Associated Papers
AI-augmented prediction of high-risk PINK1 variants associated with Parkinson's disease: integrating multilayered bioinformatics, MD simulation, and deep learning.
Rehman HU et al.
Methods (san Diego, Calif.), 2025
Inborn errors of canonical autophagy in neurodegenerative diseases.
Freisem D et al.
Human Molecular Genetics, 2025
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
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
Systematic analysis of PINK1 variants of unknown significance shows intact mitophagy function for most variants.
Ma KY et al.
Npj Parkinson's Disease, 2021
Dysfunction of Synaptic Vesicle Endocytosis in Parkinson's Disease.
Zou L et al.
Frontiers in Integrative Neuroscience, 2021
Structural insights into ubiquitin phosphorylation by PINK1.
Okatsu K et al.
Scientific Reports, 2018
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
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
Analysis of the regulatory and catalytic domains of PTEN-induced kinase-1 (PINK1).
Sim CH et al.
Human Mutation, 2012
Dysfunction of mitochondrial respiratory chain complex I in neurological disorders: genetics and pathogenetic mechanisms.
Petruzzella V et al.
Advances in Experimental Medicine and Biology, 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
PARK6 PINK1 mutants are defective in maintaining mitochondrial membrane potential and inhibiting ROS formation of substantia nigra dopaminergic neurons.
Wang HL et al.
Biochimica Et Biophysica Acta, 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
Tickled PINK1: mitochondrial homeostasis and autophagy in recessive Parkinsonism.
Chu CT
Biochimica Et Biophysica Acta, 2010
Parkin stabilizes PINK1 through direct interaction.
Shiba K et al.
Biochemical and Biophysical Research Communications, 2009
Pathogenetic mechanisms in hereditary dysfunctions of complex I of the respiratory chain in neurological diseases.
Papa S et al.
Biochimica Et Biophysica Acta, 2009
PINK1 defect causes mitochondrial dysfunction, proteasomal deficit and alpha-synuclein aggregation in cell culture models of Parkinson's disease.
Liu W et al.
Plos One, 2009
Biochemical aspects of the neuroprotective mechanism of PTEN-induced kinase-1 (PINK1).
Mills RD et al.
Journal of Neurochemistry, 2008
PINK1 mutants associated with recessive Parkinson's disease are defective in inhibiting mitochondrial release of cytochrome c.
Wang HL et al.
Neurobiology of Disease, 2007
Novel features in a patient homozygous for the L347P mutation in the PINK1 gene.
Doostzadeh J et al.
Parkinsonism & Related Disorders, 2007
In vitro and in silico analysis reveals an efficient algorithm to predict the splicing consequences of mutations at the 5' splice sites.
Sahashi K et al.
Nucleic Acids Research, 2007
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
Homozygous and heterozygous PINK1 mutations: considerations for diagnosis and care of Parkinson's disease patients.
Zadikoff C et al.
Movement Disorders : Official Journal of the Movement Disorder Society, 2006
Early-onset parkinsonism associated with PINK1 mutations: frequency, genotypes, and phenotypes.
Bonifati V et al.
Neurology, 2005
Novel PINK1 mutations in early-onset parkinsonism.
Hatano Y et al.
Annals of Neurology, 2004