Sumoylation inhibits α-synuclein aggregation and toxicity

@inproceedings{Krumova2011SumoylationI,
  title={Sumoylation inhibits α-synuclein aggregation and toxicity},
  author={Petranka Krumova and Erik Meulmeester and M. Garrido and Marilyn Tirard and He-Hsuan Hsiao and Guillaume Bossis and Henning Urlaub and Markus Zweckstetter and Sebastian K{\"u}gler and Frauke Melchior and Mathias B{\"a}hr and Jochen H Weishaupt},
  booktitle={The Journal of cell biology},
  year={2011}
}
Posttranslational modification of proteins by attachment of small ubiquitin-related modifier (SUMO) contributes to numerous cellular phenomena. Sumoylation sometimes creates and abolishes binding interfaces, but increasing evidence points to another role for sumoylation in promoting the solubility of aggregation-prone proteins. Using purified α-synuclein, an aggregation-prone protein implicated in Parkinson's disease that was previously reported to be sumoylated upon overexpression, we compared… CONTINUE READING
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