{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T18:11:50Z","timestamp":1790878310014,"version":"4.1.0"},"reference-count":47,"publisher":"Elsevier BV","issue":"4","license":[{"start":{"date-parts":[[2019,5,1]],"date-time":"2019-05-01T00:00:00Z","timestamp":1556668800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2019,5,1]],"date-time":"2019-05-01T00:00:00Z","timestamp":1556668800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2019,3,19]],"date-time":"2019-03-19T00:00:00Z","timestamp":1552953600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["A01"],"award-info":[{"award-number":["A01"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["A07"],"award-info":[{"award-number":["A07"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["SFB969"],"award-info":[{"award-number":["SFB969"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000854","name":"Human Frontier Science Program","doi-asserted-by":"publisher","award":["RGP0025"],"award-info":[{"award-number":["RGP0025"]}],"id":[{"id":"10.13039\/501100000854","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100010269","name":"Wellcome Trust","doi-asserted-by":"publisher","award":["09154\/Z\/15\/Z"],"award-info":[{"award-number":["09154\/Z\/15\/Z"]}],"id":[{"id":"10.13039\/100010269","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000781","name":"European Research Council","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100000781","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100004412","name":"Human Frontier Science Program","doi-asserted-by":"publisher","award":["RGP0025\/2012"],"award-info":[{"award-number":["RGP0025\/2012"]}],"id":[{"id":"10.13039\/100004412","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100011102","name":"Seventh Framework Programme","doi-asserted-by":"publisher","award":["322408"],"award-info":[{"award-number":["322408"]}],"id":[{"id":"10.13039\/100011102","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000268","name":"Biotechnology and Biological Sciences Research Council","doi-asserted-by":"publisher","award":["BB\/J014443\/1"],"award-info":[{"award-number":["BB\/J014443\/1"]}],"id":[{"id":"10.13039\/501100000268","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000268","name":"Biotechnology and Biological Sciences Research Council","doi-asserted-by":"publisher","award":["BB\/P000037\/1"],"award-info":[{"award-number":["BB\/P000037\/1"]}],"id":[{"id":"10.13039\/501100000268","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000268","name":"Biotechnology and Biological Sciences Research Council","doi-asserted-by":"publisher","award":["BB\/K01451X\/1"],"award-info":[{"award-number":["BB\/K01451X\/1"]}],"id":[{"id":"10.13039\/501100000268","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["cell.com","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Molecular Cell"],"published-print":{"date-parts":[[2019,5]]},"DOI":"10.1016\/j.molcel.2019.03.012","type":"journal-article","created":{"date-parts":[[2019,4,11]],"date-time":"2019-04-11T12:05:53Z","timestamp":1554984353000},"page":"729-741.e7","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":51,"title":["Dual Role of Ribosome-Binding Domain of NAC as a Potent Suppressor of Protein Aggregation and Aging-Related Proteinopathies"],"prefix":"10.1016","volume":"74","author":[{"given":"Koning","family":"Shen","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Martin","family":"Gamerdinger","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rebecca","family":"Chan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Karina","family":"Gense","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Esther M.","family":"Martin","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nadine","family":"Sachs","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Patrick D.","family":"Knight","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Renate","family":"Schl\u00f6mer","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Antonio N.","family":"Calabrese","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Katie L.","family":"Stewart","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lukas","family":"Leiendecker","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ankit","family":"Baghel","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sheena E.","family":"Radford","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Judith","family":"Frydman","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Elke","family":"Deuerling","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.molcel.2019.03.012_bib1","doi-asserted-by":"crossref","first-page":"aac4354","DOI":"10.1126\/science.aac4354","article-title":"In\u00a0vivo aspects of protein folding and quality control","volume":"353","author":"Balchin","year":"2016","journal-title":"Science"},{"key":"10.1016\/j.molcel.2019.03.012_bib2","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1093\/genetics\/77.1.71","article-title":"The