Associated Papers
Genetic analysis of LRRK2 variants in Han Chinese patients with Parkinson's disease.
Deng X et al.
Plos One, 2026
14-3-3 binding maintains the Parkinson's associated kinase LRRK2 in an inactive state.
Martinez Fiesco JA et al.
Nature Communications, 2025
Leucine-Rich Repeat Kinase 2: Pathways to Parkinson's Disease.
Pfeffer SR et al.
Cold Spring Harbor Perspectives in Medicine, 2025
14-3-3 binding maintains the Parkinson's associated kinase LRRK2 in an inactive state.
Martinez Fiesco JA et al.
Biorxiv : the Preprint Server for Biology, 2024
LRRK2 exonic variants are associated with lysosomal hydrolase activities and lysosphingolipid alterations in Parkinson's disease.
Usenko TS et al.
Gene, 2023
Impact of 100 LRRK2 variants linked to Parkinson's disease on kinase activity and microtubule binding.
Kalogeropulou AF et al.
The Biochemical Journal, 2022
Low Levels of LRRK2 Gene Expression are Associated with LRRK2 SNPs and Contribute to Parkinson's Disease Progression.
Yılmazer S et al.
Neuromolecular Medicine, 2021
Structure and nucleotide-induced conformational dynamics of the Chlorobium tepidum Roco protein.
Deyaert E et al.
The Biochemical Journal, 2019
The LRRK2 Variant E193K Prevents Mitochondrial Fission Upon MPP+ Treatment by Altering LRRK2 Binding to DRP1.
Perez Carrion M et al.
Frontiers in Molecular Neuroscience, 2018
Leucine-Rich Repeat Kinase (LRRK2) Genetics and Parkinson's Disease.
Monfrini E et al.
Advances in Neurobiology, 2017
I2020T mutant LRRK2 iPSC-derived neurons in the Sagamihara family exhibit increased Tau phosphorylation through the AKT/GSK-3β signaling pathway.
Ohta E et al.
Human Molecular Genetics, 2015
Evidence that the LRRK2 ROC domain Parkinson's disease-associated mutants A1442P and R1441C exhibit increased intracellular degradation.
Greene ID et al.
Journal of Neuroscience Research, 2014
Structural and functional in silico analysis of LRRK2 missense substitutions.
Cardona F et al.
Molecular Biology Reports, 2014
LRRK2 kinase activity and biology are not uniformly predicted by its autophosphorylation and cellular phosphorylation site status.
Reynolds A et al.
Frontiers in Molecular Neuroscience, 2014
P268S in NOD2 associates with susceptibility to Parkinson's disease in Chinese population.
Ma Q et al.
Behavioral and Brain Functions : Bbf, 2013
Small molecule kinase inhibitors for LRRK2 and their application to Parkinson's disease models.
Kramer T et al.
Acs Chemical Neuroscience, 2012
Phosphorylation of LRRK2 serines 955 and 973 is disrupted by Parkinson's disease mutations and LRRK2 pharmacological inhibition.
Doggett EA et al.
Journal of Neurochemistry, 2012
Association of LRRK2 exonic variants with susceptibility to Parkinson's disease: a case-control study.
Ross OA et al.
The Lancet. Neurology, 2011
14-3-3 binding to LRRK2 is disrupted by multiple Parkinson's disease-associated mutations and regulates cytoplasmic localization.
Nichols RJ et al.
The Biochemical Journal, 2010
14-3-3 proteins are promising LRRK2 interactors.
Rudenko IN et al.
The Biochemical Journal, 2010
Genetic etiology of Parkinson disease associated with mutations in the SNCA, PARK2, PINK1, PARK7, and LRRK2 genes: a mutation update.
Nuytemans K et al.
Human Mutation, 2010
Identification of four novel potentially Parkinson's disease associated LRRK2 variations among Iranian patients.
Shojaee S et al.
Neuroscience Letters, 2009
LRRK2 in Parkinson's disease: genetic and clinical studies from patients.
Kumari U et al.
The Febs Journal, 2009
Molecular analyses of the LRRK2 gene in European and North African autosomal dominant Parkinson's disease.
Lesage S et al.
Journal of Medical Genetics, 2009
Leucine-rich repeat kinase 2 (LRRK2): a key player in the pathogenesis of Parkinson's disease.
Gandhi PN et al.
Journal of Neuroscience Research, 2009
Parkinson's disease: from monogenic forms to genetic susceptibility factors.
Lesage S et al.
Human Molecular Genetics, 2009
Lrrk2 R1441C parkinsonism is clinically similar to sporadic Parkinson disease.
Haugarvoll K et al.
Neurology, 2008
Structure of the ROC domain from the Parkinson's disease-associated leucine-rich repeat kinase 2 reveals a dimeric GTPase.
Deng J et al.
Proceedings of the National Academy of Sciences of the United States of America, 2008
Prevalence and clinical features of common LRRK2 mutations in Australians with Parkinson's disease.
Huang Y et al.
Movement Disorders : Official Journal of the Movement Disorder Society, 2007