Progressive neurodegeneration in Parkinson's Disease is associated with the formation of toxic protein aggregates made largely of the protein alpha-synuclein. Therefore understanding the cellular factors that promote or inhibit alpha-synuclein aggregation should uncover targets for therapeutic intervention. Posttranslational modifications on alpha-synuclein are especially placed with the potential to directly alter protein aggregation. Here, I will present the use of synthetic protein-chemistry combined with in vitro biochemistry to investigate the consequences of two of these posttranslational modifications, ubiquitination and O-GlcNAc modification.

Posttranslational modifications in Parkinson's and related diseases

245th National Meeting (2013)

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