BSc (Hons) (Glasgow, 1977); PhD (Glasgow, 1980)
Senior Research Fellow
- About
-
- Email Address
- c.harrington@abdn.ac.uk
- Telephone Number
- +44 (0)1224 438563
- Office Address
Liberty Building, Institute of Medical Sciences, Foresterhill Road, Aberdeen AB25 2ZP United Kingdom
- School/Department
- School of Medicine, Medical Sciences and Nutrition
Biography
Charlie Harrington graduated in Microbiology from Glasgow University where he developed an interest in chemical microbiology and the study of microbial cell walls. He completed his PhD working with Dr Julia Douglas on cell wall synthesis in yeast and followed with a one-year NIH-funded Fellowship with Dr Wilf Arnold in Kansas City, Missouri studying enzymes within the yeast cell envelope. After this, Charlie joined Professor Sir James Baddiley in the Department of Biochemistry at the University of Cambridge as a Research Fellow, where he spent four years investigating the synthesis of bacterial cell wall polymers. Dr Harrington then spent over two years at Murex Medical Research Ltd., Cambridge, developing diagnostic tests for microbial diseases, including methicillin-resistant Staphylococcus aureus and sexually transmitted diseases. This combined monoclonal antibody technology with his knowledge of the microbial cell surface.
In 1988, he joined Claude Wischik working at the Medical Research Council’s Laboratory of Molecular Biology. Working in the Cambridge Brain Bank Laboratory over a period of 10 years. During this time, Wischik, Harrington and colleagues developed an assay for screening agents having the potential to prevent the tau pathology that is the hallmark of Alzheimer’s disease. Charlie moved with Professor Wischik, in 1998, to the University of Aberdeen, where he was appointed as a Senior Research Fellow.
The Alzheimer's research was translated to the clinic, through a spin-out company, TauRx Therapeutics, who are conducting phase 3 trials of hydromethylthionine. Dr Harrington is Chief Scientific Officer for TauRx Therapeutics Ltd responsible for the non-clinical activities of the company.
Qualifications
- BSc (Hons) Microbiology1977 - University of Glasgow
- PhD Microbiology1980 - University of Glasgow
Latest Publications
Rivastigmine interferes with the pharmacological activity of hydromethylthionine on presynaptic proteins in the line 66 model of frontotemporal dementia
Brain Research Bulletin, 111172Contributions to Journals: Articles- [ONLINE] DOI: https://doi.org/10.1016/j.brainresbull.2024.111172
High-affinity antibodies specific to the core region of the tau protein exhibit diagnostic and therapeutic potential for Alzheimer’s disease
Alzheimer's Research & Therapy, vol. 16, 209Contributions to Journals: ArticlesRescue of synaptosomal glutamate release defects in tau transgenic mice by the tau aggregation inhibitor hydromethylthionine
Cellular Signalling, vol. 121, 111269Contributions to Journals: ArticlesHydromethylthionine rescues synaptic SNARE proteins in a mouse model of tauopathies: interference by cholinesterase inhibitors
Brain Research Bulletin, vol. 212, 110955Contributions to Journals: ArticlesConsiderations for biomarker strategies in clinical trials investigating tau-targeting therapeutics for Alzheimer's disease
Translational neurodegeneration, vol. 13, 25Contributions to Journals: Review articles- [ONLINE] DOI: https://doi.org/10.1186/s40035-024-00417-w
- [OPEN ACCESS] http://aura.abdn.ac.uk/bitstream/2164/23668/1/s40035-024-00417-w.pdf
- Research
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Research Overview
Dr Harrington has research interests in the neurodegenerative diseases and, in particular, Alzheimer’s disease. His main focus has been on the biology of tau protein in aging and in Alzheimer’s disease. Dr Harrington’s research is aimed at diseases that are characterised by protein aggregation and methods by which these processes might be prevented.
- Publications
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Page 1 of 10 Results 1 to 10 of 100
Rivastigmine interferes with the pharmacological activity of hydromethylthionine on presynaptic proteins in the line 66 model of frontotemporal dementia
Brain Research Bulletin, 111172Contributions to Journals: Articles- [ONLINE] DOI: https://doi.org/10.1016/j.brainresbull.2024.111172
High-affinity antibodies specific to the core region of the tau protein exhibit diagnostic and therapeutic potential for Alzheimer’s disease
Alzheimer's Research & Therapy, vol. 16, 209Contributions to Journals: ArticlesRescue of synaptosomal glutamate release defects in tau transgenic mice by the tau aggregation inhibitor hydromethylthionine
Cellular Signalling, vol. 121, 111269Contributions to Journals: ArticlesHydromethylthionine rescues synaptic SNARE proteins in a mouse model of tauopathies: interference by cholinesterase inhibitors
Brain Research Bulletin, vol. 212, 110955Contributions to Journals: ArticlesConsiderations for biomarker strategies in clinical trials investigating tau-targeting therapeutics for Alzheimer's disease
Translational neurodegeneration, vol. 13, 25Contributions to Journals: Review articles- [ONLINE] DOI: https://doi.org/10.1186/s40035-024-00417-w
- [OPEN ACCESS] http://aura.abdn.ac.uk/bitstream/2164/23668/1/s40035-024-00417-w.pdf
LETC inhibits α-Syn aggregation and ameliorates motor deficiencies in the L62 mouse model of synucleinopathy
European Journal of Pharmacology, vol. 970, 176505Contributions to Journals: ArticlesNeuroprotection of Cholinergic Neurons with a Tau Aggregation Inhibitor and Rivastigmine in an Alzheimer's-like Tauopathy Mouse Model
Cells, vol. 13, no. 7, 642Contributions to Journals: ArticlesAssays for the Screening and Characterization of Tau Aggregation Inhibitors
Tau Protein: Methods and Protocols. 2 edition, pp. 93-104, 12 pagesChapters in Books, Reports and Conference Proceedings: Chapters (Peer-Reviewed)- [ONLINE] DOI: https://doi.org/10.1007/978-1-0716-3629-9_5
Solubility of α-synuclein species in the L62 mouse model of synucleinopathy
Scientific Reports, vol. 14, 6239Contributions to Journals: ArticlesApathy-like behaviour in tau mouse models of Alzheimer’s disease and frontotemporal dementia
Behavioural Brain Research, vol. 456, 114707Contributions to Journals: Articles