{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,4]],"date-time":"2026-10-04T12:26:04Z","timestamp":1791116764671,"version":"4.1.0"},"reference-count":42,"publisher":"Elsevier BV","issue":"4","license":[{"start":{"date-parts":[[2009,12,1]],"date-time":"2009-12-01T00:00:00Z","timestamp":1259625600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2009,12,1]],"date-time":"2009-12-01T00:00:00Z","timestamp":1259625600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2009,12,1]],"date-time":"2009-12-01T00:00:00Z","timestamp":1259625600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2009,12,1]],"date-time":"2009-12-01T00:00:00Z","timestamp":1259625600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2009,12,1]],"date-time":"2009-12-01T00:00:00Z","timestamp":1259625600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2009,12,1]],"date-time":"2009-12-01T00:00:00Z","timestamp":1259625600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2009,12,1]],"date-time":"2009-12-01T00:00:00Z","timestamp":1259625600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["30670654"],"award-info":[{"award-number":["30670654"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["90919004"],"award-info":[{"award-number":["90919004"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biochemical and Biophysical Research Communications"],"published-print":{"date-parts":[[2009,12]]},"DOI":"10.1016\/j.bbrc.2009.10.139","type":"journal-article","created":{"date-parts":[[2009,10,29]],"date-time":"2009-10-29T04:13:00Z","timestamp":1256789580000},"page":"1294-1298","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":23,"title":["Overexpression of F0F1-ATP synthase \u03b1 suppresses mutant huntingtin aggregation and toxicity in vitro"],"prefix":"10.1016","volume":"390","author":[{"given":"Hong-Quan","family":"Wang","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yu-Xia","family":"Xu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xiao-Yan","family":"Zhao","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hong","family":"Zhao","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jie","family":"Yan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xiao-Bo","family":"Sun","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jing-Chun","family":"Guo","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Cui-Qing","family":"Zhu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.bbrc.2009.10.139_bib1","doi-asserted-by":"crossref","first-page":"753","DOI":"10.1016\/S0092-8674(00)80464-X","article-title":"Ectopically expressed CAG repeats cause intranuclear inclusions and a progressive late onset neurological phenotype in the mouse","volume":"91","author":"Ordway","year":"1997","journal-title":"Cell"},{"key":"10.1016\/j.bbrc.2009.10.139_bib2","doi-asserted-by":"crossref","first-page":"937","DOI":"10.1515\/BC.2000.114","article-title":"Protein aggregation and pathogenesis of Huntington\u2019s disease: mechanisms and correlations","volume":"381","author":"Wanker","year":"2000","journal-title":"Biol Chem"},{"key":"10.1016\/j.bbrc.2009.10.139_bib3","doi-asserted-by":"crossref","first-page":"549","DOI":"10.1016\/S0092-8674(00)80514-0","article-title":"Huntingtin-encoded polyglutamine expansions form amyloid-like protein aggregates in vitro and in vivo","volume":"90","author":"Scherzinger","year":"1997","journal-title":"Cell"},{"key":"10.1016\/j.bbrc.2009.10.139_bib4","doi-asserted-by":"crossref","first-page":"8747","DOI":"10.1523\/JNEUROSCI.0973-08.2008","article-title":"Suppression of mutant huntingtin aggregate formation by Cdk5\/p35 through the effect on microtubule stability","volume":"28","author":"Kaminosono","year":"2008","journal-title":"J. Neurosci."