{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,14]],"date-time":"2026-10-14T17:35:54Z","timestamp":1791999354965,"version":"4.4.0"},"reference-count":43,"publisher":"Elsevier BV","issue":"42","license":[{"start":{"date-parts":[[2015,10,1]],"date-time":"2015-10-01T00:00:00Z","timestamp":1443657600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,9,6]],"date-time":"2020-09-06T00:00:00Z","timestamp":1599350400000},"content-version":"vor","delay-in-days":1802,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000065","name":"National Institute of Neurological Disorders and Stroke","doi-asserted-by":"publisher","award":["NS073936"],"award-info":[{"award-number":["NS073936"]}],"id":[{"id":"10.13039\/100000065","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Advancing a Healthier Wisconsin"}],"content-domain":{"domain":["jbc.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2015,10]]},"DOI":"10.1074\/jbc.m115.676247","type":"journal-article","created":{"date-parts":[[2015,9,2]],"date-time":"2015-09-02T23:58:04Z","timestamp":1441238284000},"page":"25571-25578","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":31,"title":["The Social Amoeba Dictyostelium discoideum Is Highly Resistant to Polyglutamine Aggregation"],"prefix":"10.1016","volume":"290","author":[{"given":"Stephanie","family":"Santarriaga","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Amber","family":"Petersen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kelechi","family":"Ndukwe","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anthony","family":"Brandt","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nashaat","family":"Gerges","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jamie","family":"Bruns Scaglione","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kenneth Matthew","family":"Scaglione","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1074\/jbc.M115.676247_bib1","doi-asserted-by":"crossref","first-page":"521","DOI":"10.1016\/j.tins.2008.07.004","article-title":"Polyglutamine neurodegeneration: protein misfolding revisited","volume":"31","author":"Williams","year":"2008","journal-title":"Trends Neurosci"},{"key":"10.1074\/jbc.M115.676247_bib2","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1007\/978-1-62703-438-8_11","article-title":"Yeast as a platform to explore polyglutamine toxicity and aggregation","volume":"1017","author":"Duennwald","year":"2013","journal-title":"Methods Mol. Biol"},{"key":"10.1074\/jbc.M115.676247_bib3","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1016\/S0092-8674(00)81781-X","article-title":"Ataxin-1 nuclear localization and aggregation: role in polyglutamine-induced disease in SCA1 transgenic mice","volume":"95","author":"Klement","year":"1998","journal-title":"Cell"},{"key":"10.1074\/jbc.M115.676247_bib4","doi-asserted-by":"crossref","first-page":"7431","DOI":"10.1074\/jbc.R800065200","article-title":"Animal models of polyglutamine diseases and therapeutic approaches","volume":"284","author":"Marsh","year":"2009","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M115.676247_bib5","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1016\/S0896-6273(00)80943-5","article-title":"Intranuclear inclusions of expanded polyglutamine protein in spinocerebellar ataxia type 3","volume":"19","author":"Paulson","year":"1997","journal-title":"Neuron"},{"key":"10.1074\/jbc.M115.676247_bib6","doi-asserted-by":"crossref","first-page":"430","DOI":"10.1007\/s12035-012-8316-3","article-title":"Mouse models of polyglutamine diseases in therapeutic approaches: review and data table. Part II","volume":"46","author":"Switonski","year":"2012","journal-title":"Mol. Neurobiol"},{"key":"10.1074\/jbc.M115.676247_bib7","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1016\/B978-0-12-387003-2.00008-2","article-title":"Modeling human trinucleotide repeat diseases in