Associated Papers
An update on the monogenic causes of Parkinson's disease: Impact on patient stratification and personalised medicine.
Asmi S et al.
Ageing Research Reviews, 2026
Computational association in parkinson's disease SNPs with brain structural and functional alterations.
Subramaniyan S et al.
Neurogenetics, 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
Gene Panel Sequencing Analysis Revealed a Strong Contribution of Rare Coding Variants to the Risk of Parkinson's Disease in Sporadic Moroccan Patients.
Smaili I et al.
Journal of Molecular Neuroscience : Mn, 2023
Systematic analysis of PINK1 variants of unknown significance shows intact mitophagy function for most variants.
Ma KY et al.
Npj Parkinson's Disease, 2021
PINK1: A Bridge between Mitochondria and Parkinson's Disease.
Gonçalves FB et al.
Life (basel, Switzerland), 2021
Dysfunction of Synaptic Vesicle Endocytosis in Parkinson's Disease.
Zou L et al.
Frontiers in Integrative Neuroscience, 2021
New insights into the structure of PINK1 and the mechanism of ubiquitin phosphorylation.
Rasool S et al.
Critical Reviews in Biochemistry and Molecular Biology, 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
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
PINK1 rendered temperature sensitive by disease-associated and engineered mutations.
Narendra DP et al.
Human Molecular Genetics, 2013
Structure and Function of Parkin, PINK1, and DJ-1, the Three Musketeers of Neuroprotection.
Trempe JF et al.
Frontiers in Neurology, 2013
Role of PINK1 binding to the TOM complex and alternate intracellular membranes in recruitment and activation of the E3 ligase Parkin.
Lazarou M et al.
Developmental Cell, 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
PINK1-mediated phosphorylation of the Parkin ubiquitin-like domain primes mitochondrial translocation of Parkin and regulates mitophagy.
Shiba-Fukushima K et al.
Scientific Reports, 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 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 selectively stabilized on impaired mitochondria to activate Parkin.
Narendra DP et al.
Plos Biology, 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
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
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
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
Novel PINK1 mutations in early-onset parkinsonism.
Hatano Y et al.
Annals of Neurology, 2004