Heinrich-Heine-Universitäte-Düsseldorf
#12 - Prion research group
Contact
Team Leader: Prof. Detlev Riesner
Universitätsstr. 1
Düsseldorf, 40225, Germany
Contact: Prof. Detlev Riesner
Tel: +49 211 81 11390
Fax: +49 211 81 15167
E-mail: riesner@biophys.uni-duesseldorf.de
Institute website:
http://www.biologie.uni-duesseldorf.de/englisch
Main area of research
- Diagnosis
- Decontamination
- Basic research
Research Team
- Researchers: 7
- Technicians: 3
- Postdocs: 3
- PHD/MD Students: 3
Facilities and Equipment
- Laboratories: BSL1, BSL2, BSL3
- General equipment: Biochemistry, Molecular biology, Biophysics, Histology, Imaging
- Special equipment: analytical ultracentrifuge, 2-colour fluorescence spectrometer (FCS) with imaging, circular dichroism spectrometer, surface plasmon resonance (Biacore), fluorescence spectrometer, high pressure incubator for temperatures up to 200 °C. All instruments are within the BSL3-facility
- Specific methods: In vitro misfolding assays, PrPC from CHO-culture, PrP-membrane interaction, diagnosis by surface-FIDA
Main references
- Elfrink K, Ollesch J, Stöhr J, Willbold D, Riesner D & Gerwert K (2008). Structural changes of membrane anchored native PrPC. Proc Natl AcadSci USA - in print.
- Stöhr J, Weinmann N, Wille H, Kaimann T, Nagel-Steger L, Birkmann E, Panza G, Prusiner SB, Eigen M & Riesner D. (2008). Mechanisms of prion protein assembly into amyloid. Proc Natl Acad Sci USA, 105(7), 2409-2414.
- Kaimann T, Metzger S, Kuhlmann K, Brandt B, Birkmann E, Höltje HD & Riesner D. (2008). Molecular model of an alpha-helical prion protein dimer and its monomeric subunits as derived from chemical cross-linking and molecular modeling calculations. J Mol Biol., 376(2), 582-596.
- Birkmann E, Henke F, Weinmann N, Dumpitak C, Groschup M, Funke A, Willbold D & Riesner D. (2007). Counting of single prion particles bound to a capture-antibody surface (surface-FIDA). Vet Microbiol, 123(4), 294-304.
- Mu.ller H, Stitz L, Wille H, Prusiner SB, Riesner D. (2007). Influence of water, fat, and glycerol on the mechanism of thermal prion inactivation. J Biol Chem, 282(49), 35855-35867.
