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Updated: Mar 25, 2026

Assaying the Kinase Activity of LRRK2 in vitro
Published on: January 18, 2012
LRRK2 pathobiology in Parkinson's disease - virtual inclusion
Ian Martin1,2, Jungwoo Wren Kim1,3, Valina L Dawson1,2,3,4,5
1Neuroregeneration and Stem Cell Programs, Institute for Cell Engineering, Johns Hopkins University School of Medicine, Baltimore, Maryland, USA.
Abstract:
A common cause of Parkinson disease are missense mutations in the leucine-rich repeat kinase 2 (LRRK2) catalytic Roc-COR domain, leading to a decrease in GTPase activity; and its kinase domain, leading to an increase in kinase activity and subsequent LRRK2 toxicity. Targeting LRRK2 with selective, brain-permeable kinase inhibitors is a promising approach to reduce toxicity, and thus is a major goal of clinical development. Understanding the specific signaling cascades triggered by LRRK2 mutations will be key to this aim. This article is part of a special issue on Parkinson disease.
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