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
Structural Biology of the DJ-1 Superfamily.
Smith N et al.
Advances in Experimental Medicine and Biology, 2017
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
Thermodynamic and structural characterization of the specific binding of Zn(II) to human protein DJ-1.
Tashiro S et al.
Biochemistry, 2014
DJ-1 is a copper chaperone acting on SOD1 activation.
Girotto S et al.
The Journal of Biological Chemistry, 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
Formation of a stabilized cysteine sulfinic acid is critical for the mitochondrial function of the parkinsonism protein DJ-1.
Blackinton J et al.
The Journal of Biological Chemistry, 2009
Cysteine pKa depression by a protonated glutamic acid in human DJ-1.
Witt AC et al.
Biochemistry, 2008
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