{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,26]],"date-time":"2026-08-26T19:55:55Z","timestamp":1787774155223,"version":"build-2784847793"},"reference-count":38,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2019,6,1]],"date-time":"2019-06-01T00:00:00Z","timestamp":1559347200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2019,6,1]],"date-time":"2019-06-01T00:00:00Z","timestamp":1559347200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"funder":[{"DOI":"10.13039\/100008714","name":"Motor Neurone Disease Research Institute of Australia","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100008714","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100010269","name":"Wellcome Trust","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100010269","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000925","name":"National Health and Medical Research Council","doi-asserted-by":"publisher","award":["1084144"],"award-info":[{"award-number":["1084144"]}],"id":[{"id":"10.13039\/501100000925","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000925","name":"National Health and Medical Research Council","doi-asserted-by":"publisher","award":["1095215"],"award-info":[{"award-number":["1095215"]}],"id":[{"id":"10.13039\/501100000925","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000925","name":"National Health and Medical Research Council","doi-asserted-by":"publisher","award":["APP1135720"],"award-info":[{"award-number":["APP1135720"]}],"id":[{"id":"10.13039\/501100000925","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Neuroscience Letters"],"published-print":{"date-parts":[[2019,6]]},"DOI":"10.1016\/j.neulet.2019.04.001","type":"journal-article","created":{"date-parts":[[2019,4,3]],"date-time":"2019-04-03T21:48:04Z","timestamp":1554328084000},"page":"89-94","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":27,"special_numbering":"C","title":["The metastability of the proteome of spinal motor neurons underlies their selective vulnerability in ALS"],"prefix":"10.1016","volume":"704","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-2528-7039","authenticated-orcid":false,"given":"Justin J.","family":"Yerbury","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9241-8268","authenticated-orcid":false,"given":"Lezanne","family":"Ooi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ian P.","family":"Blair","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Prajwal","family":"Ciryam","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christopher M.","family":"Dobson","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michele","family":"Vendruscolo","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.neulet.2019.04.001_bib0005","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1146\/annurev-biochem-061516-045115","article-title":"Protein misfolding, amyloid formation, and human disease: a summary of progress over the last decade","volume":"86","author":"Chiti","year":"2017","journal-title":"Annu. Rev. Biochem."},{"issue":"8","key":"10.1016\/j.neulet.2019.04.001_bib0010","doi-asserted-by":"crossref","first-page":"649","DOI":"10.1097\/01.jnen.0000173889.71434.ea","article-title":"The pathobiology of amyotrophic lateral sclerosis: a proteinopathy?","volume":"64","author":"Strong","year":"2005","journal-title":"J. Neuropathol. Exp. Neurol."},{"issue":"10107","key":"10.1016\/j.neulet.2019.04.001_bib0015","doi-asserted-by":"crossref","first-page":"2084","DOI":"10.1016\/S0140-6736(17)31287-4","article-title":"Amyotrophic lateral sclerosis","volume":"390","author":"van Es","year":"2017","journal-title":"Lancet"},{"key":"10.1016\/j.neulet.2019.04.001_bib0020","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1146\/annurev.biochem.75.101304.123901","article-title":"Protein misfolding, functional amyloid, and human disease","volume":"75","author":"Chiti","year":"2006","journal-title":"Annu. Rev. Biochem."},{"issue":"6","key":"10.1016\/j.neulet.2019.04.001_bib0025","doi-asserted-by":"crossref","first-page":"384","DOI":"10.1038\/nrm3810","article-title":"The amyloid state and its association with protein misfolding diseases","volume":"15","author":"Knowles","year":"2014","journal-title":"Nat. Rev. Mol. Cell Biol."