Professor Claude Wischik

High-affinity antibodies specific to the core region of the tau protein exhibit diagnostic and therapeutic potential for Alzheimer’s disease

• [ONLINE] DOI: https://doi.org/10.1186/s13195-024-01561-1
• [OPEN ACCESS] http://aura.abdn.ac.uk/bitstream/2164/24444/1/Arastoo_etal_ART_High-affinity_antibodies_specific_VOR.pdf
• [ONLINE] View publication in Scopus

Rescue of synaptosomal glutamate release defects in tau transgenic mice by the tau aggregation inhibitor hydromethylthionine

• [ONLINE] DOI: https://doi.org/10.1016/j.cellsig.2024.111269
• [OPEN ACCESS] http://aura.abdn.ac.uk/bitstream/2164/24087/1/Cranston_etal_CS_Rescue_of_synaptosomal_VoR.pdf

Hydromethylthionine rescues synaptic SNARE proteins in a mouse model of tauopathies: interference by cholinesterase inhibitors

• [ONLINE] https://www.sciencedirect.com/science/article/pii/S0361923024000881
• [ONLINE] DOI: https://doi.org/10.1016/j.brainresbull.2024.110955
• [OPEN ACCESS] http://aura.abdn.ac.uk/bitstream/2164/23339/2/Schwab_etal_BRB_Hydromethylthionine_rescues_synaptic_VOR.pdf

Considerations for biomarker strategies in clinical trials investigating tau-targeting therapeutics for Alzheimer's disease

• [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

• [ONLINE] DOI: https://doi.org/10.1016/j.ejphar.2024.176505
• [OPEN ACCESS] http://aura.abdn.ac.uk/bitstream/2164/23810/1/Schwab_etal_EJP_LETC_inhibits_-Syn_VOR.pdf

Neuroprotection of Cholinergic Neurons with a Tau Aggregation Inhibitor and Rivastigmine in an Alzheimer's-like Tauopathy Mouse Model

• [ONLINE] DOI: https://doi.org/10.3390/cells13070642
• [OPEN ACCESS] http://aura.abdn.ac.uk/bitstream/2164/23504/1/Zadrozny_etal_C_Neuroprotection_of_Cholinergic_VOR.pdf

Assays for the Screening and Characterization of Tau Aggregation Inhibitors

• [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

• [ONLINE] DOI: https://doi.org/10.1038/s41598-024-56735-6
• [OPEN ACCESS] http://aura.abdn.ac.uk/bitstream/2164/23245/1/Schwab_etal_SR_Solubility_of_Synuclein_VOR.pdf

Apathy-like behaviour in tau mouse models of Alzheimer’s disease and frontotemporal dementia

• [ONLINE] https://www.sciencedirect.com/science/article/pii/S0166432823004254
• [ONLINE] DOI: https://doi.org/10.1016/j.bbr.2023.114707
• [OPEN ACCESS] http://aura.abdn.ac.uk/bitstream/2164/21953/1/Robinson_etal_BBR_Apathy-like_behaviour_in_VOR.pdf

A Meta-Analysis on Presynaptic Changes in Alzheimer's Disease

• [ONLINE] DOI: https://doi.org/10.3233/JAD-231034
• [OPEN ACCESS] http://aura.abdn.ac.uk/bitstream/2164/22521/1/Anschuetz_etal_JAD_A_Meta-Analysis_on_Presynaptic_VOR.pdf

Significant dose-dependent reduction in neurofilament light chain concentration in plasma with oral tau aggregation inhibitor hydromethylthionine mesylate

• [ONLINE] DOI: https://doi.org/10.1002/alz.083153

Exploring the Anti-Hypoxaemia Effect of Hydromethylthionine: A Prospective Study of Phase 3 Clinical Trial Participants