genetics of Caenorhabditis elegans","volume":"77","author":"Brenner","year":"1974","journal-title":"Genetics"},{"key":"10.1016\/j.molcel.2019.03.012_bib3","doi-asserted-by":"crossref","first-page":"1604","DOI":"10.1126\/science.1124646","article-title":"Opposing activities protect against age-onset proteotoxicity","volume":"313","author":"Cohen","year":"2006","journal-title":"Science"},{"key":"10.1016\/j.molcel.2019.03.012_bib4","doi-asserted-by":"crossref","first-page":"e1001100","DOI":"10.1371\/journal.pbio.1001100","article-title":"Defining the specificity of cotranslationally acting chaperones by systematic analysis of mRNAs associated with ribosome-nascent chain complexes","volume":"9","author":"del Alamo","year":"2011","journal-title":"PLoS Biol."},{"key":"10.1016\/j.molcel.2019.03.012_bib5","doi-asserted-by":"crossref","first-page":"379","DOI":"10.1016\/j.molcel.2013.03.010","article-title":"Principles of cotranslational ubiquitination and quality control at the ribosome","volume":"50","author":"Duttler","year":"2013","journal-title":"Mol. Cell"},{"key":"10.1016\/j.molcel.2019.03.012_bib6","doi-asserted-by":"crossref","first-page":"1375","DOI":"10.1038\/ng.248","article-title":"Single-copy insertion of transgenes in Caenorhabditis elegans","volume":"40","author":"Fr\u00f8kjaer-Jensen","year":"2008","journal-title":"Nat. Genet."},{"key":"10.1016\/j.molcel.2019.03.012_bib7","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1126\/science.aaa5335","article-title":"The principle of antagonism ensures protein targeting specificity at the endoplasmic reticulum","volume":"348","author":"Gamerdinger","year":"2015","journal-title":"Science"},{"key":"10.1016\/j.molcel.2019.03.012_bib8","doi-asserted-by":"crossref","first-page":"76","DOI":"10.1007\/s13361-011-0261-2","article-title":"StavroX--a software for analyzing crosslinked products in protein interaction studies","volume":"23","author":"G\u00f6tze","year":"2012","journal-title":"J.\u00a0Am. Soc. Mass Spectrom."},{"key":"10.1016\/j.molcel.2019.03.012_bib9","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":"10.1016\/j.molcel.2019.03.012_bib10","first-page":"838","article-title":"Screening for amyloid aggregation by Semi-Denaturing Detergent-Agarose Gel Electrophoresis","volume":"17","author":"Halfmann","year":"2008","journal-title":"J.\u00a0Vis. Exp."},{"key":"10.1016\/j.molcel.2019.03.012_bib11","doi-asserted-by":"crossref","first-page":"e1601625","DOI":"10.1126\/sciadv.1601625","article-title":"A molecular mechanism of chaperone-client recognition","volume":"2","author":"He","year":"2016","journal-title":"Sci. Adv."},{"key":"10.1016\/j.molcel.2019.03.012_bib12","doi-asserted-by":"crossref","first-page":"691","DOI":"10.1038\/nsmb.3237","article-title":"Visualizing chaperone-assisted protein folding","volume":"23","author":"Horowitz","year":"2016","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.molcel.2019.03.012_bib13","doi-asserted-by":"crossref","first-page":"1042","DOI":"10.1016\/j.cell.2014.10.042","article-title":"The structural basis of substrate recognition by the eukaryotic chaperonin TRiC\/CCT","volume":"159","author":"Joachimiak","year":"2014","journal-title":"Cell"},{"key":"10.1016\/j.molcel.2019.03.012_bib14","doi-asserted-by":"crossref","first-page":"272","DOI":"10.1016\/j.molcel.2016.03.017","article-title":"The S\/T-rich motif in the DNAJB6 chaperone delays polyglutamine aggregation and the onset of disease in a mouse model","volume":"62","author":"Kakkar","year":"2016","journal-title":"Mol. Cell"},{"key":"10.1016\/j.molcel.2019.03.012_bib15","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.molcel.2019.03.012_bib16","doi-asserted-by":"crossref","first-page":"1451","DOI":"10.1038\/emboj.2013.87","article-title":"The nascent polypeptide-associated complex is a key regulator of proteostasis","volume":"32","author":"Kirstein-Miles","year":"2013","journal-title":"EMBO J."},{"key":"10.1016\/j.molcel.2019.03.012_bib17","doi-asserted-by":"crossref","first-page":"378","DOI":"10.1016\/j.tibs.2013.05.003","article-title":"Huntington\u2019s disease: underlying molecular mechanisms and emerging concepts","volume":"38","author":"Labbadia","year":"2013","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.molcel.2019.03.012_bib18","doi-asserted-by":"crossref","first-page":"2890","DOI":"10.1021\/bi902050p","article-title":"The crystal structure of the human nascent polypeptide-associated complex domain reveals a nucleic acid-binding region on the NACA subunit","volume":"49","author":"Liu","year":"2010","journal-title":"Biochemistry"},{"key":"10.1016\/j.molcel.2019.03.012_bib19","doi-asserted-by":"crossref","first-page":"8554","DOI":"10.1074\/jbc.RA117.001568","article-title":"Conformational flexibility within the nascent polypeptide-associated complex enables its interactions with structurally diverse client proteins","volume":"293","author":"Martin","year":"2018","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.molcel.2019.03.012_bib20","doi-asserted-by":"crossref","first-page":"26","DOI":"10.1016\/j.pneurobio.2011.06.007","article-title":"Polyglutamine diseases: the special case of ataxin-3 and Machado-Joseph disease","volume":"95","author":"Matos","year":"2011","journal-title":"Prog. Neurobiol."