Short CV/Education and training

  • Diplom degree in the biochemistry of natural products, University of Bayreuth, Germany

  • Doctorate from the Max Planck Institute of Molecular Physiology, Dortmund, Germany (Prof. Roger Goody/Dr Jochen Reinstein)

  • Postdoc, The Scripps Research Institute, La Jolla, California, USA (Prof. David Millar)

  • Director of an independent junior research group, University of Bayreuth

  • Professor of biophysical chemistry, University of Basel, Switzerland

  • Professor of physical chemistry, University of Münster, Germany

Selected publications

  • Hilbert, M., Karow, A.R., Klostermeier, D.: The mechanism of ATP-dependent RNA unwinding by DEAD box proteins. In: Biol Chem 390(12), 2009. pp. 1237-1250.

  • Karow, A.R., Klostermeier, D.: A conformational change in the helicase core is necessary but not sufficient for RNA unwinding by the DEAD box helicase YxiN. In: Nucleic Acids Res, 37, 2009. pp. 4464-4471.

  • Gubaev, A., Hilbert, M., Klostermeier, D.: The DNA-gate of Bacillus subtilis gyrase is predominantly in the closed conformation during the DNA supercoiling reaction. In: Proc Natl Acad Sci USA 106(32), 2009. pp. 13278-13283.

  • Aregger, R., Klostermeier, D.: The DEAD Box Helicase YxiN Maintains a Closed Conformation during ATP Hydrolysis. In: Biochemistry 48(45), 2009. pp. 10679-10681.

  • Klostermeier, D., Rudolph, M.G.: A novel dimerization motif in the C-terminal domain of the Thermus thermophilus DEAD box helicase Hera confers substantial flexibility. In: Nucleic Acids Res 37, 2009. pp. 421-430.

  • Linden, M.H., Hartmann, R.K., Klostermeier, D.: The putative RNase P motif in the DEAD box helicase Hera is dispensable for efficient interaction with RNA and helicase activity. In: Nucleic Acids Res 36(18), 2008. pp. 5800-5811.

  • Theissen, B. et al.: Cooperative binding of ATP and RNA induces a closed conformation in a DEAD box RNA helicase. In: Proc Natl Acad Sci USA 105(2), 2008. pp. 548-553.



Complete list of publications

Selected projects

  • Conformational changes in the catalytic cycle of ATP-powered molecular machines and their role in the biological function: RNA helicases, DNA topoisomerases, nanobiology

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