• [ONLINE] DOI: https://doi.org/10.3390/ijms241813747
• [OPEN ACCESS] http://aura.abdn.ac.uk/bitstream/2164/22092/1/Arastoo_etal_IJMS_Exploring_the_Anti-Hypoxaemia_VOR.pdf
• [ONLINE] View publication in Scopus

Mitochondrial Effects of Hydromethylthionine, Rivastigmine and Memantine in Tau-Transgenic Mice

• [ONLINE] DOI: https://doi.org/10.3390/ijms241310810
• [OPEN ACCESS] http://aura.abdn.ac.uk/bitstream/2164/21353/1/Kondak_etal_IJMS_Mitochondrial_Effects_of_VOR.pdf

Utility of Blood-Based Tau Biomarkers for Mild Cognitive Impairment and Alzheimer’s Disease: Systematic Review and Meta-Analysis

• [ONLINE] DOI: https://doi.org/10.3390/cells12081184
• [OPEN ACCESS] http://aura.abdn.ac.uk/bitstream/2164/20726/1/Zabala_Findlay_etal_cells_Utility_Blood_Based_VOR.pdf
• [ONLINE] View publication in Scopus

An Additive-Free Model for Tau Self-Assembly

• [ONLINE] DOI: https://doi.org/10.1007/978-1-0716-2597-2_12
• [ONLINE] View publication in Scopus

Solid-state NMR of paired helical filaments formed by the core tau fragment tau(297-391)

• [ONLINE] DOI: https://doi.org/10.3389/fnins.2022.988074
• [OPEN ACCESS] http://aura.abdn.ac.uk/bitstream/2164/20524/1/Al_Hilaly_FN_Solid_State_NMR_Of_VoR.pdf
• [ONLINE] View publication in Scopus

Dityrosine Cross-links are Present in Alzheimer's Disease-derived Tau Oligomers and Paired Helical Filaments (PHF) which Promotes the Stability of the PHF-core Tau (297–391) In Vitro

• [ONLINE] DOI: https://doi.org/10.1016/j.jmb.2022.167785
• [OPEN ACCESS] http://aura.abdn.ac.uk/bitstream/2164/19515/1/Maina_et_al_Dityrosine_cross_links_JMB_vor.pdf
• [ONLINE] View publication in Scopus

Oral Tau Aggregation Inhibitor for Alzheimer’s Disease: Design, Progress and Basis for Selection of the 16 mg/day Dose in a Phase 3, Randomized, Placebo-Controlled Trial of Hydromethylthionine Mesylate

• [ONLINE] DOI: https://doi.org/10.14283/jpad.2022.63
• [OPEN ACCESS] http://aura.abdn.ac.uk/bitstream/2164/19291/1/Wischik_et_al_Oral_Tau_Journal_of_Prevention_of_Alzheimers_Disease_vor.pdf
• [ONLINE] View publication in Scopus

Glutamatergic transmission and receptor expression in the synucleinopathy h-α-synL62 mouse model: Effects of hydromethylthionine

• [ONLINE] https://www.sciencedirect.com/science/article/pii/S0898656822001486
• [ONLINE] DOI: https://doi.org/10.1016/j.cellsig.2022.110386
• [OPEN ACCESS] http://aura.abdn.ac.uk/bitstream/2164/18722/1/Schwab_etal_CS_Glutamatergic_transmission_and_VOR.pdf

Structural Identification of Individual Helical Amyloid Filaments by Integration of Cryo-Electron Microscopy-Derived Maps in Comparative Morphometric Atomic Force Microscopy Image Analysis

• [ONLINE] DOI: https://doi.org/10.1016/j.jmb.2022.167466
• [OPEN ACCESS] http://aura.abdn.ac.uk/bitstream/2164/18328/1/Lutter_et_al_Structural_Identification_jmb_vor.pdf
• [ONLINE] View publication in Scopus

HMTM-Mediated Enhancement of Brain Bioenergetics in a Mouse Tauopathy Model Is Blocked by Chronic Administration of Rivastigmine

