Project Details
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Comparative Protein Biochemistry

Subject Area Biochemistry
Term from 2014 to 2017
Project identifier Deutsche Forschungsgemeinschaft (DFG) - Project number 257653716
 
Final Report Year 2018

Final Report Abstract

No abstract available

Publications

  • 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 V., Djuika C.F., Koduka J., Schlossarek S., Kopp J., Büchler M., Lanzer M., Deponte M.
    (See online at https://doi.org/10.1016/j.freeradbiomed.2015.04.030)
  • 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 P., Staudacher V., Deponte M.
    (See online at https://doi.org/10.1039/c5sc01051a)
  • Glutaredoxin catalysis requires two distinct glutathione interaction sites. Nature Communications, Vol. 8. 2017, Article number: 14835.
    Begas P., Liedgens L., Moseler A., Meyer A.J., Deponte M.
    (See online at https://doi.org/10.1038/ncomms14835)
  • 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 V., Trujillo M., Diederichs T., Dick T.P., Radi R., Morgan B., Deponte M.
    (See online at https://doi.org/10.1016/j.redox.2017.10.017)
  • The cytosolic glyoxalases of Plasmodium falciparum are dispensable during asexual blood-stage development. Microbial Cell, Vol. 5. 2018, No. 1, pp. 32 - 41.
    Wezena C.A., Alisch R., Golzmann A., Liedgens L., Staudacher V., Pradel G., Deponte M.
    (See online at https://doi.org/10.15698/mic2018.01.608)
 
 

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