},{"issue":"8","key":"10.1016\/j.neulet.2019.04.001_bib0030","doi-asserted-by":"crossref","first-page":"735","DOI":"10.1021\/cb1001203","article-title":"ANS binding reveals common features of cytotoxic amyloid species","volume":"5","author":"Bolognesi","year":"2010","journal-title":"ACS Chem. Biol."},{"issue":"2","key":"10.1016\/j.neulet.2019.04.001_bib0035","doi-asserted-by":"crossref","first-page":"351","DOI":"10.1111\/j.1750-3639.2009.00284.x","article-title":"TDP-43 redistribution is an early event in sporadic amyotrophic lateral sclerosis","volume":"20","author":"Giordana","year":"2010","journal-title":"Brain Pathol."},{"issue":"3","key":"10.1016\/j.neulet.2019.04.001_bib0040","doi-asserted-by":"crossref","first-page":"423","DOI":"10.1007\/s00401-014-1299-6","article-title":"TDP-43 pathology and neuronal loss in amyotrophic lateral sclerosis spinal cord","volume":"128","author":"Brettschneider","year":"2014","journal-title":"Acta Neuropathol."},{"issue":"3","key":"10.1016\/j.neulet.2019.04.001_bib0045","doi-asserted-by":"crossref","first-page":"285","DOI":"10.2174\/187152710791292585","article-title":"Protein aggregation and defective RNA metabolism as mechanisms for motor neuron damage","volume":"9","author":"Ticozzi","year":"2010","journal-title":"Cns Neurol. Disord. - Drug Targets"},{"issue":"2","key":"10.1016\/j.neulet.2019.04.001_bib0050","doi-asserted-by":"crossref","first-page":"775","DOI":"10.1093\/brain\/114.2.775","article-title":"Ubiquitin-immunoreactive intraneuronal inclusions in amyotrophic lateral sclerosis. Morphology, distribution, and specificity","volume":"114","author":"Leigh","year":"1991","journal-title":"Brain"},{"key":"10.1016\/j.neulet.2019.04.001_bib0055","doi-asserted-by":"crossref","first-page":"499","DOI":"10.3389\/fnins.2016.00499","article-title":"Susceptibility of mutant SOD1 to form a destabilized monomer predicts cellular aggregation and toxicity but not in vitro aggregation propensity","volume":"10","author":"McAlary","year":"2016","journal-title":"Front. Neurosci."},{"issue":"6","key":"10.1016\/j.neulet.2019.04.001_bib0060","doi-asserted-by":"crossref","first-page":"791","DOI":"10.1007\/s00401-014-1342-7","article-title":"Experimental transmissibility of mutant SOD1 motor neuron disease","volume":"128","author":"Ayers","year":"2014","journal-title":"Acta Neuropathol."},{"issue":"9","key":"10.1016\/j.neulet.2019.04.001_bib0065","doi-asserted-by":"crossref","first-page":"3620","DOI":"10.1073\/pnas.1312245111","article-title":"Intercellular propagated misfolding of wild-type Cu\/Zn superoxide dismutase occurs via exosome-dependent and -independent mechanisms","volume":"111","author":"Grad","year":"2014","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.neulet.2019.04.001_bib0070","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1186\/s13024-015-0053-4","article-title":"SOD1 protein aggregates stimulate macropinocytosis in neurons to facilitate their propagation","volume":"10","author":"Zeineddine","year":"2015","journal-title":"Mol. Neurodegener."},{"issue":"4","key":"10.1016\/j.neulet.2019.04.001_bib0075","doi-asserted-by":"crossref","first-page":"489","DOI":"10.1111\/jnc.13575","article-title":"Walking the tightrope: proteostasis and neurodegenerative disease","volume":"137","author":"Yerbury","year":"2016","journal-title":"J. Neurochem."},{"issue":"5","key":"10.1016\/j.neulet.2019.04.001_bib0080","doi-asserted-by":"crossref","first-page":"204","DOI":"10.1016\/j.tibs.2007.03.005","article-title":"Life on the edge: a link between gene expression levels and aggregation rates of human proteins","volume":"32","author":"Tartaglia","year":"2007","journal-title":"Trends Biochem. Sci."},{"issue":"36","key":"10.1016\/j.neulet.2019.04.001_bib0085","doi-asserted-by":"crossref","first-page":"14160","DOI":"10.1021\/ja2017703","article-title":"Metastability of native proteins and the phenomenon of amyloid formation","volume":"133","author":"Baldwin","year":"2011","journal-title":"J. Am. Chem. Soc."