The microtubule associated protein tau plays a crucial role in Alzheimer's disease and in many neurodegenerative disorders collectively known as tauopathies. Recently, tau pathology has been also documented in prion diseases although the possible molecular events linking these two proteins are still unknown. We have investigated the fate of normal cellular prion protein (PrP(C)) in primary cort...

‎Let $R$ be a $*$-prime ring with center‎ ‎$Z(R)$‎, ‎$d$ a non-zero $(sigma,tau)$-derivation of $R$ with associated‎ ‎automorphisms $sigma$ and $tau$ of $R$‎, ‎such that $sigma$‎, ‎$tau$‎ ‎and $d$ commute with $'*'$‎. ‎Suppose that $U$ is an ideal of $R$ such that $U^*=U$‎, ‎and $C_{sigma,tau}={cin‎ ‎R~|~csigma(x)=tau(x)c~mbox{for~all}~xin R}.$ In the present paper‎, ‎it is shown that if charac...

Tau is a microtubule-associated protein that is important for establishing and maintaining neuronal morphology. In addition to its role in normal cells, tau protein is involved in many neurodegenerative diseases, e.g. Alzheimer's disease (AD) and frontotemporal dementia, as the main component of intraneuronal aggregates. Alternative splicing of tau gene in the brain can give rise to at least si...

Tau protein is an integral component of paired helical filaments, a pathological feature of Alzheimer's disease. tau extracted from these filaments displays decreased electrophoretic mobility due to aberrant phosphorylation. Here we show that recombinant human tau can be phosphorylated by cAMP-dependent protein kinase resulting in decreased electrophoretic mobility. Phosphorylation of tau by cA...

Tau protein, a neuronal microtubule-associated protein is phosphorylated on several sites when extracted from brain tissue and is a substrate for many protein kinases in vitro. In Alzheimer's disease it becomes hyperphosphorylated, notably at Ser-Pro or Thr-Pro motifs, and forms the paired helical filaments (PHFs). The increased phosphorylation can be detected by several antibodies raised again...

The structure, dynamic behavior, and spatial organization of microtubules are regulated by microtubule-associated proteins. An important microtubule-associated protein is the protein Tau, because its microtubule interaction is impaired in the course of Alzheimer's disease and several other neurodegenerative diseases. Here, we show that Tau binds to microtubules by using small groups of evolutio...

Following our discovery of a fragment from the repeat domain of tau protein as a structural constituent of the PHF-core in Alzheimer's disease (AD), we developed an assay that captured several key features of the aggregation process. Tau-tau binding through the core tau fragment could be blocked by the same diaminophenothiazines found to dissolve proteolytically stable PHFs isolated from AD bra...

Alzheimer's disease (AD) brains contain neurofibrillary tangles (NFTs) composed of abnormally hyperphosphorylated tau protein. Regional reductions in cerebral glucose metabolism correlating to NFT densities have been reported in AD brains. Assuming that reduced glucose metabolism might cause abnormal tau hyperphosphorylation, we induced in vivo alterations of glucose metabolism in mice by starv...

Immunotherapies for various neurodegenerative diseases have recently emerged as a promising approach for clearing pathological protein conformers in these disorders. This type of treatment has not been assessed in models that develop neuronal tau aggregates as observed in frontotemporal dementia and Alzheimer's disease. Here, we present that active immunization with a phosphorylated tau epitope...