Dr Charles Harrington
BSc (Hons) (Glasgow, 1977); PhD (Glasgow, 1980)
Senior Research Fellow
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.
- BSc (Hons) Microbiology1977 - University of Glasgow
- PhD Microbiology1980 - University of Glasgow
Proteomic analysis of hydromethylthionine in the line 66 model of frontotemporal dementia demonstrates actions on tau-dependent and tau-independent networksCells, vol. 10, no. 8, 2162Contributions to Journals: Articles
Degeneration of basal and limbic networks is a core feature of behavioural variant frontotemporal dementiaBrain CommunicationsContributions to Journals: Articles
Tau Protein Phosphorylated at Threonine-231 Is Expressed Abundantly in the Cerebellum in Prion EncephalopathiesJournal of Alzheimer's Disease, vol. 81, no. 2, pp. 769-785Contributions to Journals: Articles
Elucidating the neuropathologic mechanisms of SARS-CoV-2 infectionFrontiers in Neurology, vol. 12, 660087Contributions to Journals: Articles
Insoluble Vascular Amyloid Deposits Trigger Disruption of the Neurovascular Unit in Alzheimer’s Disease BrainsInternational Journal of Molecular Sciences, vol. 22, no. 7, 3654Contributions to Journals: Articles
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.
Page 3 of 8 Results 21 to 30 of 78
Phospho-Tau Protein Expression in the Cell Cycle of SH-SY5Y Neuroblastoma Cells: A Morphological StudyJournal of Alzheimer's Disease, vol. 71, no. 2, pp. 631-645Contributions to Journals: Articles
Increased Cholinergic Response in α-Synuclein Transgenic Mice (h-α-synL62)ACS Chemical Neuroscience, vol. 10, no. 4, pp. 1915-1922Contributions to Journals: Articles
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: Articles
Modeling Prion-Like Processing of Tau Protein in Alzheimer's Disease for Pharmaceutical DevelopmentJournal of Alzheimer's Disease, vol. 62, no. 3, pp. 1287-1303Contributions to Journals: Articles
Alpha-Synuclein transgenic mice, h-α-SynL62, display α-Syn aggregation and a dopaminergic phenotype reminiscent of Parkinson's diseaseBehavioural Brain Research, vol. 339, pp. 153-168Contributions to Journals: Articles
A Protein Aggregation Inhibitor, Leuco-Methylthioninium Bis(Hydromethanesulfonate), Decreases α-Synuclein Inclusions in a Transgenic Mouse Model of SynucleinopathyFrontiers in Molecular Neuroscience, vol. 10, 447Contributions to Journals: Articles
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 TrialJournal of Alzheimer's Disease, vol. 61, no. 1, pp. 435-457Contributions to Journals: Articles
Alzheimer's Disease-like Paired Helical Filament Assembly from Truncated Tau Protein Is Independent of Disulfide CrosslinkingJournal of Molecular Biology, vol. 429, no. 23, pp. 3650-3665Contributions to Journals: Articles
LMTM DECREASES α-SYNUCLEIN PATHOLOGY AND REDUCES BEHAVIOURAL DEFECTS IN α-SYNUCLEIN TRANSGENIC MICEAlzheimer's and Dementia, vol. 13, no. 7 Suppl., pp. P945-P945Contributions to Journals: Abstracts
Monoaminergic Neuropathology in Alzheimer's diseaseProgress in Neurobiology, vol. 151, pp. 101-138Contributions to Journals: Articles