Associated Papers
LRRK2 rare-variant per-domain genetic burden in Parkinson's Disease: association confined to the kinase domain.
Parlar SC et al.
Npj Parkinson's Disease, 2025
LRRK2 Structure-Based Activation Mechanism and Pathogenesis.
Zhang X et al.
Biomolecules, 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
Identification of LRRK2 missense variants in the accelerating medicines partnership Parkinson's disease cohort.
Bryant N et al.
Human Molecular Genetics, 2021
Leucine-Rich Repeat Kinase (LRRK2) Genetics and Parkinson's Disease.
Monfrini E et al.
Advances in Neurobiology, 2017
Prediction of the repeat domain structures and impact of parkinsonism-associated variations on structure and function of all functional domains of leucine-rich repeat kinase 2 (LRRK2).
Mills RD et al.
Human Mutation, 2014
Structural and functional in silico analysis of LRRK2 missense substitutions.
Cardona F et al.
Molecular Biology Reports, 2014
Analysis of LRRK2 accessory repeat domains: prediction of repeat length, number and sites of Parkinson's disease mutations.
Mills RD et al.
Biochemical Society Transactions, 2012
Small molecule kinase inhibitors for LRRK2 and their application to Parkinson's disease models.
Kramer T et al.
Acs Chemical Neuroscience, 2012
Expression, purification and preliminary biochemical and structural characterization of the leucine rich repeat namesake domain of leucine rich repeat kinase 2.
Vancraenenbroeck R et al.
Biochimica Et Biophysica Acta, 2012
Association of LRRK2 exonic variants with susceptibility to Parkinson's disease: a case-control study.
Ross OA et al.
The Lancet. Neurology, 2011
Screening of Brazilian families with primary dystonia reveals a novel THAP1 mutation and a de novo TOR1A GAG deletion.
De Carvalho Aguiar P et al.
Movement Disorders : Official Journal of the Movement Disorder Society, 2010
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
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
LRRK2 gene variation and its contribution to Parkinson disease.
Paisán-Ruiz C
Human Mutation, 2009
Zeroing in on LRRK2-linked pathogenic mechanisms in Parkinson's disease.
Biskup S et al.
Biochimica Et Biophysica Acta, 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
Molecular biology changes associated with LRRK2 mutations in Parkinson's disease.
Lu YW et al.
Journal of Neuroscience Research, 2008
Comprehensive analysis of LRRK2 in publicly available Parkinson's disease cases and neurologically normal controls.
Paisán-Ruíz C et al.
Human Mutation, 2008
Mutations in LRRK2 as a cause of Parkinson's disease.
Giasson BI et al.
Neuro-signals, 2008
LRRK2 expression in normal and pathologic human brain and in human cell lines.
Miklossy J et al.
Journal of Neuropathology and Experimental Neurology, 2006
LRRK2 in Parkinson's disease: protein domains and functional insights.
Mata IF et al.
Trends in Neurosciences, 2006
Type and frequency of mutations in the LRRK2 gene in familial and sporadic Parkinson's disease*.
Berg D et al.
Brain : a Journal of Neurology, 2005