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tauopathies/prolina
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Pagina 1 a partire dal 48 risultati
MRNA Levels of ACh-Related Enzymes in the Hippocampus of THY-Tau22 Mouse: A Model of Human Tauopathy with No Signs of Motor Disturbance.
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The microtubule-associated protein Tau tends to form aggregates in neurodegenerative disorders referred to as tauopathies. The tauopathy model transgenic (Tg) THY-Tau22 (Tau22) mouse shows disturbed septo-hippocampal transmission, memory deficits and no signs of motor dysfunction. The reports
N-phenylamine derivatives as aggregation inhibitors in cell models of tauopathy.
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Cell models of tauopathy were generated in order to study mechanisms of neurodegeneration involving abnormal changes of tau. They are based on neuroblastoma cell lines (N2a) that inducibly express different forms of the repeat domain of tau (tau(RD)), e.g. the 4-repeat domain of tau with the
'Prion-like' propagation of mouse and human tau aggregates in an inducible mouse model of tauopathy.
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BACKGROUND
Aggregates of the tau protein are a hallmark of Alzheimer's and several other neurodegenerative diseases. Various transgenic mouse models have been generated to study the aggregation process. Since wild-type tau is highly soluble and does not aggregate readily, most models make use of tau
Selective tau tyrosine nitration in non-AD tauopathies.
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Previously, we reported the characterization of two novel antibodies that react with tau nitrated at tyrosine 197 (Tau-nY197) and tyrosine 394 (Tau-nY394) in Alzheimer's disease (AD). In this report, we examined whether tau nitration at these sites also occurs in corticobasal degeneration (CBD),
The protein phosphatase PP2A/Bα binds to the microtubule-associated proteins Tau and MAP2 at a motif also recognized by the kinase Fyn: implications for tauopathies.
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The predominant brain microtubule-associated proteins MAP2 and tau play a critical role in microtubule cytoskeletal organization and function. We have previously reported that PP2A/Bα, a major protein phosphatase 2A (PP2A) holoenzyme, binds to and dephosphorylates tau, and regulates microtubule
Immunophilin FKBP52 induces Tau-P301L filamentous assembly in vitro and modulates its activity in a model of tauopathy.
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The Tau protein is the major component of intracellular filaments observed in a number of neurodegenerative diseases known as tauopathies. The pathological mutant of Tau containing a proline-to-leucine mutation at position 301 (P301L) leads to severe human tauopathy. Here, we assess the impact of
Targeting the ensemble of heterogeneous tau oligomers in cells: A novel small molecule screening platform for tauopathies.
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Effect of Phosphorylation and O-GlcNAcylation on Proline-Rich Domains of Tau.
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Microtubule associated protein Tau (MAPT) is a phospho-protein within neurons of the brain. Aggregation of tau is the leading cause of tauopathies such as Alzheimer's disease. Tau undergoes several post-translational modifications of which phosphorylation and O-GlcNAcylation are key chemical
Analysis of in vivo turnover of tau in a mouse model of tauopathy.
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BACKGROUND
Intracellular accumulation of tau as neurofibrillary tangles (NFTs) is the hallmark of Alzheimer's disease (AD) as well as in other tauopathies. Tau is present not only in the cytoplasm but also in the extracellular space such as cerebrospinal fluid (CSF) and brain interstitial fluid
The beta-propensity of Tau determines aggregation and synaptic loss in inducible mouse models of tauopathy.
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Neurofibrillary lesions are characteristic for a group of human diseases, named tauopathies, which are characterized by prominent intracellular accumulations of abnormal filaments formed by the microtubule-associated protein Tau. The tauopathies are accompanied by abnormal changes in Tau protein,
Inducible expression of Tau repeat domain in cell models of tauopathy: aggregation is toxic to cells but can be reversed by inhibitor drugs.
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We generated several cell models of tauopathy in order to study the mechanisms of neurodegeneration in diseases involving abnormal changes of tau protein. N2a neuroblastoma cell lines were created that inducibly express different variants of the repeat domain of tau (tau(RD)) when exposed to
Inhibition of tau aggregation in cell models of tauopathy.
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The pathological aggregation of tau into paired helical filaments is a hallmark of several neurodegenerative diseases, including Alzheimer's disease. We have generated cell models of tau aggregation in order to study mechanisms involving abnormal changes of tau. In the cell models the repeat domain
Pinning down phosphorylated tau and tauopathies.
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Neurofibrillary tangles (NFTs) are prominent neuronal lesions in a large subset of neurodegenerative diseases, including Alzheimer's disease (AD). NFTs are mainly composed of insoluble Tau that is hyperphosphorylated on many serine or threonine residues preceding proline (pSer/Thr-Pro). Tau
The potential for beta-structure in the repeat domain of tau protein determines aggregation, synaptic decay, neuronal loss, and coassembly with endogenous Tau in inducible mouse models of tauopathy.
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We describe two new transgenic mouse lines for studying pathological changes of Tau protein related to Alzheimer's disease. They are based on the regulatable expression of the four-repeat domain of human Tau carrying the FTDP17 (frontotemporal dementia and parkinsonism linked to chromosome 17)
Ultrastructural alterations of Alzheimer's disease paired helical filaments by grape seed-derived polyphenols.
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Abnormal folding of the microtubule-associated protein tau leads to aggregation of tau into paired helical filaments (PHFs) and neurofibrillary tangles, the major hallmark of Alzheimer's disease (AD). We have recently shown that grape seed polyphenol extract (GSPE) reduces tau pathology in the TMHT
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