Cellular Models of Aggregation-dependent Template-directed Proteolysis to Characterize Tau Aggregation Inhibitors for Treatment of Alzheimer Disease.
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Tau-Centric Targets and Drugs in Clinical Development for the Treatment of Alzheimer's DiseaseMolecular Mechanisms in the Pathogenesis of Alzheimer's disease and Tauopathies-Prion-Like Seeded Aggregation and PhosphorylationTau Protein Hyperphosphorylation and Aggregation in Alzheimer's Disease and Other Tauopathies, and Possible Neuroprotective StrategiesTau Biology and Tau-Directed Therapies for Alzheimer's DiseaseDifferent pathways of molecular pathophysiology underlie cognitive and motor tauopathy phenotypes in transgenic models for Alzheimer's disease and frontotemporal lobar degenerationEffects of oxidized and reduced forms of methylthioninium in two transgenic mouse tauopathy models.Salidroside reduces tau hyperphosphorylation via up-regulating GSK-3β phosphorylation in a tau transgenic Drosophila model of Alzheimer's 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.Tau and neurodegenerative disease: the story so far.Intracellular and extracellular microtubule associated protein tau as a therapeutic target in Alzheimer disease and other tauopathies.Tau-directed approaches for the treatment of Alzheimer's disease: focus on leuco-methylthioninium.Genetics of Frontotemporal Dementia.Interactions between Microtubule-Associated Protein Tau (MAPT) and Small Molecules.Methylene blue and its analogues as antidepressant compounds.An ATR-FTIR Sensor Unraveling the Drug Intervention of Methylene Blue, Congo Red, and Berberine on Human Tau and Aβ.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.Alzheimer's Disease: The Role of Microglia in Brain Homeostasis and Proteopathy.Modeling Prion-Like Processing of Tau Protein in Alzheimer's Disease for Pharmaceutical Development.A Protein Aggregation Inhibitor, Leuco-Methylthioninium Bis(Hydromethanesulfonate), Decreases α-Synuclein Inclusions in a Transgenic Mouse Model of Synucleinopathy.A Quantitative Analysis of Brain Soluble Tau and the Tau Secretion Factor.Applications of the real-time quaking-induced conversion assay in diagnosis, prion strain-typing, drug pre-screening and other amyloidopathies.Tau aggregation inhibitors: the future of Alzheimer's pharmacotherapy?Tau-based therapeutics for Alzheimer's disease: active and passive immunotherapy.Assays for the Screening and Characterization of Tau Aggregation Inhibitors.X-Ray Structural Study of Amyloid-Like Fibrils of Tau Peptides Bound to Small-Molecule Ligands.
P2860
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P2860
Cellular Models of Aggregation-dependent Template-directed Proteolysis to Characterize Tau Aggregation Inhibitors for Treatment of Alzheimer Disease.
description
2015 nî lūn-bûn
@nan
2015年の論文
@ja
2015年学术文章
@wuu
2015年学术文章
@zh-cn
2015年学术文章
@zh-hans
2015年学术文章
@zh-my
2015年学术文章
@zh-sg
2015年學術文章
@yue
2015年學術文章
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2015年學術文章
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name
Cellular Models of Aggregation ...... reatment of Alzheimer Disease.
@en
type
label
Cellular Models of Aggregation ...... reatment of Alzheimer Disease.
@en
prefLabel
Cellular Models of Aggregation ...... reatment of Alzheimer Disease.
@en
P2093
P2860
P356
P1476
Cellular Models of Aggregation ...... reatment of Alzheimer Disease.
@en
P2093
Ahtsham Ishaq
Charles R Harrington
Christopher P Larch
Claude M Wischik
Colin Marshall
David Horsley
James P Sinclair
Janet E Rickard
John M D Storey
Kathleen A Harrington
P2860
P304
10862-10875
P356
10.1074/JBC.M114.616029
P407
P577
2015-03-10T00:00:00Z