Associated Papers
Cis or trans: a puzzle of Parkin activation mechanism.
Sherawat M et al.
Essays in Biochemistry, 2026
Post-translational modification and mitochondrial function in Parkinson's disease.
Luo S et al.
Frontiers in Molecular Neuroscience, 2023
Comparative analysis of web-based programs for single amino acid substitutions in proteins.
Choudhury A et al.
Plos One, 2022
Age-associated insolubility of parkin in human midbrain is linked to redox balance and sequestration of reactive dopamine metabolites.
Tokarew JM et al.
Acta Neuropathologica, 2021
Assessing the relationship between monoallelic PRKN mutations and Parkinson's risk.
Lubbe SJ et al.
Human Molecular Genetics, 2021
The Role of VPS35 in the Pathobiology of Parkinson's Disease.
Sassone J et al.
Cellular and Molecular Neurobiology, 2021
Multitasking guardian of mitochondrial quality: Parkin function and Parkinson's disease.
Kamienieva I et al.
Translational Neurodegeneration, 2021
Dysfunction of Synaptic Vesicle Endocytosis in Parkinson's Disease.
Zou L et al.
Frontiers in Integrative Neuroscience, 2021
The landscape of Parkin variants reveals pathogenic mechanisms and therapeutic targets in Parkinson's disease.
Yi W et al.
Human Molecular Genetics, 2019
Bioenergetics and Autophagic Imbalance in Patients-Derived Cell Models of Parkinson Disease Supports Systemic Dysfunction in Neurodegeneration.
González-Casacuberta I et al.
Frontiers in Neuroscience, 2019
Parkin mediates the ubiquitination of VPS35 and modulates retromer-dependent endosomal sorting.
Williams ET et al.
Human Molecular Genetics, 2018
The M458L missense mutation disrupts the catalytic properties of Parkin.
Do YJ et al.
Febs Letters, 2018
Twenty years since the discovery of the parkin gene.
Hattori N et al.
Journal of Neural Transmission (vienna, Austria : 1996), 2017
The Effects of Variants in the Parkin, PINK1, and DJ-1 Genes along with Evidence for their Pathogenicity.
Hauser DN et al.
Current Protein & Peptide Science, 2017
Mechanisms of mitophagy: PINK1, Parkin, USP30 and beyond.
Bingol B et al.
Free Radical Biology & Medicine, 2016
Dual Function of Phosphoubiquitin in E3 Activation of Parkin.
Walinda E et al.
The Journal of Biological Chemistry, 2016
Covalent ISG15 conjugation positively regulates the ubiquitin E3 ligase activity of parkin.
Im E et al.
Open Biology, 2016
Probes of ubiquitin E3 ligases enable systematic dissection of parkin activation.
Pao KC et al.
Nature Chemical Biology, 2016
Site-specific Interaction Mapping of Phosphorylated Ubiquitin to Uncover Parkin Activation.
Yamano K et al.
The Journal of Biological Chemistry, 2015
Parkin maintains mitochondrial levels of the protective Parkinson's disease-related enzyme 17-β hydroxysteroid dehydrogenase type 10.
Bertolin G et al.
Cell Death and Differentiation, 2015
Structural studies of parkin and sacsin: Mitochondrial dynamics in neurodegenerative diseases.
Li X et al.
Movement Disorders : Official Journal of the Movement Disorder Society, 2015
Structural and Functional Impact of Parkinson Disease-Associated Mutations in the E3 Ubiquitin Ligase Parkin.
Fiesel FC et al.
Human Mutation, 2015
Functional interplay between Parkin and Drp1 in mitochondrial fission and clearance.
Buhlman L et al.
Biochimica Et Biophysica Acta, 2014
Phosphorylation of Parkin at Serine65 is essential for activation: elaboration of a Miro1 substrate-based assay of Parkin E3 ligase activity.
Kazlauskaite A et al.
Open Biology, 2014
Genetic insights into sporadic Parkinson's disease pathogenesis.
Chai C et al.
Current Genomics, 2013
Mutations in PRKN and SNCA Genes Important for the Progress of Parkinson's Disease.
Oczkowska A et al.
Current Genomics, 2013
The TOMM machinery is a molecular switch in PINK1 and PARK2/PARKIN-dependent mitochondrial clearance.
Bertolin G et al.
Autophagy, 2013
Structure of parkin reveals mechanisms for ubiquitin ligase activation.
Trempe JF et al.
Science (new York, N.y.), 2013
Mitochondrial dynamics and Parkinson's disease: focus on parkin.
Lim KL et al.
Antioxidants & Redox Signaling, 2012
[Role of mitophagy in hereditary Parkinson's disease].
Matsuda N et al.
Brain and Nerve = Shinkei Kenkyu No Shinpo, 2012
Parkin promotes the ubiquitination and degradation of the mitochondrial fusion factor mitofusin 1.
Glauser L et al.
Journal of Neurochemistry, 2011
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
PINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondria and activates latent Parkin for mitophagy.
Matsuda N et al.
The Journal of Cell Biology, 2010
PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1.
Geisler S et al.
Nature Cell Biology, 2010
Parkin-mediated ubiquitination regulates phospholipase C-gamma1.
Dehvari N et al.
Journal of Cellular and Molecular Medicine, 2009
Protein misfolding and aggregation in Parkinson's disease.
Tan JM et al.
Antioxidants & Redox Signaling, 2009
Parkin deficiency disrupts calcium homeostasis by modulating phospholipase C signalling.
Sandebring A et al.
The Febs Journal, 2009
Parkin mediates the degradation-independent ubiquitination of Hsp70.
Moore DJ et al.
Journal of Neurochemistry, 2008
Rare heterozygous parkin variants in French early-onset Parkinson disease patients and controls.
Lesage S et al.
Journal of Medical Genetics, 2008
Drosophila overexpressing parkin R275W mutant exhibits dopaminergic neuron degeneration and mitochondrial abnormalities.
Wang C et al.
The Journal of Neuroscience : the Official Journal of the Society for Neuroscience, 2007
Structure of the Parkin in-between-ring domain provides insights for E3-ligase dysfunction in autosomal recessive Parkinson's disease.
Beasley SA et al.
Proceedings of the National Academy of Sciences of the United States of America, 2007
Biochemical analysis of Parkinson's disease-causing variants of Parkin, an E3 ubiquitin-protein ligase with monoubiquitylation capacity.
Hampe C et al.
Human Molecular Genetics, 2006
Diverse effects of pathogenic mutations of Parkin that catalyze multiple monoubiquitylation in vitro.
Matsuda N et al.
The Journal of Biological Chemistry, 2006
Effect of overexpression of wild-type or mutant parkin on the cellular response induced by toxic insults.
Hyun DH et al.
Journal of Neuroscience Research, 2005
Familial-associated mutations differentially disrupt the solubility, localization, binding and ubiquitination properties of parkin.
Sriram SR et al.
Human Molecular Genetics, 2005
Prevalence of parkin gene mutations and variations in idiopathic Parkinson's disease.
Sinha R et al.
Parkinsonism & Related Disorders, 2005
Alterations in the solubility and intracellular localization of parkin by several familial Parkinson's disease-linked point mutations.
Wang C et al.
Journal of Neurochemistry, 2005