Publications

Professor Claude M. Wischik, co-founder and Executive Chairman of TauRx Therapeutics, along with colleagues at the University of Aberdeen, has devoted nearly 30 years to investigating the structure and role of tau tangles in the development of Alzheimer’s, frontotemporal dementia and other neurodegenerative diseases. He is the scientist who discovered that the neurofibrillary tangles seen in Alzheimer’s disease are made of sub-units of the tau protein and he and his team have published extensively in the field.

Arastoo, M, et al, (2020) Current Progress and Future Directions for Tau-Based Fluid Biomarker Diagnostics. Available at: International Journal of Molecular Sciences

Oakley, S.S., et al. (2020) Tau Filament Self-Assembly and Structure: Tau as a Therapeutic Target. Available at: Frontiers in Neurology

Reidel, G, et al. (2020) Mechanisms of Anticholinesterase Interference with Tau Aggregation Inhibitor Activity in a Tau-Transgenic Mouse Model.

Available at: Current Alzheimer Research

Shiells, H, et al. (2020) Concentration-Dependent Activity of Hydromethylthionine on Clinical Decline and Brain Atrophy in a Randomized Controlled Trial in Behavioral Variant Frontotemporal Dementia. Available at: Journal of Alzheimer's Disease

Al-Hilaly, Y.K. et al. (2019) Tau (297-391) forms filaments that structurally mimic the core of paired helical filaments in Alzheimer's disease brain. Available at FEBS Letters

Schelter, B, et al. (2019) Concentration-Dependent Activity of Hydromethylthionine on Cognitive Decline and Brain Atrophy in Mild to Moderate Alzheimer’s Disease. Available at: Journal of Alzheimer's Disease

Al-Hilaly, Y.K. et al. (2018) Cysteine-independent inhibition of Alzheimer’s disease-like paired helical filament assembly by leuco-methylthioninium (LMT) J. Molec. Biol., Available at: Journal of Molecular Biology

Schwab, K, et al. (2018) A Protein Aggregation Inhibitor, Leuco-Methylthioninium Bis(Hydromethanesulfonate), Decreases α-Synuclein Inclusions in a Transgenic Mouse Model of Synucleinopathy. Available at: Frontiers in Molecular Neuroscience

Wischik, C.M. et al. (2018) Modeling prion-like processing of tau protein in Alzheimer’s disease for pharmaceutical development. J. Alzheimer's Dis.62:1287-1303. Available at: Journal of Alzheimer's Disease

Al-Hilaly, Y.K., et al. (2017) Alzheimer's disease-like paired helical filament assembly from truncated tau protein is independent of disulphide cross-linking. Available at: Journal of Molecular Biology

Wilcock, G.K., et al. (2017) 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. Available at: Journal of Alzheimer's Disease

Gauthier, S, et al. (2016) Efficacy and safety of tau-aggregation inhibitor therapy in patients with mild or moderate Alzheimer’s disease: a randomized, controlled, double-blind, parallel-arm, phase 3 trial. Available at: The Lancet

Lai, R.Y.K., et al. (2016) Absence of a Role for Phosphorylation in the Tau Pathology of Alzheimer’s Disease. Available at: Biomolecules

Šimic, G, et al. (2016) Tau protein hyperphosphorylation and aggregation in Alzheimer's disease and other tauopathies, and possible neuroprotective strategies. Available at: Biomolecules

Vuksanovic V, Staff RT, Ahearn T, et al. (2016) Frontotemporal atrophy and clinical estimates of disease severity in behavioural variant frontotemporal dementia: The role of cognitive reserve. Presented at the Alzheimer’s Research UK Conference, Manchester, UK.

Baddeley, T.C., et al. (2015) Complex disposition of methylthioninium redox forms determines efficacy in tau aggregation inhibitor therapy for Alzheimer’s disease. Available at: The Journal of Pharmacology and Experimental Therapeutics

Flores-Rodríguez, P, et al. (2015) The relationship between truncation and phosphorylation at the C-terminus of tau protein in the paired helical filaments of Alzheimer’s disease. Available at: Frontiers in Neuroscience

Harrington, C.R., et al. (2015) Cellular models of aggregation-dependent template-directed proteolysis to characterize tau aggregation inhibitors for treatment of Alzheimer disease. Available at: The Journal of Biological Chemistry

Melis, V, et al. (2015) Effects of oxidized and reduced forms of methylthioninium in two transgenic mouse tauopathy models. Available at: Behavioural Pharmacology

Melis, V, et al. (2015) Different pathways of molecular pathophysiology underlie cognitive and motor tauopathy phenotypes in transgenic models for Alzheimer’s disease and frontotemporal lobar degeneration. Available at: Cellular and Molecular Life Sciences

Wischik, C.M. et al. (2015) Tau Aggregation Inhibitor Therapy: An Exploratory Phase 2 Study in Mild or Moderate Alzheimer’s Disease. Available at: Journal of Alzheimer’s Disease