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Plos One|November 11, 2016
Activation of FADD-Dependent Neuronal Death Pathways as a Predictor of Pathogenicity for LRRK2 MutationsKaterina Melachroinou, Emmanouela Leandrou, Polytimi-Eleni Valkimadi, et al.Brain Research|September 7, 2021
Defining (and blocking) neuronal death in Parkinson's disease: Does it matter what we call it?Anna Memou, Lampros Dimitrakopoulos, Maria Kedariti, et al.Journal of Extracellular Biology|February 2, 2026
Extracellular Vesicle-Mediated Delivery of Constrained Peptides Disrupts the Pathogenic Interaction of LRRK2-FADD in Parkinson's DiseaseYaochao Zheng, Brian Joseph Jurgielewicz, Leah G Helton, et al.Plos One|December 31, 2009
The WD40 domain is required for LRRK2 neurotoxicityNathan D Jorgensen, Yong Peng, Cherry C-Y Ho, et al.Human Molecular Genetics|November 15, 2011
LRRK2 Parkinson disease mutations enhance its microtubule associationLauren R Kett, Daniela Boassa, Cherry Cheng-Ying Ho, et al.Annals of Neurology|July 25, 2006
Proteasome inhibition and Parkinson's disease modelingJordi Bové, Chun Zhou, Vernice Jackson-Lewis, et al.The Biochemical Journal|March 10, 2018
P62/SQSTM1 is a novel leucine-rich repeat kinase 2 (LRRK2) substrate that enhances neuronal toxicityAlexia F Kalogeropulou, Jing Zhao, Marc F Bolliger, et al.Scientific Reports|February 24, 2018
A motif within the armadillo repeat of Parkinson's-linked LRRK2 interacts with FADD to hijack the extrinsic death pathwayNasia Antoniou, Dimitrios Vlachakis, Anna Memou, et al.NPJ Parkinson'S Disease|June 8, 2022
Distinct profiles of LRRK2 activation and Rab GTPase phosphorylation in clinical samples from different PD cohortsLilian Petropoulou-Vathi, Athina Simitsi, Politymi-Eleni Valkimadi, et al.Frontiers in Neuroscience|October 5, 2020
The Current State-of-the Art of LRRK2-Based Biomarker Assay Development in Parkinson's DiseaseHardy J Rideout, Marie-Christine Chartier-Harlin, Matthew J Fell, et al.Pageof 4