{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,25]],"date-time":"2026-07-25T18:43:58Z","timestamp":1785005038645,"version":"3.55.0"},"reference-count":54,"publisher":"Elsevier BV","issue":"6","license":[{"start":{"date-parts":[[2023,6,1]],"date-time":"2023-06-01T00:00:00Z","timestamp":1685577600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2023,6,1]],"date-time":"2023-06-01T00:00:00Z","timestamp":1685577600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2023,5,5]],"date-time":"2023-05-05T00:00:00Z","timestamp":1683244800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"funder":[{"DOI":"10.13039\/100009619","name":"Japan Agency for Medical Research and Development","doi-asserted-by":"publisher","award":["JP21ek0109426"],"award-info":[{"award-number":["JP21ek0109426"]}],"id":[{"id":"10.13039\/100009619","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001691","name":"Japan Society for the Promotion of Science","doi-asserted-by":"publisher","award":["JP19KK0214"],"award-info":[{"award-number":["JP19KK0214"]}],"id":[{"id":"10.13039\/501100001691","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001691","name":"Japan Society for the Promotion of Science","doi-asserted-by":"publisher","award":["JP22H00467"],"award-info":[{"award-number":["JP22H00467"]}],"id":[{"id":"10.13039\/501100001691","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001691","name":"Japan Society for the Promotion of Science","doi-asserted-by":"publisher","award":["JP22J15394"],"award-info":[{"award-number":["JP22J15394"]}],"id":[{"id":"10.13039\/501100001691","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001700","name":"Ministry of Education, Culture, Sports, Science and Technology","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100001700","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002241","name":"Japan Science and Technology Agency","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100002241","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["jbc.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2023,6]]},"DOI":"10.1016\/j.jbc.2023.104798","type":"journal-article","created":{"date-parts":[[2023,5,6]],"date-time":"2023-05-06T10:54:23Z","timestamp":1683370463000},"page":"104798","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":7,"title":["Intrinsic structural vulnerability in the hydrophobic core induces species-specific aggregation of canine SOD1 with degenerative myelopathy\u2013linked E40K mutation"],"prefix":"10.1016","volume":"299","author":[{"given":"Kei","family":"Hashimoto","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Seiji","family":"Watanabe","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Masato","family":"Akutsu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4112-2955","authenticated-orcid":false,"given":"Norifumi","family":"Muraki","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hiroaki","family":"Kamishina","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1918-372X","authenticated-orcid":false,"given":"Yoshiaki","family":"Furukawa","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4655-0035","authenticated-orcid":false,"given":"Koji","family":"Yamanaka","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jbc.2023.104798_bib1","doi-asserted-by":"crossref","first-page":"6049","DOI":"10.1016\/S0021-9258(18)63504-5","article-title":"Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein)","volume":"244","author":"McCord","year":"1969","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2023.104798_bib2","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1093\/jhered\/93.2.119","article-title":"Structure, chromosomal location, and analysis of the canine Cu\/Zn superoxide dismutase (SOD1) gene","volume":"93","author":"Green","year":"2002","journal-title":"J.\u00a0Hered."},{"key":"10.1016\/j.jbc.2023.104798_bib3","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1016\/0022-2836(82)90174-7","article-title":"Determination and analysis of the 2 A-structure of copper, zinc superoxide dismutase","volume":"160","author":"Tainer","year":"1982","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.jbc.2023.104798_bib4","doi-asserted-by":"crossref","first-page":"7339","DOI":"10.1016\/S0021-9258(19)42109-1","article-title":"Bovine erythrocyte superoxide dismutase. Subunit structure and sequence location of the intrasubunit disulfide bond","volume":"249","author":"Abernethy","year":"1974","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2023.104798_bib5","doi-asserted-by":"crossref","first-page":"393","DOI":"10.1016\/j.molmed.2004.06.009","article-title":"Lessons from models of SOD1-linked familial ALS","volume":"10","author":"Bendotti","year":"2004","journal-title":"Trends Mol. Med."