The G2385R variant of leucine-rich repeat kinase 2 associated with Parkinson's disease is a partial loss-of-function mutation

Is inhibition of kinase activity the only therapeutic strategy for LRRK2-associated Parkinson's disease?

(2012) Iakov N Rudenko et al.   BMC Medicine

Impact of inter-subunit interactions on the dimeric arginine kinase activity and structural stability

(2011) Qing-Yun Wu et al.   ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS

Re-examination of the dimerization state of leucine-rich repeat kinase 2: predominance of the monomeric form

(2011) Genta Ito et al.   BIOCHEMICAL JOURNAL

Mechanism of kinase inactivation and nonbinding of fratide to GSK3β due to K85M mutation: Molecular dynamics simulation and normal mode analysis

(2011) ShaoYong Lu et al.   BIOPOLYMERS

Milestones in Parkinson's disease-Clinical and pathologic features

(2011) Glenda Halliday et al.   MOVEMENT DISORDERS

Characterization of a selective inhibitor of the Parkinson's disease kinase LRRK2

(2011) Xianming Deng et al.   Nature Chemical Biology

Phosphorylation-Dependent 14-3-3 Binding to LRRK2 Is Impaired by Common Mutations of Familial Parkinson's Disease

(2011) Xianting Li et al.   PLoS One

Inhibition of LRRK2 kinase activity leads to dephosphorylation of Ser910/Ser935, disruption of 14-3-3 binding and altered cytoplasmic localization

(2010) Nicolas Dzamko et al.   BIOCHEMICAL JOURNAL

14-3-3 binding to LRRK2 is disrupted by multiple Parkinson's disease-associated mutations and regulates cytoplasmic localization

(2010) R. Jeremy Nichols et al.   BIOCHEMICAL JOURNAL

Membrane Localization of LRRK2 Is Associated with Increased Formation of the Highly Active LRRK2 Dimer and Changes in Its Phosphorylation

(2010) Zdenek Berger et al.   BIOCHEMISTRY

Insight into the mode of action of the LRRK2 Y1699C pathogenic mutant

(2010) Veronique Daniëls et al.   JOURNAL OF NEUROCHEMISTRY

Inhibitors of leucine-rich repeat kinase-2 protect against models of Parkinson's disease

(2010) Byoung Dae Lee et al.   NATURE MEDICINE

The role of leucine-rich repeat kinase 2 (LRRK2) in Parkinson's disease

(2010) Mark R. Cookson   NATURE REVIEWS NEUROSCIENCE

Structural and Functional Consequences of the Substitution of Glycine 65 with Arginine in the N-Lobe of Human Transferrin†

(2009) Anne B. Mason et al.   BIOCHEMISTRY

The R1441C mutation alters the folding properties of the ROC domain of LRRK2

(2009) Yongchao Li et al.   BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR BASIS OF DISEASE

Homo- and heterodimerization of ROCO kinases: LRRK2 kinase inhibition by the LRRK2 ROCO fragment

(2009) Christian L. Klein et al.   JOURNAL OF NEUROCHEMISTRY

Leucine-Rich Repeat Kinase 2 Expression Leads to Aggresome Formation That Is Not Associated With α-Synuclein Inclusions

(2009) Elisa A. Waxman et al.   JOURNAL OF NEUROPATHOLOGY AND EXPERIMENTAL NEUROLOGY

Clinical features of LRRK2 parkinsonism

(2009) Kristoffer Haugarvoll et al.   PARKINSONISM & RELATED DISORDERS

Regulation of LRRK2 Stability by the E3 Ubiquitin Ligase CHIP

(2009) Xiaodong Ding et al.   PLoS One

The WD40 Domain Is Required for LRRK2 Neurotoxicity

(2009) Nathan D. Jorgensen et al.   PLoS One

CHIP regulates leucine-rich repeat kinase-2 ubiquitination, degradation, and toxicity

(2009) Han Seok Ko et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

The Parkinson Disease-associated Leucine-rich Repeat Kinase 2 (LRRK2) Is a Dimer That Undergoes Intramolecular Autophosphorylation

(2008) Elisa Greggio et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

The Chaperone Activity of Heat Shock Protein 90 Is Critical for Maintaining the Stability of Leucine-Rich Repeat Kinase 2

(2008) L. Wang et al.   JOURNAL OF NEUROSCIENCE