3380","article-title":"NUB1 snubs huntingtin toxicity","volume":"16","author":"Aron","year":"2013","journal-title":"Nat. Neurosci."},{"key":"10.1016\/j.arr.2018.11.006_bib0030","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.expneurol.2011.12.013","article-title":"Protein aggregates in Huntington\u2019s disease","volume":"238","author":"Arrasate","year":"2012","journal-title":"Exp. Neurol."},{"key":"10.1016\/j.arr.2018.11.006_bib0035","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.arr.2018.11.006_bib0040","doi-asserted-by":"crossref","first-page":"108","DOI":"10.1038\/nature22078","article-title":"Polyglutamine tracts regulate beclin 1-dependent autophagy","volume":"545","author":"Ashkenazi","year":"2017","journal-title":"Nature"},{"key":"10.1016\/j.arr.2018.11.006_bib0045","doi-asserted-by":"crossref","first-page":"453","DOI":"10.1038\/nchembio.582","article-title":"Kinase inhibitors modulate huntingtin cell localization and toxicity","volume":"7","author":"Atwal","year":"2011","journal-title":"Nat. Chem. Biol."},{"key":"10.1016\/j.arr.2018.11.006_bib0050","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0053606","article-title":"Attenuation of Rhes activity significantly delays the appearance of behavioral symptoms in a mouse model of Huntington\u2019s disease","volume":"8","author":"Baiamonte","year":"2013","journal-title":"PLoS One"},{"key":"10.1016\/j.arr.2018.11.006_bib0055","doi-asserted-by":"crossref","first-page":"1406","DOI":"10.1074\/jbc.M111.294801","article-title":"A screen for enhancers of clearance identifies huntingtin as a heat shock protein 90 (Hsp90) client protein","volume":"287","author":"Baldo","year":"2012","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.arr.2018.11.006_bib0060","doi-asserted-by":"crossref","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":"10.1016\/j.arr.2018.11.006_bib0065","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":"Bauerlein","year":"2017","journal-title":"Cell"},{"key":"10.1016\/j.arr.2018.11.006_bib0070","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1083\/jcb.201511024","article-title":"Protein misfolding specifies recruitment to cytoplasmic inclusion bodies","volume":"213","author":"Bersuker","year":"2016","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.arr.2018.11.006_bib0075","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":"Bhat","year":"2014","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.arr.2018.11.006_bib0080","doi-asserted-by":"crossref","first-page":"583","DOI":"10.1016\/j.devcel.2017.02.020","article-title":"The putative Drp1 inhibitor mdivi-1 is a reversible mitochondrial complex I inhibitor that modulates reactive oxygen species","volume":"40","author":"Bordt","year":"2017","journal-title":"Dev. Cell"},{"key":"10.1016\/j.arr.2018.11.006_bib0085","doi-asserted-by":"crossref","first-page":"3763","DOI":"10.1093\/hmg\/ddx260","article-title":"Protein phosphatase 1 regulates huntingtin exon 1 aggregation and toxicity","volume":"26","author":"Branco-Santos","year":"2017","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.arr.2018.11.006_bib0090","doi-asserted-by":"crossref","first-page":"441","DOI":"10.1016\/j.tcb.2017.02.007","article-title":"With the help of MOM: mitochondrial contributions to cellular quality control","volume":"27","author":"Braun","year":"2017","journal-title":"Trends Cell Biol."},{"key":"10.1016\/j.arr.2018.11.006_bib0095","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":"Brehme","year":"2014","journal-title":"Cell Rep."},{"key":"10.1016\/j.arr.2018.11.006_bib0100","doi-asserted-by":"crossref","first-page":"E10809","DOI":"10.1073\/pnas.1705372114","article-title":"Phosphorylation of huntingtin at residue T3 is decreased in Huntington\u2019s disease and modulates mutant huntingtin protein conformation","volume":"114","author":"Cariulo","year":"2017","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.arr.2018.11.006_bib0105","doi-asserted-by":"crossref","first-page":"388","DOI":"10.1016\/j.nbd.2005.12.007","article-title":"Mutant huntingtin aggregates impair mitochondrial movement and trafficking in cortical neurons","volume":"22","author":"Chang","year":"2006","journal-title":"Neurobiol. Dis."},{"key":"10.1016\/j.arr.2018.11.006_bib0110","doi-asserted-by":"crossref","first-page":"1063","DOI":"10.1016\/j.bbrc.2016.08.042","article-title":"Mitochondrial fragmentation in neuronal degeneration: toward an understanding of HD striatal susceptibility","volume":"483","author":"Cherubini","year":"2017","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.arr.2018.11.006_bib0115","doi-asserted-by":"crossref","first-page":"5202","DOI":"10.1002\/anie.201611750","article-title":"Mutant exon1 huntingtin aggregation is regulated by T3 phosphorylation-induced structural changes and crosstalk between T3 phosphorylation and acetylation at K6","volume":"56","author":"Chiki","year":"2017","journal-title":"Angew. Chem. Int. Ed. Engl."},{"key":"10.1016\/j.arr.2018.11.006_bib0120","doi-asserted-by":"crossref","first-page":"611","DOI":"10.1096\/fj.14-252189","article-title":"20S proteasome activation promotes life span extension and resistance to proteotoxicity in Caenorhabditis elegans","volume":"29","author":"Chondrogianni","year":"2015","journal-title":"FASEB J."},{"key":"10.1016\/j.arr.2018.11.006_bib0125","doi-asserted-by":"crossref","first-page":"1127","DOI":"10.1042\/BCJ20160762","article-title":"Chemical approaches to targeted protein degradation through modulation of the ubiquitin-proteasome pathway","volume":"474","author":"Collins","year":"2017","journal-title":"Biochem. J."},{"key":"10.1016\/j.arr.2018.11.006_bib0130","doi-asserted-by":"crossref","first-page":"963","DOI":"10.1016\/j.drudis.2014.02.014","article-title":"The many faces of autophagy dysfunction in Huntington\u2019s disease: from mechanism to therapy","volume":"19","author":"Cortes","year":"2014","journal-title":"Drug Discov. Today"},{"key":"10.1016\/j.arr.2018.11.006_bib0135","doi-asserted-by":"crossref","first-page":"379","DOI":"10.1038\/nrneurol.2016.81","article-title":"The mTOR signalling cascade: paving new roads to cure neurological disease","volume":"12","author":"Crino","year":"2016","journal-title":"Nat. Rev. Neurol."},{"key":"10.1016\/j.arr.2018.11.006_bib0140","doi-asserted-by":"crossref","first-page":"5070","DOI":"10.1038\/s41598-017-05336-7","article-title":"Polyglutamine expansion affects huntingtin conformation in multiple Huntington\u2019s disease models","volume":"7","author":"Daldin","year":"2017","journal-title":"Sci. Rep."},{"key":"10.1016\/j.arr.2018.11.006_bib0145","doi-asserted-by":"crossref","first-page":"52","DOI":"10.1016\/j.bbadis.2009.07.012","article-title":"Mitochondria in Huntington\u2019s disease","volume":"1802","author":"Damiano","year":"2010","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.arr.2018.11.006_bib0150","doi-asserted-by":"crossref","first-page":"70","DOI":"10.3389\/fnmol.2014.00070","article-title":"The ubiquitin-proteasome system in neurodegenerative diseases: precipitating factor, yet part of the solution","volume":"7","author":"Dantuma","year":"2014","journal-title":"Front. Mol. Neurosci."