• [ONLINE] DOI: https://doi.org/10.3390/biomedicines10040867
• [OPEN ACCESS] http://aura.abdn.ac.uk/bitstream/2164/18559/1/Santos_et_al_HMTM_Mediated_Biomedicines_vor.pdf
• [ONLINE] View publication in Scopus

Crossed cerebellar diaschisis in Alzheimer's disease

• [ONLINE] DOI: https://doi.org/10.1097/MNM.0000000000001531
• [ONLINE] View publication in Scopus

Hydromethylthionine enhancement of central cholinergic signalling is blocked by rivastigmine and memantine

• [ONLINE] DOI: https://doi.org/10.1111/jnc.15553
• [OPEN ACCESS] http://aura.abdn.ac.uk/bitstream/2164/18249/2/Kondak_etal_JN_Hydromethylthionine_Enhancement_Of_AAM.pdf
• [OPEN ACCESS] http://aura.abdn.ac.uk/bitstream/2164/18249/1/Kondak_etal_JNC_Hydromethylthionine_Enhancement_Central_VoR.pdf

Degeneration of basal and limbic networks is a core feature of behavioural variant frontotemporal dementia

• [ONLINE] DOI: https://doi.org/10.1093/braincomms/fcab241
• [OPEN ACCESS] http://aura.abdn.ac.uk/bitstream/2164/17967/1/Vucksanovic_etal_BC_Degeneration_of_basal_VOR.pdf

Long-term hydromethylthionine treatment is associated with delayed clinical onset and slowing of cerebral atrophy in a pre-symptomatic P301S MAPT mutation carrier

• [ONLINE] DOI: https://doi.org/10.3233/JAD-210390
• [OPEN ACCESS] http://aura.abdn.ac.uk/bitstream/2164/17505/1/Bentham_et_al_Long_term_Journal_of_alzheimers_disease_vor.pdf
• [ONLINE] View publication in Scopus

Proteomic analysis of hydromethylthionine in the line 66 model of frontotemporal dementia demonstrates actions on tau-dependent and tau-independent networks

• [ONLINE] DOI: https://doi.org/10.3390/cells10082162
• [OPEN ACCESS] http://aura.abdn.ac.uk/bitstream/2164/17282/1/Schwab_cells_Proteomic_analysis_of_vor.pdf
• [ONLINE] View publication in Scopus

Oxidative Stress Conditions Result in Trapping of PHF-Core Tau (297–391) Intermediates

• [ONLINE] DOI: https://doi.org/10.3390/cells10030703
• [OPEN ACCESS] http://aura.abdn.ac.uk/bitstream/2164/16165/1/Maina_etal_CELLS_Oxidative_Stress_Conditions_VoR.pdf

Differential compartmental processing and phosphorylation of pathogenic human tau and native mouse tau in the Line 66 model of frontotemporal dementia

• [ONLINE] http://www.jbc.org/content/early/2020/10/30/jbc.RA120.014890.abstract
• [ONLINE] DOI: https://doi.org/10.1074/jbc.RA120.014890
• [OPEN ACCESS] http://aura.abdn.ac.uk/bitstream/2164/15308/2/Lemke_etal_Differential_compartmental_VOR.pdf
• [ONLINE] View publication in Scopus

Adaptive neurological testing method

Current Progress and Future Directions for Tau-Based Fluid Biomarker Diagnostics in Alzheimer’s Disease

• [ONLINE] DOI: https://doi.org/10.3390/ijms21228673
• [OPEN ACCESS] http://aura.abdn.ac.uk/bitstream/2164/15385/1/Arastoo_et_al_IJMS_CurrentProgressAndFuture_VoR.pdf
• [ONLINE] View publication in Scopus

Tau Filament Self-Assembly and Structure: Tau as a Therapeutic Target.

