{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,16]],"date-time":"2026-05-16T11:17:03Z","timestamp":1778930223886,"version":"3.51.4"},"reference-count":47,"publisher":"Elsevier BV","issue":"28","license":[{"start":{"date-parts":[[2015,7,1]],"date-time":"2015-07-01T00:00:00Z","timestamp":1435708800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,9,1]],"date-time":"2020-09-01T00:00:00Z","timestamp":1598918400000},"content-version":"vor","delay-in-days":1889,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"crossref","award":["NIBIB T32EB009270"],"award-info":[{"award-number":["NIBIB T32EB009270"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"crossref","award":["PN2EY016525"],"award-info":[{"award-number":["PN2EY016525"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"crossref","award":["P41GM103832"],"award-info":[{"award-number":["P41GM103832"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"crossref","award":["R01NS084345"],"award-info":[{"award-number":["R01NS084345"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"crossref","award":["R01GM080139"],"award-info":[{"award-number":["R01GM080139"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":["jbc.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2015,7]]},"DOI":"10.1074\/jbc.m115.655373","type":"journal-article","created":{"date-parts":[[2015,5,20]],"date-time":"2015-05-20T22:10:58Z","timestamp":1432159858000},"page":"17451-17461","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":44,"title":["Structural Mechanisms of Mutant Huntingtin Aggregation Suppression by the Synthetic Chaperonin-like CCT5 Complex Explained by Cryoelectron Tomography"],"prefix":"10.1016","volume":"290","author":[{"given":"Michele C.","family":"Darrow","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Oksana A.","family":"Sergeeva","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jose M.","family":"Isas","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jes\u00fas G.","family":"Galaz-Montoya","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jonathan A.","family":"King","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ralf","family":"Langen","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Michael F.","family":"Schmid","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Wah","family":"Chiu","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1074\/jbc.M115.655373_bib1","doi-asserted-by":"crossref","first-page":"766","DOI":"10.1038\/nrg1686","article-title":"History of genetic disease: the molecular genetics of Huntington disease: a history","volume":"6","author":"Bates","year":"2005","journal-title":"Nat. Rev. Genet"},{"key":"10.1074\/jbc.M115.655373_bib2","doi-asserted-by":"crossref","first-page":"218","DOI":"10.1016\/S0140-6736(07)60111-1","article-title":"Huntington's disease","volume":"369","author":"Walker","year":"2007","journal-title":"Lancet"},{"key":"10.1074\/jbc.M115.655373_bib3","doi-asserted-by":"crossref","first-page":"466","DOI":"10.1016\/j.jmb.2012.01.030","article-title":"Physical chemistry of polyglutamine: intriguing tales of a monotonous sequence","volume":"421","author":"Wetzel","year":"2012","journal-title":"J. Mol. Biol"},{"key":"10.1074\/jbc.M115.655373_bib4","doi-asserted-by":"crossref","first-page":"537","DOI":"10.1016\/S0092-8674(00)80513-9","article-title":"Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation","volume":"90","author":"Davies","year":"1997","journal-title":"Cell"},{"key":"10.1074\/jbc.M115.655373_bib5","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":"10.1074\/jbc.M115.655373_bib6","doi-asserted-by":"crossref","first-page":"2611","DOI":"10.2174\/1568026611212220013","article-title":"Putting huntingtin \u201caggregation\u201d in view with windows into the cellular milieu","volume":"12","author":"Hatters","year":"2012","journal-title":"Curr. Top. Med. Chem"},{"key":"10.1074\/jbc.M115.655373_bib7","doi-asserted-by":"crossref","first-page":"1647","DOI":"10.4161\/rna.26706","article-title":"Aberrantly spliced HTT, a new player in Huntington's disease pathogenesis","volume":"10","author":"Gipson","year":"2013","journal-title":"RNA Biol"},{"key":"10.1074\/jbc.M115.655373_bib8","doi-asserted-by":"crossref","first-page":"2366","DOI":"10.1073\/pnas.1221891110","article-title":"Aberrant