},{"key":"10.1016\/j.arr.2018.11.006_bib0155","doi-asserted-by":"crossref","first-page":"982","DOI":"10.1016\/j.cell.2018.05.057","article-title":"A Single-cell transcriptome atlas of the aging drosophila brain","volume":"174","author":"Davie","year":"2018","journal-title":"Cell"},{"key":"10.1016\/j.arr.2018.11.006_bib0160","doi-asserted-by":"crossref","first-page":"10263","DOI":"10.1074\/jbc.M115.695825","article-title":"Loss of mitochondrial function impairs lysosomes","volume":"291","author":"Demers-Lamarche","year":"2016","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.arr.2018.11.006_bib0165","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.arr.2018.11.006_bib0170","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0004637","article-title":"Normal aging modulates the neurotoxicity of mutant huntingtin","volume":"4","author":"Diguet","year":"2009","journal-title":"PLoS One"},{"key":"10.1016\/j.arr.2018.11.006_bib0175","doi-asserted-by":"crossref","first-page":"267","DOI":"10.3233\/JHD-170264","article-title":"Towards an understanding of energy impairment in Huntington\u2019s disease brain","volume":"6","author":"Dubinsky","year":"2017","journal-title":"J. Huntingtons Dis."},{"key":"10.1016\/j.arr.2018.11.006_bib0180","doi-asserted-by":"crossref","first-page":"777","DOI":"10.18632\/aging.100939","article-title":"Aging causes decreased resistance to multiple stresses and a failure to activate specific stress response pathways","volume":"8","author":"Dues","year":"2016","journal-title":"Aging (Albany NY)"},{"key":"10.1016\/j.arr.2018.11.006_bib0185","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1016\/j.molcel.2015.05.031","article-title":"Small molecule inhibition of the autophagy kinase ULK1 and identification of ULK1 substrates","volume":"59","author":"Egan","year":"2015","journal-title":"Mol. Cell"},{"key":"10.1016\/j.arr.2018.11.006_bib0190","doi-asserted-by":"crossref","first-page":"270","DOI":"10.1007\/s13311-012-0112-2","article-title":"Huntington\u2019s disease and the striatal medium spiny neuron: cell-autonomous and non-cell-autonomous mechanisms of disease","volume":"9","author":"Ehrlich","year":"2012","journal-title":"Neurotherapeutics"},{"key":"10.1016\/j.arr.2018.11.006_bib0195","doi-asserted-by":"crossref","first-page":"475","DOI":"10.1177\/1073858410390378","article-title":"Small changes, big impact: posttranslational modifications and function of huntingtin in Huntington disease","volume":"17","author":"Ehrnhoefer","year":"2011","journal-title":"Neuroscientist"},{"key":"10.1016\/j.arr.2018.11.006_bib0200","doi-asserted-by":"crossref","first-page":"2255","DOI":"10.15252\/embj.201490808","article-title":"Huntingtin proteolysis releases non-polyQ fragments that cause toxicity through dynamin 1 dysregulation","volume":"34","author":"El-Daher","year":"2015","journal-title":"EMBO J."},{"key":"10.1016\/j.arr.2018.11.006_bib0205","doi-asserted-by":"crossref","first-page":"114","DOI":"10.1016\/j.bbamcr.2013.06.027","article-title":"Regulation of proteolysis by human deubiquitinating enzymes","volume":"1843","author":"Eletr","year":"2014","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.arr.2018.11.006_bib0210","first-page":"3","article-title":"Huntington\u2019s disease","author":"Finkbeiner","year":"2011","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"10.1016\/j.arr.2018.11.006_bib0215","doi-asserted-by":"crossref","first-page":"342","DOI":"10.3389\/fnins.2018.00342","article-title":"Mitochondrial quality control in neurodegenerative diseases: focus on Parkinson\u2019s disease and Huntington\u2019s disease","volume":"12","author":"Franco-Iborra","year":"2018","journal-title":"Front. Neurosci."},{"key":"10.1016\/j.arr.2018.11.006_bib0220","doi-asserted-by":"crossref","first-page":"1350","DOI":"10.1038\/s41593-018-0221-2","article-title":"Selective vulnerability in neurodegenerative diseases","volume":"21","author":"Fu","year":"2018","journal-title":"Nat. Neurosci."},{"key":"10.1016\/j.arr.2018.11.006_bib0225","doi-asserted-by":"crossref","first-page":"7454","DOI":"10.1523\/JNEUROSCI.6379-11.2012","article-title":"Caspase-6 activity in a BACHD mouse modulates steady-state levels of mutant huntingtin protein but is not necessary for production of a 586 amino acid proteolytic fragment","volume":"32","author":"Gafni","year":"2012","journal-title":"J. Neurosci."},{"key":"10.1016\/j.arr.2018.11.006_bib0230","doi-asserted-by":"crossref","first-page":"48","DOI":"10.1016\/j.neuron.2017.03.027","article-title":"Polyglutamine-expanded huntingtin exacerbates age-related disruption of nuclear integrity and nucleocytoplasmic transport","volume":"94","author":"Gasset-Rosa","year":"2017","journal-title":"Neuron"},{"key":"10.1016\/j.arr.2018.11.006_bib0235","doi-asserted-by":"crossref","DOI":"10.1126\/scitranslmed.aag2210","article-title":"Mitochondrial pyruvate carrier regulates autophagy, inflammation, and neurodegeneration in experimental models of Parkinson\u2019s disease","volume":"8","author":"Ghosh","year":"2016","journal-title":"Sci. Transl. Med."},{"key":"10.1016\/j.arr.2018.11.006_bib0240","doi-asserted-by":"crossref","first-page":"2690","DOI":"10.1038\/onc.2013.228","article-title":"Mitochondrial matrix proteases as novel therapeutic targets in malignancy","volume":"33","author":"Goard","year":"2014","journal-title":"Oncogene"},{"key":"10.1016\/j.arr.2018.11.006_bib0245","doi-asserted-by":"crossref","first-page":"14405","DOI":"10.1038\/ncomms14405","article-title":"Abnormal degradation of the neuronal stress-protective transcription factor HSF1 in Huntington\u2019s disease","volume":"8","author":"Gomez-Pastor","year":"2017","journal-title":"Nat. Commun."},{"key":"10.1016\/j.arr.2018.11.006_bib0250","doi-asserted-by":"crossref","first-page":"1179","DOI":"10.1016\/j.cell.2006.04.026","article-title":"Cleavage at the caspase-6 site is required for neuronal dysfunction and degeneration due to mutant huntingtin","volume":"125","author":"Graham","year":"2006","journal-title":"Cell"},{"key":"10.1016\/j.arr.2018.11.006_bib0255","doi-asserted-by":"crossref","first-page":"15019","DOI":"10.1523\/JNEUROSCI.2071-10.2010","article-title":"Cleavage at the 586 amino acid caspase-6 site in mutant huntingtin influences caspase-6 activation in vivo","volume":"30","author":"Graham","year":"2010","journal-title":"J. Neurosci."},{"key":"10.1016\/j.arr.2018.11.006_bib0260","doi-asserted-by":"crossref","first-page":"412","DOI":"10.1038\/nchembio.604","article-title":"Huntington\u2019s disease: flipping a switch on huntingtin","volume":"7","author":"Greiner","year":"2011","journal-title":"Nat. Chem. Biol."},{"key":"10.1016\/j.arr.2018.11.006_bib0265","doi-asserted-by":"crossref","first-page":"913","DOI":"10.1007\/s12192-014-0516-5","article-title":"The oxidation of HSP70 is associated with functional impairment and lack of stimulatory capacity","volume":"19","author":"Grunwald","year":"2014","journal-title":"Cell Stress Chaperones"},{"key":"10.1016\/j.arr.2018.11.006_bib0270","doi-asserted-by":"crossref","first-page":"2484","DOI":"10.1016\/j.bbadis.2015.08.012","article-title":"HDAC6 inhibition induces mitochondrial fusion, autophagic flux and reduces diffuse mutant huntingtin in striatal neurons","volume":"1852","author":"Guedes-Dias","year":"2015","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.arr.2018.11.006_bib0275","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1016\/j.nbd.2015.09.008","article-title":"Mitochondrial dynamics and quality control in Huntington\u2019s disease","volume":"90","author":"Guedes-Dias","year":"2016","journal-title":"Neurobiol. Dis."