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Tatzelt Lab - Aberrant protein folding and neurodegeneration
Aberrant protein folding and neurodegeneration
Various approaches coming from neuropathology, genetics, animal modeling and biophysics have established a crucial role of protein misfolding in the pathogenic process of different neurodegenerative diseases, such as Alzheimer's disease, Parkinson’s disease, polyglutamine expansion diseases and prion diseases. However, there is an ongoing debate about the nature of the harmful proteinaceous species and how toxic conformers selectively damage neuronal populations.
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
Newest Publications
Cellular Prion Protein Mediates Toxic Signaling of Amyloid Beta
In this minireview Tatzelt and colleagues summarize current work on the role of the cellular pion protein (PrPC) as a mediator of amyloid beta-induced toxicity.
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Neuroprotective and Neurotoxic Signaling by the Prion Protein
In this review we will summarize current knowledge of neurotoxic PrP conformers and discuss the role of PrP(C) as a mediator of both stress-protective and neurotoxic signaling cascades.
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Responsible for content: Prof. Dr. Jörg Tatzelt