![Dr Charles Harrington Dr Charles Harrington](/img/200x200/staffpages/uploads/men133/avatar/kBqwgKooixTI7MNVVdJc5pUUCNjCSdzdKOJ7rv3M.jpeg)
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
Rescue of synaptosomal glutamate release defects in tau transgenic mice by the tau aggregation inhibitor hydromethylthionine
Cellular Signalling, 111269Contributions to Journals: Articles- [ONLINE] DOI: https://doi.org/10.1016/j.cellsig.2024.111269
Hydromethylthionine 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: 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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The Neurovascular Unit Dysfunction in Alzheimer's Disease
International Journal of Molecular Sciences, vol. 22, no. 4, 2022Contributions to Journals: Review articlesMolecular Processing of Tau Protein in Progressive Supranuclear Palsy: Neuronal and Glial Degeneration
Journal of Alzheimer's Disease, vol. 79, no. 4, pp. 1517-1531Contributions to Journals: ArticlesDifferential compartmental processing and phosphorylation of pathogenic human tau and native mouse tau in the Line 66 model of frontotemporal dementia
Journal of Biological Chemistry, vol. 295, no. 52, pp. 18508-18523Contributions to Journals: ArticlesCurrent Progress and Future Directions for Tau-Based Fluid Biomarker Diagnostics in Alzheimer’s Disease
International Journal of Molecular Sciences, vol. 21, no. 22, pp. 1-19Contributions to Journals: ArticlesTau Filament Self-Assembly and Structure: Tau as a Therapeutic Target.
Frontiers in Neurology, vol. 11, 590754Contributions to Journals: ArticlesPHF-Core Tau as the Potential Initiating Event for Tau Pathology in Alzheimer’s Disease
Frontiers in cellular neuroscience, vol. 14, 247Contributions to Journals: ArticlesPaired helical filament forming region of tau (297-391) influences endogenous tau protein and accumulates in acidic compartments in human neuronal cells
Journal of Molecular Biology, vol. 432, no. 17, pp. 4891-4907Contributions to Journals: Articles- [ONLINE] DOI: https://doi.org/10.1016/j.jmb.2020.05.027
- [OPEN ACCESS] http://aura.abdn.ac.uk/bitstream/2164/14862/1/Pollack_etal_Paired_helical_VOR.pdf
- [ONLINE] View publication in Scopus
National Dementia BioBank: A Strategy for the Diagnosis and Study of Neurodegenerative Diseases in México
Journal of Alzheimer's Disease, vol. 76, no. 3, pp. 853-862Contributions to Journals: Articles- [ONLINE] DOI: https://doi.org/10.3233/JAD-191015
- [ONLINE] View publication in Scopus
Analysis of the Relationship Between Metalloprotease-9 and Tau Protein in Alzheimer's Disease
Journal of Alzheimer's Disease, vol. 76, no. 2, pp. 553-569Contributions to Journals: Articles- [ONLINE] DOI: https://doi.org/10.3233/JAD-200146
- [ONLINE] View publication in Scopus
Concentration-Dependent Activity of Hydromethylthionine on Clinical Decline and Brain Atrophy in a Randomized Controlled Trial in Behavioral Variant Frontotemporal Dementia
Journal of Alzheimer's Disease, vol. 75, no. 2, pp. 501-519Contributions to Journals: ArticlesMechanisms of anticholinesterase interference with tau aggregation inhibitor activity in a tau-transgenic mouse model
Current Alzheimer Research, vol. 17, no. 3, pp. 285-296Contributions to Journals: ArticlesCholinergic and inflammatory phenotypes in transgenic tau mouse models of Alzheimer’s Disease and Frontotemporal Lobar Degeneration
Brain Communications, vol. 2, no. 1, fcaa033Contributions to Journals: ArticlesTau (297-391) forms filaments that structurally mimic the core of paired helical filaments in Alzheimer's disease brain