},{"key":"10.1016\/j.molcel.2019.03.012_bib21","doi-asserted-by":"crossref","first-page":"451","DOI":"10.1016\/S0091-679X(08)61399-0","article-title":"DNA transformation","volume":"48","author":"Mello","year":"1995","journal-title":"Methods Cell Biol."},{"key":"10.1016\/j.molcel.2019.03.012_bib22","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. USA"},{"key":"10.1016\/j.molcel.2019.03.012_bib23","doi-asserted-by":"crossref","first-page":"e0143457","DOI":"10.1371\/journal.pone.0143457","article-title":"Functional dissection of the nascent polypeptide-associated complex in saccharomyces cerevisiae","volume":"10","author":"Ott","year":"2015","journal-title":"PLoS ONE"},{"key":"10.1016\/j.molcel.2019.03.012_bib24","doi-asserted-by":"crossref","first-page":"19679","DOI":"10.1074\/jbc.M109.092536","article-title":"Dual binding mode of the nascent polypeptide-associated complex reveals a novel universal adapter site on the ribosome","volume":"285","author":"Pech","year":"2010","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.molcel.2019.03.012_bib25","doi-asserted-by":"crossref","first-page":"411","DOI":"10.1016\/j.molcel.2013.01.020","article-title":"The ribosome as a hub for protein quality control","volume":"49","author":"Pechmann","year":"2013","journal-title":"Mol. Cell"},{"key":"10.1016\/j.molcel.2019.03.012_bib26","doi-asserted-by":"crossref","first-page":"274","DOI":"10.1016\/j.tibs.2012.03.002","article-title":"Ribosome-associated chaperones as key players in proteostasis","volume":"37","author":"Preissler","year":"2012","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.molcel.2019.03.012_bib27","doi-asserted-by":"crossref","first-page":"7809","DOI":"10.1074\/jbc.M611436200","article-title":"Association of protein biogenesis factors at the yeast ribosomal tunnel exit is affected by the translational status and nascent polypeptide sequence","volume":"282","author":"Raue","year":"2007","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.molcel.2019.03.012_bib28","doi-asserted-by":"crossref","first-page":"630","DOI":"10.1038\/nrm3658","article-title":"Chaperone machines for protein folding, unfolding and disaggregation","volume":"14","author":"Saibil","year":"2013","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.molcel.2019.03.012_bib29","doi-asserted-by":"crossref","first-page":"1250494","DOI":"10.1126\/science.1250494","article-title":"Structural basis for protein antiaggregation activity of the trigger factor chaperone","volume":"344","author":"Saio","year":"2014","journal-title":"Science"},{"key":"10.1016\/j.molcel.2019.03.012_bib30","doi-asserted-by":"crossref","first-page":"1231","DOI":"10.1083\/jcb.201612111","article-title":"Shaping proteostasis at the cellular, tissue, and organismal level","volume":"216","author":"Sala","year":"2017","journal-title":"J.\u00a0Cell Biol."},{"key":"10.1016\/j.molcel.2019.03.012_bib31","doi-asserted-by":"crossref","first-page":"447","DOI":"10.1093\/protein\/gzp033","article-title":"Multi-domain misfolding: understanding the aggregation pathway of polyglutamine proteins","volume":"22","author":"Saunders","year":"2009","journal-title":"Protein Eng. Des. Sel."},{"key":"10.1016\/j.molcel.2019.03.012_bib32","doi-asserted-by":"crossref","first-page":"1241","DOI":"10.1074\/mcp.M114.044610","article-title":"Examination of Ataxin-3 (atx-3) aggregation by structural mass spectrometry techniques: a rationale for expedited aggregation upon polyglutamine (polyQ) expansion","volume":"14","author":"Scarff","year":"2015","journal-title":"Mol. Cell. Proteomics"},{"key":"10.1016\/j.molcel.2019.03.012_bib33","doi-asserted-by":"crossref","first-page":"676","DOI":"10.1038\/nmeth.2019","article-title":"Fiji: an open-source platform for biological-image analysis","volume":"9","author":"Schindelin","year":"2012","journal-title":"Nat. Methods"},{"key":"10.1016\/j.molcel.2019.03.012_bib34","doi-asserted-by":"crossref","first-page":"4137","DOI":"10.1002\/j.1460-2075.1993.tb06097.x","article-title":"DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage","volume":"12","author":"Schr\u00f6der","year":"1993","journal-title":"EMBO J."},{"key":"10.1016\/j.molcel.2019.03.012_bib35","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1007\/s12013-010-9138-4","article-title":"Novel cell- and tissue-based assays for detecting misfolded and aggregated protein accumulation within aggresomes and inclusion bodies","volume":"60","author":"Shen","year":"2011","journal-title":"Cell Biochem. Biophys."