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Freie Universität Berlin Charité University Medicine Berlin Humboldt University Berlin Max-Delbrück-Center for Molecular Medicine, Berlin-Buch |
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Freie Universität Berlin Charité University Medicine Berlin Humboldt University Berlin Max-Delbrück-Center for Molecular Medicine, Berlin-Buch |
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GRK 1123: |
Cellular Mechanisms of Learning and Memory Consolidation |
This Research Training Group is funded by the German Research Council DFG
| Christian Barucker Address: Freie Universitaet Berlin Institute of Chemisty and Biochemistry Thielallee 63 D-14195 Berlin Tel +49 (30) 83852906 Fax +49 (30) 83856509 |
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| PhD-Project "Toxicity of the amyloid Aß peptide: a possible role in the nucleus" Synopsis The amyloid precursor protein (APP) is central to the pathogenesis of Alzheimer’s disease (AD). APP is cleaved by the ß-site-APP-cleaving enzyme (BACE) and the gamma-secretase complex to generate Aß peptides. The pathogenic effects observed in AD are ascribed to soluble low-n oligomers of Aß42. Recently, it was shown that toxicity of Aß is not a simple cause of Aß oligomerization but a consequence of the adoption of a specific conformation determined by the GxxxG interaction motif. This motif is contained within the hydrophobic C-terminus of the Aß peptide and places two glycines on the same face of a ß-sheet. The topic of my project is to characterize a possible role for Aß in gene regulation, which we could specifically assign to Aß42 meanwhile. This function of Aß42 is further analyzed to clarify if it is a normal or a gain-of-function of Aß.
Freie Universität Berlin (supervisor: Gerd Multhaup)
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