Associated Papers
LRRK2 controls COX assembly through regulation of redox status of mitochondrial copper chaperones.
Kim TY et al.
Redox Biology, 2026
LRRK2 regulates ArfGAP1 membrane localization, activity and neuronal toxicity via phosphorylation within its lipid-sensing ALPS2 motif.
Shariful Islam M et al.
Biorxiv : the Preprint Server for Biology, 2026
Deacetylation of ATG16L1 is required for LC3-associated lysosomal microautophagy.
Wang Q et al.
Autophagy, 2025
Lysosomal TPC2 channels disrupt Ca2+ entry and dopaminergic function in models of LRRK2-Parkinson's disease.
Gregori M et al.
The Journal of Cell Biology, 2025
Molecular dynamics studies reveal the structural impacts of LRRK2 R1441C and LRRK2 D1994A mutations in Parkinson's disease.
Rahman RA et al.
Biochemistry and Biophysics Reports, 2024
Ca2+ signalling: A common language for organelles crosstalk in Parkinson's disease.
Peggion C et al.
Cell Calcium, 2023
LRRK2 aggravates kidney injury through promoting MFN2 degradation and abnormal mitochondrial integrity.
Zhang S et al.
Redox Biology, 2023
Post-translational modification and mitochondrial function in Parkinson's disease.
Luo S et al.
Frontiers in Molecular Neuroscience, 2023
LRRK2 deficiency protects the heart against myocardial infarction injury in mice via the P53/HMGB1 pathway.
Liu Y et al.
Free Radical Biology & Medicine, 2022
Precision Medicine in Parkinson's Disease: From Genetic Risk Signals to Personalized Therapy.
Straccia G et al.
Brain Sciences, 2022
Exploring the focal role of LRRK2 kinase in Parkinson's disease.
Kumar S et al.
Environmental Science and Pollution Research International, 2022
Endoplasmic reticulum-mitochondria signaling in neurons and neurodegenerative diseases.
Markovinovic A et al.
Journal of Cell Science, 2022
Protein phosphatase 2A holoenzymes regulate leucine-rich repeat kinase 2 phosphorylation and accumulation.
Drouyer M et al.
Neurobiology of Disease, 2021
Dysregulation of the AP2M1 phosphorylation cycle by LRRK2 impairs endocytosis and leads to dopaminergic neurodegeneration.
Liu Q et al.
Science Signaling, 2021
The C-Terminal Domain of LRRK2 with the G2019S Substitution Increases Mutant A53T α-Synuclein Toxicity in Dopaminergic Neurons In Vivo.
Cresto N et al.
International Journal of Molecular Sciences, 2021
Oligomerization of Lrrk controls actin severing and α-synuclein neurotoxicity in vivo.
Sarkar S et al.
Molecular Neurodegeneration, 2021
LRRK2 inhibition potentiates PARP inhibitor cytotoxicity through inhibiting homologous recombination-mediated DNA double strand break repair.
Chen L et al.
Clinical and Translational Medicine, 2021
Elevated In Vitro Kinase Activity in Peripheral Blood Mononuclear Cells of Leucine-Rich Repeat Kinase 2 G2019S Carriers: A Novel Enzyme-Linked Immunosorbent Assay-Based Method.
Melachroinou K et al.
Movement Disorders : Official Journal of the Movement Disorder Society, 2020
LRRK2 mediates microglial neurotoxicity via NFATc2 in rodent models of synucleinopathies.
Kim C et al.
Science Translational Medicine, 2020
Defects in mRNA Translation in LRRK2-Mutant hiPSC-Derived Dopaminergic Neurons Lead to Dysregulated Calcium Homeostasis.
Kim JW et al.
Cell Stem Cell, 2020
Chetomin rescues pathogenic phenotype of LRRK2 mutation in drosophila.
Chua LL et al.
Aging, 2020
Dietary Amino Acids Impact LRRK2-Induced Neurodegeneration in Parkinson's Disease Models.
Chittoor-Vinod VG et al.
The Journal of Neuroscience : the Official Journal of the Society for Neuroscience, 2020
LRRK2 mediates axon development by regulating Frizzled3 phosphorylation and growth cone-growth cone communication.
Onishi K et al.
Proceedings of the National Academy of Sciences of the United States of America, 2020
Dopaminergic neurodegeneration induced by Parkinson's disease-linked G2019S LRRK2 is dependent on kinase and GTPase activity.
Nguyen APT et al.
Proceedings of the National Academy of Sciences of the United States of America, 2020
Identification of PP2A and S6 Kinase as Modifiers of Leucine-Rich Repeat Kinase-Induced Neurotoxicity.
Sim JPL et al.
Neuromolecular Medicine, 2020
Glycogen synthase kinase 3 β activity is essential for Polo-like kinase 2- and Leucine-rich repeat kinase 2-mediated regulation of α-synuclein.
Kofoed RH et al.
Neurobiology of Disease, 2020
The C-terminal domain of LRRK2 with the G2019S mutation is sufficient to produce neurodegeneration of dopaminergic neurons in vivo.
Cresto N et al.
Neurobiology of Disease, 2020
LRRK2 regulates endoplasmic reticulum-mitochondrial tethering through the PERK-mediated ubiquitination pathway.
Toyofuku T et al.
The Embo Journal, 2020
LRRK2 Phosphorylation, More Than an Epiphenomenon.
Marchand A et al.
Frontiers in Neuroscience, 2020
LRRK2 and Protein Aggregation in Parkinson's Disease: Insights From Animal Models.
Dues DJ et al.
Frontiers in Neuroscience, 2020
Progress in LRRK2-Associated Parkinson's Disease Animal Models.
Seegobin SP et al.
Frontiers in Neuroscience, 2020
From Synaptic Dysfunction to Neuroprotective Strategies in Genetic Parkinson's Disease: Lessons From LRRK2.
Mancini A et al.
Frontiers in Cellular Neuroscience, 2020
Mitochondrial Mechanisms of LRRK2 G2019S Penetrance.
Delcambre S et al.
Frontiers in Neurology, 2020
The Current State-of-the Art of LRRK2-Based Biomarker Assay Development in Parkinson's Disease.
Rideout HJ et al.
Frontiers in Neuroscience, 2020
LRRK2 impairs PINK1/Parkin-dependent mitophagy via its kinase activity: pathologic insights into Parkinson's disease.
Bonello F et al.
Human Molecular Genetics, 2019
Parkinson's disease-associated LRRK2-G2019S mutant acts through regulation of SERCA activity to control ER stress in astrocytes.
Lee JH et al.
Acta Neuropathologica Communications, 2019
Autophagy and LRRK2 in the Aging Brain.
Albanese F et al.
Frontiers in Neuroscience, 2019
LRRK2 impairs autophagy by mediating phosphorylation of leucyl-tRNA synthetase.
Ho DH et al.
Cell Biochemistry and Function, 2018
Lrrk promotes tau neurotoxicity through dysregulation of actin and mitochondrial dynamics.
Bardai FH et al.
Plos Biology, 2018
LRRK2 kinase regulates α-synuclein propagation via RAB35 phosphorylation.
Bae EJ et al.
Nature Communications, 2018