},{"key":"10.1016\/j.arr.2018.11.006_bib0280","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1038\/nature25502","article-title":"The cryo-electron microscopy structure of huntingtin","volume":"555","author":"Guo","year":"2018","journal-title":"Nature"},{"key":"10.1016\/j.arr.2018.11.006_bib0285","doi-asserted-by":"crossref","first-page":"3953","DOI":"10.1093\/hmg\/ddr314","article-title":"Novel mechanism of Hsp70 chaperone-mediated prevention of polyglutamine aggregates in a cellular model of Huntington disease","volume":"20","author":"Guzhova","year":"2011","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.arr.2018.11.006_bib0290","doi-asserted-by":"crossref","first-page":"656","DOI":"10.1016\/j.cell.2010.04.009","article-title":"Mitochondria supply membranes for autophagosome biogenesis during starvation","volume":"141","author":"Hailey","year":"2010","journal-title":"Cell"},{"key":"10.1016\/j.arr.2018.11.006_bib0295","doi-asserted-by":"crossref","first-page":"389","DOI":"10.1038\/nature11910","article-title":"Autophagosomes form at ER-mitochondria contact sites","volume":"495","author":"Hamasaki","year":"2013","journal-title":"Nature"},{"key":"10.1016\/j.arr.2018.11.006_bib0300","doi-asserted-by":"crossref","first-page":"507","DOI":"10.1016\/j.bbagrm.2008.05.008","article-title":"Polyglutamine gene function and dysfunction in the ageing brain","volume":"1779","author":"Hands","year":"2008","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.arr.2018.11.006_bib0305","doi-asserted-by":"crossref","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":"10.1016\/j.arr.2018.11.006_bib0310","doi-asserted-by":"crossref","first-page":"1389","DOI":"10.1093\/hmg\/ddh144","article-title":"Progressive decrease in chaperone protein levels in a mouse model of Huntington\u2019s disease and induction of stress proteins as a therapeutic approach","volume":"13","author":"Hay","year":"2004","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.arr.2018.11.006_bib0315","article-title":"Cytoplasmic ubiquitin-specific protease 19 (USP19) modulates aggregation of polyglutamine-expanded Ataxin-3 and huntingtin through the HSP90 chaperone","volume":"11","author":"He","year":"2016","journal-title":"PLoS One"},{"key":"10.1016\/j.arr.2018.11.006_bib0320","doi-asserted-by":"crossref","first-page":"14797","DOI":"10.1038\/s41598-017-13711-7","article-title":"HSP90 recognizes the N-terminus of huntingtin involved in regulation of huntingtin aggregation by USP19","volume":"7","author":"He","year":"2017","journal-title":"Sci. Rep."},{"key":"10.1016\/j.arr.2018.11.006_bib0325","doi-asserted-by":"crossref","first-page":"573","DOI":"10.1083\/jcb.201110093","article-title":"Indirect inhibition of 26S proteasome activity in a cellular model of Huntington\u2019s disease","volume":"196","author":"Hipp","year":"2012","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.arr.2018.11.006_bib0330","doi-asserted-by":"crossref","first-page":"506","DOI":"10.1016\/j.tcb.2014.05.003","article-title":"Proteostasis impairment in protein-misfolding and -aggregation diseases","volume":"24","author":"Hipp","year":"2014","journal-title":"Trends Cell Biol."},{"key":"10.1016\/j.arr.2018.11.006_bib0335","doi-asserted-by":"crossref","first-page":"935","DOI":"10.1016\/j.cell.2016.07.001","article-title":"UBQLN2 mediates autophagy-independent protein aggregate clearance by the proteasome","volume":"166","author":"Hjerpe","year":"2016","journal-title":"Cell"},{"key":"10.1016\/j.arr.2018.11.006_bib0340","doi-asserted-by":"crossref","first-page":"1485","DOI":"10.18632\/aging.101005","article-title":"Huntington\u2019s disease accelerates epigenetic aging of human brain and disrupts DNA methylation levels","volume":"8","author":"Horvath","year":"2016","journal-title":"Aging (Albany NY)"},{"key":"10.1016\/j.arr.2018.11.006_bib0345","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1146\/annurev-biochem-061516-044820","article-title":"Mechanisms of autophagy initiation","volume":"86","author":"Hurley","year":"2017","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.arr.2018.11.006_bib0350","first-page":"5","article-title":"Expanding proteostasis by membrane trafficking networks","author":"Hutt","year":"2013","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"10.1016\/j.arr.2018.11.006_bib0355","doi-asserted-by":"crossref","first-page":"5928","DOI":"10.1093\/hmg\/ddu317","article-title":"Ubiquitin-specific protease-14 reduces cellular aggregates and protects against mutant huntingtin-induced cell degeneration: involvement of the proteasome and ER stress-activated kinase IRE1alpha","volume":"23","author":"Hyrskyluoto","year":"2014","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.arr.2018.11.006_bib0360","doi-asserted-by":"crossref","first-page":"30","DOI":"10.1111\/j.1460-9568.2008.06323.x","article-title":"Omi\/HtrA2 is relevant to the selective vulnerability of striatal neurons in Huntington\u2019s disease","volume":"28","author":"Inagaki","year":"2008","journal-title":"Eur. J. Neurosci."},{"key":"10.1016\/j.arr.2018.11.006_bib0365","doi-asserted-by":"crossref","first-page":"2972","DOI":"10.1172\/JCI59190","article-title":"Shock and awe: unleashing the heat shock response to treat Huntington disease","volume":"121","author":"Jackrel","year":"2011","journal-title":"J. Clin. Invest."},{"key":"10.1016\/j.arr.2018.11.006_bib0370","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.arr.2018.11.006_bib0375","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1016\/j.neuroscience.2016.02.054","article-title":"Gene therapy by proteasome activator, PA28gamma, improves motor coordination and proteasome function in Huntington\u2019s disease YAC128 mice","volume":"324","author":"Jeon","year":"2016","journal-title":"Neuroscience"},{"key":"10.1016\/j.arr.2018.11.006_bib0380","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.arr.2018.11.006_bib0385","doi-asserted-by":"crossref","first-page":"251","DOI":"10.3389\/fnmol.2017.00251","article-title":"Cellular chaperones As therapeutic targets in ALS to restore protein homeostasis and improve cellular function","volume":"10","author":"Kalmar","year":"2017","journal-title":"Front. Mol. Neurosci."},{"key":"10.1016\/j.arr.2018.11.006_bib0390","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1016\/j.tibs.2014.12.002","article-title":"Hsp90 interaction with clients","volume":"40","author":"Karagoz","year":"2015","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.arr.2018.11.006_bib0395","doi-asserted-by":"crossref","first-page":"R318","DOI":"10.1016\/j.cub.2017.02.061","article-title":"The cytoskeleton-autophagy connection","volume":"27","author":"Kast","year":"2017","journal-title":"Curr. Biol."},{"key":"10.1016\/j.arr.2018.11.006_bib0400","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1038\/nm0204-123","article-title":"Sweet relief for Huntington disease","volume":"10","author":"Katsuno","year":"2004","journal-title":"Nat. Med."},{"key":"10.1016\/j.arr.2018.11.006_bib0405","doi-asserted-by":"crossref","first-page":"1406","DOI":"10.1038\/nm.4001","article-title":"Proteostasis and aging","volume":"21","author":"Kaushik","year":"2015","journal-title":"Nat. Med."},{"key":"10.1016\/j.arr.2018.11.006_bib0410","doi-asserted-by":"crossref","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":"10.1016\/j.arr.2018.11.006_bib0415","doi-asserted-by":"crossref","DOI":"10.1002\/jcb.26887","article-title":"Protein kinase C activator bryostatin-1 modulates proteasome function","author":"Khan","year":"2018","journal-title":"J. Cell. Biochem."},{"key":"10.1016\/j.arr.2018.11.006_bib0420","doi-asserted-by":"crossref","first-page":"132","DOI":"10.1038\/ncb2152","article-title":"AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1","volume":"13","author":"Kim","year":"2011","journal-title":"Nat. Cell Biol."