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BIOCHEMISTRY OF NEURODEGENERATIVE DISEASES

Prof. Dr. Jörg Tatzelt

Current Position: Head of Department Biochemistry of Neurodegenerative Disease, Institute of Biochemistry and Pathobiochemistry, Ruhr University Bochum.
Professor: Neurobiochemistry, Adolf Butenandt Institute, Ludwig Maximilians University Munich.
Group Leader: Max-Planck-Institute for Biochemistry, Department of Cellular Biochemistry.
Postdoctoral Fellow: in the laboratory of Dr. Stanley B. Prusiner, Department of Neurology, University of California, San Francisco.
PhD: University of Cologne, Department of Virology.

Research Interest
Aberrant protein folding and neurodegeneration
The main aim of our biochemical research is to identify cellular factors and signaling cascades implicated in neuronal integrity and in the pathophysiological alterations leading to neurodegeneration. Our integrative research has a strong focus on the biochemical and cell biological analysis of cellular pathways, which are also of broad neurobiological interest.
Specifically, we are employing in vitro, yeast, neuronal cell culture and animal models to focus on three major topics:

• Cellular mechanisms underlying the formation and toxic activity of aberrant protein conformers
• Signaling pathways induced by neurotoxic conformers
• Therapeutic strategies for neurodegenerative diseases

Techniques
Cell culture models, including primary neurons to study formation, spreading and signaling of neurotoxic protein conformers.
In vitro and cell culture models to study import of proteins into the endoplasmic reticulum and mitochondria.

Selected Reading
Woerner AC, Frottin F, Hornburg D, Feng LR, Meissner F, Patra M, Tatzelt J, Mann M, Winklhofer KF, Hartl FU and Hipp MS (2016) Cytoplasmic protein aggregates interfere with nucleo-cytoplasmic transport of protein and RNA. Science 2016, 351, 173-176

Pfeiffer NV, Dirndorfer D, Lang S, Resenberger UK, Restelli MR, Hemion C, Miesbauer M, Frank A, Neutzner A, Zimmermann R, Winklhofer KF and Tatzelt J. Structural features within the nascent chain regulate alternative targeting of secretory proteins to mitochondria. EMBO J 2013, 32, 1036-1051.


Resenberger UK, Harmeier A, Woerner AC, Goodman JL, Müller V, Krishnan R, Vabulas RM, Kretzschmar HA, Lindquist S, Hartl FU, Multhaup G, Winklhofer KF and Tatzelt J. The cellular prion protein mediates neurotoxic signaling of ß-sheet-rich conformers independent of prion replication. EMBO J 2011, 30, 2057-70.

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