Mudher, Amritpal - University of Southampton - Discipline of Biological Sciences

个人简介

Career history Associate Professor in Neuroscience. University of Southampton, UK. Senior Lecturer in Neurosciences. University of Southampton, UK. Lecturer in Neurosciences. University of Southampton, UK. Alzheimer Society Research Fellow (Modelling Tauopathies in Drosophila). Institute of Psychiatry, University of London, UK. Post Doctoral Research Worker (Wnt signalling and Alzheimer's Disease). Institute of Psychiatry, University of London, UK. Academic qualifications BSc (Biomedical Sciences). King's College, University of London, UK. DPhil (Neuroscience). Merton College, University of Oxford, UK.

研究领域

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The overarching aim our research is to investigate the mechanisms that underpin tau-mediated dysfunction and degeneration in tauopathies such as Alzheimer’s disease and fronto-temporal dementia (see Mudher et al 2004, Mol Psychiatry, Chee et al 2005 for early investigations). This work led us to identify disease-modifying tau-centred therapeutic targets (See Quriase et al 2013 Mol. Psychiatry). It has also raised interesting questions about the pathological significance of estasblished tau aggregates such as soluble forms of tau, tau oligomers and tau filaments. More recently we are assessing whether tau-mediated axonal degeneration is wallerian in nature. A related project investigates the cross talk between tau and other disease-associated proteins such as Abeta peptide and alpha-synuclein. Using transgenic models in which tau is co-expressed with these proteins, we investigate the effect of co-expression on established tau phenotypes and then assess the molecular mechanism(s) underpinning this. Another branch of research focuses on understanding how cellular processes such as TOR signalling, autophagic/proteosomal clearance, oxidative stress and others change with age. In parallel we seek to investigate how these changes contribute to development of Alzhiemer’s disease by studying their interaction with both tau and amyloid pathologies and phenotypes. We are also interested in using label-free Raman spectroscopic techniques to identify aggregated tau and amyloid proteins. By generating unique spectral signatures for various disease associated forms of these proteins, we hope to use this technology to probe biological fluids for biomarkers of early disease.