Results 31 to 40 of about 243,600 (356)

Toxic Tau Oligomers Modulated by Novel Curcumin Derivatives [PDF]

open access: yes, 2019
The pathological aggregation and accumulation of tau, a microtubule-associated protein, is a common feature amongst more than 18 different neurodegenerative diseases that are collectively known as tauopathies.
Bucchieri, Fabio   +6 more
core   +1 more source

Transgenic Zebrafish as a Novel Animal Model to Study Tauopathies and Other Neurodegenerative Disorders in vivo [PDF]

open access: yes, 2010
Our ageing society is confronted with a dramatic increase in patients suffering from tauopathies such as Alzheimer's disease, frontotemporal dementia and others.
Haass, Christian   +2 more
core   +1 more source

Phenothiazine-mediated rescue of cognition in tau transgenic mice requires neuroprotection and reduced soluble tau burden [PDF]

open access: yes, 2010
Background It has traditionally been thought that the pathological accumulation of tau in Alzheimer's disease and other tauopathies facilitates neurodegeneration, which in turn leads to cognitive impairment.
A de Calignon   +38 more
core   +6 more sources

Tau’s Three-Repeat Domain and EFhd2 Co-incubation Leads to Increased Thioflavin Signal

open access: yesFrontiers in Neuroscience, 2018
Aggregation of the protein tau is a pathological hallmark of Alzheimer’s disease (AD) and related disorders. However, the molecular mechanisms that lead to tau protein aggregation are still unclear.
Irving E. Vega   +7 more
doaj   +1 more source

Identification and characterization of a MAPT-targeting locked nucleic acid antisense oligonucleotide therapeutic for tauopathies

open access: yesMolecular Therapy: Nucleic Acids, 2022
Tau is a microtubule-associated protein (MAPT, tau) implicated in the pathogenesis of tauopathies, a spectrum of neurodegenerative disorders characterized by accumulation of hyperphosphorylated, aggregated tau.
Amy Easton   +37 more
doaj   +1 more source

Phosphorylation of nuclear Tau is modulated by distinct cellular pathways [PDF]

open access: yes, 2018
Post-translational protein modification controls the function of Tau as a scaffold protein linking a variety of molecular partners. This is most studied in the context of microtubules, where Tau regulates their stability as well as the distribution of ...
Boersema, Paul   +8 more
core   +2 more sources

Expression and Clinical Significance of Cytoskeleton microtubule-associated - Tau in gastric carcinoma

open access: yesJournal of College of Medical Sciences-Nepal, 2015
Background and Objectives: Microtubules, the main components of spindles in the mitotic phase, can provide the suitable conditions for unlimited proliferation of tumor cells.
Chun-Hui Li, Meiling Hao, Rajina Sahi
doaj   +1 more source

The cellular distribution and Ser262 phosphorylation of tau protein are regulated by BDNF in vitro. [PDF]

open access: yesPLoS ONE, 2014
The brain-enriched microtubule-associated protein tau, a critical regulator of cytoskeletal dynamics, forms insoluble aggregates in a number of neurodegenerative diseases termed tauopathies, including Alzheimer's disease (AD). Hyperphosphorylation of tau
Qian Chen   +5 more
doaj   +1 more source

Follow-up investigations of tau protein and S-100B levels in cerebrospinal fluid of patients with Creutzfeldt-Jakob disease [PDF]

open access: yes, 2005
Background: S-100B and tau protein have a high differential diagnostic potential for the diagnosis of Creutzfeldt-Jakob disease (CJD). So far there has been only limited information available about the dynamics of these parameters in the cerebrospinal ...
Barbara Ciesielczyk   +18 more
core   +1 more source

Neuronal Excitation Induces Tau Protein Dephosphorylation via Protein Phosphatase 1 Activation to Promote Its Binding with Stable Microtubules

open access: yesNeurology International
The tau protein is a microtubule-associated protein that promotes microtubule stabilization. The phosphorylation of the tau protein has been linked to its dissociation from microtubules.
Sosuke Yagishita   +4 more
doaj   +1 more source

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