• [ONLINE] DOI: https://doi.org/10.3389/fneur.2020.590754
• [OPEN ACCESS] http://aura.abdn.ac.uk/bitstream/2164/15357/1/Oakley_et_al_Fneur_TauFilamentSelf_Assembly_VoR.pdf
• [ONLINE] View publication in Scopus

Paired helical filament forming region of tau (297-391) influences endogenous tau protein and accumulates in acidic compartments in human neuronal cells

• [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

Analysis of the Relationship Between Metalloprotease-9 and Tau Protein in Alzheimer's Disease

• [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

• [ONLINE] DOI: https://doi.org/10.3233/JAD-191173
• [OPEN ACCESS] http://aura.abdn.ac.uk/bitstream/2164/14427/2/Shiells_et_al_JAD_ConcentrationDependentActivity_VoR.pdf
• [ONLINE] View publication in Scopus

Mechanisms of anticholinesterase interference with tau aggregation inhibitor activity in a tau-transgenic mouse model

• [ONLINE] DOI: https://doi.org/10.2174/1567205017666200224120926
• [OPEN ACCESS] http://aura.abdn.ac.uk/bitstream/2164/15752/1/Riedel_et_al_CAR_MechanismsOfAnticholinesterase_AAM.pdf
• [ONLINE] View publication in Scopus

Cholinergic and inflammatory phenotypes in transgenic tau mouse models of Alzheimer’s Disease and Frontotemporal Lobar Degeneration

• [ONLINE] DOI: https://doi.org/10.1093/braincomms/fcaa033
• [OPEN ACCESS] http://aura.abdn.ac.uk/bitstream/2164/14871/1/Cranston_etal_BC_Cholinergenic_VOR.pdf

Tau (297-391) forms filaments that structurally mimic the core of paired helical filaments in Alzheimer's disease brain

• [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

• [ONLINE] DOI: https://doi.org/10.3233/JAD-190772
• [OPEN ACCESS] http://aura.abdn.ac.uk/bitstream/2164/13339/1/Schelter_et_al_JoAD_ConcentrationDependentActivity_VoR.pdf

Phospho-Tau Protein Expression in the Cell Cycle of SH-SY5Y Neuroblastoma Cells: A Morphological Study

• [ONLINE] DOI: https://doi.org/10.3233/JAD-190155
• [OPEN ACCESS] http://aura.abdn.ac.uk/bitstream/2164/12795/1/JAD_Flores_Accepted_Manuscript.pdf
• [ONLINE] https://www.medra.org/servlet/aliasResolver?alias=iospress&doi=10.3233/JAD-190155
• [ONLINE] View publication in Mendeley

Cortical Thickness and Surface Area Networks in Healthy Aging, Alzheimer’s Disease and Behavioral Variant Fronto-Temporal Dementia

• [ONLINE] DOI: https://doi.org/10.1142/S0129065718500557
• [OPEN ACCESS] http://aura.abdn.ac.uk/bitstream/2164/11981/3/Cortical_Thickness_and_Surface_Area_Networks_in_Healthy_Aging_Alzheimer_s_Disease_and_Behavioral_Variant_Fronto_Temporal_Dementia.pdf
• [ONLINE] View publication in Scopus
• [ONLINE] View publication in Mendeley

Increased Cholinergic Response in α-Synuclein Transgenic Mice (h-α-synL62)

• [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)

• [ONLINE] DOI: https://doi.org/10.1016/j.jmb.2018.08.010
• [OPEN ACCESS] http://aura.abdn.ac.uk/bitstream/2164/11249/1/1_s2.0_S0022283618305606_main.pdf

Modeling Prion-Like Processing of Tau Protein in Alzheimer's Disease for Pharmaceutical Development

• [ONLINE] DOI: https://doi.org/10.3233/JAD-170727
• [OPEN ACCESS] http://aura.abdn.ac.uk/bitstream/2164/10181/1/Modeling_Prion_Like_Processing_of_Tau_Protein_in_Alzheimer_s_Disease_for_Pharmaceutical_Development.pdf

