Associated Papers
Targeting mitophagy in neurodegenerative diseases.
Antico O et al.
Nature Reviews. Drug Discovery, 2025
Transmembrane Parkinson's disease mutation of PINK1 leads to altered mitochondrial anchoring.
Brassard R et al.
The Journal of Biological Chemistry, 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
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
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
Ubiquitin phosphorylation in Parkinson's disease: Implications for pathogenesis and treatment.
Chin LS et al.
Translational Neurodegeneration, 2016
Differential submitochondrial localization of PINK1 as a molecular switch for mediating distinct mitochondrial signaling pathways.
Fallaize D et al.
Cellular Signalling, 2015
Genetic deficiency of the mitochondrial protein PGAM5 causes a Parkinson's-like movement disorder.
Lu W et al.
Nature Communications, 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
PINK1 autophosphorylation upon membrane potential dissipation is essential for Parkin recruitment to damaged mitochondria.
Okatsu K et al.
Nature Communications, 2012
PINK1 cleavage at position A103 by the mitochondrial protease PARL.
Deas E et al.
Human Molecular Genetics, 2011
Biochemical aspects of the neuroprotective mechanism of PTEN-induced kinase-1 (PINK1).
Mills RD et al.
Journal of Neurochemistry, 2008
Pink1 Parkinson mutations, the Cdc37/Hsp90 chaperones and Parkin all influence the maturation or subcellular distribution of Pink1.
Weihofen A et al.
Human Molecular Genetics, 2008
A cell biological perspective on mitochondrial dysfunction in Parkinson disease and other neurodegenerative diseases.
Mandemakers W et al.
Journal of Cell Science, 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
PINK1, Parkin, and DJ-1 mutations in Italian patients with early-onset parkinsonism.
Klein C et al.
European Journal of Human Genetics : Ejhg, 2005
Early-onset parkinsonism associated with PINK1 mutations: frequency, genotypes, and phenotypes.
Bonifati V et al.
Neurology, 2005
PINK1 mutations are associated with sporadic early-onset parkinsonism.
Valente EM et al.
Annals of Neurology, 2004