},{"key":"10.1016\/j.jbc.2023.104798_bib6","doi-asserted-by":"crossref","first-page":"723","DOI":"10.1146\/annurev.neuro.27.070203.144244","article-title":"Unraveling the mechanisms involved in motor neuron degeneration in ALS","volume":"27","author":"Bruijn","year":"2004","journal-title":"Annu. Rev. Neurosci."},{"key":"10.1016\/j.jbc.2023.104798_bib7","doi-asserted-by":"crossref","first-page":"933","DOI":"10.1006\/nbdi.2001.0443","article-title":"Histological evidence of protein aggregation in mutant SOD1 transgenic mice and in amyotrophic lateral sclerosis neural tissues","volume":"8","author":"Watanabe","year":"2001","journal-title":"Neurobiol. Dis."},{"key":"10.1016\/j.jbc.2023.104798_bib8","doi-asserted-by":"crossref","first-page":"253","DOI":"10.3389\/fncel.2013.00253","article-title":"An emerging role for misfolded wild-type SOD1 in sporadic ALS pathogenesis","volume":"7","author":"Rotunno","year":"2013","journal-title":"Front. Cell. Neurosci."},{"key":"10.1016\/j.jbc.2023.104798_bib9","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1016\/j.sbi.2020.12.002","article-title":"SOD1 oligomers in amyotrophic lateral sclerosis","volume":"66","author":"Choi","year":"2021","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.jbc.2023.104798_bib10","doi-asserted-by":"crossref","first-page":"929","DOI":"10.1016\/j.cvsm.2010.05.001","article-title":"Canine degenerative myelopathy","volume":"40","author":"Coates","year":"2010","journal-title":"Vet. Clin. North Am. Small Anim. Pract."},{"key":"10.1016\/j.jbc.2023.104798_bib11","doi-asserted-by":"crossref","first-page":"2794","DOI":"10.1073\/pnas.0812297106","article-title":"Genome-wide association analysis reveals a SOD1 mutation in canine degenerative myelopathy that resembles amyotrophic lateral sclerosis","volume":"106","author":"Awano","year":"2009","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2023.104798_bib12","doi-asserted-by":"crossref","first-page":"1166","DOI":"10.1111\/j.1939-1676.2011.0760.x","article-title":"Degenerative myelopathy in a bernese mountain dog with a novel SOD1 missense mutation","volume":"25","author":"Wininger","year":"2011","journal-title":"J.\u00a0Vet. Intern. Med."},{"key":"10.1016\/j.jbc.2023.104798_bib13","doi-asserted-by":"crossref","first-page":"E3091","DOI":"10.1073\/pnas.1600084113","article-title":"Variants within the SP110 nuclear body protein modify risk of canine degenerative myelopathy","volume":"113","author":"Ivansson","year":"2016","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2023.104798_bib14","doi-asserted-by":"crossref","first-page":"515","DOI":"10.1111\/jvim.12317","article-title":"Breed distribution of SOD1 alleles previously associated with canine degenerative myelopathy","volume":"28","author":"Zeng","year":"2014","journal-title":"J.\u00a0Vet. Intern. Med."},{"key":"10.1016\/j.jbc.2023.104798_bib15","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.expneurol.2013.05.009","article-title":"Canine degenerative myelopathy: biochemical characterization of superoxide dismutase 1 in the first naturally occurring non-human amyotrophic lateral sclerosis model","volume":"248","author":"Crisp","year":"2013","journal-title":"Exp. Neurol."},{"key":"10.1016\/j.jbc.2023.104798_bib16","doi-asserted-by":"crossref","first-page":"3896","DOI":"10.1111\/ejn.14526","article-title":"In\u00a0vitro evidence consistent with an interaction between wild-type and mutant SOD1 protein associated with canine degenerative myelopathy","volume":"50","author":"Qi","year":"2019","journal-title":"Eur. J. Neurosci."},{"key":"10.1016\/j.jbc.2023.104798_bib17","doi-asserted-by":"crossref","first-page":"369","DOI":"10.1016\/j.jns.2016.10.034","article-title":"Localization of a mutant SOD1 protein in E40K-heterozygous dogs: implications for non-cell-autonomous pathogenesis of degenerative myelopathy","volume":"372","author":"Kobatake","year":"2017","journal-title":"J.\u00a0Neurol. Sci."