11 research outputs found
Proteomic analysis of hydromethylthionine in the line 66 model of frontotemporal dementia demonstrates actions on tau-dependent and tau-independent networks
Funding: This research received no external funding. Acknowledgments: The authors acknowledge Boris Neumann and Karola Lehmann for the excellent support with the proteomics data.Peer reviewedPublisher PD
Glutamatergic transmission and receptor expression in the synucleinopathy h-α-synL62 mouse model : Effects of hydromethylthionine
Acknowledgements The authors acknowledge Dr. Dilyara Lauer and Heide Lueck for the excellent technical support with the administration of drugs, collection of brains and sectioning of brain tissue for immunohistochemistry. Funding This work was funded by TauRx Therapeutics Ltd., Singapore. Z. C. was funded by the Erasmus+ programme of the European Union.Peer reviewedPublisher PD
Hydromethylthionine rescues synaptic SNARE proteins in a mouse model of tauopathies : interference by cholinesterase inhibitors
The authors acknowledge Malgorzata Wydrych and Joanna Lewandowska for the technical support with perfusion of mice and collection of brains, and of Soumya Palliyil Soman for the development of the s1D12 antibody.Peer reviewe
Differential compartmental processing and phosphorylation of pathogenic human tau and native mouse tau in the Line 66 model of frontotemporal dementia
Funding Information: Funding and additional information—This work was supported by EMPIR programme in Research Project 15HLT02 ReMiND cofinanced by the Participating States and the European Union's Horizon 2020 research and innovation programme (to N. L.). Work was also supported by WisTa Laboratories Ltd. (to V. M., D. L., M. M., C. R. H., G. R., C. M. W., F. T., and K. S.). Conflict of interest—This work was sponsored by WisTa Laboratories Ltd., an affiliate of TauRx Therapeutics Ltd. C. R. H. and C. M. W. are employees and officers of TauRx Therapeutics Ltd.Peer reviewedPublisher PD
LETC inhibits α-Syn aggregation and ameliorates motor deficiencies in the L62 mouse model of synucleinopathy
Peer reviewe
Mechanisms of anticholinesterase interference with tau aggregation inhibitor activity in a tau-transgenic mouse model
AVAILABILITY OF DATA AND MATERIALS The data that support the findings of this study are available from the corresponding author [CMW], upon reasonable request. FUNDING This study was sponsored entirely by WisTa Laboratories Ltd. under the following grants: PAR1395, PAR1561, PAR1562, PAR1577 and PAR1763. The sponsor was involved in the design of the study; in the collection, analysis and interpretation of data; and in the writing of the report. The corresponding author had full access to all the data and had final responsibility for submission of the report for publication.Peer reviewedPostprin
Different pathways of molecular pathophysiology underlie cognitive and motor tauopathy phenotypes in transgenic models for Alzheimer’s disease and frontotemporal lobar degeneration
Open Access This article is distributed under the terms of the Creative Commons Attribution License which permits any use, distribution, and reproduction in any medium, provided the original author(s) and the source are credited. Acknowledgments From the Berlin Laboratory, we thank Ingo Voigt for performing the injections of the two constructs into the oocytes, Bettina Seelhorst for her extensive technical assistance, Anna Thoma for taking specific care of the animals, and John Horn, Charite Core Facility for electron microscopy for performing expert analyses in ultra-cryosections with immunogold technique. Expert comments on the manuscript from Silke Frahm-Barske (Berlin) are also acknowledged. Special thanks to Bob Switzer at NeuroScience Associates Inc. for embedding, sectioning and staining mouse brains. This work was funded by TauRx Therapeutics, Singapore. C.R.H. and C.M.W. declare that they are officers in TauRx Therapeutics Ltd.Peer reviewedPublisher PD
Effects of oxidized and reduced forms of methylthioninium in two transgenic mouse tauopathy models
Acknowledgements The authors acknowledge the contributions of Bettina Seelhorst (histological analysis), Anna Thoma (animal care), Marlene Arthur (animal dosing) and Pierre-Henri Moreau (experimental discussions). This work was supported by TauRx Therapeutics Ltd., Singapore.Peer reviewedPublisher PD
A Protein Aggregation Inhibitor, Leuco-Methylthioninium Bis(Hydromethanesulfonate), Decreases α-Synuclein Inclusions in a Transgenic Mouse Model of Synucleinopathy
The authors acknowledge Heide Lueck for excellent technical assistance and for maintenance of animals. AMS Biotechnology generated monoclonal antibodies from recombinant α-Syn prepared by JR.Peer reviewedPublisher PD