splicing of HTT generates the pathogenic exon 1 protein in Huntington disease","volume":"110","author":"Sathasivam","year":"2013","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M115.655373_bib9","first-page":"217","article-title":"Huntington's disease: the past, present, and future search for disease modifiers","volume":"86","author":"Clabough","year":"2013","journal-title":"Yale J. Biol. Med"},{"key":"10.1074\/jbc.M115.655373_bib10","doi-asserted-by":"crossref","first-page":"1997","DOI":"10.1016\/j.febslet.2013.05.022","article-title":"Pharmacological protein targets in polyglutamine diseases: Mutant polypeptides and their interactors","volume":"587","author":"Margulis","year":"2013","journal-title":"FEBS Lett"},{"key":"10.1074\/jbc.M115.655373_bib11","doi-asserted-by":"crossref","first-page":"416","DOI":"10.1007\/s13311-013-0186-5","article-title":"Opportunities and challenges for molecular chaperone modulation to treat protein-conformational brain diseases","volume":"10","author":"Van der Putten","year":"2013","journal-title":"Neurother"},{"key":"10.1074\/jbc.M115.655373_bib12","doi-asserted-by":"crossref","first-page":"887","DOI":"10.1016\/j.molcel.2006.08.017","article-title":"Chaperonin TRiC promotes the assembly of polyQ expansion proteins into nontoxic oligomers","volume":"23","author":"Behrends","year":"2006","journal-title":"Mol. Cell"},{"key":"10.1074\/jbc.M115.655373_bib13","doi-asserted-by":"crossref","first-page":"603","DOI":"10.1146\/annurev.biochem.70.1.603","article-title":"Folding of newly translated proteins in vivo: the role of molecular chaperones","volume":"70","author":"Frydman","year":"2001","journal-title":"Annu. Rev. Biochem"},{"key":"10.1074\/jbc.M115.655373_bib14","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1146\/annurev.cellbio.23.090506.123555","article-title":"Two families of chaperonin: physiology and mechanism","volume":"23","author":"Horwich","year":"2007","journal-title":"Annu. Rev. Cell Dev. Biol"},{"key":"10.1074\/jbc.M115.655373_bib15","doi-asserted-by":"crossref","first-page":"1163","DOI":"10.1038\/ncb1478","article-title":"Cytosolic chaperonin prevents polyglutamine toxicity with altering the aggregation state","volume":"8","author":"Kitamura","year":"2006","journal-title":"Nat. Cell Biol"},{"key":"10.1074\/jbc.M115.655373_bib16","doi-asserted-by":"crossref","first-page":"e00710","DOI":"10.7554\/eLife.00710","article-title":"TRiC's tricks inhibit huntingtin aggregation","volume":"2","author":"Shahmoradian","year":"2013","journal-title":"eLife"},{"key":"10.1074\/jbc.M115.655373_bib17","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":"10.1074\/jbc.M115.655373_bib18","doi-asserted-by":"crossref","first-page":"4767","DOI":"10.1002\/j.1460-2075.1992.tb05582.x","article-title":"Function in protein folding of TRiC, a cytosolic ring complex containing TCP-1 and structurally related subunits","volume":"11","author":"Frydman","year":"1992","journal-title":"EMBO J"},{"key":"10.1074\/jbc.M115.655373_bib19","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1093\/emboj\/18.1.85","article-title":"In vivo newly translated polypeptides are sequestered in a protected folding environment","volume":"18","author":"Thulasiraman","year":"1999","journal-title":"EMBO J"},{"key":"10.1074\/jbc.M115.655373_bib20","doi-asserted-by":"crossref","first-page":"578","DOI":"10.1038\/371578a0","article-title":"The crystal structure of the bacterial chaperonin GroEL at 2.8 A","volume":"371","author":"Braig","year":"1994","journal-title":"Nature"},{"key":"10.1074\/jbc.M115.655373_bib21","doi-asserted-by":"crossref","first-page":"2905","DOI":"10.1093\/hmg\/11.23.2905","article-title":"Aggregated polyglutamine peptides delivered to nuclei are toxic to mammalian cells","volume":"11","author":"Yang","year":"2002","journal-title":"Hum. Mol. Genet"},{"key":"10.1074\/jbc.M115.655373_bib22","doi-asserted-by":"crossref","first-page":"3077","DOI":"10.1073\/pnas.1222663110","article-title":"Exogenous delivery of chaperonin subunit fragment ApiCCT1 modulates mutant Huntingtin cellular