Alpha-Synuclein transgenic mice, h-α-SynL62, display α-Syn aggregation and a dopaminergic phenotype reminiscent of Parkinson's disease

• [ONLINE] DOI: https://doi.org/10.1016/j.bbr.2017.11.025
• [OPEN ACCESS] http://aura.abdn.ac.uk/bitstream/2164/9815/1/Alpha_Synuclein_transgenic_mice_h_SynL62_display_Syn_aggregation_and_a_dopaminergic_phenotype_reminiscent_of_Parkinson_s_disease.pdf

A Protein Aggregation Inhibitor, Leuco-Methylthioninium Bis(Hydromethanesulfonate), Decreases α-Synuclein Inclusions in a Transgenic Mouse Model of Synucleinopathy

• [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

• [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

• [ONLINE] DOI: https://doi.org/10.1016/j.jmb.2017.09.007
• [OPEN ACCESS] http://aura.abdn.ac.uk/bitstream/2164/9614/1/Alzheimer_s_Disease_like_Paired_Helical_Filament_Assembly_from_Truncated_Tau_Protein_Is_Independent_of_Disulfide_Crosslinking.pdf

The effect of latent confounding processes on the estimation of the strength of causal influences in chain-type networks

• [ONLINE] http://www.journals.ke-i.org/index.php/mra/article/view/1298
• [OPEN ACCESS] http://aura.abdn.ac.uk/bitstream/2164/9406/1/document.pdf

Organisation of cortical thickness networks in Alzheimer’s disease and behavioural variant frontotemporal dementia across brain lobes

Method and system for determining network connections

LMTM DECREASES α-SYNUCLEIN PATHOLOGY AND REDUCES BEHAVIOURAL DEFECTS IN α-SYNUCLEIN TRANSGENIC MICE

• [ONLINE] DOI: https://doi.org/10.1016/j.jalz.2017.06.1854

Monoaminergic Neuropathology in Alzheimer's disease

• [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

Distinct anatomical subtypes of behavioural variant frontotemporal dementia and involvement of intrinsic brain networks: a clustering study

Assays for the Screening and Characterization of Tau Aggregation Inhibitors

• [ONLINE] DOI: https://doi.org/10.1007/978-1-4939-6598-4_8

Efficacy and safety of tau-aggregation inhibitor therapy in patients with mild or moderate Alzheimer's disease: a randomised, controlled, double-blind, parallel-arm, phase 3 trial

• [ONLINE] DOI: https://doi.org/10.1016/S0140-6736(16)31275-2
• [OPEN ACCESS] http://aura.abdn.ac.uk/bitstream/2164/8639/3/Gauthier_et_al_R2_19July2016_FINAL_CLEAN.pdf
• [OPEN ACCESS] http://aura.abdn.ac.uk/bitstream/2164/8639/2/Gauthier_et_al_R2_Supplementary_tables_19July2016.docx

Inhibition of Tau Aggregation as a Basis for Treatment and Prevention of Alzheimer's Disease

• [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

• [ONLINE] DOI: https://doi.org/10.3390/biom6020019
• [OPEN ACCESS] http://aura.abdn.ac.uk/bitstream/2164/5864/1/biomolecules_06_00019_v2.pdf

Tau Protein Hyperphosphorylation and Aggregation in Alzheimer’s Disease and Other Tauopathies, and Possible Neuroprotective Strategies

• [ONLINE] DOI: https://doi.org/10.3390/biom6010006
• [OPEN ACCESS] http://aura.abdn.ac.uk/bitstream/2164/8985/1/biomolecules_06_00006_v2.pdf
• [ONLINE] View publication in Scopus

Neural correlates of cognitive and behavioural impairments in behavioural variant of frontotemporal dementia: A voxel based morphometry analysis

