Project Details
Comparative Protein Biochemistry
Applicant
Professor Dr. Marcel Deponte
Subject Area
Biochemistry
Term
from 2014 to 2017
Project identifier
Deutsche Forschungsgemeinschaft (DFG) - Project number 257653716
Final Report Year
2018
No abstract available
Publications
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Plasmodium falciparum antioxidant protein reveals a novel mechanism for balancing turnover and inactivation of peroxiredoxins. Free Radical Biology and Medicine, Vol. 85. 2015, pp. 228-236.
Staudacher, Verena; Djuika, Carine F.; Koduka, Joshua; Schlossarek, Sarah; Kopp, Jürgen; Büchler, Marleen; Lanzer, Michael & Deponte, Marcel
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Systematic re-evaluation of the bis(2-hydroxyethyl)disulfide (HEDS) assay reveals an alternative mechanism and activity of glutaredoxins. Chemical Science, Vol. 6. 2015, pp. 3788-3796.
Begas, Patricia; Staudacher, Verena & Deponte, Marcel
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Glutaredoxin catalysis requires two distinct glutathione interaction sites. Nature Communications, Vol. 8. 2017, Article number: 14835.
Begas, Patricia; Liedgens, Linda; Moseler, Anna; Meyer, Andreas J. & Deponte, Marcel
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Redox-sensitive GFP fusions for monitoring the catalytic mechanism and inactivation of peroxiredoxins in living cells. Redox Biology, Vol. 14. 2018, pp. 549-556.
Staudacher, Verena; Trujillo, Madia; Diederichs, Tim; Dick, Tobias P.; Radi, Rafael; Morgan, Bruce & Deponte, Marcel
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The cytosolic glyoxalases of Plasmodium falciparum are dispensable during asexual blood-stage development. Microbial Cell, Vol. 5. 2018, No. 1, pp. 32 - 41.
Wezena, Cletus A.; Alisch, Romy; Golzmann, Alexandra; Liedgens, Linda; Staudacher, Verena; Pradel, Gabriele & Deponte, Marcel
