Associated Papers
The reaction mechanism for glycolysis side product degradation by Parkinson's disease-linked DJ-1.
Watanabe A et al.
The Journal of Cell Biology, 2025
Comparative analysis of web-based programs for single amino acid substitutions in proteins.
Choudhury A et al.
Plos One, 2022
35507592 (PubMed )
Supplement: pone.0267084.s001.xlsx › PARK7
Unfolding is the driving force for mitochondrial import and degradation of the Parkinson's disease-related protein DJ-1.
Queliconi BB et al.
Journal of Cell Science, 2021
Mitochondrial LonP1 protease is implicated in the degradation of unstable Parkinson's disease-associated DJ-1/PARK 7 missense mutants.
Sánchez-Lanzas R et al.
Scientific Reports, 2021
Parkinson's disease-related DJ-1 functions in thiol quality control against aldehyde attack in vitro.
Matsuda N et al.
Scientific Reports, 2017
DJ-1 as a Biomarker of Parkinson's Disease.
Saito Y
Advances in Experimental Medicine and Biology, 2017
Oxidation and interaction of DJ-1 with 20S proteasome in the erythrocytes of early stage Parkinson's disease patients.
Saito Y et al.
Scientific Reports, 2016
Unexpected mitochondrial matrix localization of Parkinson's disease-related DJ-1 mutants but not wild-type DJ-1.
Kojima W et al.
Genes to Cells : Devoted to Molecular & Cellular Mechanisms, 2016
Use of cysteine-reactive cross-linkers to probe conformational flexibility of human DJ-1 demonstrates that Glu18 mutations are dimers.
Prahlad J et al.
Journal of Neurochemistry, 2014
Reactive oxygen species-mediated DJ-1 monomerization modulates intracellular trafficking involving karyopherin β2.
Björkblom B et al.
Molecular and Cellular Biology, 2014
Monomer DJ-1 and its N-terminal sequence are necessary for mitochondrial localization of DJ-1 mutants.
Maita C et al.
Plos One, 2013
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