Semisynthetic, site-specific ubiquitin modification of ?-synuclein reveals differential effects on aggregation.
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ABSTRACT:
SUBMITTER: Meier F
PROVIDER: S-EPMC3315850 | biostudies-literature | 2012 Mar
REPOSITORIES: biostudies-literature
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Semisynthetic, site-specific ubiquitin modification of α-synuclein reveals differential effects on aggregation.
Meier Franziska F Abeywardana Tharindumala T Dhall Abhinav A Marotta Nicholas P NP Varkey Jobin J Langen Ralf R Chatterjee Champak C Pratt Matthew R MR
Journal of the American Chemical Society 20120314 12
The process of neurodegeneration in Parkinson's Disease is intimately associated with the aggregation of the protein α-synuclein into toxic oligomers and fibrils. Interestingly, many of these protein aggregates are found to be post-translationally modified by ubiquitin at several different lysine residues. However, the inability to generate homogeneously ubiquitin modified α-synuclein at each site has prevented the understanding of the specific biochemical consequences. We have used protein semi ...[more]
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