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\u03b1-synuclein","volume":"25","author":"Levine","year":"2017","journal-title":"Bioorg Med Chem"},{"key":"10.1124\/pharmrev.123.001111_bib236","doi-asserted-by":"crossref","first-page":"1511","DOI":"10.1073\/pnas.1808845116","article-title":"\u03b1-Synuclein O-GlcNAcylation alters aggregation and toxicity, revealing certain residues as potential inhibitors of Parkinson\u2019s disease","volume":"116","author":"Levine","year":"2019","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1124\/pharmrev.123.001111_bib237","doi-asserted-by":"crossref","first-page":"16970","DOI":"10.1073\/pnas.1011751107","article-title":"Polyamine pathway contributes to the pathogenesis of Parkinson disease","volume":"107","author":"Lewandowski","year":"2010","journal-title":"Proceedings of the National Academy of Sciences"},{"key":"10.1124\/pharmrev.123.001111_bib238","doi-asserted-by":"crossref","first-page":"1020","DOI":"10.1021\/acschembio.7b00113","article-title":"O-GlcNAcylation of \u03b1-synuclein at Serine 87 reduces aggregation without affecting membrane binding","volume":"12","author":"Lewis","year":"2017","journal-title":"ACS Chem Biol"},{"key":"10.1124\/pharmrev.123.001111_bib239","doi-asserted-by":"crossref","first-page":"994","DOI":"10.3390\/biom12070994","article-title":"\u03b1-Synuclein conformational plasticity: physiologic states, pathologic strains, and biotechnological applications","volume":"12","author":"Li","year":"2022","journal-title":"Biomolecules"},{"key":"10.1124\/pharmrev.123.001111_bib240","doi-asserted-by":"crossref","first-page":"416","DOI":"10.1111\/bph.14538","article-title":"Sirtuin 1 represses PKC-\u03b6 activity through regulating interplay of acetylation and phosphorylation in cardiac hypertrophy","volume":"176","author":"Li","year":"2019","journal-title":"Br J Pharmacol"},{"key":"10.1124\/pharmrev.123.001111_bib241","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1007\/s10735-020-09924-2","article-title":"SUMO modification in 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