phenotypes","volume":"110","author":"Sontag","year":"2013","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M115.655373_bib23","doi-asserted-by":"crossref","first-page":"17734","DOI":"10.1074\/jbc.M112.443929","article-title":"Human CCT4 and CCT5 chaperonin subunits expressed in Escherichia coli form biologically active homo-oligomers","volume":"288","author":"Sergeeva","year":"2013","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M115.655373_bib24","doi-asserted-by":"crossref","first-page":"27470","DOI":"10.1074\/jbc.M114.576033","article-title":"Biochemical characterization of mutants in chaperonin proteins CCT4 and CCT5 Associated with hereditary sensory neuropathy","volume":"289","author":"Sergeeva","year":"2014","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M115.655373_bib25","doi-asserted-by":"crossref","first-page":"11634","DOI":"10.1073\/pnas.182393899","article-title":"A linear lattice model for polyglutamine in CAG-expansion diseases","volume":"99","author":"Bennett","year":"2002","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M115.655373_bib26","doi-asserted-by":"crossref","first-page":"e112262","DOI":"10.1371\/journal.pone.0112262","article-title":"Polyglutamine- and temperature-dependent conformational rigidity in mutant huntingtin revealed by immunoassays and circular dichroism spectroscopy","volume":"9","author":"Fodale","year":"2014","journal-title":"PloS ONE"},{"key":"10.1074\/jbc.M115.655373_bib27","doi-asserted-by":"crossref","first-page":"671","DOI":"10.1038\/nmeth.2089","article-title":"NIH Image to ImageJ: 25 years of image analysis","volume":"9","author":"Schneider","year":"2012","journal-title":"Nat. Methods"},{"key":"10.1074\/jbc.M115.655373_bib28","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1111\/j.1365-2818.1983.tb04163.x","article-title":"Electron microscopy of frozen biological suspensions","volume":"129","author":"Lepault","year":"1983","journal-title":"J. Microsc"},{"key":"10.1074\/jbc.M115.655373_bib29","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1016\/j.jsb.2005.07.007","article-title":"Automated electron microscope tomography using robust prediction of specimen movements","volume":"152","author":"Mastronarde","year":"2005","journal-title":"J. Struct. Biol"},{"key":"10.1074\/jbc.M115.655373_bib30","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1006\/jsbi.1996.0013","article-title":"Computer visualization of three-dimensional image data using IMOD","volume":"116","author":"Kremer","year":"1996","journal-title":"J. Struct. Biol"},{"key":"10.1074\/jbc.M115.655373_bib31","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1016\/j.jsb.2008.05.003","article-title":"A visualization and segmentation toolbox for electron microscopy","volume":"164","author":"Pruggnaller","year":"2008","journal-title":"J. Struct. Biol"},{"key":"10.1074\/jbc.M115.655373_bib32","doi-asserted-by":"crossref","first-page":"38","DOI":"10.1016\/j.jsb.2006.05.009","article-title":"EMAN2: An extensible image processing suite for electron microscopy","volume":"157","author":"Tang","year":"2007","journal-title":"J. Struct. Biol"},{"key":"10.1074\/jbc.M115.655373_bib33","doi-asserted-by":"crossref","first-page":"279","DOI":"10.1016\/j.jsb.2015.04.016","article-title":"Single particle tomography in EMAN2","volume":"190","author":"Galaz-Montoya","year":"2015","journal-title":"J. Struct. Biol"},{"key":"10.1074\/jbc.M115.655373_bib34","doi-asserted-by":"crossref","first-page":"243","DOI":"10.1016\/j.jsb.2007.09.018","article-title":"Methods for aligning and for averaging 3D volumes with missing data","volume":"161","author":"Schmid","year":"2008","journal-title":"J. Struct. Biol"},{"key":"10.1074\/jbc.M115.655373_bib35","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1016\/j.jsb.2006.06.010","article-title":"Visualizing density maps with UCSF Chimera","volume":"157","author":"Goddard","year":"2007","journal-title":"J. Struct. Biol"},{"key":"10.1074\/jbc.M115.655373_bib36","doi-asserted-by":"crossref","first-page":"3621","DOI":"10.1021\/bi500383h","article-title":"Fluorescence anisotropy uncovers changes in protein packing with inclusion growth in a cellular model of polyglutamine aggregation","volume":"53","author":"Bhardwaj","year":"2014","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.M115.655373_bib37","doi-asserted-by":"crossref","first-page":"2324","DOI":"10.1093\/hmg\/ddt625","article-title":"Live