Drosophila","volume":"99","author":"Yu","year":"2011","journal-title":"Int. Rev. Neurobiol"},{"key":"10.1074\/jbc.M115.676247_bib8","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1016\/j.jbiotec.2015.05.003","article-title":"A plant cell model of polyglutamine aggregation: identification and characterisation of macromolecular and small-molecule anti-protein aggregation activity in vivo","volume":"207","author":"Liu","year":"2015","journal-title":"J. Biotechnol"},{"key":"10.1074\/jbc.M115.676247_bib9","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1038\/nature03481","article-title":"The genome of the social amoeba Dictyostelium discoideum","volume":"435","author":"Eichinger","year":"2005","journal-title":"Nature"},{"key":"10.1074\/jbc.M115.676247_bib10","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0046150","article-title":"Amino acid repeats cause extraordinary coding sequence variation in the social amoeba Dictyostelium discoideum","volume":"7","author":"Scala","year":"2012","journal-title":"PLoS One"},{"key":"10.1074\/jbc.M115.676247_bib11","doi-asserted-by":"crossref","first-page":"E2620","DOI":"10.1073\/pnas.1504459112","article-title":"Dictyostelium discoideum has a highly Q\/N-rich proteome and shows an unusual resilience to protein aggregation","volume":"112","author":"Malinovska","year":"2015","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M115.676247_bib12","doi-asserted-by":"crossref","first-page":"1127","DOI":"10.1083\/jcb.201005046","article-title":"Molecular architecture of a dynamin adaptor: implications for assembly of mitochondrial fission complexes","volume":"191","author":"Koirala","year":"2010","journal-title":"J. Cell Biol"},{"key":"10.1074\/jbc.M115.676247_bib13","doi-asserted-by":"crossref","first-page":"493","DOI":"10.1002\/yea.320110602","article-title":"Isolation and biochemical characterization of organelles from the yeast, Saccharomyces cerevisiae","volume":"11","author":"Zinser","year":"1995","journal-title":"Yeast"},{"key":"10.1074\/jbc.M115.676247_bib14","doi-asserted-by":"crossref","first-page":"1307","DOI":"10.1038\/nprot.2007.178","article-title":"Protocols for growth and development of Dictyostelium discoideum","volume":"2","author":"Fey","year":"2007","journal-title":"Nat. Protoc"},{"key":"10.1074\/jbc.M115.676247_bib15","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1006\/plas.1999.1391","article-title":"Variables controlling the expression level of exogenous genes in Dictyostelium","volume":"41","author":"Pang","year":"1999","journal-title":"Plasmid"},{"key":"10.1074\/jbc.M115.676247_bib16","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1083\/jcb.200504050","article-title":"Structural properties and neuronal toxicity of amyotrophic lateral sclerosis-associated Cu\/Zn superoxide dismutase 1 aggregates","volume":"171","author":"Matsumoto","year":"2005","journal-title":"J. Cell Biol"},{"key":"10.1074\/jbc.M115.676247_bib17","doi-asserted-by":"crossref","DOI":"10.1101\/pdb.top065482","article-title":"Live cell imaging of yeast","volume":"2011","author":"Rines","year":"2011","journal-title":"Cold Spring Harb. Protoc"},{"key":"10.1074\/jbc.M115.676247_bib18","doi-asserted-by":"crossref","DOI":"10.1038\/srep11135","article-title":"Neurogranin regulates CaM dynamics at dendritic spines","volume":"5","author":"Petersen","year":"2015","journal-title":"Sci. Rep"},{"key":"10.1074\/jbc.M115.676247_bib19","doi-asserted-by":"crossref","first-page":"1135","DOI":"10.1016\/j.celrep.2014.09.042","article-title":"A chaperone subnetwork safeguards proteostasis in aging and neurodegenerative disease","volume":"9","author":"Brehme","year":"2014","journal-title":"Cell Rep"},{"key":"10.1074\/jbc.M115.676247_bib20","doi-asserted-by":"crossref","first-page":"457","DOI":"10.1007\/s12192-009-0155-4","article-title":"Why proteins without an \u03b1-crystallin domain should not be included in the human small heat shock protein family