Results 21 to 30 of about 1,790,741 (301)

Total and phosphorylated tau proteins: Evaluation as core biomarker candidates in frontotemporal dementia [PDF]

open access: yes, 2004
An ever increasing number of patients with neurodegenerative disorders calls for the evaluation of potential diagnostic markers that allow an early diagnosis and an early initiation of specific therapy. Clinical diagnosis of Alzheimer's disease (AD), the
Teipel, S. J.   +3 more
core   +1 more source

Serum heart-type fatty acid-binding protein and cerebrospinal fluid tau: Marker candidates for dementia with Lewy bodies [PDF]

open access: yes, 2007
Background: The measurement of biomarkers in cerebrospinal fluid (CSF) has gained increasing acceptance in establishing the diagnosis of some neurodegenerative diseases.
Steinacker, Petra   +11 more
core   +1 more source

The Molecular Chaperone Artemin Efficiently Blocks Fibrillization of TAU Protein In Vitro

open access: yesCell Journal, 2017
Objective: Aggregation of the TAU proteins in the form of neurofibrillary tangles (NFTs) in the brain is a common risk factor in tauopathies including Alzheimer’s disease (AD).
Zahra Khosravi   +4 more
doaj   +1 more source

TTBK2: A Tau Protein Kinase beyond Tau Phosphorylation [PDF]

open access: yesBioMed Research International, 2015
Tau tubulin kinase 2 (TTBK2) is a kinase known to phosphorylate tau and tubulin. It has recently drawn much attention due to its involvement in multiple important cellular processes. Here, we review the current understanding of TTBK2, including its sequence, structure, binding sites, phosphorylation substrates, and cellular processes involved.
Liao, Jung-Chi   +4 more
openaire   +2 more sources

Analytical performance and clinical utility of the INNOTEST (R) PHOSPHO-TAU(181P) assay for discrimination between Alzheimer's disease and dementia with Lewy bodies [PDF]

open access: yes, 2006
Background: Total tau (T-tau) and beta-amyloid((1-42)) (A beta(1-42)) levels in cerebrospinal fluid (CSF) can differentiate Alzheimer's disease (AD) from normal aging or depressive pseudo-dementia.
Bläser, Miriam   +64 more
core   +2 more sources

Folding of the Tau Protein on Microtubules

open access: yesAngewandte Chemie International Edition, 2015
Abstract Microtubules are regulated by microtubule‐associated proteins. However, little is known about the structure of microtubule‐associated proteins in complex with microtubules. Herein we show that the microtubule‐associated protein Tau, which is intrinsically disordered in solution, locally folds into a stable structure upon ...
Kadavath, Harindranath   +5 more
openaire   +6 more sources

Tau pathology is present in vivo and develops in vitro in sensory neurons from human P301S Tau transgenic mice : a system for screening drugs against tauopathies [PDF]

open access: yes, 2015
Intracellular tau aggregates are the neuropathological hallmark of several neurodegenerative diseases, including Alzheimer's disease, progressive supranuclear palsy, and cases of frontotemporal dementia, but the link between these aggregates and ...
Horne, Graeme   +10 more
core   +1 more source

Distinct tau fibril types and their role in prion diseases [PDF]

open access: yes, 2023
Neurodegenerative diseases are often characterized by the co-deposition of different amyloidogenic proteins, normally defining distinct proteinopathies.
CELAURO, LUIGI
core  

The regulatory effect of Tau protein on polymerization of MCF7 microtubules in vitro

open access: yesBiochemistry and Biophysics Reports, 2019
Growing evidence continues to point toward the critical role of beta tubulin isotypes in regulating some intracellular functions. Changes that were observed in the microtubules’ intrinsic dynamics, the way they interact with some chemotherapeutic agents,
Mitra Shojania Feizabadi   +3 more
doaj   +1 more source

MARK4 enhances stress granule formation under oxidative stress and increases tau accumulation. [PDF]

open access: yesFEBS Open Bio
MARK4 (red dots) localizes to stress granules (orange dots) and promotes their formation under oxidative stress by modulating TIA1 (blue dots). MARK4 and TIA1 synergistically increase tau (purple) accumulation, and the reduction of the TIA1 ortholog suppresses neurodegeneration in a fly model.
Nakajima S   +8 more
europepmc   +2 more sources

Home - About - Disclaimer - Privacy