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Tardiff","year":"2013","journal-title":"Science"},{"key":"ref50","doi-asserted-by":"crossref","first-page":"865","DOI":"10.1126\/science.1067389","article-title":"Chaperone suppression of alpha-synuclein toxicity in a Drosophila model for Parkinson's disease","volume":"295","author":"PK Auluck","year":"2002","journal-title":"Science"},{"key":"ref51","doi-asserted-by":"crossref","first-page":"846","DOI":"10.1046\/j.1471-4159.2002.01190.x","article-title":"TorsinA and heat shock proteins act as molecular chaperones: suppression of alpha-synuclein aggregation","volume":"83","author":"PJ McLean","year":"2002","journal-title":"J Neurochem"},{"key":"ref52","doi-asserted-by":"crossref","first-page":"352","DOI":"10.1007\/s004010051135","article-title":"alpha-Synuclein immunoreactivity in dementia with Lewy bodies: morphological staging and comparison with ubiquitin immunostaining","volume":"99","author":"E Gomez-Tortosa","year":"2000","journal-title":"Acta 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Miake","year":"2002","journal-title":"J Biol Chem"},{"key":"ref63","doi-asserted-by":"crossref","first-page":"2380","DOI":"10.1074\/jbc.M008919200","article-title":"A hydrophobic stretch of 12 amino acid residues in the middle of alpha-synuclein is essential for filament assembly","volume":"276","author":"BI Giasson","year":"2001","journal-title":"The Journal of biological chemistry"},{"key":"ref64","doi-asserted-by":"crossref","first-page":"1408","DOI":"10.1110\/ps.052048706","article-title":"Structure and topology of the non-amyloid-beta component fragment of human alpha-synuclein bound to micelles: implications for the aggregation process","volume":"15","author":"M Bisaglia","year":"2006","journal-title":"Protein Sci"},{"key":"ref65","doi-asserted-by":"crossref","first-page":"33855","DOI":"10.1074\/jbc.274.48.33855","article-title":"Degradation of alpha-synuclein by proteasome","volume":"274","author":"MC Bennett","year":"1999","journal-title":"J Biol 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alpha-synuclein by parkin from human brain: implications for Parkinson's disease","volume":"293","author":"H Shimura","year":"2001","journal-title":"Science"},{"key":"ref70","article-title":"Chip targets toxic alpha -synuclein oligomers for degradation","author":"JE Tetzlaff","year":"2008","journal-title":"J Biol Chem"},{"key":"ref71","doi-asserted-by":"crossref","first-page":"3316","DOI":"10.1074\/jbc.M704809200","article-title":"Monoubiquitylation of alpha-synuclein by seven in absentia homolog (SIAH) promotes its aggregation in dopaminergic cells","volume":"283","author":"R Rott","year":"2008","journal-title":"J Biol Chem"},{"key":"ref72","doi-asserted-by":"crossref","first-page":"1955","DOI":"10.1111\/j.1471-4159.2009.06293.x","article-title":"The ubiquitin ligase E6-AP promotes degradation of alpha-synuclein","volume":"110","author":"SA Mulherkar","year":"2009","journal-title":"J 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Pathol"},{"key":"ref79","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1002\/path.1711610210","article-title":"Ubiquitin carboxyl-terminal hydrolase (PGP 9.5) is selectively present in ubiquitinated inclusion bodies characteristic of human neurodegenerative diseases","volume":"161","author":"J Lowe","year":"1990","journal-title":"J Pathol"},{"issue":"Pt 6","key":"ref80","first-page":"1447","article-title":"Ubiquitin-positive degenerating neurites in the brainstem in Parkinson's disease","volume":"118","author":"WP Gai","year":"1995","journal-title":"Brain"},{"key":"ref81","doi-asserted-by":"crossref","first-page":"345","DOI":"10.1007\/BF00687787","article-title":"Lewy bodies are ubiquitinated. A light and electron microscopic immunocytochemical study","volume":"75","author":"S Kuzuhara","year":"1988","journal-title":"Acta Neuropathol"},{"key":"ref82","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1097\/00005072-199702000-00002","article-title":"Immunocytochemical co-localization of the proteasome in ubiquitinated structures in neurodegenerative diseases and the elderly","volume":"56","author":"K Ii","year":"1997","journal-title":"J Neuropathol Exp Neurol"},{"key":"ref83","doi-asserted-by":"crossref","first-page":"1140","DOI":"10.3390\/biom4041140","article-title":"Proteins directly interacting with mammalian 20S proteasomal subunits and ubiquitin-independent proteasomal degradation","volume":"4","author":"R Sanchez-Lanzas","year":"2014","journal-title":"Biomolecules"},{"key":"ref84","doi-asserted-by":"crossref","first-page":"352","DOI":"10.1016\/j.bbamcr.2013.11.018","article-title":"Mechanism of cleavage of alpha-synuclein by the 20S proteasome and modulation of its degradation by the RedOx state of the N-terminal methionines","volume":"1843","author":"B Alvarez-Castelao","year":"2014","journal-title":"Biochim Biophys Acta"}],"container-title":["PLOS ONE"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/dx.plos.org\/10.1371\/journal.pone.0184262","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,6,26]],"date-time":"2024-06-26T19:10:26Z","timestamp":1719429026000},"score":1,"resource":{"primary":{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.pone.0184262"}},"subtitle":[],"editor":[{"given":"Stephan N.","family":"Witt","sequence":"first","affiliation":[],"role":[{"role":"editor","vocabulary":"crossref"}]}],"short-title":[],"issued":{"date-parts":[[2017,9,6]]},"references-count":84,"journal-issue":{"issue":"9","published-online":{"date-parts":[[2017,9,6]]}},"URL":"https:\/\/doi.org\/10.1371\/journal.pone.0184262","relation":{},"ISSN":["1932-6203"],"issn-type":[{"value":"1932-6203","type":"electronic"}],"subject":[],"published":{"date-parts":[[2017,9,6]]}}}