},{"key":"10.1016\/j.jbc.2023.104798_bib18","doi-asserted-by":"crossref","first-page":"1152","DOI":"10.1016\/j.jmb.2005.11.081","article-title":"Variable metallation of human superoxide dismutase: atomic resolution crystal structures of Cu-Zn, Zn-Zn and as-isolated wild-type enzymes","volume":"356","author":"Strange","year":"2006","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.jbc.2023.104798_bib19","doi-asserted-by":"crossref","first-page":"719","DOI":"10.1534\/g3.118.200787","article-title":"Experimental mutations in superoxide dismutase 1 provide insight into potential mechanisms involved in aberrant aggregation in familial amyotrophic lateral sclerosis","volume":"9","author":"Crown","year":"2019","journal-title":"G3 (Bethesda)"},{"key":"10.1016\/j.jbc.2023.104798_bib20","doi-asserted-by":"crossref","DOI":"10.7717\/peerj.9512","article-title":"Canine SOD1 harboring E40K or T18S mutations promotes protein aggregation without reducing the global structural stability","volume":"8","author":"Kimura","year":"2020","journal-title":"PeerJ"},{"key":"10.1016\/j.jbc.2023.104798_bib21","doi-asserted-by":"crossref","first-page":"1302","DOI":"10.1038\/nbt1012","article-title":"Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins","volume":"22","author":"Fernandez-Escamilla","year":"2004","journal-title":"Nat. Biotechnol."},{"key":"10.1016\/j.jbc.2023.104798_bib22","doi-asserted-by":"crossref","first-page":"4890","DOI":"10.1038\/s41467-019-12740-2","article-title":"Phase separation-deficient TDP43 remains functional in splicing","volume":"10","author":"Schmidt","year":"2019","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jbc.2023.104798_bib23","doi-asserted-by":"crossref","first-page":"42","DOI":"10.1186\/s13024-019-0341-5","article-title":"Wild-type Cu\/Zn-superoxide dismutase is misfolded in cerebrospinal fluid of sporadic amyotrophic lateral sclerosis","volume":"14","author":"Tokuda","year":"2019","journal-title":"Mol. neurodegener."},{"key":"10.1016\/j.jbc.2023.104798_bib24","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1016\/j.cbpa.2006.02.034","article-title":"Pathogenic superoxide dismutase structure, folding, aggregation and turnover","volume":"10","author":"Hart","year":"2006","journal-title":"Curr. Opin. Chem. Biol."},{"key":"10.1016\/j.jbc.2023.104798_bib25","doi-asserted-by":"crossref","first-page":"461","DOI":"10.1038\/nsb935","article-title":"Amyloid-like filaments and water-filled nanotubes formed by SOD1 mutant proteins linked to familial ALS","volume":"10","author":"Elam","year":"2003","journal-title":"Nat. Struct. Biol."},{"key":"10.1016\/j.jbc.2023.104798_bib26","doi-asserted-by":"crossref","first-page":"545","DOI":"10.1002\/pro.5560070302","article-title":"Subunit asymmetry in the three-dimensional structure of a human CuZnSOD mutant found in familial amyotrophic lateral sclerosis","volume":"7","author":"Hart","year":"1998","journal-title":"Protein Sci."},{"key":"10.1016\/j.jbc.2023.104798_bib27","doi-asserted-by":"crossref","first-page":"1890","DOI":"10.1021\/bi026704y","article-title":"Dynamic properties of the G93A mutant of copper-zinc superoxide dismutase as detected by NMR spectroscopy: implications for the pathology of familial amyotrophic lateral sclerosis","volume":"42","author":"Shipp","year":"2003","journal-title":"Biochemistry"},{"key":"10.1016\/j.jbc.2023.104798_bib28","doi-asserted-by":"crossref","first-page":"2119","DOI":"10.1016\/j.bbadis.2018.03.015","article-title":"A\u00a0copper-deficient form of mutant Cu\/Zn-superoxide dismutase as an early pathological species in amyotrophic lateral sclerosis","volume":"1864","author":"Tokuda","year":"2018","journal-title":"Biochim. Biophys. Acta Mol. Basis Dis."},{"key":"10.1016\/j.jbc.2023.104798_bib29","doi-asserted-by":"crossref","first-page":"5984","DOI":"10.1074\/jbc.M210419200","article-title":"Familial amyotrophic lateral sclerosis mutants of copper\/zinc superoxide dismutase are susceptible to disulfide reduction","volume":"278","author":"Tiwari","year":"2003","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2023.104798_bib30","doi-asserted-by":"crossref","first-page":"319","DOI":"10.1002\/psc.310010507","article-title":"Relationship of sidechain hydrophobicity and alpha-helical propensity on the stability of the single-stranded amphipathic alpha-helix","volume":"1","author":"Monera","year":"1995","journal-title":"J.\u00a0Pept. Sci."