},{"key":"10.1016\/j.arr.2018.11.006_bib0425","doi-asserted-by":"crossref","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":"10.1016\/j.arr.2018.11.006_bib0430","doi-asserted-by":"crossref","first-page":"1539","DOI":"10.1016\/j.cell.2016.08.027","article-title":"Lipid biosynthesis coordinates a mitochondrial-to-cytosolic stress response","volume":"166","author":"Kim","year":"2016","journal-title":"Cell"},{"key":"10.1016\/j.arr.2018.11.006_bib0435","doi-asserted-by":"crossref","first-page":"2334","DOI":"10.15252\/embj.201591711","article-title":"Proteotoxic stress and ageing triggers the loss of redox homeostasis across cellular compartments","volume":"34","author":"Kirstein","year":"2015","journal-title":"EMBO J."},{"key":"10.1016\/j.arr.2018.11.006_bib0440","doi-asserted-by":"crossref","first-page":"18492","DOI":"10.1523\/JNEUROSCI.3219-11.2011","article-title":"Constitutive upregulation of chaperone-mediated autophagy in Huntington\u2019s disease","volume":"31","author":"Koga","year":"2011","journal-title":"J. Neurosci."},{"key":"10.1016\/j.arr.2018.11.006_bib0445","doi-asserted-by":"crossref","first-page":"2886","DOI":"10.1038\/s41467-018-05320-3","article-title":"The ubiquitin ligase UBR5 suppresses proteostasis collapse in pluripotent stem cells from Huntington\u2019s disease patients","volume":"9","author":"Koyuncu","year":"2018","journal-title":"Nat. Commun."},{"key":"10.1016\/j.arr.2018.11.006_bib0450","doi-asserted-by":"crossref","first-page":"3585","DOI":"10.1172\/JCI80339","article-title":"Serine 421 regulates mutant huntingtin toxicity and clearance in mice","volume":"126","author":"Kratter","year":"2016","journal-title":"J. Clin. Invest."},{"key":"10.1016\/j.arr.2018.11.006_bib0455","doi-asserted-by":"crossref","first-page":"435","DOI":"10.1146\/annurev-biochem-060614-033955","article-title":"The biology of proteostasis in aging and disease","volume":"84","author":"Labbadia","year":"2015","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.arr.2018.11.006_bib0460","doi-asserted-by":"crossref","first-page":"3306","DOI":"10.1172\/JCI57413","article-title":"Altered chromatin architecture underlies progressive impairment of the heat shock response in mouse models of Huntington disease","volume":"121","author":"Labbadia","year":"2011","journal-title":"J. Clin. Invest."},{"key":"10.1016\/j.arr.2018.11.006_bib0465","doi-asserted-by":"crossref","first-page":"1481","DOI":"10.1016\/j.celrep.2017.10.038","article-title":"Mitochondrial stress restores the heat shock response and prevents proteostasis collapse during aging","volume":"21","author":"Labbadia","year":"2017","journal-title":"Cell Rep."},{"key":"10.1016\/j.arr.2018.11.006_bib0470","doi-asserted-by":"crossref","first-page":"5483","DOI":"10.1016\/j.bmc.2015.07.034","article-title":"Discovery and structure of a new inhibitor scaffold of the autophagy initiating kinase ULK1","volume":"23","author":"Lazarus","year":"2015","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.arr.2018.11.006_bib0475","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1021\/cb500835z","article-title":"Structure of the human autophagy initiating kinase ULK1 in complex with potent inhibitors","volume":"10","author":"Lazarus","year":"2015","journal-title":"ACS Chem. Biol."},{"key":"10.1016\/j.arr.2018.11.006_bib0480","doi-asserted-by":"crossref","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":"10.1016\/j.arr.2018.11.006_bib0485","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1093\/hmg\/ddr445","article-title":"IRE1 plays an essential role in ER stress-mediated aggregation of mutant huntingtin via the inhibition of autophagy flux","volume":"21","author":"Lee","year":"2012","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.arr.2018.11.006_bib0490","doi-asserted-by":"crossref","first-page":"303","DOI":"10.1016\/j.neuron.2014.12.019","article-title":"Reinstating aberrant mTORC1 activity in Huntington\u2019s disease mice improves disease phenotypes","volume":"85","author":"Lee","year":"2015","journal-title":"Neuron"},{"key":"10.1016\/j.arr.2018.11.006_bib0495","doi-asserted-by":"crossref","first-page":"398","DOI":"10.1038\/nature17433","article-title":"USP14 deubiquitinates proteasome-bound substrates that are ubiquitinated at multiple sites","volume":"532","author":"Lee","year":"2016","journal-title":"Nature"},{"key":"10.1016\/j.arr.2018.11.006_bib0500","doi-asserted-by":"crossref","first-page":"725","DOI":"10.1016\/j.chembiol.2017.05.010","article-title":"Proteasome activation by small molecules","volume":"24","author":"Leestemaker","year":"2017","journal-title":"Cell Chem. Biol."},{"key":"10.1016\/j.arr.2018.11.006_bib0505","doi-asserted-by":"crossref","first-page":"4","DOI":"10.1016\/j.nbd.2010.11.018","article-title":"Proteasomal dysfunction in aging and Huntington disease","volume":"43","author":"Li","year":"2011","journal-title":"Neurobiol. Dis."},{"key":"10.1016\/j.arr.2018.11.006_bib0510","doi-asserted-by":"crossref","first-page":"3339","DOI":"10.1007\/s00018-014-1558-7","article-title":"Altered proteostasis in aging and heat shock response in C. elegans revealed by analysis of the global and de novo synthesized proteome","volume":"71","author":"Liang","year":"2014","journal-title":"Cell. Mol. Life Sci."},{"key":"10.1016\/j.arr.2018.11.006_bib0515","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1016\/j.cmet.2013.03.002","article-title":"Mitochondrial dynamics in the regulation of nutrient utilization and energy expenditure","volume":"17","author":"Liesa","year":"2013","journal-title":"Cell Metab."},{"key":"10.1016\/j.arr.2018.11.006_bib0520","doi-asserted-by":"crossref","first-page":"562","DOI":"10.1038\/nn.3367","article-title":"Identification of NUB1 as a suppressor of mutant Huntington toxicity via enhanced protein clearance","volume":"16","author":"Lu","year":"2013","journal-title":"Nat. Neurosci."},{"key":"10.1016\/j.arr.2018.11.006_bib0525","doi-asserted-by":"crossref","first-page":"7652","DOI":"10.1007\/s12035-018-0900-8","article-title":"Herp promotes degradation of mutant huntingtin: involvement of the proteasome and molecular chaperones","volume":"55","author":"Luo","year":"2018","journal-title":"Mol. Neurobiol."},{"key":"10.1016\/j.arr.2018.11.006_bib0530","doi-asserted-by":"crossref","first-page":"7308","DOI":"10.1093\/hmg\/ddv429","article-title":"Mitochondrial division inhibitor 1 protects against mutant huntingtin-induced abnormal mitochondrial dynamics and neuronal damage in Huntington\u2019s disease","volume":"24","author":"Manczak","year":"2015","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.arr.2018.11.006_bib0535","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0044457","article-title":"Fragments of HdhQ150 mutant huntingtin form a soluble oligomer pool that declines with aggregate deposition upon aging","volume":"7","author":"Marcellin","year":"2012","journal-title":"PLoS One"},{"key":"10.1016\/j.arr.2018.11.006_bib0540","doi-asserted-by":"crossref","first-page":"218","DOI":"10.3389\/fncel.2014.00218","article-title":"Proteostasis in striatal cells and selective neurodegeneration in Huntington\u2019s disease","volume":"8","author":"Margulis","year":"2014","journal-title":"Front. Cell. Neurosci."},{"key":"10.1016\/j.arr.2018.11.006_bib0545","doi-asserted-by":"crossref","first-page":"26","DOI":"10.1016\/j.tins.2014.09.003","article-title":"Autophagy in Huntington disease and huntingtin in autophagy","volume":"38","author":"Martin","year":"2015","journal-title":"Trends Neurosci."