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In this study, we investigate how N\u2010terminal acetylation affects misfolding and self\u2010assembly of the enzyme superoxide dismutase 1 (SOD1), implicated in amyotrophic lateral sclerosis (ALS). Studies of protein inclusions in patient samples and animal models have shown that wild\u2010type SOD1 can form amyloid fibrils even when no mutations are found in the\n                    <jats:italic>sod1<\/jats:italic>\n                    gene. This has identified SOD1 amyloid formation as a possible common denominator of ALS and may suggest that co\u2010 and post\u2010translational modifications, like N\u2010terminal acetylation found in human SOD1, can be a factor in disease development. In this work, the impact of N\u2010terminal acetylation of SOD1 on stability and aggregation is characterized. Results show that the structure and thermal stability of the apo state are unaffected by the modification while the amyloid formation rate is significantly enhanced. This is caused by a shortening of the nucleation phase together with an increase of fibril elongation by more than 10\u2010fold upon N\u2010terminal acetylation of SOD1. Collectively, the findings demonstrate how regulation by co\u2010 and post\u2010translational modifications can influence protein misfolding and self\u2010assembly.\n                  <\/jats:p>","DOI":"10.1002\/pro.70267","type":"journal-article","created":{"date-parts":[[2025,8,15]],"date-time":"2025-08-15T14:31:02Z","timestamp":1755268262000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":4,"title":["N\u2010terminal acetylation of superoxide dismutase 1 accelerates amyloid formation without general destabilization of the apo state"],"prefix":"10.1002","volume":"34","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-9174-8361","authenticated-orcid":false,"given":"Kristine Steen","family":"Jensen","sequence":"first","affiliation":[{"name":"Division for Biophysical Chemistry, Center for Molecular Protein Science, Department of Chemistry Lund University  Lund 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