A Protein Aggregation Inhibitor, Leuco-Methylthioninium Bis(Hydromethanesulfonate), Decreases α-Synuclein Inclusions in a Transgenic Mouse Model of Synucleinopathy
Published 2018 View Full Article
- Home
- Publications
- Publication Search
- Publication Details
Title
A Protein Aggregation Inhibitor, Leuco-Methylthioninium Bis(Hydromethanesulfonate), Decreases α-Synuclein Inclusions in a Transgenic Mouse Model of Synucleinopathy
Authors
Keywords
-
Journal
Frontiers in Molecular Neuroscience
Volume 10, Issue -, Pages -
Publisher
Frontiers Media SA
Online
2018-01-10
DOI
10.3389/fnmol.2017.00447
References
Ask authors/readers for more resources
Related references
Note: Only part of the references are listed.- Alpha-Synuclein transgenic mice, h-α-SynL62, display α-Syn aggregation and a dopaminergic phenotype reminiscent of Parkinson’s disease
- (2018) Silke Frahm et al. BEHAVIOURAL BRAIN RESEARCH
- A routinely used protein staining dye acts as an inhibitor of wild type and mutant alpha-synuclein aggregation and modulator of neurotoxicity
- (2018) Nuzhat Ahsan et al. EUROPEAN JOURNAL OF MEDICINAL CHEMISTRY
- 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
- (2017) Gordon K. Wilcock et al. JOURNAL OF ALZHEIMERS DISEASE
- α-Synuclein aggregation, seeding and inhibition by scyllo-inositol
- (2016) Tarek Ibrahim et al. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
- Baicalein inhibits α-synuclein oligomer formation and prevents progression of α-synuclein accumulation in a rotenone mouse model of Parkinson's disease
- (2016) Qi Hu et al. BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR BASIS OF DISEASE
- 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
- (2016) Serge Gauthier et al. LANCET
- Potential Pathways of Abnormal Tau and α-Synuclein Dissemination in Sporadic Alzheimer's and Parkinson's Diseases
- (2016) Heiko Braak et al. Cold Spring Harbor Perspectives in Biology
- Fasudil attenuates aggregation of α-synuclein in models of Parkinson’s disease
- (2016) Lars Tatenhorst et al. Acta Neuropathologica Communications
- Effects of oxidized and reduced forms of methylthioninium in two transgenic mouse tauopathy models
- (2015) Valeria Melis et al. BEHAVIOURAL PHARMACOLOGY
- Cellular Models of Aggregation-dependent Template-directed Proteolysis to Characterize Tau Aggregation Inhibitors for Treatment of Alzheimer Disease
- (2015) Charles R. Harrington et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Parkinson Disease Mutant E46K Enhances α-Synuclein Phosphorylation in Mammalian Cell Lines, in Yeast, andin Vivo
- (2015) Martial Kamdem Mbefo et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Serotonergic dysfunction in the A53T alpha-synuclein mouse model of Parkinson's disease
- (2015) Janina Deusser et al. JOURNAL OF NEUROCHEMISTRY
- Targeting α-synuclein for treatment of Parkinson's disease: mechanistic and therapeutic considerations
- (2015) Benjamin Dehay et al. LANCET NEUROLOGY
- Binding interactions of agents that alter α-synuclein aggregation
- (2015) K. Sivanesam et al. RSC Advances
- Next-generation active immunization approach for synucleinopathies: implications for Parkinson’s disease clinical trials
- (2014) Markus Mandler et al. ACTA NEUROPATHOLOGICA
- Different pathways of molecular pathophysiology underlie cognitive and motor tauopathy phenotypes in transgenic models for Alzheimer’s disease and frontotemporal lobar degeneration
- (2014) V. Melis et al. CELLULAR AND MOLECULAR LIFE SCIENCES
- Immunotherapy targeting α-synuclein protofibrils reduced pathology in (Thy-1)-h[A30P] α-synuclein mice
- (2014) Veronica Lindström et al. NEUROBIOLOGY OF DISEASE
- Immunolocalization of human alpha-synuclein in the Thy1-aSyn (“Line 61”) transgenic mouse line
- (2014) M. Delenclos et al. NEUROSCIENCE
- α-Synuclein Immunotherapy Blocks Uptake and Templated Propagation of Misfolded α-Synuclein and Neurodegeneration
- (2014) Hien T. Tran et al. Cell Reports
- Anle138b: a novel oligomer modulator for disease-modifying therapy of neurodegenerative diseases such as prion and Parkinson’s disease
- (2013) Jens Wagner et al. ACTA NEUROPATHOLOGICA
- Methylthioninium chloride (methylene blue) induces autophagy and attenuates tauopathy in vitro and in vivo
- (2012) Erin E. Congdon et al. Autophagy
- Cognitive deficits in a mouse model of pre-manifest Parkinson’s disease
- (2012) Iddo Magen et al. EUROPEAN JOURNAL OF NEUROSCIENCE
- Antibody-Aided Clearance of Extracellular -Synuclein Prevents Cell-to-Cell Aggregate Transmission
- (2012) E.-J. Bae et al. JOURNAL OF NEUROSCIENCE
- Exosomal cell-to-cell transmission of alpha synuclein oligomers
- (2012) Karin M Danzer et al. Molecular Neurodegeneration
- The many faces of α-synuclein: from structure and toxicity to therapeutic target
- (2012) Hilal A. Lashuel et al. NATURE REVIEWS NEUROSCIENCE
- Comparison of motor performance, brain biochemistry and histology of two A30P α-synuclein transgenic mouse strains
- (2012) M. Piltonen et al. NEUROSCIENCE
- Pathological -Synuclein Transmission Initiates Parkinson-like Neurodegeneration in Nontransgenic Mice
- (2012) K. C. Luk et al. SCIENCE
- Enhancement of proteasome activity by a small-molecule inhibitor of USP14
- (2010) Byung-Hoon Lee et al. NATURE
- Cell-to-cell transmission of non-prion protein aggregates
- (2010) Seung-Jae Lee et al. Nature Reviews Neurology
- Inclusion formation and neuronal cell death through neuron-to-neuron transmission of -synuclein
- (2009) P. Desplats et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Disease-modifying drugs and Parkinson's disease
- (2007) Hervé Allain et al. PROGRESS IN NEUROBIOLOGY
Find Funding. Review Successful Grants.
Explore over 25,000 new funding opportunities and over 6,000,000 successful grants.
ExploreAsk a Question. Answer a Question.
Quickly pose questions to the entire community. Debate answers and get clarity on the most important issues facing researchers.
Get Started