},{"key":"10.1016\/j.arr.2018.11.006_bib0550","doi-asserted-by":"crossref","first-page":"567","DOI":"10.1038\/nn.2528","article-title":"Cargo recognition failure is responsible for inefficient autophagy in Huntington\u2019s disease","volume":"13","author":"Martinez-Vicente","year":"2010","journal-title":"Nat. Neurosci."},{"key":"10.1016\/j.arr.2018.11.006_bib0555","doi-asserted-by":"crossref","first-page":"2302","DOI":"10.1089\/ars.2013.5802","article-title":"The ubiquitin-proteasome system in neurodegeneration","volume":"21","author":"McKinnon","year":"2014","journal-title":"Antioxid. Redox Signal."},{"key":"10.1016\/j.arr.2018.11.006_bib0560","doi-asserted-by":"crossref","first-page":"411","DOI":"10.1007\/s00401-015-1508-y","article-title":"Prion-mediated neurodegeneration is associated with early impairment of the ubiquitin-proteasome system","volume":"131","author":"McKinnon","year":"2016","journal-title":"Acta Neuropathol."},{"key":"10.1016\/j.arr.2018.11.006_bib0565","doi-asserted-by":"crossref","first-page":"15703","DOI":"10.1523\/JNEUROSCI.0552-11.2011","article-title":"The mitochondria-targeted antioxidant MitoQ prevents loss of spatial memory retention and early neuropathology in a transgenic mouse model of Alzheimer\u2019s disease","volume":"31","author":"McManus","year":"2011","journal-title":"J. Neurosci."},{"key":"10.1016\/j.arr.2018.11.006_bib0570","doi-asserted-by":"crossref","first-page":"4206","DOI":"10.1523\/JNEUROSCI.3730-12.2013","article-title":"Rhes deletion is neuroprotective in the 3-nitropropionic acid model of Huntington\u2019s disease","volume":"33","author":"Mealer","year":"2013","journal-title":"J. Neurosci."},{"key":"10.1016\/j.arr.2018.11.006_bib0575","doi-asserted-by":"crossref","first-page":"3547","DOI":"10.1074\/jbc.M113.536912","article-title":"Rhes, a striatal-selective protein implicated in Huntington disease, binds beclin-1 and activates autophagy","volume":"289","author":"Mealer","year":"2014","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.arr.2018.11.006_bib0580","doi-asserted-by":"crossref","first-page":"345","DOI":"10.1038\/nrn3961","article-title":"Compromised autophagy and neurodegenerative diseases","volume":"16","author":"Menzies","year":"2015","journal-title":"Nat. Rev. Neurosci."},{"key":"10.1016\/j.arr.2018.11.006_bib0585","doi-asserted-by":"crossref","first-page":"651","DOI":"10.1016\/j.neuron.2017.09.055","article-title":"Mitostasis in neurons: maintaining mitochondria in an extended cellular architecture","volume":"96","author":"Misgeld","year":"2017","journal-title":"Neuron"},{"key":"10.1016\/j.arr.2018.11.006_bib0590","doi-asserted-by":"crossref","first-page":"4398","DOI":"10.1074\/jbc.M806269200","article-title":"Single neuron ubiquitin-proteasome dynamics accompanying inclusion body formation in Huntington disease","volume":"284","author":"Mitra","year":"2009","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.arr.2018.11.006_bib0595","doi-asserted-by":"crossref","first-page":"449","DOI":"10.1038\/cdd.2008.166","article-title":"Mitochondrial dysfunction triggered by loss of HtrA2 results in the activation of a brain-specific transcriptional stress response","volume":"16","author":"Moisoi","year":"2009","journal-title":"Cell Death Differ."},{"key":"10.1016\/j.arr.2018.11.006_bib0600","doi-asserted-by":"crossref","first-page":"10417","DOI":"10.1073\/pnas.152161099","article-title":"The threshold for polyglutamine-expansion protein aggregation and cellular toxicity is dynamic and influenced by aging in Caenorhabditis elegans","volume":"99","author":"Morley","year":"2002","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.arr.2018.11.006_bib0605","doi-asserted-by":"crossref","first-page":"2776","DOI":"10.1523\/JNEUROSCI.2006-14.2016","article-title":"Histone deacetylase inhibitors protect against pyruvate dehydrogenase dysfunction in Huntington\u2019s disease","volume":"37","author":"Naia","year":"2017","journal-title":"J. Neurosci."},{"key":"10.1016\/j.arr.2018.11.006_bib0610","doi-asserted-by":"crossref","first-page":"5385","DOI":"10.1007\/s12035-016-0048-3","article-title":"Comparative mitochondrial-based protective effects of resveratrol and nicotinamide in Huntington\u2019s disease models","volume":"54","author":"Naia","year":"2017","journal-title":"Mol. Neurobiol."},{"key":"10.1016\/j.arr.2018.11.006_bib0615","doi-asserted-by":"crossref","first-page":"12556","DOI":"10.1038\/s41598-017-12897-0","article-title":"HSF1-dependent and -independent regulation of the mammalian in vivo heat shock response and its impairment in Huntington\u2019s disease mouse models","volume":"7","author":"Neueder","year":"2017","journal-title":"Sci. Rep."},{"key":"10.1016\/j.arr.2018.11.006_bib0620","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1016\/j.tibs.2018.02.003","article-title":"Protein disaggregation in multicellular organisms","volume":"43","author":"Nillegoda","year":"2018","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.arr.2018.11.006_bib0625","doi-asserted-by":"crossref","first-page":"16889","DOI":"10.1073\/pnas.1420103111","article-title":"Potential function for the Huntingtin protein as a scaffold for selective autophagy","volume":"111","author":"Ochaba","year":"2014","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.arr.2018.11.006_bib0630","doi-asserted-by":"crossref","first-page":"507","DOI":"10.1016\/j.neuron.2016.03.016","article-title":"PIAS1 regulates mutant huntingtin accumulation and Huntington\u2019s disease-associated phenotypes in vivo","volume":"90","author":"Ochaba","year":"2016","journal-title":"Neuron"},{"key":"10.1016\/j.arr.2018.11.006_bib0635","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1111\/j.1471-4159.2010.06741.x","article-title":"Nature and cause of mitochondrial dysfunction in Huntington\u2019s disease: focusing on huntingtin and the striatum","volume":"114","author":"Oliveira","year":"2010","journal-title":"J. Neurochem."},{"key":"10.1016\/j.arr.2018.11.006_bib0640","doi-asserted-by":"crossref","first-page":"2783","DOI":"10.1523\/JNEUROSCI.0106-08.2008","article-title":"N-Terminal mutant huntingtin associates with mitochondria and impairs mitochondrial trafficking","volume":"28","author":"Orr","year":"2008","journal-title":"J. Neurosci."},{"key":"10.1016\/j.arr.2018.11.006_bib0645","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1042\/bse0560053","article-title":"Protein folding, misfolding and quality control: the role of molecular chaperones","volume":"56","author":"Papsdorf","year":"2014","journal-title":"Essays Biochem."},{"key":"10.1016\/j.arr.2018.11.006_bib0650","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":"Park","year":"2013","journal-title":"Cell"},{"key":"10.1016\/j.arr.2018.11.006_bib0655","doi-asserted-by":"crossref","first-page":"753","DOI":"10.1126\/science.aaf6846","article-title":"ATP as a biological hydrotrope","volume":"356","author":"Patel","year":"2017","journal-title":"Science"},{"key":"10.1016\/j.arr.2018.11.006_bib0660","doi-asserted-by":"crossref","first-page":"13821","DOI":"10.1038\/ncomms13821","article-title":"CCT complex restricts neuropathogenic protein aggregation via autophagy","volume":"7","author":"Pavel","year":"2016","journal-title":"Nat. Commun."