},{"key":"10.1016\/j.jbc.2023.104798_bib31","doi-asserted-by":"crossref","first-page":"54","DOI":"10.1126\/science.2787053","article-title":"Influence of interior packing and hydrophobicity on the stability of a protein","volume":"245","author":"Sandberg","year":"1989","journal-title":"Science"},{"key":"10.1016\/j.jbc.2023.104798_bib32","doi-asserted-by":"crossref","first-page":"383","DOI":"10.1002\/pro.5560020310","article-title":"Packing and hydrophobicity effects on protein folding and stability: effects of beta-branched amino acids, valine and isoleucine, on the formation and stability of two-stranded alpha-helical coiled coils\/leucine zippers","volume":"2","author":"Zhu","year":"1993","journal-title":"Protein Sci."},{"key":"10.1016\/j.jbc.2023.104798_bib33","doi-asserted-by":"crossref","first-page":"7392","DOI":"10.1021\/acs.langmuir.6b01550","article-title":"Differential effects of hydrophobic core packing residues for Thermodynamic and mechanical stability of a Hyperthermophilic protein","volume":"32","author":"Tych","year":"2016","journal-title":"Langmuir"},{"key":"10.1016\/j.jbc.2023.104798_bib34","doi-asserted-by":"crossref","first-page":"904","DOI":"10.1016\/j.ijbiomac.2019.09.181","article-title":"Changes in hydrophobicity mainly promotes the aggregation tendency of ALS associated SOD1 mutants","volume":"145","author":"Tompa","year":"2020","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.jbc.2023.104798_bib35","doi-asserted-by":"crossref","first-page":"12402","DOI":"10.1073\/pnas.1511308112","article-title":"Thermodynamics of protein destabilization in live cells","volume":"112","author":"Danielsson","year":"2015","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2023.104798_bib36","doi-asserted-by":"crossref","first-page":"515","DOI":"10.1016\/j.jmb.2003.09.069","article-title":"Folding of Cu, Zn superoxide dismutase and familial amyotrophic lateral sclerosis","volume":"334","author":"Khare","year":"2003","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.jbc.2023.104798_bib37","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1016\/j.neuroscience.2015.06.066","article-title":"Accumulation and aggregate formation of mutant superoxide dismutase 1 in canine degenerative myelopathy","volume":"303","author":"Nakamae","year":"2015","journal-title":"Neuroscience"},{"key":"10.1016\/j.jbc.2023.104798_bib38","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1186\/s12896-015-0162-8","article-title":"A\u00a0simple and efficient seamless DNA cloning method using SLiCE from Escherichia coli laboratory strains and its application to SLiP site-directed mutagenesis","volume":"15","author":"Motohashi","year":"2015","journal-title":"BMC Biotechnol."},{"key":"10.1016\/j.jbc.2023.104798_bib39","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1002\/aja.1001940306","article-title":"Neuroblastoma x spinal cord (NSC) hybrid cell lines resemble developing motor neurons","volume":"194","author":"Cashman","year":"1992","journal-title":"Dev. Dyn."},{"key":"10.1016\/j.jbc.2023.104798_bib40","doi-asserted-by":"crossref","first-page":"e1497","DOI":"10.1038\/cddis.2014.459","article-title":"Cystatin C protects neuronal cells against mutant copper-zinc superoxide dismutase-mediated toxicity","volume":"5","author":"Watanabe","year":"2014","journal-title":"Cell Death Dis."},{"key":"10.1016\/j.jbc.2023.104798_bib41","doi-asserted-by":"crossref","first-page":"909","DOI":"10.1038\/s41419-020-03116-2","article-title":"Aggresome formation and liquid-liquid phase separation independently induce cytoplasmic aggregation of TAR DNA-binding protein 43","volume":"11","author":"Watanabe","year":"2020","journal-title":"Cell Death Dis."},{"key":"10.1016\/j.jbc.2023.104798_bib42","doi-asserted-by":"crossref","first-page":"118","DOI":"10.1186\/s40478-019-0776-5","article-title":"Mice deficient in the C-terminal domain of TAR DNA-binding protein 43 develop age-dependent motor dysfunction associated with impaired Notch1-Akt signaling pathway","volume":"7","author":"Nishino","year":"2019","journal-title":"Acta Neuropathol. Commun."},{"key":"10.1016\/j.jbc.2023.104798_bib43","doi-asserted-by":"crossref","first-page":"60","DOI":"10.1016\/j.freeradbiomed.2022.03.014","article-title":"Metal distribution in Cu\/Zn-superoxide dismutase revealed by native mass spectrometry","volume":"183","author":"Tajiri","year":"2022","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/j.jbc.2023.104798_bib44","first-page":"311","article-title":"A\u00a0simple ultraviolet spectrophotometric method for the determination of protein","volume":"48","author":"WADDELL","year":"1956","journal-title":"J.