There is now a considerable body of experimental evidence that Parkinson's disease arises through physiological interaction of causative molecules, leading to tau pathology. In this review, we discuss the physiological role of α-synuclein and LRRK2 in the abnormal phosphorylation of tau. In addition, as recent reports have indicated that heat shock proteins- (HSPs-) inducing drugs can help to a...

Tau protein is the primary constituent of protein aggregates known as neurofibrillary tangles, a pathological hallmark of Alzheimer's disease (AD). Previous studies suggest that tau protein may play a contributing role in neurodegenerative diseases such as AD. Thus characterizing the structural properties of tau is critical to understanding disease pathogenesis. However, obtaining a detailed st...

When the microtubule (MT)-associated protein tau is not bound to axonal MTs, it becomes hyperphosphorylated and vulnerable to proteolytic cleavage and other changes typically seen in the hallmark tau deposits (neurofibrillary tangles) of tau-associated neurodegenerative diseases (tauopathies). Neurofibrillary tangle formation is preceded by tau oligomerization and accompanied by covalent crossl...

Intraneuronal aggregation of specific hyperphosphorylated tau isoforms in subsets of neurons may explain many neurodegenerative processes. Only some antibodies including AP422 and AT100 are specific to the abnormal phosphorylation of tau proteins in these processes. AT100-immunoreactivity was never observed in cell models with the exception of Sf9 cells. In the present study, we developed a way...

Abnormal tau hyperphosphorylation is an early pathological marker of Alzheimer's disease (AD), however, the upstream factors that regulate tau phosphorylation are not illustrated and there is no efficient strategy to arrest tau hyperphosphorylation. Here, we find that activation of endogenous EphB2 receptor by ligand stimulation (ephrinB1/Fc) or by ectopic expression of EphB2 plus the ligand st...

Background: Tau phosphorylation affects synaptic transmission, but the underlying mechanism remains elusive. Results: NMDA-receptor activation leads to phosphorylation of endogenous tau, thereby regulating the interaction of tau with Fyn and postsynaptic scaffolding protein PSD95. Conclusions: Phosphorylation of tau controls the interaction of tau with the postsynaptic PSD95/Fyn/NMDA-receptor c...

we first characterize $tau$-complemented modules with relative (pre)-covers. we also introduce an extending module relative to $tau$-pure submodules on a hereditary torsion theory $tau$ and give its relationship with $tau$-complemented modules.

Multiple tau gene mutations are pathogenic for hereditary frontotemporal dementia and parkinsonism linked to chromosome 17 (FTDP-17), with filamentous tau aggregates as the major lesions in the CNS of these patients. Recent studies have shown that bacterially expressed recombinant tau proteins with FTDP-17 missense mutations cause functional impairments, i.e., a reduced ability of mutant tau to...

In this paper, we introduce the notions of expansion of ideals in $MV$-algebras, $ (tau,sigma)- $primary, $ (tau,sigma)$-obstinate  and $ (tau,sigma)$-Boolean  in $ MV- $algebras. We investigate the relations of them. For example, we show that every $ (tau,sigma)$-obstinate ideal of an $ MV-$ algebra is $ (tau,sigma)$-primary  and $ (tau,sigma)$-Boolean. In particular, we define an expansion $ ...

Alpha-synuclein (alpha-syn) and tau polymerize into amyloid fibrils and form intraneuronal filamentous inclusions characteristic of neurodegenerative diseases. We demonstrate that alpha-syn induces fibrillization of tau and that coincubation of tau and alpha-syn synergistically promotes fibrillization of both proteins. The in vivo relevance of these findings is grounded in the co-occurrence of ...