Associated Papers
Impact of Single Amino Acid Substitutions in Parkinsonism-Associated Deglycase-PARK7 and Their Association with Parkinson's Disease.
Anjum F et al.
Journal of Personalized Medicine, 2022
35207708 (PubMed )
Supplement: jpm-12-00220-s001.zip › jpm-1518127-supplementary.pdf
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
A transient post-translational modification of active site cysteine alters binding properties of the parkinsonism protein DJ-1.
Mussakhmetov A et al.
Biochemical and Biophysical Research Communications, 2018
Structural Biology of the DJ-1 Superfamily.
Smith N et al.
Advances in Experimental Medicine and Biology, 2017
Structural and functional insight into the different oxidation states of SAV1875 from Staphylococcus aureus.
Kim HJ et al.
The Biochemical Journal, 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
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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