HSPB","volume":"15","author":"Kapp\u00e9","year":"2010","journal-title":"Cell Stress Chaperones"},{"key":"10.1074\/jbc.M115.676247_bib21","doi-asserted-by":"crossref","first-page":"575","DOI":"10.1146\/annurev.neuro.29.051605.113042","article-title":"Trinucleotide repeat disorders","volume":"30","author":"Orr","year":"2007","journal-title":"Annu. Rev. Neurosci"},{"key":"10.1074\/jbc.M115.676247_bib22","doi-asserted-by":"crossref","first-page":"403","DOI":"10.1038\/378403a0","article-title":"Polyglutamine expansion as a pathological epitope in Huntington's disease and four dominant cerebellar ataxias","volume":"378","author":"Trottier","year":"1995","journal-title":"Nature"},{"issue":"Suppl. 1","key":"10.1074\/jbc.M115.676247_bib23","doi-asserted-by":"crossref","first-page":"S277","DOI":"10.1111\/j.1440-169X.2008.01013.x","article-title":"Developmental biology of the social amoeba: history, current knowledge and prospects","volume":"50","author":"Urushihara","year":"2008","journal-title":"Dev. Growth Differ"},{"key":"10.1074\/jbc.M115.676247_bib24","doi-asserted-by":"crossref","first-page":"1589","DOI":"10.1073\/pnas.97.4.1589","article-title":"Aggregation of huntingtin in yeast varies with the length of the polyglutamine expansion and the expression of chaperone proteins","volume":"97","author":"Krobitsch","year":"2000","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M115.676247_bib25","doi-asserted-by":"crossref","first-page":"997","DOI":"10.1083\/jcb.200112104","article-title":"Huntington toxicity in yeast model depends on polyglutamine aggregation mediated by a prion-like protein Rnq1","volume":"157","author":"Meriin","year":"2002","journal-title":"J. Cell Biol"},{"key":"10.1074\/jbc.M115.676247_bib26","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.M115.676247_bib27","doi-asserted-by":"crossref","first-page":"777","DOI":"10.1093\/hmg\/7.5.777","article-title":"Aggregation of N-terminal huntingtin is dependent on the length of its glutamine repeats","volume":"7","author":"Li","year":"1998","journal-title":"Hum. Mol. Genet"},{"key":"10.1074\/jbc.M115.676247_bib28","doi-asserted-by":"crossref","DOI":"10.1038\/ncomms2306","article-title":"Plasmodium falciparum heat shock protein 110 stabilizes the asparagine repeat-rich parasite proteome during malarial fevers","volume":"3","author":"Muralidharan","year":"2012","journal-title":"Nat. Commun"},{"key":"10.1074\/jbc.M115.676247_bib29","doi-asserted-by":"crossref","first-page":"630","DOI":"10.1016\/j.febslet.2011.01.020","article-title":"Both plant and animal LEA proteins act as kinetic stabilisers of polyglutamine-dependent protein aggregation","volume":"585","author":"Liu","year":"2011","journal-title":"FEBS Lett"},{"key":"10.1074\/jbc.M115.676247_bib30","doi-asserted-by":"crossref","first-page":"6","DOI":"10.1104\/pp.108.120725","article-title":"The enigmatic LEA proteins and other hydrophilins","volume":"148","author":"Battaglia","year":"2008","journal-title":"Plant Physiol"},{"key":"10.1074\/jbc.M115.676247_bib31","doi-asserted-by":"crossref","first-page":"475","DOI":"10.1007\/BF00036962","article-title":"Common amino acid sequence domains among the LEA proteins of higher plants","volume":"12","author":"Dure","year":"1989","journal-title":"Plant Mol. Biol"},{"key":"10.1074\/jbc.M115.676247_bib32","doi-asserted-by":"crossref","first-page":"5668","DOI":"10.1074\/jbc.275.8.5668","article-title":"Highly hydrophilic proteins in prokaryotes and eukaryotes are common during conditions of water deficit","volume":"275","author":"Garay-Arroyo","year":"2000","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M115.676247_bib33","doi-asserted-by":"crossref","first-page":"140","DOI":"10.1006\/cryo.2001.2358","article-title":"Induction of desiccation tolerance in plant somatic embryos: how exclusive is the protective role of