{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,10]],"date-time":"2026-02-10T17:46:13Z","timestamp":1770745573206,"version":"3.49.0"},"reference-count":22,"publisher":"Elsevier BV","issue":"33","license":[{"start":{"date-parts":[[2013,8,1]],"date-time":"2013-08-01T00:00:00Z","timestamp":1375315200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,9,12]],"date-time":"2020-09-12T00:00:00Z","timestamp":1599868800000},"content-version":"vor","delay-in-days":2599,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2013,8]]},"DOI":"10.1074\/jbc.c113.481945","type":"journal-article","created":{"date-parts":[[2013,7,10]],"date-time":"2013-07-10T04:44:17Z","timestamp":1373431457000},"page":"23633-23638","source":"Crossref","is-referenced-by-count":52,"title":["Heat Shock Response Activation Exacerbates Inclusion Body Formation in a Cellular Model of Huntington Disease"],"prefix":"10.1016","volume":"288","author":[{"given":"Kirill","family":"Bersuker","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mark S.","family":"Hipp","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Barbara","family":"Calamini","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Richard I.","family":"Morimoto","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ron R.","family":"Kopito","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"issue":"suppl.","key":"10.1074\/jbc.C113.481945_bib1","doi-asserted-by":"crossref","first-page":"S10","DOI":"10.1038\/nm1066","article-title":"Protein aggregation and neurodegenerative disease","volume":"10","author":"Ross","year":"2004","journal-title":"Nat. Med"},{"key":"10.1074\/jbc.C113.481945_bib2","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.C113.481945_bib3","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.C113.481945_bib4","doi-asserted-by":"crossref","first-page":"4604","DOI":"10.1073\/pnas.96.8.4604","article-title":"Self-assembly of polyglutamine-containing huntingtin fragments into amyloid-like fibrils: implications for Huntington's disease pathology","volume":"96","author":"Scherzinger","year":"1999","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.C113.481945_bib5","doi-asserted-by":"crossref","first-page":"2623","DOI":"10.2174\/1568026611212220014","article-title":"Protein homeostasis as a therapeutic target for diseases of protein conformation","volume":"12","author":"Calamini","year":"2012","journal-title":"Curr. Top. Med. Chem"},{"key":"10.1074\/jbc.C113.481945_bib6","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1101\/sqb.2012.76.010637","article-title":"The heat shock response: systems biology of proteotoxic stress in aging and disease","volume":"76","author":"Morimoto","year":"2011","journal-title":"Cold Spring Harbor Symp. Quant. Biol"},{"key":"10.1074\/jbc.C113.481945_bib7","doi-asserted-by":"crossref","first-page":"a004390","DOI":"10.1101\/cshperspect.a004390","article-title":"Protein folding in the cytoplasm and the heat shock response","volume":"2","author":"Vabulas","year":"2010","journal-title":"Cold Spring Harb. Perspect. Biol"},{"key":"10.1074\/jbc.C113.481945_bib8","doi-asserted-by":"crossref","first-page":"1254","DOI":"10.1091\/mbc.e03-10-0738","article-title":"The role of heat shock transcription factor 1 in the genome-wide regulation of the mammalian heat shock response","volume":"15","author":"Trinklein","year":"2004","journal-title":"Mol. Biol. Cell"},{"key":"10.1074\/jbc.C113.481945_bib9","doi-asserted-by":"crossref","first-page":"188","DOI":"10.2174\/138920110790909650","article-title":"Induction of molecular chaperones as a therapeutic strategy for the polyglutamine diseases","volume":"11","author":"Nagai","year":"2010","journal-title":"Curr. Pharm. Biotechnol"},{"key":"10.1074\/jbc.C113.481945_bib10","doi-asserted-by":"crossref","first-page":"1307","DOI":"10.1093\/hmg\/10.12.1307","article-title":"Geldanamycin activates a heat shock response and inhibits huntingtin aggregation in a cell culture model of Huntington's disease","volume":"10","author":"Sittler","year":"2001","journal-title":"Hum. Mol. Genet"},{"key":"10.1074\/jbc.C113.481945_bib11","doi-asserted-by":"crossref","first-page":"1088","DOI":"10.1038\/nm1298","article-title":"17-AAG, an Hsp90 inhibitor, ameliorates polyglutamine-mediated motor neuron degeneration","volume":"11","author":"Waza","year":"2005","journal-title":"Nat. Med"},{"key":"10.1074\/jbc.C113.481945_bib12","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1038\/nchembio.763","article-title":"Small-molecule proteostasis regulators for protein conformational diseases","volume":"8","author":"Calamini","year":"2012","journal-title":"Nat. Chem. Biol"},{"key":"10.1074\/jbc.C113.481945_bib13","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":"10.1074\/jbc.C113.481945_bib14","doi-asserted-by":"crossref","first-page":"33","DOI":"10.3233\/JHD-2012-120020","article-title":"Poly-glutamine expanded huntingtin dramatically alters the genome wide binding of HSF1","volume":"1","author":"Riva","year":"2012","journal-title":"J. Huntingtons. Dis"},{"key":"10.1074\/jbc.C113.481945_bib15","doi-asserted-by":"crossref","first-page":"e37929","DOI":"10.1371\/journal.pone.0037929","article-title":"Impaired heat shock response in cells expressing full-length polyglutamine-expanded huntingtin","volume":"7","author":"Chafekar","year":"2012","journal-title":"PLoS One"},{"key":"10.1074\/jbc.C113.481945_bib16","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's disease and induction of stress proteins as a therapeutic approach","volume":"13","author":"Hay","year":"2004","journal-title":"Hum. Mol. Genet"},{"key":"10.1074\/jbc.C113.481945_bib17","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's disease","volume":"196","author":"Hipp","year":"2012","journal-title":"J. Cell Biol"},{"key":"10.1074\/jbc.C113.481945_bib18","first-page":"4736","article-title":"Coordinate changes in heat shock element-binding activity and HSP70 gene transcription rates in human cells","volume":"8","author":"Mosser","year":"1988","journal-title":"Mol. Cell. Biol"},{"key":"10.1074\/jbc.C113.481945_bib19","doi-asserted-by":"crossref","first-page":"467","DOI":"10.1038\/nmeth.1930","article-title":"Tracking protein aggregation and mislocalization in cells with flow cytometry","volume":"9","author":"Ramdzan","year":"2012","journal-title":"Nat. Methods"},{"key":"10.1074\/jbc.C113.481945_bib20","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1038\/embor.2010.203","article-title":"BAG3 mediates chaperone-based aggresome-targeting and selective autophagy of misfolded proteins","volume":"12","author":"Gamerdinger","year":"2011","journal-title":"EMBO Rep"},{"key":"10.1074\/jbc.C113.481945_bib21","doi-asserted-by":"crossref","first-page":"879","DOI":"10.1038\/nmeth.1697","article-title":"Firefly luciferase mutants as sensors of proteome stress","volume":"8","author":"Gupta","year":"2011","journal-title":"Nat. Methods"},{"key":"10.1074\/jbc.C113.481945_bib22","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:S0021925820452536?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820452536?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/syndication.highwire.org\/content\/doi\/10.1074\/jbc.C113.481945","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,1,4]],"date-time":"2022-01-04T14:19:15Z","timestamp":1641305955000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925820452536"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2013,8]]},"references-count":22,"journal-issue":{"issue":"33","published-print":{"date-parts":[[2013,8]]}},"alternative-id":["S0021925820452536"],"URL":"https:\/\/doi.org\/10.1074\/jbc.c113.481945","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2013,8]]}}}