},{"key":"10.1016\/j.bbrc.2009.10.139_bib5","doi-asserted-by":"crossref","first-page":"3224","DOI":"10.1073\/pnas.0400243101","article-title":"Cytoplasmic aggregates trap polyglutamine-containing proteins and block axonal transport in a Drosophila model of Huntington\u2019s disease","volume":"101","author":"Lee","year":"2004","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.bbrc.2009.10.139_bib6","doi-asserted-by":"crossref","first-page":"839","DOI":"10.1093\/hmg\/8.5.839","article-title":"Impaired synaptic plasticity in mice carrying the Huntington\u2019s disease mutation","volume":"8","author":"Usdin","year":"1999","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.bbrc.2009.10.139_bib7","doi-asserted-by":"crossref","first-page":"819","DOI":"10.1016\/S0896-6273(02)00872-3","article-title":"Polyglutamine pathogenesis: emergence of unifying mechanisms for Huntington\u2019s disease and related disorders","volume":"35","author":"Ross","year":"2002","journal-title":"Neuron"},{"key":"10.1016\/j.bbrc.2009.10.139_bib8","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1007\/s004410000228","article-title":"Cell death in polyglutamine diseases","volume":"301","author":"Evert","year":"2000","journal-title":"Cell Tissue Res."},{"key":"10.1016\/j.bbrc.2009.10.139_bib9","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.bbrc.2009.10.139_bib10","doi-asserted-by":"crossref","first-page":"531","DOI":"10.1016\/S0962-8924(00)01853-5","article-title":"Huntington\u2019s disease: the challenge for cell biologists","volume":"10","author":"Tobin","year":"2000","journal-title":"Trends Cell Biol."},{"key":"10.1016\/j.bbrc.2009.10.139_bib11","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1016\/S0968-0004(03)00168-3","article-title":"The hunt for huntingtin function: interaction partners tell many different stories","volume":"28","author":"Harjes","year":"2003","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.bbrc.2009.10.139_bib12","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1016\/j.cell.2004.06.018","article-title":"Huntingtin controls neurotrophic support and survival of neurons by enhancing BDNF vesicular transport along microtubules","volume":"118","author":"Gauthier","year":"2004","journal-title":"Cell"},{"key":"10.1016\/j.bbrc.2009.10.139_bib13","doi-asserted-by":"crossref","first-page":"146","DOI":"10.1016\/j.tig.2004.01.008","article-title":"Huntingtin\u2013protein interactions and the pathogenesis of Huntington\u2019s disease","volume":"20","author":"Li","year":"2004","journal-title":"Trends Genet."},{"key":"10.1016\/j.bbrc.2009.10.139_bib14","doi-asserted-by":"crossref","first-page":"919","DOI":"10.1038\/nrn1806","article-title":"Normal huntingtin function: an alternative approach to Huntington\u2019s disease","volume":"6","author":"Cattaneo","year":"2005","journal-title":"Nat. Rev. Neurosci."},{"key":"10.1016\/j.bbrc.2009.10.139_bib15","doi-asserted-by":"crossref","first-page":"704","DOI":"10.1038\/nature06022","article-title":"Global changes to the ubiquitin system in Huntington\u2019s disease","volume":"448","author":"Bennett","year":"2007","journal-title":"Nature"},{"key":"10.1016\/j.bbrc.2009.10.139_bib16","doi-asserted-by":"crossref","first-page":"367","DOI":"10.1038\/ng864","article-title":"A bivalent huntingtin binding peptide suppresses polyglutamine aggregation and pathogenesis in Drosophila","volume":"30","author":"Kazantsev","year":"2002","journal-title":"Nat. Genet."},{"key":"10.1016\/j.bbrc.2009.10.139_bib17","doi-asserted-by":"crossref","first-page":"373","DOI":"10.1038\/nature01301","article-title":"Pivotal role of oligomerization in expanded polyglutamine neurodegenerative disorders","volume":"421","author":"S\u00e1nchez","year":"2003","journal-title":"Nature"},{"key":"10.1016\/j.bbrc.2009.10.139_bib18","doi-asserted-by":"crossref","first-page":"6739","DOI":"10.1073\/pnas.110138997","article-title":"Inhibition of huntingtin fibrillogenesis by specific antibodies and small molecules: implications for Huntington\u2019s disease therapy","volume":"97","author":"Heiser","year":"2000","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.bbrc.2009.10.139_bib19","doi-asserted-by":"crossref","first-page":"10437","DOI":"10.1074\/jbc.275.14.10437","article-title":"Inhibition of polyglutamine protein aggregation and cell death by novel peptides identified by phage display screening","volume":"275","author":"Nagai","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbrc.2009.10.139_bib20","doi-asserted-by":"crossref","first-page":"669","DOI":"10.1038\/35089509","article-title":"ATP synthase \u2013 a marvellous rotary engine of the cell","volume":"2","author":"Yoshida","year":"2001","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.bbrc.2009.10.139_bib21","doi-asserted-by":"crossref","first-page":"276","DOI":"10.1016\/S0005-2728(00)00080-3","article-title":"Synthase (H(+) ATPase): coupling between catalysis, mechanical work, and proton translocation","volume":"1458","author":"Futai","year":"2000","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbrc.2009.10.139_bib22","doi-asserted-by":"crossref","first-page":"7713","DOI":"10.1016\/S0021-9258(19)38984-7","article-title":"The alpha regulatory subunit of the mitochondrial F1-ATPase complex is a heat-shock protein. Identification of two highly conserved amino acid sequences among the alpha-subunits and molecular chaperones","volume":"265","author":"Luis","year":"1990","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbrc.2009.10.139_bib23","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1016\/0014-5793(90)81024-I","article-title":"Identification of a 66kDa protein associated with yeast mitochondrial ATP synthase as heat shock protein hsp60","volume":"268","author":"Gray","year":"1990","journal-title":"FEBS Lett."},{"key":"10.1016\/j.bbrc.2009.10.139_bib24","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1016\/j.neulet.2007.01.026","article-title":"Abnormal levels of prohibitin and ATP synthase in the substantia nigra and frontal cortex in Parkinson\u2019s disease","volume":"415","author":"Ferrer","year":"2007","journal-title":"Neurosci. Lett."},{"key":"10.1016\/j.bbrc.2009.10.139_bib25","doi-asserted-by":"crossref","first-page":"3943","DOI":"10.1002\/pmic.200400848","article-title":"Proteome analysis of human substantia nigra in Parkinson\u2019s disease","volume":"4","author":"Basso","year":"2004","journal-title":"Proteomics"},{"key":"10.1016\/j.bbrc.2009.10.139_bib26","doi-asserted-by":"crossref","first-page":"953","DOI":"10.1038\/sj.mp.4002077","article-title":"Amyloid precursor protein and amyloid beta-peptide bind to ATP synthase and regulate its activity at the surface of neural cells","volume":"13","author":"Schmidt","year":"2008","journal-title":"Mol. Psychiatry"},{"key":"10.1016\/j.bbrc.2009.10.139_bib27","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1007\/s11064-004-9692-5","article-title":"Quantitative proteomic analysis of mitochondria from primary neuron cultures treated with amyloid beta peptide","volume":"30","author":"Lovell","year":"2005","journal-title":"Neurochem. Res."},{"key":"10.1016\/j.bbrc.2009.10.139_bib28","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1016\/S0306-4522(02)00747-9","article-title":"Association of ATP synthase alpha-chain with neurofibrillary degeneration in Alzheimer\u2019s disease","volume":"117","author":"Sergeant","year":"2003","journal-title":"Neuroscience"},{"key":"10.1016\/j.bbrc.2009.10.139_bib29","doi-asserted-by":"crossref","first-page":"2009","DOI":"10.1093\/hmg\/9.13.2009","article-title":"Polyglutamine length-dependent interaction of Hsp40 and Hsp70 family chaperones with truncated N-terminal huntingtin: their role in suppression of aggregation and cellular toxicity","volume":"9","author":"Jana","year":"2000","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.bbrc.2009.10.139_bib30","doi-asserted-by":"crossref","first-page":"1137","DOI":"10.1093\/hmg\/11.9.1137","article-title":"Heat shock protein 27 prevents cellular polyglutamine toxicity and suppresses the increase of reactive oxygen species caused by huntingtin","volume":"11","author":"Wyttenbach","year":"2002","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.bbrc.2009.10.139_bib31","doi-asserted-by":"crossref","first-page":"8772","DOI":"10.1074\/jbc.275.12.8772","article-title":"Chaperones Hsp70 and Hsp40 suppress aggregate formation and apoptosis in cultured neuronal cells expressing truncated androgen receptor protein with expanded polyglutamine tract","volume":"275","author":"Kobayashi","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbrc.2009.10.139_bib32","doi-asserted-by":"crossref","first-page":"3568","DOI":"10.1016\/j.yexcr.2007.07.034","article-title":"Modulation of polyglutamine inclusion formation by the Hsp70 chaperone machine","volume":"313","author":"Rujano","year":"2007","journal-title":"Exp. Cell Res."