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- W8379359 endingPage "148" @default.
- W8379359 startingPage "111" @default.
- W8379359 abstract "Mutations in the leucine-rich repeat kinase 2 (LRRK2) are the most common known cause of autosomal dominant Parkinson’s disease (PD), accounting for approximately 1% of “sporadic” and 4% of familial cases. These mutations either lead directly to an increased kinase activity (G2019S and I2020T are in the kinase activation loop) or to a reduced GTPase activity (R1441C/G and Y1699C), that in turn positively regulate kinase activity. The physiological substrate of the LRRK2 kinase has yet to be definitively identified, yet autophosphorylation is emerging as a relatively robust measure of its activity. LRRK2 has been implicated in a number of diverse cellular processes such as vesicular trafficking, microtubule dynamics, protein translation control, inflammation, and immune function, all of which have been linked to PD. LRRK2 is a large, multi-domain protein; a thorough understanding of the protein domain organization and identification of interacting partners is important to determine the underlying mechanism of LRRK2. Substantial recent effort has been directed towards identifying potent LRRK2 kinase inhibitors, from the repurposed kinase inhibitors to the first through third generation of LRRK2-focused kinase inhibitors, from a range of chemotypes, which are now providing researchers with new tools to better interrogate LRRK2 function." @default.
- W8379359 created "2016-06-24" @default.
- W8379359 creator A5037517823 @default.
- W8379359 creator A5043639901 @default.
- W8379359 creator A5061574500 @default.
- W8379359 creator A5084920274 @default.
- W8379359 date "2014-01-01" @default.
- W8379359 modified "2023-09-27" @default.
- W8379359 title "Leucine-Rich Repeat Kinase 2 (LRRK2) Inhibitors" @default.
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