},{"key":"10.1016\/j.arr.2018.11.006_bib0665","doi-asserted-by":"crossref","first-page":"28726","DOI":"10.1074\/jbc.A114.627778","article-title":"Pharmacological inhibition of ULK1 kinase blocks mammalian target of rapamycin (mTOR)-dependent autophagy","volume":"290","author":"Petherick","year":"2015","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.arr.2018.11.006_bib0670","article-title":"Mitochondrial superoxide generation induces a parkinsonian phenotype in zebrafish and huntingtin aggregation in human cells","author":"Pinho","year":"2018","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/j.arr.2018.11.006_bib0675","doi-asserted-by":"crossref","first-page":"919","DOI":"10.1093\/brain\/awp006","article-title":"Prevention of depressive behaviour in the YAC128 mouse model of Huntington disease by mutation at residue 586 of huntingtin","volume":"132","author":"Pouladi","year":"2009","journal-title":"Brain"},{"key":"10.1016\/j.arr.2018.11.006_bib0680","doi-asserted-by":"crossref","first-page":"353","DOI":"10.1146\/annurev-pharmtox-010814-124332","article-title":"Targeting Hsp90\/Hsp70-based protein quality control for treatment of adult onset neurodegenerative diseases","volume":"55","author":"Pratt","year":"2015","journal-title":"Annu. Rev. Pharmacol. Toxicol."},{"key":"10.1016\/j.arr.2018.11.006_bib0685","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0046834","article-title":"The role of chaperone-mediated autophagy in huntingtin degradation","volume":"7","author":"Qi","year":"2012","journal-title":"PLoS One"},{"key":"10.1016\/j.arr.2018.11.006_bib0690","doi-asserted-by":"crossref","first-page":"30","DOI":"10.3389\/fnagi.2018.00030","article-title":"Dissecting endoplasmic reticulum unfolded protein response (UPR(ER)) in managing clandestine modus operandi of Alzheimer\u2019s disease","volume":"10","author":"Rahman","year":"2018","journal-title":"Front. Aging Neurosci."},{"key":"10.1016\/j.arr.2018.11.006_bib0695","doi-asserted-by":"crossref","first-page":"919","DOI":"10.1016\/j.celrep.2017.04.029","article-title":"Huntingtin inclusions trigger cellular quiescence, deactivate apoptosis, and lead to delayed necrosis","volume":"19","author":"Ramdzan","year":"2017","journal-title":"Cell Rep."},{"key":"10.1016\/j.arr.2018.11.006_bib0700","doi-asserted-by":"crossref","first-page":"2692","DOI":"10.1021\/acs.jproteome.6b00991","article-title":"Post-translational modifications (PTMs), identified on endogenous huntingtin, cluster within proteolytic domains between HEAT repeats","volume":"16","author":"Ratovitski","year":"2017","journal-title":"J. Proteome Res."},{"key":"10.1016\/j.arr.2018.11.006_bib0705","doi-asserted-by":"crossref","first-page":"585","DOI":"10.1038\/ng1362","article-title":"Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease","volume":"36","author":"Ravikumar","year":"2004","journal-title":"Nat. Genet."},{"key":"10.1016\/j.arr.2018.11.006_bib0710","doi-asserted-by":"crossref","first-page":"144","DOI":"10.1159\/000443738","article-title":"The prevalence of Huntington\u2019s disease","volume":"46","author":"Rawlins","year":"2016","journal-title":"Neuroepidemiology"},{"key":"10.1016\/j.arr.2018.11.006_bib0715","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1016\/j.freeradbiomed.2016.08.002","article-title":"The molecular chaperone Hsp70 promotes the proteolytic removal of oxidatively damaged proteins by the proteasome","volume":"99","author":"Reeg","year":"2016","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/j.arr.2018.11.006_bib0720","doi-asserted-by":"crossref","first-page":"5829","DOI":"10.1007\/s12035-016-0120-z","article-title":"Modulation of molecular chaperones in Huntington\u2019s disease and other polyglutamine disorders","volume":"54","author":"Reis","year":"2017","journal-title":"Mol. Neurobiol."},{"key":"10.1016\/j.arr.2018.11.006_bib0725","doi-asserted-by":"crossref","first-page":"187","DOI":"10.3389\/fnmol.2017.00187","article-title":"The endoplasmic reticulum unfolded protein response in neurodegenerative disorders and its potential therapeutic significance","volume":"10","author":"Remondelli","year":"2017","journal-title":"Front. Mol. Neurosci."},{"key":"10.1016\/j.arr.2018.11.006_bib0730","doi-asserted-by":"crossref","first-page":"1600","DOI":"10.1093\/hmg\/ddw036","article-title":"Interactome network analysis identifies multiple caspase-6 interactors involved in the pathogenesis of HD","volume":"25","author":"Riechers","year":"2016","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.arr.2018.11.006_bib0735","doi-asserted-by":"crossref","first-page":"72","DOI":"10.3389\/fnmol.2014.00072","article-title":"An optimal ubiquitin-proteasome pathway in the nervous system: the role of deubiquitinating enzymes","volume":"7","author":"Ristic","year":"2014","journal-title":"Front. Mol. Neurosci."},{"key":"10.1016\/j.arr.2018.11.006_bib0740","doi-asserted-by":"crossref","first-page":"398","DOI":"10.1111\/j.1471-4159.2011.07435.x","article-title":"Induction of autophagy with catalytic mTOR inhibitors reduces huntingtin aggregates in a neuronal cell model","volume":"119","author":"Roscic","year":"2011","journal-title":"J. Neurochem."},{"key":"10.1016\/j.arr.2018.11.006_bib0745","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1016\/S1474-4422(10)70245-3","article-title":"Huntington\u2019s disease: from molecular pathogenesis to clinical treatment","volume":"10","author":"Ross","year":"2011","journal-title":"Lancet Neurol."},{"key":"10.1016\/j.arr.2018.11.006_bib0750","doi-asserted-by":"crossref","first-page":"1351","DOI":"10.1002\/mds.26012","article-title":"Determinants of functional disability in Huntington\u2019s disease: role of cognitive and motor dysfunction","volume":"29","author":"Ross","year":"2014","journal-title":"Mov. Disord."},{"key":"10.1016\/j.arr.2018.11.006_bib0755","doi-asserted-by":"crossref","first-page":"443","DOI":"10.1038\/nature21695","article-title":"Cytosolic proteostasis through importing of misfolded proteins into mitochondria","volume":"543","author":"Ruan","year":"2017","journal-title":"Nature"},{"key":"10.1016\/j.arr.2018.11.006_bib0760","doi-asserted-by":"crossref","first-page":"262","DOI":"10.1038\/ncb3101","article-title":"Huntingtin functions as a scaffold for selective macroautophagy","volume":"17","author":"Rui","year":"2015","journal-title":"Nat. Cell Biol."},{"key":"10.1016\/j.arr.2018.11.006_bib0765","doi-asserted-by":"crossref","first-page":"858","DOI":"10.1080\/15548627.2015.1039219","article-title":"HTT\/huntingtin in selective autophagy and Huntington disease: a foe or a friend within?","volume":"11","author":"Rui","year":"2015","journal-title":"Autophagy"},{"key":"10.1016\/j.arr.2018.11.006_bib0770","doi-asserted-by":"crossref","first-page":"4070","DOI":"10.1172\/JCI46305","article-title":"IRS2 increases mitochondrial dysfunction and oxidative stress in a mouse model of Huntington disease","volume":"121","author":"Sadagurski","year":"2011","journal-title":"J. Clin. Invest."},{"key":"10.1016\/j.arr.2018.11.006_bib0775","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1016\/j.neuron.2011.06.031","article-title":"Selective neuronal vulnerability in neurodegenerative diseases: from stressor thresholds to degeneration","volume":"71","author":"Saxena","year":"2011","journal-title":"Neuron"},{"key":"10.1016\/j.arr.2018.11.006_bib0780","doi-asserted-by":"crossref","first-page":"282","DOI":"10.15252\/embj.201797212","article-title":"Complete suppression of Htt fibrilization and disaggregation of Htt fibrils by a trimeric chaperone complex","volume":"37","author":"Scior","year":"2018","journal-title":"EMBO J."