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Mutations in the Parkinson's disease (PD)-associated protein leucine-rich repeat kinase 2 (LRRK2) commonly lead to a reduction of GTPase activity and increase in kinase activity. Therefore, strategies for drug development have mainly been focusing on the design of LRRK2 kinase inhibitors. We recently showed that the central RocCOR domains (Roc Ras of complex proteins; COR C-terminal of Roc) of a bacterial LRRK2 homologue cycle between a dimeric and monomeric form concomitant with GTP binding and hydrolysis. PD-associated mutations can s