sugars?","volume":"43","author":"Hoekstra","year":"2001","journal-title":"Cryobiology"},{"key":"10.1074\/jbc.M115.676247_bib34","doi-asserted-by":"crossref","first-page":"12085","DOI":"10.1073\/pnas.1412504111","article-title":"Prion-like proteins sequester and suppress the toxicity of huntingtin exon 1","volume":"111","author":"Kayatekin","year":"2014","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M115.676247_bib35","doi-asserted-by":"crossref","first-page":"18219","DOI":"10.1073\/pnas.1421313111","article-title":"Overexpression of Q-rich prion-like proteins suppresses polyQ cytotoxicity and alters the polyQ interactome","volume":"111","author":"Ripaud","year":"2014","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M115.676247_bib36","doi-asserted-by":"crossref","first-page":"1950","DOI":"10.1371\/journal.pgen.0030177","article-title":"Genome-wide screen for modifiers of ataxin-3 neurodegeneration in Drosophila","volume":"3","author":"Bilen","year":"2007","journal-title":"PLoS Genet"},{"key":"10.1074\/jbc.M115.676247_bib37","doi-asserted-by":"crossref","first-page":"1659","DOI":"10.1093\/hmg\/ddi174","article-title":"HspB8, a small heat shock protein mutated in human neuromuscular disorders, has in vivo chaperone activity in cultured cells","volume":"14","author":"Carra","year":"2005","journal-title":"Hum. Mol. Genet"},{"key":"10.1074\/jbc.M115.676247_bib38","doi-asserted-by":"crossref","first-page":"10424","DOI":"10.1073\/pnas.0914773107","article-title":"Small heat-shock proteins interact with a flanking domain to suppress polyglutamine aggregation","volume":"107","author":"Robertson","year":"2010","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M115.676247_bib39","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1042\/BJ20090907","article-title":"Identification of the key structural motifs involved in HspB8\/HspB6-Bag3 interaction","volume":"425","author":"Fuchs","year":"2010","journal-title":"Biochem. J"},{"key":"10.1074\/jbc.M115.676247_bib40","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"},{"issue":"Suppl. 1","key":"10.1074\/jbc.M115.676247_bib41","doi-asserted-by":"crossref","first-page":"S33","DOI":"10.1093\/gerona\/glu049","article-title":"Proteostasis and the aging proteome in health and disease","volume":"69","author":"Morimoto","year":"2014","journal-title":"J. Gerontol. A Biol. Sci. Med. Sci"},{"key":"10.1074\/jbc.M115.676247_bib42","doi-asserted-by":"crossref","first-page":"349","DOI":"10.1016\/j.neuron.2013.12.002","article-title":"Age-dependent decrease in chaperone activity impairs MANF expression, leading to Purkinje cell degeneration in inducible SCA17 mice","volume":"81","author":"Yang","year":"2014","journal-title":"Neuron"},{"key":"10.1074\/jbc.M115.676247_bib43","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0072457","article-title":"Total protein analysis as a reliable loading control for quantitative fluorescent Western blotting","volume":"8","author":"Eaton","year":"2013","journal-title":"PLoS One"}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820445739?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820445739?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/syndication.highwire.org\/content\/doi\/10.1074\/jbc.M115.676247","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,12,18]],"date-time":"2021-12-18T13:55:46Z","timestamp":1639835746000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925820445739"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2015,10]]},"references-count":43,"journal-issue":{"issue":"42","published-print":{"date-parts":[[2015,10]]}},"alternative-id":["S0021925820445739"],"URL":"https:\/\/doi.org\/10.1074\/jbc.m115.676247","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2015,10]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"The Social Amoeba Dictyostelium discoideum Is Highly Resistant to Polyglutamine Aggregation","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1074\/jbc.M115.676247","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"}]}}