LRRK2 kinase activity and biology are not uniformly predicted by its autophosphorylation and cellular phosphorylation site status

@inproceedings{Reynolds2014LRRK2KA,
  title={LRRK2 kinase activity and biology are not uniformly predicted by its autophosphorylation and cellular phosphorylation site status},
  author={April G Reynolds and Elizabeth A. Doggett and Steve M. Riddle and Connie S. Lebakken and R. Jeremy Nichols},
  booktitle={Front. Mol. Neurosci.},
  year={2014}
}
Missense mutations in the Leucine-Rich Repeat protein Kinase 2 (LRRK2) gene are the most common genetic predisposition to develop Parkinson's disease (PD) (Farrer et al., 2005; Skipper et al., 2005; Di Fonzo et al., 2006; Healy et al., 2008; Paisan-Ruiz et al., 2008; Lesage et al., 2010). LRRK2 is a large multi-domain phosphoprotein with a GTPase domain and a serine/threonine protein kinase domain whose activity is implicated in neuronal toxicity; however the precise mechanism is unknown. LRRK2… CONTINUE READING
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LRRK2 kinase activity and biology are not uniformly predicted by its autophosphorylation and cellular phosphorylation site status

  • A Citation Reynolds, EA Doggett, SM Riddle, CS Lebakken, RJ Nichols
  • Front. Mol. Neurosci. 7:54
  • 2014

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