Results 11 to 20 of about 110,474 (301)

Cerebrospinal fluid tau levels are associated with abnormal neuronal plasticity markers in Alzheimer’s disease

open access: yesMolecular Neurodegeneration, 2022
Background Increased total tau (t-tau) in cerebrospinal fluid (CSF) is a key characteristic of Alzheimer’s disease (AD) and is considered to result from neurodegeneration.
Pieter Jelle Visser   +29 more
doaj   +1 more source

Alzheimer PHF-tau aggregates do not spread tau pathology to the brain via the Retino-tectal projection after intraocular injection in male mouse models

open access: yesNeurobiology of Disease, 2022
Neurofibrillary tangles (NFT), a neuronal lesion found in Alzheimer's disease (AD), are composed of fibrillary aggregates of modified forms of tau proteins.
M.-A. de Fisenne   +7 more
doaj   +1 more source

Tau: A Signaling Hub Protein [PDF]

open access: yesFrontiers in Molecular Neuroscience, 2021
Over four decades ago,in vitroexperiments showed that tau protein interacts with and stabilizes microtubules in a phosphorylation-dependent manner. This observation fueled the widespread hypotheses that these properties extend to living neurons and that reduced stability of microtubules represents a major disease-driving event induced by pathological ...
Rebecca L. Mueller   +11 more
openaire   +4 more sources

Predicting AT(N) pathologies in Alzheimer’s disease from blood-based proteomic data using neural networks

open access: yesFrontiers in Aging Neuroscience, 2022
Background and objectiveBlood-based biomarkers represent a promising approach to help identify early Alzheimer’s disease (AD). Previous research has applied traditional machine learning (ML) to analyze plasma omics data and search for potential ...
Yuting Zhang   +30 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   +3 more sources

The novel MAPT mutation K298E:mechanisms of mutant tau toxicity, brain pathology and tau expression in induced fibroblast-derived neurons [PDF]

open access: yes, 2013
Frontotemporal lobar degeneration (FTLD) is the one of the most frequent neurodegenerative disorders characterized by behavioral and executive impairment, language disorders and motor dysfunction.
Holton, Janice L.   +27 more
core   +1 more source

RNA binding proteins co-localize with small tau inclusions in tauopathy

open access: yesActa Neuropathologica Communications, 2018
The development of insoluble, intracellular neurofibrillary tangles composed of the microtubule-associated protein tau is a defining feature of tauopathies, including Alzheimer’s disease (AD).
Brandon F. Maziuk   +11 more
doaj   +1 more source

Fibril-forming motifs are essential and sufficient for the fibrillization of human Tau. [PDF]

open access: yesPLoS ONE, 2012
BACKGROUND: The misfolding of amyloidogenic proteins including human Tau protein, human prion protein, and human α-synuclein is involved in neurodegenerative diseases such as Alzheimer disease, prion disease, and Parkinson disease.
Sheng-Rong Meng   +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 ...
Cepek, L.   +15 more
core   +1 more source

EFhd2 Affects Tau Liquid–Liquid Phase Separation

open access: yesFrontiers in Neuroscience, 2019
The transition of tau proteins from its soluble physiological conformation to the pathological aggregate forms found in Alzheimer’s disease and related dementias, is poorly understood.
Irving E. Vega   +6 more
doaj   +1 more source

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