Serum Tau Proteins as Potential Biomarkers for the Assessment of Alzheimer's Disease Progression. [PDF]
Total tau (t-tau) and phosphorylated tau (p-tau) protein elevations in cerebrospinal fluid (CFS) are well-established hallmarks of Alzheimer’s disease (AD), while the associations of serum t-tau and p-tau levels with AD have been inconsistent across ...
Nam E, Lee YB, Moon C, Chang KA.
europepmc +2 more sources
Spread of pathological tau proteins through communicating neurons in human Alzheimer's disease. [PDF]
Tau is a hallmark pathology of Alzheimer’s disease, and animal models have suggested that tau spreads from cell to cell through neuronal connections, facilitated by β-amyloid (Aβ). We test this hypothesis in humans using an epidemic spreading model (ESM)
Vogel JW +8 more
europepmc +2 more sources
RNA binding proteins co-localize with small tau inclusions in tauopathy
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 +2 more sources
Role of Amyloid-β and Tau Proteins in Alzheimer's Disease: Confuting the Amyloid Cascade. [PDF]
The “Amyloid Cascade Hypothesis” has dominated the Alzheimer’s disease (AD) field in the last 25 years. It posits that the increase of amyloid-β (Aβ) is the key event in AD that triggers tau pathology followed by neuronal death and eventually, the ...
Gulisano W +11 more
europepmc +2 more sources
Deletion of endogenous Tau proteins is not detrimental in Drosophila. [PDF]
Human Tau (hTau) is a highly soluble and natively unfolded protein that binds to microtubules within neurons. Its dysfunction and aggregation into insoluble paired helical filaments is involved in the pathogenesis of Alzheimer’s disease (AD ...
Burnouf S +9 more
europepmc +2 more sources
Intravenous Injection of PHF-Tau Proteins From Alzheimer Brain Exacerbates Neuroinflammation, Amyloid Beta, and Tau Pathologies in 5XFAD Transgenic Mice [PDF]
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
Competing protein-protein interactions regulate binding of Hsp27 to its client protein tau [PDF]
Small heat shock proteins (sHSPs) limit the aggregation of proteins, such as tau. Here the authors show that Hsp27 recognizes two aggregation-prone regions of tau and that this interaction competes with Hsp27 oligomerization.
Rebecca Freilich +8 more
doaj +3 more sources
Amyloid Beta and Tau Cooperate to Cause Reversible Behavioral and Transcriptional Deficits in a Model of Alzheimer’s Disease [PDF]
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
Tau Proteins and Tauopathies in Alzheimer's Disease. [PDF]
Chong FP, Ng KY, Koh RY, Chye SM.
europepmc +2 more sources
Autophagy and Tau Protein [PDF]
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