\u00a0Lab. Clin. Med."},{"key":"10.1016\/j.jbc.2023.104798_bib45","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1002\/pro.3703","article-title":"SimpleDSFviewer: a tool to analyze and view differential scanning fluorimetry data for characterizing protein thermal stability and interactions","volume":"29","author":"Sun","year":"2020","journal-title":"Protein Sci."},{"key":"10.1016\/j.jbc.2023.104798_bib46","doi-asserted-by":"crossref","first-page":"1421","DOI":"10.15252\/emmm.201606403","article-title":"Mitochondria-associated membrane collapse is a common pathomechanism in SIGMAR1- and SOD1-linked ALS","volume":"8","author":"Watanabe","year":"2016","journal-title":"EMBO Mol. Med."},{"key":"10.1016\/j.jbc.2023.104798_bib47","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1107\/S0907444909047337","article-title":"Xds","volume":"66","author":"Kabsch","year":"2010","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.jbc.2023.104798_bib48","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1107\/S0907444910045749","article-title":"Overview of the CCP4 suite and current developments","volume":"67","author":"Winn","year":"2011","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.jbc.2023.104798_bib49","doi-asserted-by":"crossref","first-page":"2777","DOI":"10.1038\/ncomms3777","article-title":"Automatic protein structure solution from weak X-ray data","volume":"4","author":"Skubak","year":"2013","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jbc.2023.104798_bib50","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1107\/S0907444909052925","article-title":"Phenix: a comprehensive Python-based system for macromolecular structure solution","volume":"66","author":"Adams","year":"2010","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.jbc.2023.104798_bib51","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1107\/S0907444910007493","article-title":"Features and development of Coot","volume":"66","author":"Emsley","year":"2010","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.jbc.2023.104798_bib52","doi-asserted-by":"crossref","first-page":"345","DOI":"10.1016\/j.jmb.2004.06.088","article-title":"A\u00a0comparative study of the relationship between protein structure and beta-aggregation in globular and intrinsically disordered proteins","volume":"342","author":"Linding","year":"2004","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.jbc.2023.104798_bib53","doi-asserted-by":"crossref","first-page":"118","DOI":"10.1016\/j.sbi.2006.01.011","article-title":"Protein aggregation and amyloidosis: confusion of the kinds?","volume":"16","author":"Rousseau","year":"2006","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.jbc.2023.104798_bib54","first-page":"369","article-title":"Hydrophobic parameters pi of amino-acid side chains from the partitioning of N-acetyl-amino-acid amides","volume":"18","author":"Fauchere","year":"1983","journal-title":"Eur. J. Med. Chem."}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925823018264?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925823018264?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,19]],"date-time":"2025-09-19T00:40:53Z","timestamp":1758242453000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925823018264"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,6]]},"references-count":54,"journal-issue":{"issue":"6","published-print":{"date-parts":[[2023,6]]}},"alternative-id":["S0021925823018264"],"URL":"https:\/\/doi.org\/10.1016\/j.jbc.2023.104798","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2023,6]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Intrinsic structural vulnerability in the hydrophobic core induces species-specific aggregation of canine SOD1 with degenerative myelopathy\u2013linked E40K mutation","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jbc.2023.104798","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2023 The Authors. Published by Elsevier Inc on behalf of American Society for Biochemistry and Molecular Biology.","name":"copyright","label":"Copyright"}],"article-number":"104798"}}