},{"key":"10.1016\/j.arr.2018.11.006_bib0785","doi-asserted-by":"crossref","first-page":"642","DOI":"10.1016\/j.cmet.2014.01.016","article-title":"Pathogenesis of human mitochondrial diseases is modulated by reduced activity of the ubiquitin\/proteasome system","volume":"19","author":"Segref","year":"2014","journal-title":"Cell Metab."},{"key":"10.1016\/j.arr.2018.11.006_bib0790","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1111\/nan.12253","article-title":"Polyglutamine aggregation in Huntington\u2019s disease and spinocerebellar ataxia type 3: similar mechanisms in aggregate formation","volume":"42","author":"Seidel","year":"2016","journal-title":"Neuropathol. Appl. Neurobiol."},{"key":"10.1016\/j.arr.2018.11.006_bib0795","doi-asserted-by":"crossref","first-page":"e238","DOI":"10.1371\/journal.pone.0000238","article-title":"Proteasome activator enhances survival of Huntington\u2019s disease neuronal model cells","volume":"2","author":"Seo","year":"2007","journal-title":"PLoS One"},{"key":"10.1016\/j.arr.2018.11.006_bib0800","doi-asserted-by":"crossref","first-page":"1438","DOI":"10.1093\/hmg\/ddr024","article-title":"Abnormal mitochondrial dynamics, mitochondrial loss and mutant huntingtin oligomers in Huntington\u2019s disease: implications for selective neuronal damage","volume":"20","author":"Shirendeb","year":"2011","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.arr.2018.11.006_bib0805","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.devcel.2010.12.010","article-title":"Shedding light on mammalian microautophagy","volume":"20","author":"Shpilka","year":"2011","journal-title":"Dev. Cell"},{"key":"10.1016\/j.arr.2018.11.006_bib0810","doi-asserted-by":"crossref","first-page":"92","DOI":"10.1006\/exnr.1998.7005","article-title":"Huntington\u2019s disease intranuclear inclusions contain truncated, ubiquitinated huntingtin protein","volume":"156","author":"Sieradzan","year":"1999","journal-title":"Exp. Neurol."},{"key":"10.1016\/j.arr.2018.11.006_bib0815","doi-asserted-by":"crossref","first-page":"6337","DOI":"10.1007\/s12035-017-0853-3","article-title":"Azadiradione restores protein quality control and ameliorates the disease pathogenesis in a mouse model of Huntington\u2019s disease","volume":"55","author":"Singh","year":"2018","journal-title":"Mol. Neurobiol."},{"key":"10.1016\/j.arr.2018.11.006_bib0820","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1038\/nature25143","article-title":"Enhancing mitochondrial proteostasis reduces amyloid-beta proteotoxicity","volume":"552","author":"Sorrentino","year":"2017","journal-title":"Nature"},{"key":"10.1016\/j.arr.2018.11.006_bib0825","doi-asserted-by":"crossref","first-page":"353","DOI":"10.1146\/annurev-pharmtox-010716-104908","article-title":"Repairing mitochondrial dysfunction in disease","volume":"58","author":"Sorrentino","year":"2018","journal-title":"Annu. Rev. Pharmacol. Toxicol."},{"key":"10.1016\/j.arr.2018.11.006_bib0830","doi-asserted-by":"crossref","first-page":"1714","DOI":"10.1002\/mds.25172","article-title":"Huntington\u2019s disease: how intermediate are intermediate repeat lengths?","volume":"27","author":"Squitieri","year":"2012","journal-title":"Mov. Disord."},{"key":"10.1016\/j.arr.2018.11.006_bib0835","doi-asserted-by":"crossref","first-page":"100","DOI":"10.1126\/science.1092194","article-title":"SUMO modification of Huntingtin and Huntington\u2019s disease pathology","volume":"304","author":"Steffan","year":"2004","journal-title":"Science"},{"key":"10.1016\/j.arr.2018.11.006_bib0840","doi-asserted-by":"crossref","first-page":"1327","DOI":"10.1126\/science.1172871","article-title":"Rhes, a striatal specific protein, mediates mutant-huntingtin cytotoxicity","volume":"324","author":"Subramaniam","year":"2009","journal-title":"Science"},{"key":"10.1016\/j.arr.2018.11.006_bib0845","doi-asserted-by":"crossref","first-page":"654","DOI":"10.1016\/j.molcel.2016.01.028","article-title":"The mitochondrial basis of aging","volume":"61","author":"Sun","year":"2016","journal-title":"Mol. Cell"},{"key":"10.1016\/j.arr.2018.11.006_bib0850","doi-asserted-by":"crossref","first-page":"66","DOI":"10.1016\/j.nbd.2015.05.011","article-title":"Ectopic expression of the striatal-enriched GTPase Rhes elicits cerebellar degeneration and an ataxia phenotype in Huntington\u2019s disease","volume":"82","author":"Swarnkar","year":"2015","journal-title":"Neurobiol. Dis."},{"key":"10.1016\/j.arr.2018.11.006_bib0855","doi-asserted-by":"crossref","first-page":"868","DOI":"10.1523\/JNEUROSCI.4522-06.2007","article-title":"The induction levels of heat shock protein 70 differentiate the vulnerabilities to mutant huntingtin among neuronal subtypes","volume":"27","author":"Tagawa","year":"2007","journal-title":"J. Neurosci."},{"key":"10.1016\/j.arr.2018.11.006_bib0860","doi-asserted-by":"crossref","first-page":"15658","DOI":"10.1523\/JNEUROSCI.1830-14.2014","article-title":"Differential effects of delayed aging on phenotype and striatal pathology in a murine model of Huntington disease","volume":"34","author":"Tallaksen-Greene","year":"2014","journal-title":"J. Neurosci."},{"key":"10.1016\/j.arr.2018.11.006_bib0865","doi-asserted-by":"crossref","first-page":"1155","DOI":"10.1038\/ncb1477","article-title":"The chaperonin TRiC controls polyglutamine aggregation and toxicity through subunit-specific interactions","volume":"8","author":"Tam","year":"2006","journal-title":"Nat. Cell Biol."},{"key":"10.1016\/j.arr.2018.11.006_bib0870","doi-asserted-by":"crossref","first-page":"148","DOI":"10.1038\/nm985","article-title":"Trehalose alleviates polyglutamine-mediated pathology in a mouse model of Huntington disease","volume":"10","author":"Tanaka","year":"2004","journal-title":"Nat. Med."},{"key":"10.1016\/j.arr.2018.11.006_bib0875","doi-asserted-by":"crossref","first-page":"1097","DOI":"10.1038\/s41467-018-03509-0","article-title":"A common mechanism of proteasome impairment by neurodegenerative disease-associated oligomers","volume":"9","author":"Thibaudeau","year":"2018","journal-title":"Nat. Commun."},{"key":"10.1016\/j.arr.2018.11.006_bib0880","doi-asserted-by":"crossref","first-page":"1083","DOI":"10.1083\/jcb.200909067","article-title":"IKK phosphorylates Huntingtin and targets it for degradation by the proteasome and lysosome","volume":"187","author":"Thompson","year":"2009","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.arr.2018.11.006_bib0885","doi-asserted-by":"crossref","first-page":"16982","DOI":"10.1073\/pnas.1004498107","article-title":"A small-molecule scaffold induces autophagy in primary neurons and protects against toxicity in a Huntington disease model","volume":"107","author":"Tsvetkov","year":"2010","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.arr.2018.11.006_bib0890","doi-asserted-by":"crossref","first-page":"586","DOI":"10.1038\/nchembio.1308","article-title":"Proteostasis of polyglutamine varies among neurons and predicts neurodegeneration","volume":"9","author":"Tsvetkov","year":"2013","journal-title":"Nat. Chem. Biol."},{"key":"10.1016\/j.arr.2018.11.006_bib0895","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":"Tydlacka","year":"2008","journal-title":"J. Neurosci."},{"key":"10.1016\/j.arr.2018.11.006_bib0900","doi-asserted-by":"crossref","first-page":"3355","DOI":"10.1042\/BCJ20160809","article-title":"Regulating protein breakdown through proteasome phosphorylation","volume":"474","author":"VerPlank","year":"2017","journal-title":"Biochem. J."