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Genet."},{"issue":"1","key":"10.1016\/j.bbrep.2026.102687_bib101","doi-asserted-by":"crossref","DOI":"10.1038\/nrdp.2017.13","article-title":"Parkinson disease","volume":"3","author":"Poewe","year":"2017","journal-title":"Nat. Rev. Dis. Primers"},{"issue":"45","key":"10.1016\/j.bbrep.2026.102687_bib102","doi-asserted-by":"crossref","first-page":"31224","DOI":"10.1074\/jbc.M114.559237","article-title":"Interplay between sumoylation and phosphorylation for protection against \u03b1-synuclein inclusions","volume":"289","author":"Shahpasandzadeh","year":"2014","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbrep.2026.102687_bib103","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1016\/S0079-6123(10)83007-9","article-title":"Role of post-translational modifications in modulating the structure, function and toxicity of \u03b1-synuclein: implications for Parkinson's disease pathogenesis and therapies","volume":"183","author":"Oueslati","year":"2010","journal-title":"Prog. 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Lett."},{"issue":"2","key":"10.1016\/j.bbrep.2026.102687_bib109","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1016\/j.neulet.2012.04.051","article-title":"Correlation of increased hippocampal Sumo 3 with spatial learning ability in old C57BL\/6 mice","volume":"518","author":"Yang","year":"2012","journal-title":"Neurosci. Lett."},{"issue":"4","key":"10.1016\/j.bbrep.2026.102687_bib110","doi-asserted-by":"crossref","DOI":"10.1111\/acel.12760","article-title":"SUMO1-conjugation is altered during normal aging but not by increased amyloid burden","volume":"17","author":"Stankova","year":"2018","journal-title":"Aging Cell"},{"issue":"2","key":"10.1016\/j.bbrep.2026.102687_bib111","doi-asserted-by":"crossref","first-page":"210","DOI":"10.1016\/j.molcel.2011.12.026","article-title":"SUMO-specific protease 1 is critical for early lymphoid development through regulation of STAT5 activation","volume":"45","author":"Van Nguyen","year":"2012","journal-title":"Mol. 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