FEBS LETTERS, vol. 594, no. 5, pp. 944-950Contributions to Journals: Articles- [ONLINE] DOI: https://doi.org/10.1002/1873-3468.13675
- [OPEN ACCESS] http://aura.abdn.ac.uk/bitstream/2164/13414/2/AlHilaly_etal_FEBS_VOR.pdf
- [ONLINE] View publication in Scopus
Concentration-Dependent Activity of Hydromethylthionine on Cognitive Decline and Brain Atrophy in Mild to Moderate Alzheimer’s Disease
Journal of Alzheimer's Disease, vol. 72, no. 3, pp. 931-946Contributions to Journals: ArticlesPhospho-Tau Protein Expression in the Cell Cycle of SH-SY5Y Neuroblastoma Cells: A Morphological Study
Journal of Alzheimer's Disease, vol. 71, no. 2, pp. 631-645Contributions to Journals: ArticlesIncreased Cholinergic Response in α-Synuclein Transgenic Mice (h-α-synL62)
ACS Chemical Neuroscience, vol. 10, no. 4, pp. 1915-1922Contributions to Journals: Articles- [ONLINE] DOI: https://doi.org/10.1021/acschemneuro.8b00274
- [OPEN ACCESS] http://aura.abdn.ac.uk/bitstream/2164/12993/1/ACSChemNsci_Konig.pdf
- [ONLINE] View publication in Mendeley
Cysteine-independent inhibition of Alzheimer's disease-like paired helical filament assembly by leuco-methylthioninium (LMT)
Journal of Molecular Biology, vol. 430, no. 21, pp. 4119-4131Contributions to Journals: ArticlesModeling Prion-Like Processing of Tau Protein in Alzheimer's Disease for Pharmaceutical Development
Journal of Alzheimer's Disease, vol. 62, no. 3, pp. 1287-1303Contributions to Journals: ArticlesAlpha-Synuclein transgenic mice, h-α-SynL62, display α-Syn aggregation and a dopaminergic phenotype reminiscent of Parkinson's disease
Behavioural Brain Research, vol. 339, pp. 153-168Contributions to Journals: ArticlesA Protein Aggregation Inhibitor, Leuco-Methylthioninium Bis(Hydromethanesulfonate), Decreases α-Synuclein Inclusions in a Transgenic Mouse Model of Synucleinopathy
Frontiers in Molecular Neuroscience, vol. 10, 447Contributions to Journals: Articles- [ONLINE] DOI: https://doi.org/10.3389/fnmol.2017.00447
- [OPEN ACCESS] http://aura.abdn.ac.uk/bitstream/2164/9976/1/fnmol_10_00447.pdf
Potential of Low Dose Leuco-Methylthioninium Bis(Hydromethanesulphonate) (LMTM) Monotherapy for Treatment of Mild Alzheimer’s Disease: Cohort Analysis as Modified Primary Outcome in a Phase III Clinical Trial
Journal of Alzheimer's Disease, vol. 61, no. 1, pp. 435-457Contributions to Journals: Articles- [ONLINE] https://www.j-alz.com/vol61-1
- [ONLINE] DOI: https://doi.org/10.3233/JAD-170560
- [OPEN ACCESS] http://aura.abdn.ac.uk/bitstream/2164/9693/1/Potential_of_Low_Dose.pdf
Alzheimer's Disease-like Paired Helical Filament Assembly from Truncated Tau Protein Is Independent of Disulfide Crosslinking
Journal of Molecular Biology, vol. 429, no. 23, pp. 3650-3665Contributions to Journals: ArticlesLMTM DECREASES α-SYNUCLEIN PATHOLOGY AND REDUCES BEHAVIOURAL DEFECTS IN α-SYNUCLEIN TRANSGENIC MICE
Alzheimer's and Dementia, vol. 13, no. 7 Suppl., pp. P945-P945Contributions to Journals: Abstracts- [ONLINE] DOI: https://doi.org/10.1016/j.jalz.2017.06.1854
Monoaminergic Neuropathology in Alzheimer's disease
Progress in Neurobiology, vol. 151, pp. 101-138Contributions to Journals: Articles- [ONLINE] DOI: https://doi.org/10.1016/j.pneurobio.2016.04.001
- [OPEN ACCESS] http://aura.abdn.ac.uk/bitstream/2164/8480/1/ProgN_Simic.pdf
Assays for the Screening and Characterization of Tau Aggregation Inhibitors
Tau Protein: Methods and Protocols. Smet-Nocca, C. (ed.). Springer, pp. 129-140, 12 pagesChapters in Books, Reports and Conference Proceedings: Chapters- [ONLINE] DOI: https://doi.org/10.1007/978-1-4939-6598-4_8