},{"key":"10.1016\/j.arr.2018.11.006_bib0905","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1096\/fj.10-167361","article-title":"Novel synthetic small-molecule activators of AMPK as enhancers of autophagy and amyloid-beta peptide degradation","volume":"25","author":"Vingtdeux","year":"2011","journal-title":"FASEB J."},{"key":"10.1016\/j.arr.2018.11.006_bib0910","doi-asserted-by":"crossref","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\u2019s disease","volume":"29","author":"Wacker","year":"2009","journal-title":"J. Neurosci."},{"key":"10.1016\/j.arr.2018.11.006_bib0915","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1523\/JNEUROSCI.1305-11.2012","article-title":"Transgenic mouse model expressing the caspase 6 fragment of mutant huntingtin","volume":"32","author":"Waldron-Roby","year":"2012","journal-title":"J. Neurosci."},{"key":"10.1016\/j.arr.2018.11.006_bib0920","doi-asserted-by":"crossref","first-page":"24","DOI":"10.1016\/j.neuropharm.2016.04.041","article-title":"Activation of AMPK-induced autophagy ameliorates Huntington disease pathology in vitro","volume":"108","author":"Walter","year":"2016","journal-title":"Neuropharmacology"},{"key":"10.1016\/j.arr.2018.11.006_bib0925","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1126\/science.aad2033","article-title":"Cytoplasmic protein aggregates interfere with nucleocytoplasmic transport of protein and RNA","volume":"351","author":"Woerner","year":"2016","journal-title":"Science"},{"key":"10.1016\/j.arr.2018.11.006_bib0930","doi-asserted-by":"crossref","first-page":"76","DOI":"10.1186\/s13024-016-0141-0","article-title":"ULK1-mediated phosphorylation of ATG14 promotes autophagy and is impaired in Huntington\u2019s disease models","volume":"11","author":"Wold","year":"2016","journal-title":"Mol. Neurodegener."},{"key":"10.1016\/j.arr.2018.11.006_bib0935","doi-asserted-by":"crossref","first-page":"1293","DOI":"10.1523\/JNEUROSCI.1870-13.2014","article-title":"The regulation of autophagosome dynamics by huntingtin and HAP1 is disrupted by expression of mutant huntingtin, leading to defective cargo degradation","volume":"34","author":"Wong","year":"2014","journal-title":"J. Neurosci."},{"key":"10.1016\/j.arr.2018.11.006_bib0940","doi-asserted-by":"crossref","first-page":"1259","DOI":"10.1242\/jcs.161216","article-title":"Autophagosome dynamics in neurodegeneration at a glance","volume":"128","author":"Wong","year":"2015","journal-title":"J. Cell. Sci."},{"key":"10.1016\/j.arr.2018.11.006_bib0945","doi-asserted-by":"crossref","first-page":"24","DOI":"10.1016\/j.nbd.2014.12.030","article-title":"Partial rescue of some features of Huntington disease in the genetic absence of caspase-6 in YAC128 mice","volume":"76","author":"Wong","year":"2015","journal-title":"Neurobiol. Dis."},{"key":"10.1016\/j.arr.2018.11.006_bib0950","doi-asserted-by":"crossref","first-page":"382","DOI":"10.1038\/nature25486","article-title":"Mitochondria-lysosome contacts regulate mitochondrial fission via RAB7 GTP hydrolysis","volume":"554","author":"Wong","year":"2018","journal-title":"Nature"},{"key":"10.1016\/j.arr.2018.11.006_bib0955","doi-asserted-by":"crossref","first-page":"827","DOI":"10.1038\/emboj.2008.23","article-title":"Mutant huntingtin reduces HSP70 expression through the sequestration of NF-Y transcription factor","volume":"27","author":"Yamanaka","year":"2008","journal-title":"EMBO J."},{"key":"10.1016\/j.arr.2018.11.006_bib0960","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":"Yang","year":"2016","journal-title":"Elife"},{"key":"10.1016\/j.arr.2018.11.006_bib0965","doi-asserted-by":"crossref","first-page":"822","DOI":"10.1038\/nn.3721","article-title":"Inhibition of mitochondrial protein import by mutant huntingtin","volume":"17","author":"Yano","year":"2014","journal-title":"Nat. Neurosci."},{"key":"10.1016\/j.arr.2018.11.006_bib0970","doi-asserted-by":"crossref","first-page":"1739","DOI":"10.1093\/hmg\/ddw045","article-title":"Mitochondria-targeted molecules MitoQ and SS31 reduce mutant huntingtin-induced mitochondrial toxicity and synaptic damage in Huntington\u2019s disease","volume":"25","author":"Yin","year":"2016","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.arr.2018.11.006_bib0975","doi-asserted-by":"crossref","first-page":"E1481","DOI":"10.1073\/pnas.1321811111","article-title":"Protein aggregation can inhibit clathrin-mediated endocytosis by chaperone competition","volume":"111","author":"Yu","year":"2014","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.arr.2018.11.006_bib0980","doi-asserted-by":"crossref","first-page":"2687","DOI":"10.1039\/C6SC05368H","article-title":"Discovery of a small molecule targeting ULK1-modulated cell death of triple negative breast cancer in vitro and in vivo","volume":"8","author":"Zhang","year":"2017","journal-title":"Chem. Sci."},{"key":"10.1016\/j.arr.2018.11.006_bib0985","doi-asserted-by":"crossref","first-page":"8317","DOI":"10.1523\/JNEUROSCI.0806-16.2016","article-title":"Compartment-dependent degradation of mutant huntingtin accounts for its preferential accumulation in neuronal processes","volume":"36","author":"Zhao","year":"2016","journal-title":"J. Neurosci."},{"key":"10.1016\/j.arr.2018.11.006_bib0990","doi-asserted-by":"crossref","first-page":"E5655","DOI":"10.1073\/pnas.1603020113","article-title":"TRiC subunits enhance BDNF axonal transport and rescue striatal atrophy in Huntington\u2019s disease","volume":"113","author":"Zhao","year":"2016","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.arr.2018.11.006_bib0995","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pgen.1000838","article-title":"Deletion of the huntingtin polyglutamine stretch enhances neuronal autophagy and longevity in mice","volume":"6","author":"Zheng","year":"2010","journal-title":"PLoS Genet."},{"key":"10.1016\/j.arr.2018.11.006_bib1000","doi-asserted-by":"crossref","first-page":"708","DOI":"10.1016\/j.bbrc.2017.08.126","article-title":"Role of the ribosomal quality control machinery in nucleocytoplasmic translocation of polyQ-expanded huntingtin exon-1","volume":"493","author":"Zheng","year":"2017","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.arr.2018.11.006_bib1005","doi-asserted-by":"crossref","first-page":"1545","DOI":"10.1093\/hmg\/ddy061","article-title":"Small molecule modulator of protein disulfide isomerase attenuates mutant huntingtin toxicity and inhibits endoplasmic reticulum stress in a mouse model of Huntington\u2019s disease","volume":"27","author":"Zhou","year":"2018","journal-title":"Hum. Mol. Genet."}],"container-title":["Ageing Research Reviews"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1568163718301910?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1568163718301910?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,27]],"date-time":"2025-10-27T18:39:19Z","timestamp":1761590359000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1568163718301910"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2019,1]]},"references-count":201,"alternative-id":["S1568163718301910"],"URL":"https:\/\/doi.org\/10.1016\/j.arr.2018.11.006","relation":{},"ISSN":["1568-1637"],"issn-type":[{"value":"1568-1637","type":"print"}],"subject":[],"published":{"date-parts":[[2019,1]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Targeting the proteostasis network in Huntington\u2019s disease","name":"articletitle","label":"Article Title"},{"value":"Ageing Research Reviews","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.arr.2018.11.006","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2018 The Authors. Published by Elsevier B.V.","name":"copyright","label":"Copyright"}]}}