},{"issue":"2","key":"10.1016\/j.neulet.2019.04.001_bib0090","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1002\/1521-3773(20020118)41:2<257::AID-ANIE257>3.0.CO;2-M","article-title":"The \"Correctly Folded\" state of proteins: is it a metastable state?","volume":"41","author":"Gazit","year":"2002","journal-title":"Angew. Chem. Int. Ed. Engl."},{"issue":"20","key":"10.1016\/j.neulet.2019.04.001_bib0095","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.1613854114","article-title":"Spinal motor neuron protein supersaturation patterns are associated with inclusion body formation in ALS","volume":"114","author":"Ciryam","year":"2017","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"2","key":"10.1016\/j.neulet.2019.04.001_bib0100","doi-asserted-by":"crossref","first-page":"72","DOI":"10.1016\/j.tips.2014.12.004","article-title":"Supersaturation is a major driving force for protein aggregation in neurodegenerative diseases","volume":"36","author":"Ciryam","year":"2015","journal-title":"Trends Pharmacol. Sci."},{"issue":"3","key":"10.1016\/j.neulet.2019.04.001_bib0105","doi-asserted-by":"crossref","first-page":"781","DOI":"10.1016\/j.celrep.2013.09.043","article-title":"Widespread aggregation and neurodegenerative diseases are associated with supersaturated proteins","volume":"5","author":"Ciryam","year":"2013","journal-title":"Cell Rep."},{"issue":"11","key":"10.1016\/j.neulet.2019.04.001_bib0110","doi-asserted-by":"crossref","DOI":"10.1242\/jcs.209122","article-title":"SOD1(A4V) aggregation alters ubiquitin homeostasis in a cell model of ALS","volume":"131","author":"Farrawell","year":"2018","journal-title":"J. Cell. Sci."},{"issue":"8","key":"10.1016\/j.neulet.2019.04.001_bib0115","doi-asserted-by":"crossref","DOI":"10.1126\/sciadv.1600947","article-title":"A protein homeostasis signature in healthy brains recapitulates tissue vulnerability to Alzheimer\u2019s disease","volume":"2","author":"Freer","year":"2016","journal-title":"Sci. Adv."},{"issue":"1","key":"10.1016\/j.neulet.2019.04.001_bib0120","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1038\/s41593-018-0298-7","article-title":"A tau homeostasis signature is linked with the cellular and regional vulnerability of excitatory neurons to tau pathology","volume":"22","author":"Fu","year":"2019","journal-title":"Nat. Neurosci."},{"issue":"17","key":"10.1016\/j.neulet.2019.04.001_bib0125","doi-asserted-by":"crossref","first-page":"4753","DOI":"10.1073\/pnas.1516604113","article-title":"A transcriptional signature of Alzheimer\u2019s disease is associated with a metastable subproteome at risk for aggregation","volume":"113","author":"Ciryam","year":"2016","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"1","key":"10.1016\/j.neulet.2019.04.001_bib0130","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1007\/s00401-012-1058-5","article-title":"Unravelling the enigma of selective vulnerability in neurodegeneration: motor neurons resistant to degeneration in ALS show distinct gene expression characteristics and decreased susceptibility to excitotoxicity","volume":"125","author":"Brockington","year":"2013","journal-title":"Acta Neuropathol."},{"issue":"1","key":"10.1016\/j.neulet.2019.04.001_bib0135","doi-asserted-by":"crossref","first-page":"10046","DOI":"10.1038\/s41598-017-10488-7","article-title":"Massive transcriptome sequencing of human spinal cord tissues provides new insights into motor neuron degeneration in ALS","volume":"7","author":"D\u2019Erchia","year":"2017","journal-title":"Sci. Rep."},{"issue":"Pt 2","key":"10.1016\/j.neulet.2019.04.001_bib0140","doi-asserted-by":"crossref","first-page":"506","DOI":"10.1093\/brain\/awq345","article-title":"Phosphatase and tensin homologue\/protein kinase B pathway linked to motor neuron survival in human superoxide dismutase 1-related amyotrophic lateral sclerosis","volume":"134","author":"Kirby","year":"2011","journal-title":"Brain."},{"issue":"5","key":"10.1016\/j.neulet.2019.04.001_bib0145","doi-asserted-by":"crossref","first-page":"1953","DOI":"10.1021\/acs.jproteome.8b00069","article-title":"Unbiased proteomic study of the axons of cultured rat cortical neurons","volume":"17","author":"Chuang","year":"2018","journal-title":"J. Proteome Res."