Tauopathic changes in the striatum of A53T α-synuclein mutant mouse model of Parkinson's disease. - Wikidata - awgldk - TriplyDB

Tauopathic changes in the striatum of A53T α-synuclein mutant mouse model of Parkinson's disease.

Tauopathic changes in the striatum of A53T α-synuclein mutant mouse model of Parkinson's disease.

http://www.wikidata.org/entity/Q34704153

about

Cerebrospinal Fluid Amyloid β1-42, Tau, and Alpha-Synuclein Predict the Heterogeneous Progression of Cognitive Dysfunction in Parkinson's Disease Microtubule-stabilizing agents as potential therapeutics for neurodegenerative disease Age-dependent effects of A53T alpha-synuclein on behavior and dopaminergic function GSK-3β dysregulation contributes to parkinson's-like pathophysiology with associated region-specific phosphorylation and accumulation of tau and α-synuclein Alpha-synuclein and tau: teammates in neurodegeneration?Interactions between Tau and α-synuclein augment neurotoxicity in a Drosophila model of Parkinson's disease.Roles of tau protein in health and disease.Association of cerebrospinal fluid β-amyloid 1-42, T-tau, P-tau181, and α-synuclein levels with clinical features of drug-naive patients with early Parkinson disease.Region-specific tauopathy and synucleinopathy in brain of the alpha-synuclein overexpressing mouse model of Parkinson's disease Motor and cognitive deficits in aged tau knockout mice in two background strains.Tau reduction does not prevent motor deficits in two mouse models of Parkinson's disease Paraquat, but not maneb, induces synucleinopathy and tauopathy in striata of mice through inhibition of proteasomal and autophagic pathways Intranasal NAP (davunetide) decreases tau hyperphosphorylation and moderately improves behavioral deficits in mice overexpressing α-synuclein.A powerful yeast model to investigate the synergistic interaction of α-synuclein and tau in neurodegeneration.Hyperphosphorylated Tau in an α-synuclein-overexpressing transgenic model of Parkinson's disease.Identification of the sites of tau hyperphosphorylation and activation of tau kinases in synucleinopathies and Alzheimer's diseases.Extracellular α-synuclein leads to microtubule destabilization via GSK-3β-dependent Tau phosphorylation in PC12 cells The transient receptor potential (TRP) channel TRPC3 TRP domain and AMP-activated protein kinase binding site are required for TRPC3 activation by erythropoietin.The hypoxia imaging agent CuII(atsm) is neuroprotective and improves motor and cognitive functions in multiple animal models of Parkinson's disease.Early start of progressive motor deficits in Line 61 α-synuclein transgenic mice.MicroRNA expressing profiles in A53T mutant alpha-synuclein transgenic mice and Parkinsonian.Interaction between pathogenic proteins in neurodegenerative disorders.Altered microtubule dynamics in neurodegenerative disease: Therapeutic potential of microtubule-stabilizing drugs.Interactions of pathological proteins in neurodegenerative diseases.Dopaminergic lesioning impairs adult hippocampal neurogenesis by distinct modification of α-synuclein.Molecular mechanisms of the co-deposition of multiple pathological proteins in neurodegenerative diseases.Tau oligomers mediate α-synuclein toxicity and can be targeted by immunotherapy.Neuroimmune Tau Mechanisms: Their Role in the Progression of Neuronal Degeneration.Interaction between α-synuclein and other proteins in neurodegenerative disorders.The Amyloid-β Oligomer Hypothesis: Beginning of the Third Decade.Characterisation of tau in the human and rodent enteric nervous system under physiological conditions and in tauopathy Tau Pathology in Parkinson's Disease

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Tauopathic changes in the striatum of A53T α-synuclein mutant mouse model of Parkinson's disease.

http://www.wikidata.org/entity/Q34704153

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2011 nî lūn-bûn

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2011 թվականի մարտին հրատարակված գիտական հոդված

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2011年の論文

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Adam W Oaks

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Anita Sidhu

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Jae-Hoon Lee

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Jonathan Wills

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Thomas Haggerty

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P2860

Absence of Ret signaling in mice causes progressive and late degeneration of the nigrostriatal system

Mutation in the alpha-synuclein gene identified in families with Parkinson's disease

GSK3B polymorphisms alter transcription and splicing in Parkinson's disease

Phosphorylation of tau at both Thr 231 and Ser 262 is required for maximal inhibition of its binding to microtubules

Alpha-synuclein induces hyperphosphorylation of Tau in the MPTP model of parkinsonism

Ala30Pro mutation in the gene encoding alpha-synuclein in Parkinson's disease

Alzheimer's disease-like tau neuropathology leads to memory deficits and loss of functional synapses in a novel mutated tau transgenic mouse without any motor deficits.

Concurrence of alpha-synuclein and tau brain pathology in the Contursi kindred.

Alpha-Synuclein contributes to GSK-3beta-catalyzed Tau phosphorylation in Parkinson's disease models.

Lewy bodies in Alzheimer's disease: a neuropathological review of 145 cases using alpha-synuclein immunohistochemistry.

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