Matches in SemOpenAlex for { <https://semopenalex.org/work/W2071469491> ?p ?o ?g. }
- W2071469491 endingPage "1138" @default.
- W2071469491 startingPage "1128" @default.
- W2071469491 abstract "Alpha synuclein (αsyn) fibrils are found in the Lewy Bodies of patients with Parkinson's disease (PD). The aggregation of the αsyn monomer to soluble oligomers and insoluble fibril aggregates is believed to be one of the causes of PD. Recently, the view of the native state of αsyn as a monomeric ensemble was challenged by a report suggesting that αsyn exists in its native state as a helical tetramer. This review reports on our current understanding of αsyn within the context of these recent developments and describes the work performed by a number of groups to address the monomer/tetramer debate. A number of in depth studies have subsequently shown that both non‐acetylated and acetylated αsyn purified under mild conditions are primarily monomer. A description of the accessible states of acetylated αsyn monomer and the ability of αsyn to self‐associate is explored." @default.
- W2071469491 created "2016-06-24" @default.
- W2071469491 creator A5036165542 @default.
- W2071469491 creator A5047782202 @default.
- W2071469491 creator A5075753849 @default.
- W2071469491 creator A5077651403 @default.
- W2071469491 date "2013-03-13" @default.
- W2071469491 modified "2023-09-26" @default.
- W2071469491 title "Exploring the accessible conformations of N-terminal acetylated α-synuclein" @default.
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