Associated Papers
Targeting mitophagy in neurodegenerative diseases.
Antico O et al.
Nature Reviews. Drug Discovery, 2025
Rethinking 'rare' PINK1 Parkinson's disease: A meta-analysis of geographical prevalence, phenotypic diversity, and α-synuclein pathology.
Yin EP et al.
Journal of Parkinson's Disease, 2025
Clinico-Genetic Profiles of Seven Patients With PINK1-Related Parkinson's Disease: A Case Series From a Tertiary Care Centre in India and a Review of the Literature.
Gunasekaran A et al.
Journal of Movement Disorders, 2024
A Novel PINK1 p.F385S Loss-of-Function Mutation in an Indian Family with Parkinson's Disease.
Sharma K et al.
Movement Disorders : Official Journal of the Movement Disorder Society, 2024
PTEN-induced kinase 1 (PINK1) and Parkin: Unlocking a mitochondrial quality control pathway linked to Parkinson's disease.
Agarwal S et al.
Current Opinion in Neurobiology, 2022
Activation mechanism of PINK1.
Gan ZY et al.
Nature, 2022
Systematic analysis of PINK1 variants of unknown significance shows intact mitophagy function for most variants.
Ma KY et al.
Npj Parkinson's Disease, 2021
Genotype-Phenotype Relations for the Parkinson's Disease Genes Parkin, PINK1, DJ1: MDSGene Systematic Review.
Kasten M et al.
Movement Disorders : Official Journal of the Movement Disorder Society, 2018
Structure of PINK1 in complex with its substrate ubiquitin.
Schubert AF et al.
Nature, 2017
Structure of PINK1 and mechanisms of Parkinson's disease-associated mutations.
Kumar A et al.
Elife, 2017
PINK1 and Parkin: emerging themes in mitochondrial homeostasis.
McWilliams TG et al.
Current Opinion in Cell Biology, 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
Antagonism of proteasome inhibitor-induced heme oxygenase-1 expression by PINK1 mutation.
Sheng XJ et al.
Plos One, 2017
Ubiquitin is phosphorylated by PINK1 to activate parkin.
Koyano F et al.
Nature, 2014
A dimeric PINK1-containing complex on depolarized mitochondria stimulates Parkin recruitment.
Okatsu K et al.
The Journal of Biological Chemistry, 2013
Parkin-catalyzed ubiquitin-ester transfer is triggered by PINK1-dependent phosphorylation.
Iguchi M et al.
The Journal of Biological Chemistry, 2013
Characterization of PINK1 (PTEN-induced putative kinase 1) mutations associated with Parkinson disease in mammalian cells and Drosophila.
Song S et al.
The Journal of Biological Chemistry, 2013
Analysis of the regulatory and catalytic domains of PTEN-induced kinase-1 (PINK1).
Sim CH et al.
Human Mutation, 2012
PINK1 autophosphorylation upon membrane potential dissipation is essential for Parkin recruitment to damaged mitochondria.
Okatsu K et al.
Nature Communications, 2012
Discovery of catalytically active orthologues of the Parkinson's disease kinase PINK1: analysis of substrate specificity and impact of mutations.
Woodroof HI et al.
Open Biology, 2011
Genetic mutations and functions of PINK1.
Kawajiri S et al.
Trends in Pharmacological Sciences, 2011
Phylogenetic and in silico structural analysis of the Parkinson disease-related kinase PINK1.
Cardona F et al.
Human Mutation, 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 is necessary for long term survival and mitochondrial function in human dopaminergic neurons.
Wood-Kaczmar A et al.
Plos One, 2008
Biochemical aspects of the neuroprotective mechanism of PTEN-induced kinase-1 (PINK1).
Mills RD et al.
Journal of Neurochemistry, 2008
C-terminal truncation and Parkinson's disease-associated mutations down-regulate the protein serine/threonine kinase activity of PTEN-induced kinase-1.
Sim CH et al.
Human Molecular Genetics, 2006
Mutational analysis of the PINK1 gene in early-onset parkinsonism in Europe and North Africa.
Ibáñez P et al.
Brain : a Journal of Neurology, 2006