Phenothiazine compounds for treating mild cognitive impairment

Different pathways of molecular pathophysiology underlie cognitive and motor tauopathy phenotypes in transgenic models for Alzheimer’s disease and frontotemporal lobar degeneration

• [ONLINE] DOI: https://doi.org/10.1007/s00018-014-1804-z
• [OPEN ACCESS] http://aura.abdn.ac.uk/bitstream/2164/4567/1/art_3A10.1007_2Fs00018_014_1804_z.pdf

Effects of oxidized and reduced forms of methylthioninium in two transgenic mouse tauopathy models

• [ONLINE] DOI: https://doi.org/10.1097/FBP.0000000000000133
• [OPEN ACCESS] http://aura.abdn.ac.uk/bitstream/2164/4568/1/Effects_of_oxidized_and_reduced_forms_of.4.pdf

Cellular Models of Aggregation-Dependent Template-Directed Proteolysis to Characterize Tau Aggregation Inhibitors for Treatment of Alzheimer's Disease

• [ONLINE] DOI: https://doi.org/10.1074/jbc.M114.616029
• [OPEN ACCESS] http://aura.abdn.ac.uk/bitstream/2164/4569/1/J._Biol._Chem._2015_Harrington_10862_75.pdf

The relationship between truncation and phosphorylation at the C-terminus of tau protein in the paired helical filaments of Alzheimer's disease

• [ONLINE] DOI: https://doi.org/10.3389/fnins.2015.00033
• [OPEN ACCESS] http://aura.abdn.ac.uk/bitstream/2164/4290/1/fnins_09_00033.pdf

Tau Aggregation Inhibitor Therapy: An Exploratory Phase 2 Study in Mild or Moderate Alzheimer's Disease

• [ONLINE] DOI: https://doi.org/10.3233/JAD-142874
• [OPEN ACCESS] http://aura.abdn.ac.uk/bitstream/2164/4205/1/fulltext.pdf

Complex Disposition of Methylthioninium Redox Forms Determines Efficacy in Tau Aggregation Inhibitor Therapy for Alzheimer's Disease

• [ONLINE] DOI: https://doi.org/10.1124/jpet.114.219352

Tau-aggregation inhibitor therapy for Alzheimer's disease

• [ONLINE] DOI: https://doi.org/10.1016/j.bcp.2013.12.008
• [OPEN ACCESS] http://aura.abdn.ac.uk/bitstream/2164/4208/1/1_s2.0_S0006295213007612_main.pdf

TauRx global phase 3 trial in Alzheimer's disease with tau aggregation inhibitor LMTX

• [ONLINE] DOI: https://doi.org/10.1016/j.neurobiolaging.2014.01.128

New phenothiazine diaminium compounds are tau protein aggregation inhibitors, useful to treat e.g. Alzheimer's disease, Pick's disease, progressive supranuclear palsy, frontotemporal dementia and frontotemporal lobar degeneration syndromes

Regional cerebral blood flow and aberrant motor behaviour in Alzheimer's disease

• [ONLINE] DOI: https://doi.org/10.1016/j.bbr.2011.04.003

The cerebral blood flow correlates of emotional facial processing in mild Alzheimer's disease

• [ONLINE] DOI: https://doi.org/10.4236/nm.2011.21002

3,7-diamino-10H-phenothiazine salts and their use: WO2007110627

• [OPEN ACCESS] http://aura.abdn.ac.uk/bitstream/2164/4352/1/WO2007110627.pdf

Stripline resonator and preamplifier for preclinical magnetic resonance imaging at 4.7 T

• [ONLINE] DOI: https://doi.org/10.1007/s10334-011-0273-8

3,6-Disubstituted xanthylium salts

Methods of chemical synthesis and purification of diaminophenothiazinium compounds including methylthioninium chloride (MTC): methods of treatment of a tauopathy condition comprising the use of thioninium compounds