cell imaging and biophotonic methods reveal two types of mutant huntingtin inclusions","volume":"23","author":"Caron","year":"2014","journal-title":"Hum. Mol. Genet"},{"key":"10.1074\/jbc.M115.655373_bib38","doi-asserted-by":"crossref","first-page":"14777","DOI":"10.1074\/jbc.M109.093708","article-title":"Mutant huntingtin fragments form oligomers in a polyglutamine length-dependent manner in vitro and in vivo","volume":"285","author":"Legleiter","year":"2010","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M115.655373_bib39","doi-asserted-by":"crossref","first-page":"426","DOI":"10.1110\/ps.8.2.426","article-title":"Is human thioredoxin monomeric or dimeric?","volume":"8","author":"Gronenborn","year":"1999","journal-title":"Protein Sci"},{"key":"10.1074\/jbc.M115.655373_bib40","doi-asserted-by":"crossref","first-page":"641","DOI":"10.1016\/S0969-2126(00)00065-4","article-title":"Volume changes on protein folding","volume":"2","author":"Harpaz","year":"1994","journal-title":"Struct"},{"key":"10.1074\/jbc.M115.655373_bib41","doi-asserted-by":"crossref","first-page":"255","DOI":"10.1602\/neurorx.1.2.255","article-title":"Huntington's disease genetics","volume":"1","author":"Myers","year":"2004","journal-title":"NeuroRX"},{"key":"10.1074\/jbc.M115.655373_bib42","doi-asserted-by":"crossref","first-page":"913","DOI":"10.1093\/hmg\/ddu504","article-title":"Comparative study of naturally occurring huntingtin fragments in Drosophila points to exon 1 as the most pathogenic species in Huntington's disease","volume":"24","author":"Barbaro","year":"2015","journal-title":"Hum. Mol. Genet"},{"key":"10.1074\/jbc.M115.655373_bib43","doi-asserted-by":"crossref","first-page":"1559","DOI":"10.1096\/fasebj.9.15.8529835","article-title":"The role of molecular chaperones in protein folding","volume":"9","author":"Hendrick","year":"1995","journal-title":"FASEB J"},{"key":"10.1074\/jbc.M115.655373_bib44","doi-asserted-by":"crossref","first-page":"781","DOI":"10.1038\/nrm1492","article-title":"Pathways of chaperone-mediated protein folding in the cytosol","volume":"5","author":"Young","year":"2004","journal-title":"Nat. Rev. Mol. Cell Biol"},{"key":"10.1074\/jbc.M115.655373_bib45","doi-asserted-by":"crossref","first-page":"21208","DOI":"10.1073\/pnas.1218836109","article-title":"Folding of large multidomain proteins by partial encapsulation in the chaperonin TRiC\/CCT","volume":"109","author":"R\u00fc\u00dfmann","year":"2012","journal-title":"Proc. Natl. Acad. Sci"},{"key":"10.1074\/jbc.M115.655373_bib46","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.expneurol.2011.12.013","article-title":"Protein aggregates in Huntington's disease","volume":"238","author":"Arrasate","year":"2012","journal-title":"Exp. Neurol"},{"key":"10.1074\/jbc.M115.655373_bib47","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"}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820353473?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820353473?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/syndication.highwire.org\/content\/doi\/10.1074\/jbc.M115.655373","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,1,4]],"date-time":"2022-01-04T01:55:12Z","timestamp":1641261312000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925820353473"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2015,7]]},"references-count":47,"journal-issue":{"issue":"28","published-print":{"date-parts":[[2015,7]]}},"alternative-id":["S0021925820353473"],"URL":"https:\/\/doi.org\/10.1074\/jbc.m115.655373","relation":{"has-review":[{"id-type":"doi","id":"10.3410\/f.725508710.793507227","asserted-by":"object"}]},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2015,7]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Structural Mechanisms of Mutant Huntingtin Aggregation Suppression by the Synthetic Chaperonin-like CCT5 Complex Explained by Cryoelectron Tomography","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1074\/jbc.M115.655373","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2015 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.","name":"copyright","label":"Copyright"}]}}