What is the molecular pathology that underlies hippocampal memory decline?

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Tau-aggregation inhibitor therapy for Alzheimer's disease

Article Accepted Date: 9 December 2013 Copyright © 2014 The Authors. Published by Elsevier Inc. All rights reserved.Peer reviewedPublisher PD

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

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Regulation of mannan synthesis in Saccharomyces cerevisiae

Although a great deal is known about the chemical structure and enzymatic mechanisms involved in the assembly of yeast mannoproteins, little is known about the regulation of mannan biosynthesis. The aim of this study, therefore, was to investigate the control mechanisms involved. Two approaches were used. Firstly, the potential role of low molecular-weight effectors of mannosyltransferases was investigated. Secondly, the possible existence of an activation-inactivation mechanism of control, analogous to that which operates during chitin synthesis was explored. Mannosyltransferase activity in sphaeroplast lysates and washed membranes prepared from Saccharomyces cerevisiae X2180 was measured by following the incorporation of [14C]cjmannose from GDP-[14C]nBnnose into material precipitable with cold 0.3M perchloric acid. Mannosyl- transferase activity was optimal at low enzyme protein concentrations (l mg/ml), 5

Absence of a Role for Phosphorylation in the Tau Pathology of Alzheimer's Disease

Acknowledgments: Depolymerised bovine tubulin was kindly donated by J. Kilmartin (MRC Laboratory of Molecular Biology, Cambridge). This work was supported by the Medical Research Council (UK), a Wellcome Trust Studentship to RL, the Leopold Muller Estate, and the Newton Trust (Trinity College, Cambridge). We gratefully acknowledge Academic Books for permission to use Table 2 and Figures 2–4 which correspond to Table 1 and Figures 20–22 from Wischik C.M., Lai, R.Y.K. and Harrington, C.R. Modelling prion-like processing of tau protein in Alzheimer’s disease for pharmaceutical development, in Brain Microtubule Associated Proteins: Modifications in Disease, Avila, J.; Brandt, R.; Kosik, K.S., Eds. Harwood Academic Publishers: Amsterdam, The Netherlands, 1997. Erratum published on 12 August 2016, see Biomolecules 2016, 6(3), 35. http://www.mdpi.com/2218-273X/6/3/35Peer reviewedPublisher PD

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

ACKNOWLEDGMENTS We thank patients and their caregivers for their participation in the study and are indebted to all the investigators involved in the study, particularly Drs. Douglas Fowlie and Donald Mowat for their helpful contributions to the clinical execution of the study in Scotland. We thank Sharon Eastwood, Parexel, for assistance in preparing initial drafts of the manuscript. We acknowledge constructive comments provided by Professors G. Wilcock and S. Gauthier on drafts of the article. CMW, CRH, and JMDS are officers of, and hold beneficial interests in, TauRx Therapeutics. RTS, PB, KK, and DJW are paid consultants to TauRx Therapeutics. The study was financed entirely by TauRx TherapeuticsPeer reviewedPublisher PD

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

This work was funded by TauRx Therapeutics Ltd.,SingaporePeer reviewedPublisher PD

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

The present study was carried out with funds supplied by TauRx Therapeutic Ltd. We are grateful to Helene Lau for assistance with 182 |KONDAK etAl.the analytical determinations. Open access funding enabled and or-ganized by ProjektDEAL TauRx Therapeutics Ltd., Aberdeen, Grant/Award Number: R0154Peer reviewedPublisher PD

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

Copyright © 2015, The American Society for Biochemistry and Molecular Biology. Acknowledgements-We thank Drs Timo Rager and Rolf Hilfiker (Solvias, Switzerland) for polymorph analyses.Peer reviewedPublisher PD

Monoaminergic Neuropathology in Alzheimer's disease

Acknowledgments This work was supported by The Croatian Science Foundation grant. no. IP-2014-09-9730 (“Tau protein hyperphosphorylation, aggregation, and trans-synaptic transfer in Alzheimer’s disease: cerebrospinal fluid analysis and assessment of potential neuroprotective compounds”) and European Cooperation in Science and Technology (COST) Action CM1103 (“Stucture-based drug design for diagnosis and treatment of neurological diseases: dissecting and modulating complex function in the monoaminergic systems of the brain”). PRH is supported in part by NIH grant P50 AG005138.Peer reviewedPostprin