Ligands for aggregated tau molecules: WO2010034982

• [OPEN ACCESS] http://aura.abdn.ac.uk/bitstream/2164/4351/1/WO2010034982.pdf

Rationale for tau aggregation inhibitor therapy in Alzheimer's disease and other tauopathies

• [ONLINE] DOI: https://doi.org/10.1039/9781849731065
• [OPEN ACCESS] http://aura.abdn.ac.uk/bitstream/2164/4066/1/Wischik_2010_RSC_Chapter.pdf

Lewy body variant of Alzheimer's disease: selective neocortical loss of t-SNARE proteins and loss of MAP2 and alpha-synuclein in medial temporal lobe

• [ONLINE] DOI: https://doi.org/10.1100/tsw.2009.151

Therapeutic Use of Diaminophenothiazines: WO2009044127

• [ONLINE] http://patentscope.wipo.int/search/en/detail.jsf?docId=WO2009044127
• [OPEN ACCESS] http://aura.abdn.ac.uk/bitstream/2164/4353/1/WO2009044127.pdf

Methylthioninium chloride reverses cognitive deficits induced by scopolamine: comparison with rivastigmine

• [ONLINE] DOI: https://doi.org/10.1007/s00213-008-1394-2

Methods of synthesis and/or purification of diaminophenothiazinium compounds

Thiazin red as a neuropathological tool for the rapid diagnosis of Alzheimer's disease in tissue imprints

• [ONLINE] DOI: https://doi.org/10.1007/s00401-008-0431-x

Inhibitors of protein aggregation: WO2007110629

• [OPEN ACCESS] http://aura.abdn.ac.uk/bitstream/2164/4488/1/WO2007110629.pdf

A55 A rCBF study of hallucinations in dementia.

• [ONLINE] DOI: https://doi.org/10.1097/00006231-200603000-00066

Methods of chemical synthesis and purification of diaminophenothiazinium compounds including methylthioninium chloride (MTC)

Inhibition of tau-tau-association

Alzheimer's disease

Naphthoquinone-type inhibitors of protein aggregation

Materials and methods relating to protein aggregation in neurodegenerative disease: WO2002059150

• [OPEN ACCESS] http://aura.abdn.ac.uk/bitstream/2164/4355/1/WO2002059150.pdf

Loss of synaptic but not cytoskeletal proteins in the cerebellum of chronic schizophrenics

• [ONLINE] DOI: https://doi.org/10.1016/S0304-3940(01)02458-2

Inhibition of tau-tau-association

Materials and methods relating to protein aggregation in neurodegenerative disease: WO2002055720

• [OPEN ACCESS] http://aura.abdn.ac.uk/bitstream/2164/4354/1/WO2002055720.pdf

Neurofibrillary labels

Accumulation of C-terminally truncated tau protein associated with vulnerability of the perforant pathway in early stages of neurofibrillary pathology in Alzheimer’s disease

• [ONLINE] DOI: https://doi.org/10.1016/S0891-0618(01)00096-5

Loss of synaptic, but not cytoskeletal proteins in the cerebellum of people with chronic schizophrenia

• [ONLINE] DOI: https://doi.org/10.1016/S0920-9964(01)00159-1

The molecular basis of tau protein pathology in Alzheimer's Disease and related neurodegenerative dementias

Staging of cytoskeletal and beta-amyloid changes in human isocortex reveals biphasic synaptic protein response during progression of Alzheimer's disease

• [ONLINE] DOI: https://doi.org/10.1016/S0002-9440(10)64573-7

α-Synuclein inclusions in Alzheimer and Lewy body diseases

• [ONLINE] DOI: https://doi.org/10.1093/jnen/59.5.408
• [ONLINE] View publication in Scopus

The extent of neurofibrillary pathology in perforant pathway neurons is the key determinant of dementia in the very old

alpha-synuclein inclusions in Alzheimer and Lewy body diseases