D. Horsley

发表

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

Thomas C. Baddeley, C. Harrington, C. Wischik, 2015, The Journal of Pharmacology and Experimental Therapeutics.

Antibodies in plant science

C. Hawes, D. Evans, D. Horsley, 1991 .

CellularModelsofAggregation-dependentTemplate-directed ProteolysistoCharacterizeTauAggregationInhibitorsfor

C. Harrington, C. Wischik, J. Storey, 2015 .

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

G. Riedel, C. Harrington, C. Wischik, 2018, Behavioural Brain Research.

A monoclonal antibody, JIM 84, recognizes the Golgi apparatus and plasma membrane in plant cells

C. Hawes, B. Satiat-Jeunemaitre, D. Evans, 1993 .

Sels de xanthylium 3,6-disubstitués

C. Harrington, C. Wischik, J. Storey, 2009 .

M33, a mammalian homologue of Drosophila Polycomb localises to euchromatin within interphase nuclei but is enriched within the centromeric heterochromatin of metaphase chromosomes.

A. Otte, D. Horsley, G. Butcher, 1997, Cytogenetics and cell genetics.

Assays for the Screening and Characterization of Tau Aggregation Inhibitors.

C. Harrington, C. Wischik, D. Horsley, 2017, Methods in molecular biology.

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

G. Riedel, C. Harrington, K. Stamer, 2014, Cellular and Molecular Life Sciences.

The M31 gene has a complex developmentally regulated expression profile and may encode alternative protein products that possess diverse subcellular localisation patterns.

C. Sapienza, K. Latham, K. Peterson, 1998, The Journal of experimental zoology.

The Gene and Pseudogenes of Cbx3/mHPlγ

M. Mattei, Prim B. Singh, D. Horsley, 2001, DNA sequence : the journal of DNA sequencing and mapping.

M32, a murine homologue of Drosophila heterochromatin protein 1 (HP1), localises to euchromatin within interphase nuclei and is largely excluded from constitutive heterochromatin.

Prim B. Singh, D. Horsley, G. Butcher, 1996, Cytogenetics and cell genetics.

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

K. Goatman, G. Riedel, C. Harrington, 2015, Behavioural pharmacology.

Cellular Models of Aggregation-dependent Template-directed Proteolysis to Characterize Tau Aggregation Inhibitors for Treatment of Alzheimer Disease

C. Harrington, C. Wischik, J. Storey, 2015, The Journal of Biological Chemistry.

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

C. Harrington, C. Wischik, J. Storey, 2010 .

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

G. Riedel, C. Harrington, C. Wischik, 2018, Front. Mol. Neurosci..

Structure and molecular organization of higher plant coated vesicles

C. Hawes, D. Horsley, J. Coleman, 1987 .

Anticancer agent development. 4. X-ray crystal structure and intermolecular crystal lattice interactions of methyltrans-4,5-dihydro-4-acetoxymethyl-5-(3,4,5-trimethoxyphenyl)-2-(3,4-methylenedioxyphenyl)-3-furancarboxylate

J. Brozik, R. Rogers, D. Horsley, 1990 .

O1-06-04: Methylthioninium chloride (MTC) acts as a Tau aggregation inhibitor (TAI) in a cellular model and reverses Tau pathology in transgenic mouse models of Alzheimer's disease

G. Riedel, C. Harrington, C. Wischik, 2008, Alzheimer's & Dementia.