Korth Group

Group leader

Title	Name	First Name	Position
Prof. Dr.	Korth	Carsten	Group leader

 For more information on the principal investigator click here...

Researchers

Title	Name	First Name	Position
Dr. rer. nat	Müller-Schiffmann	Andreas	Postdoc
Dr. rer. nat.	Bader	Verian	Postdoc
Dr. rer. nat.	Muyrers	Janine	Postdoc
Dipl.-Biol.	Trossbach	Svenja	Graduate student

BioStruct Fellow

Title	Name	First Name	Position
	N.N.	N.N.	N.N.

 For more information on the biostruct fellow click here...

Further Team Members

Technicians:	1
Master/Diploma students:	1
PHD/MD students:	2

Contact

Korth Lab /Research Group Neurodegeneration
Neuropathology
Heinrich Heine University of Düsseldorf Medical School
Moorenstrasse 5
40225 Düsseldorf
Germany

+49(0)-211-8116153


website:
http://www.neuropathology-duesseldorf.de/NUKD/Deutsch/Forschung/AG+Korth/Contact?sid=AJWnmGejtRJhSYAcV1slW0&iid=2

Special methodical expertise

• Generation of targeted ligands: mono- and polyclonal antibodies, recombinant scFv antibody fragements and in silico affinity purification of those
• Generation of conformation-specific ligands
• Proteomics of protein conformers

 click here for further information

Main areas of research interest

Research Focus:
Investigation of protein misassembly, misfolding or misprocessing in brain diseases, and the development of pharmacotherapies to interfer with or prevent these protein pathologies. There is a focus on neurobiology and proteinbiochemistry. Generation of (mis)assembled proteins is investigated at the levels of generation, recognition and degradation in in vivo and in vitro models.

• Neurobiology of chronic mental diseases (CMD) schizophrenia and recurrent affective disorders: Identification and characterization of CMD-associated proteins by proteomics, biochemistry, cell biology. Characterizing sporadic CMD as protein misassembly disorders. Development of animal models for CMD. Translational research for identifying biological markers as diagnostic tests for CMD and CMD-associated conformers as pharmacological targets.
• Cell biology and functional regulation of protein misfolding: Generation of conformation-sensitive ligands, monoclonal antibodies and recombinant antibodies for disgnosing and characterizing protein conformational diseases, in particular prion-protein associated diseases and Alzheimer's disease. Development of animal models for protein conformational disorders.
• Pharmacotherapy of protein conformational diseases: Using prion protein conformers and Abeta oligomers as models, neutralizing chimeric small molecules and recombinant antibody fragments have been and are currently developed that target specific, toxicity-associated conformations.
• Neurobiology of Aging: Insoluble and aggregated protein deposits are not only hallmarks of neurodegenerative disorders but are also hallmarks of the aging brain in the form of acculumating lipofuscin and other cellular debris. Dysfunctional protein degradation in the aging post-mitotic cell is investigated by proteomic, biochemical and cell biological techniques. Cross-influences to protein conformatonal diseases are revealed.

Facilities

The laboratories cover the following gene technology security levels:	S1, S2
The laboratories cover the following biohazard levels:	BSL1, BSL2, BSL3***

Laboratory Equipment

General equipment available in the laboratories:

• Biochemistry
• Cell culture
• Molecular biology
• Cell Biology
• Microbiology
• Histology

Special equipment, which is not generally available in most laboratories:

• Fluorescence spectrometer (Saphire), ultracentrifuges (under S2 conditions), cell culture robot, DNA sequencer

Important References

• Leliveld SR, Bader V, Hendriks P, Prikulis I, Sajnani G, Requena J, Korth C (2008). Insolubility of DISC1 disrupts oligomer-dependent interactions with NDEL1 and is associated with sporadic mental disease. Journal of Neuroscience 28:3839-45.
• Müller-Schiffmann A, Petsch B, Leliveld SR, Muyrers J, Salwierz A, Mangels C, Schwarzinger S, Riesner D, Stitz L, Korth C (2009). Complementarity determining regions of a funtional anti-PrP scFv orchestrate conformation-specificity and antiprion activity. Molecular Immunology, 46:532-540.
• Leliveld SR, Dame RT, Wuite G, Stitz L, Korth C (2006) The expanded octarepeat domain selectively binds prions and disrupts homomeric prion protein interactions. Journal of Biological Chemistry 281:3268-3275.
• Korth C, Kaneko K, Groth D, Heye N, Telling G, Mastrianni J, Parchi P, Gambetti P, Will R, Ironside J, Heinrich C, Tremblay P, DeArmond S, Prusiner SB (2003) Abbreviated transmission of Creutzfeldt-Jakob disease to mice expressing a novel chimeric mouse-human prion protein transgene. Proceedings of the National Academy of Sciences USA 100: 4784-88.
• Korth C, May BCM, Cohen FE, Prusiner SB (2001) Acridine and phenothiazine derivatives as pharmacotherapeutics for prion disease. Proceedings of the National Academy of Sciences USA 98: 9836-41.
• Korth C, Stierli B, Streit P, Moser M, Schaller O, Fischer R, Schulz-Schaeffer W, Kretzschmar H, Raeber A, Braun U, Ehrensperger F, Hornemann S, Glockshuber R, Riek R, Billeter M, Wuthrich K, Oesch B (1997) Prion (PrPSc)-specific epitope defined by a monoclonal antibody. Nature 390: 74-77.