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Intravenous Injection of PHF-Tau Proteins From Alzheimer Brain Exacerbates Neuroinflammation, Amyloid Beta, and Tau Pathologies in 5XFAD Transgenic Mice [PDF]

open access: yesFrontiers in Molecular Neuroscience, 2020
Alzheimer’s disease (AD) is characterized by the accumulation in the brain of intraneuronal aggregates of abnormally and hyperphosphorylated tau proteins and of extracellular deposits of amyloid-β surrounded by dystrophic neurites.
Sarah Houben   +9 more
doaj   +2 more sources

Amyloid Beta and Tau Cooperate to Cause Reversible Behavioral and Transcriptional Deficits in a Model of Alzheimer’s Disease [PDF]

open access: yesCell Reports, 2019
Summary: A key knowledge gap blocking development of effective therapeutics for Alzheimer’s disease (AD) is the lack of understanding of how amyloid beta (Aβ) peptide and pathological forms of the tau protein cooperate in causing disease phenotypes ...
Eleanor K. Pickett   +29 more
doaj   +5 more sources

Autophagy and Tau Protein [PDF]

open access: yesInternational Journal of Molecular Sciences, 2021
Neurofibrillary tangles, which consist of highly phosphorylated tau protein, and senile plaques (SPs) are pathological hallmarks of Alzheimer’s disease (AD). In swollen axons, many autophagic vacuoles are observed around SP in the AD brain. This suggests that autophagy function is disturbed in AD.
Tadanori Hamano   +6 more
openaire   +2 more sources

Tau interactome and RNA binding proteins in neurodegenerative diseases

open access: yesMolecular Neurodegeneration, 2022
Pathological tau aggregation is a primary neuropathological feature of many neurodegenerative diseases. Intriguingly, despite the common presence of tau aggregates in these diseases the affected brain regions, clinical symptoms, and morphology ...
Tomas Kavanagh   +2 more
doaj   +1 more source

Tau mRNA Metabolism in Neurodegenerative Diseases: A Tangle Journey

open access: yesBiomedicines, 2022
Tau proteins are known to be mainly involved in regulation of microtubule dynamics. Besides this function, which is critical for axonal transport and signal transduction, tau proteins also have other roles in neurons.
Paulo J. da Costa   +3 more
doaj   +1 more source

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

The C291R Tau variant forms different types of protofibrils [PDF]

open access: yes, 2020
Mutations in the MAPT gene can lead to disease-associated variants of tau. However, the pathological mechanisms behind these genetic tauopathies are poorly understood. Here, we characterized the aggregation stages and conformational changes of tau C291R,
Karikari, Thomas K.   +2 more
core   +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

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

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