Neurodegenerative Disorders
Tauopathies
How does tau become toxic and drive tauopathies like Alzheimer’s disease?
How can we stop it?
The microtubule associated protein tau (MAPT) is misfolded, hyperphosphorylated and aggregated in tauopathies. Yet, how these properties arise and interact to convert tau into a toxic form that drives neurotoxicity/neuropathology remains elusive. We are developing models to examine interactions between tau coding variants, genetic modifiers such as ApoE4 and Aβ, misfolding, hyperphosphorylation and aggregation. We aim to identify which of these represent optimal targets for therapeutic targeting to prevent tauopathy. With our collaborators, we are developing novel methods in Drosophila to efficiently test the contribution and interactions between contributors to tau protein conversion into a toxic species. We are also developing drug screening approaches to identify those that prevent tau toxic conversion and/or the damage that it does.Collaborators
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Amrit Mudher, D.Phil.
We use Drosophila to study the mechanisms that underpin tau-mediated dysfunction and degeneration in tauopathies such as Alzheimer’s disease and fronto-temporal dementia
School of Biological Sciences
Faculty of Environmental and Life Sciences
Life Sciences Building 85
University of Southampton
Highfield Campus
Southampton
SO17 1BJ
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Efthimios Skoulakis, Ph.D.
We use Drosophila to study processes essential for learning and memory and model the action of genes implicated in human neuronal dysfunctions such as Tauopathies, Fragile X syndrome, Neurofibromatosis 1, Noonan syndrome-like and attention deficit disorder (ADD)
Institute for Fundamental Biomedical Research
Biomedical Sciences Research Centre
"Alexander Fleming”
34 Fleming str
Vari 16672 Greece