Varaico: Literature-Extracted Genetic Variants

Gene:PINK1
Variant:p.G409V
Back to variants list

PINK1

NM_032409.3:p.G409V

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

Discriminating activating, deactivating and resistance variants in protein kinases.

Singh G et al.

Genome Medicine, 2025

41152984 (PubMed )
Supplement: 13073_2025_1564_MOESM2_ESM.xlsx › Table_S6

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

A molecular simulation study of the clinical G409V mutant in PINK1 associated with early-onset Parkinson's disease.

Lo HH et al.

International Journal of Biological Macromolecules, 2024

Activation mechanism of PINK1.

Gan ZY et al.

Nature, 2022

34933320 (PubMed )
Supplement: 41586_2021_4340_MOESM4_ESM.pdf

Mapping of a N-terminal α-helix domain required for human PINK1 stabilization, Serine228 autophosphorylation and activation in cells.

Kakade P et al.

Open Biology, 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

Ubiquitin phosphorylation in Parkinson's disease: Implications for pathogenesis and treatment.

Chin LS et al.

Translational Neurodegeneration, 2016

Recurrent and fatal akinetic crisis in genetic-mitochondrial parkinsonisms.

Bonanni L et al.

European Journal of Neurology, 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

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

Phylogenetic and in silico structural analysis of the Parkinson disease-related kinase PINK1.

Cardona F et al.

Human Mutation, 2011

Genetic mutations and mitochondrial toxins shed new light on the pathogenesis of Parkinson's disease.

Sato S et al.

Parkinson's Disease, 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

20506312 (PubMed )
Supplement: humu0031-0763-SD1.pdf

PINK1 is recruited to mitochondria with parkin and associates with LC3 in mitophagy.

Kawajiri S et al.

Febs Letters, 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

Select a paper to view details
UCSC Genome Browser·Imprint·Privacy·Terms·Feedback·Email Updates·

Regarding the variants extracted from papers and shown text snippets from research papers, the following holds: "Some rights reserved. This work permits non-commercial use, distribution and reproduction in any medium, provided the original author and source are credited."