},{"key":"10.1016\/j.molcel.2019.03.012_bib36","doi-asserted-by":"crossref","first-page":"2449","DOI":"10.1016\/j.jmb.2017.07.003","article-title":"Molecular Origins of the Compatibility between Glycosaminoglycans and A\u03b240 Amyloid Fibrils","volume":"429","author":"Stewart","year":"2017","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.molcel.2019.03.012_bib37","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1038\/nsmb.3133","article-title":"Substrate protein folds while it is bound to the ATP-independent chaperone Spy","volume":"23","author":"Stull","year":"2016","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.molcel.2019.03.012_bib38","doi-asserted-by":"crossref","first-page":"e33980","DOI":"10.1371\/journal.pone.0033980","article-title":"The lid domain of Caenorhabditis elegans Hsc70 influences ATP turnover, cofactor binding and protein folding activity","volume":"7","author":"Sun","year":"2012","journal-title":"PLoS ONE"},{"key":"10.1016\/j.molcel.2019.03.012_bib39","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.molcel.2019.03.012_bib40","doi-asserted-by":"crossref","first-page":"1279","DOI":"10.1038\/nsmb.1700","article-title":"The chaperonin TRiC blocks a huntingtin sequence element that promotes the conformational switch to aggregation","volume":"16","author":"Tam","year":"2009","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.molcel.2019.03.012_bib41","doi-asserted-by":"crossref","first-page":"2799","DOI":"10.1093\/hmg\/9.19.2799","article-title":"Dominant phenotypes produced by the HD mutation in STHdh(Q111) striatal cells","volume":"9","author":"Trettel","year":"2000","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.molcel.2019.03.012_bib42","doi-asserted-by":"crossref","first-page":"1266","DOI":"10.1111\/j.1742-4658.2008.06862.x","article-title":"A facile method for expression and purification of the Alzheimer\u2019s disease-associated amyloid beta-peptide","volume":"276","author":"Walsh","year":"2009","journal-title":"FEBS J."},{"key":"10.1016\/j.molcel.2019.03.012_bib43","doi-asserted-by":"crossref","first-page":"519","DOI":"10.1083\/jcb.130.3.519","article-title":"NAC covers ribosome-associated nascent chains thereby forming a protective environment for regions of nascent chains just emerging from the peptidyl transferase center","volume":"130","author":"Wang","year":"1995","journal-title":"J.\u00a0Cell Biol."},{"key":"10.1016\/j.molcel.2019.03.012_bib44","doi-asserted-by":"crossref","first-page":"406","DOI":"10.1007\/s13238-010-0049-3","article-title":"Crystal structures of NAC domains of human nascent polypeptide-associated complex (NAC) and its \u03b1NAC subunit","volume":"1","author":"Wang","year":"2010","journal-title":"Protein Cell"},{"key":"10.1016\/j.molcel.2019.03.012_bib45","doi-asserted-by":"crossref","first-page":"368","DOI":"10.1016\/j.molcel.2013.03.009","article-title":"A cotranslational ubiquitination pathway for quality control of misfolded proteins","volume":"50","author":"Wang","year":"2013","journal-title":"Mol. Cell"},{"key":"10.1016\/j.molcel.2019.03.012_bib46","doi-asserted-by":"crossref","first-page":"2847","DOI":"10.1074\/jbc.M511420200","article-title":"A conserved motif is prerequisite for the interaction of NAC with ribosomal protein L23 and nascent chains","volume":"281","author":"Wegrzyn","year":"2006","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.molcel.2019.03.012_bib47","doi-asserted-by":"crossref","first-page":"434","DOI":"10.1038\/370434a0","article-title":"A protein complex required for signal-sequence-specific sorting and translocation","volume":"370","author":"Wiedmann","year":"1994","journal-title":"Nature"}],"container-title":["Molecular Cell"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1097276519301868?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1097276519301868?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,5,12]],"date-time":"2026-05-12T12:49:40Z","timestamp":1778590180000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1097276519301868"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2019,5]]},"references-count":47,"journal-issue":{"issue":"4","published-print":{"date-parts":[[2019,5]]}},"alternative-id":["S1097276519301868"],"URL":"https:\/\/doi.org\/10.1016\/j.molcel.2019.03.012","relation":{},"ISSN":["1097-2765"],"issn-type":[{"value":"1097-2765","type":"print"}],"subject":[],"published":{"date-parts":[[2019,5]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Dual Role of Ribosome-Binding Domain of NAC as a Potent Suppressor of Protein Aggregation and Aging-Related Proteinopathies","name":"articletitle","label":"Article Title"},{"value":"Molecular Cell","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.molcel.2019.03.012","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2019 The Authors. Published by Elsevier Inc.","name":"copyright","label":"Copyright"}]}}