},{"key":"10.1016\/j.bbrc.2009.10.139_bib33","doi-asserted-by":"crossref","first-page":"1511","DOI":"10.1093\/hmg\/10.14.1511","article-title":"Over-expression of inducible HSP70 chaperone suppresses neuropathology and improves motor function in SCA1 mice","volume":"10","author":"Cummings","year":"2001","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.bbrc.2009.10.139_bib34","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1038\/70532","article-title":"Suppression of polyglutamine-mediated neurodegeneration in Drosophila by the molecular chaperone HSP70","volume":"23","author":"Warrick","year":"1999","journal-title":"Nat. Genet."},{"key":"10.1016\/j.bbrc.2009.10.139_bib35","doi-asserted-by":"crossref","first-page":"10338","DOI":"10.1523\/JNEUROSCI.19-23-10338.1999","article-title":"Analysis of the role of heat shock protein (Hsp) molecular chaperones in polyglutamine disease","volume":"19","author":"Chai","year":"1999","journal-title":"J. Neurosci."},{"key":"10.1016\/j.bbrc.2009.10.139_bib36","doi-asserted-by":"crossref","first-page":"2811","DOI":"10.1093\/hmg\/9.19.2811","article-title":"Mechanisms of chaperone suppression of polyglutamine disease: selectivity, synergy and modulation of protein solubility in Drosophila","volume":"9","author":"Chan","year":"2000","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.bbrc.2009.10.139_bib37","doi-asserted-by":"crossref","first-page":"2203","DOI":"10.1523\/JNEUROSCI.23-06-02203.2003","article-title":"Heat shock protein 70 chaperone overexpression ameliorates phenotypes of the spinal and bulbar muscular atrophy transgenic mouse model by reducing nuclear-localized mutant androgen receptor protein","volume":"23","author":"Adachi","year":"2003","journal-title":"J. Neurosci."},{"key":"10.1016\/j.bbrc.2009.10.139_bib38","doi-asserted-by":"crossref","first-page":"13153","DOI":"10.1074\/jbc.M809229200","article-title":"Inhibition of Rho kinases enhances the degradation of mutant huntingtin","volume":"284","author":"Bauer","year":"2009","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbrc.2009.10.139_bib39","doi-asserted-by":"crossref","first-page":"9152","DOI":"10.1523\/JNEUROSCI.3001-05.2005","article-title":"CHIP suppresses polyglutamine aggregation and toxicity in vitro and in vivo","volume":"25","author":"Miller","year":"2005","journal-title":"J. Neurosci."},{"key":"10.1016\/j.bbrc.2009.10.139_bib40","doi-asserted-by":"crossref","first-page":"184","DOI":"10.1016\/j.bbrc.2006.01.136","article-title":"Oxidative stress promotes mutant huntingtin aggregation and mutant huntingtin-dependent cell death by mimicking proteasomal malfunction","volume":"342","author":"Goswami","year":"2006","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bbrc.2009.10.139_bib41","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.bbrc.2009.10.139_bib42","doi-asserted-by":"crossref","first-page":"26714","DOI":"10.1074\/jbc.M601603200","article-title":"CHIP protects from the neurotoxicity of expanded and wild-type ataxin-1 and promotes their ubiquitination and degradation","volume":"281","author":"Al-Ramahi","year":"2006","journal-title":"J. Biol. Chem."}],"container-title":["Biochemical and Biophysical Research Communications"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0006291X09021305?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0006291X09021305?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,13]],"date-time":"2025-09-13T10:47:47Z","timestamp":1757760467000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0006291X09021305"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2009,12]]},"references-count":42,"journal-issue":{"issue":"4","published-print":{"date-parts":[[2009,12]]}},"alternative-id":["S0006291X09021305"],"URL":"https:\/\/doi.org\/10.1016\/j.bbrc.2009.10.139","relation":{},"ISSN":["0006-291X"],"issn-type":[{"value":"0006-291X","type":"print"}],"subject":[],"published":{"date-parts":[[2009,12]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Overexpression of F0F1-ATP synthase \u03b1 suppresses mutant huntingtin aggregation and toxicity in vitro","name":"articletitle","label":"Article Title"},{"value":"Biochemical and Biophysical Research Communications","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bbrc.2009.10.139","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2009 Elsevier Inc. All rights reserved.","name":"copyright","label":"Copyright"}]}}