},{"issue":"Pt 4","key":"10.1016\/j.neulet.2019.04.001_bib0150","doi-asserted-by":"crossref","first-page":"953","DOI":"10.1093\/brain\/awl024","article-title":"Altered axonal excitability properties in amyotrophic lateral sclerosis: impaired potassium channel function related to disease stage","volume":"129","author":"Kanai","year":"2006","journal-title":"Brain."},{"issue":"7","key":"10.1016\/j.neulet.2019.04.001_bib0155","doi-asserted-by":"crossref","first-page":"1458","DOI":"10.1016\/j.clinph.2006.04.016","article-title":"Axonal excitability properties in amyotrophic lateral sclerosis","volume":"117","author":"Vucic","year":"2006","journal-title":"Clin. Neurophysiol."},{"issue":"2","key":"10.1016\/j.neulet.2019.04.001_bib0160","doi-asserted-by":"crossref","first-page":"1410","DOI":"10.1007\/s12035-017-0392-y","article-title":"Impairments in motor neurons, interneurons and astrocytes contribute to hyperexcitability in ALS: underlying mechanisms and paths to therapy","volume":"55","author":"Do-Ha","year":"2018","journal-title":"Mol. Neurobiol."},{"issue":"22","key":"10.1016\/j.neulet.2019.04.001_bib0165","first-page":"5379","article-title":"In vivo evidence for reduced ion channel expression in motor axons of patients with amyotrophic lateral sclerosis","volume":"596","author":"Howells","year":"2018","journal-title":"J. Physiol. (Paris)"},{"issue":"7","key":"10.1016\/j.neulet.2019.04.001_bib0170","doi-asserted-by":"crossref","first-page":"1444","DOI":"10.1016\/j.clinph.2006.04.005","article-title":"Distal excitability changes in motor axons in amyotrophic lateral sclerosis","volume":"117","author":"Nakata","year":"2006","journal-title":"Clin. Neurophysiol."},{"issue":"2","key":"10.1016\/j.neulet.2019.04.001_bib0175","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1016\/j.jmb.2008.05.013","article-title":"Prediction of aggregation-prone regions in structured proteins","volume":"380","author":"Tartaglia","year":"2008","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.neulet.2019.04.001_bib0180","doi-asserted-by":"crossref","first-page":"252","DOI":"10.3389\/fnins.2014.00252","article-title":"ALS as a distal axonopathy: molecular mechanisms affecting neuromuscular junction stability in the presymptomatic stages of the disease","volume":"8","author":"Moloney","year":"2014","journal-title":"Front. Neurosci."},{"issue":"3","key":"10.1016\/j.neulet.2019.04.001_bib0185","doi-asserted-by":"crossref","first-page":"341","DOI":"10.1016\/j.coph.2009.03.007","article-title":"Neuromuscular junction destruction during amyotrophic lateral sclerosis: insights from transgenic models","volume":"9","author":"Dupuis","year":"2009","journal-title":"Curr. Opin. Pharmacol."},{"key":"10.1016\/j.neulet.2019.04.001_bib0190","doi-asserted-by":"crossref","first-page":"5999","DOI":"10.1038\/ncomms6999","article-title":"Human iPSC-derived motoneurons harbouring TARDBP or C9ORF72 ALS mutations are dysfunctional despite maintaining viability","volume":"6","author":"Devlin","year":"2015","journal-title":"Nat. Commun."}],"container-title":["Neuroscience Letters"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0304394019302290?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0304394019302290?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,5,13]],"date-time":"2026-05-13T15:10:45Z","timestamp":1778685045000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0304394019302290"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2019,6]]},"references-count":38,"alternative-id":["S0304394019302290"],"URL":"https:\/\/doi.org\/10.1016\/j.neulet.2019.04.001","relation":{},"ISSN":["0304-3940"],"issn-type":[{"value":"0304-3940","type":"print"}],"subject":[],"published":{"date-parts":[[2019,6]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"The metastability of the proteome of spinal motor neurons underlies their selective vulnerability in ALS","name":"articletitle","label":"Article Title"},{"value":"Neuroscience Letters","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.neulet.2019.04.001","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2019 Elsevier B.V. All rights reserved.","name":"copyright","label":"Copyright"}]}}