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
Inhibiting disulphide bonding in truncated tau297-391 results in enhanced self-assembly of tau into seed-competent assemblies
ACS Chemical NeuroscienceContributions to Journals: ArticlesBlood Biomarkers from Research Use to Clinical Practice: What Must Be Done? A Report from the EU/US CTAD Task Force
Journal of Prevention of Alzheimer's Disease, vol. 9, no. 4, pp. 569-579Contributions to Journals: ArticlesSystematic gait analysis in alpha-synuclein transgenic line 62 mice using the CatWalk
Behavioural Brain Research, vol. 496, 115819Contributions to Journals: ArticlesA key region of Tau that is able to drive assembly and modulate inhibition by Hydromethylthionine
Journal of Molecular Biology, vol. 437, no. 17, 169231Contributions to Journals: Articles- [ONLINE] DOI: https://doi.org/10.1016/j.jmb.2025.169231
- [OPEN ACCESS] http://aura.abdn.ac.uk/bitstreams/7a09658e-98e2-46e0-b61c-ea4a48f823ab/download
- [ONLINE] View publication in Scopus
Proteomic and non-proteomic changes of presynaptic proteins in animal models of Alzheimer’s disease: A meta-analysis 2015-2023
Journal of Alzheimer's Disease, vol. 107, no. 2, pp. 452-476Contributions to Journals: Articles
- 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 7 of 11 Results 61 to 70 of 107
Inhibition of Tau Aggregation as a Basis for Treatment and Prevention of Alzheimer's Disease
Developing Therapeutics for Alzheimer's Disease: Progress and Challenges. Wolfe, M. S. (ed.). Elsevier Inc., pp. 385-436, 52 pagesChapters in Books, Reports and Conference Proceedings: Chapters- [ONLINE] DOI: https://doi.org/10.1016/B978-0-12-802173-6.00015-0
- [ONLINE] View publication in Scopus
Absence of a Role for Phosphorylation in the Tau Pathology of Alzheimer's Disease
Biomolecules, vol. 6, no. 2, pp. 1-19Contributions to Journals: ArticlesTau Protein Hyperphosphorylation and Aggregation in Alzheimer’s Disease and Other Tauopathies, and Possible Neuroprotective Strategies
Biomolecules, vol. 6, no. 1, 6Contributions to Journals: Review articles- [ONLINE] DOI: https://doi.org/10.3390/biom6010006
- [OPEN ACCESS] http://aura.abdn.ac.uk/bitstreams/033fbdcb-c092-4ef5-b49d-2928ba7ed3db/download
- [ONLINE] View publication in Scopus
Different pathways of molecular pathophysiology underlie cognitive and motor tauopathy phenotypes in transgenic models for Alzheimer’s disease and frontotemporal lobar degeneration
Cellular and Molecular Life Sciences, vol. 72, no. 11, pp. 2199-2222Contributions to Journals: ArticlesEffects of oxidized and reduced forms of methylthioninium in two transgenic mouse tauopathy models
Behavioural Pharmacology, vol. 26, no. 4, pp. 353-368Contributions to Journals: ArticlesCellular Models of Aggregation-Dependent Template-Directed Proteolysis to Characterize Tau Aggregation Inhibitors for Treatment of Alzheimer's Disease
The Journal of Biological Chemistry, vol. 290, no. 17, pp. 10862-10875Contributions to Journals: ArticlesThe relationship between truncation and phosphorylation at the C-terminus of tau protein in the paired helical filaments of Alzheimer's disease
Frontiers in Neuroscience, vol. 9, 33Contributions to Journals: ArticlesTau Aggregation Inhibitor Therapy: An Exploratory Phase 2 Study in Mild or Moderate Alzheimer's Disease
Journal of Alzheimer's Disease, vol. 44, no. 2, pp. 705-720Contributions to Journals: ArticlesComplex Disposition of Methylthioninium Redox Forms Determines Efficacy in Tau Aggregation Inhibitor Therapy for Alzheimer's Disease
Journal of Pharmacology and Experimental Therapeutics, vol. 352, no. 1, pp. 110-118Contributions to Journals: Articles- [ONLINE] DOI: https://doi.org/10.1124/jpet.114.219352
Tau-aggregation inhibitor therapy for Alzheimer's disease
Biochemical Pharmacology, vol. 88, no. 4, pp. 529-539Contributions to Journals: Articles