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      Hyperphosphorylation and aggregation of tau in mice expressing normal human tau isoforms.

      Journal of Neurochemistry
      Age Factors, Alternative Splicing, Alzheimer Disease, genetics, metabolism, pathology, Animals, Brain, Brain Chemistry, Dendrites, Disease Models, Animal, Humans, Macromolecular Substances, Mice, Mice, Transgenic, Neurofibrillary Tangles, chemistry, Neurons, Phosphorylation, Protein Isoforms, Reverse Transcriptase Polymerase Chain Reaction, tau Proteins

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          Neurofibrillary tangles are composed of insoluble aggregates of the microtubule-associated protein tau. In Alzheimer's disease the accumulation of neurofibrillary tangles occurs in the absence of tau mutations. Here we present mice that develop pathology from non-mutant human tau, in the absence of other exogenous factors, including beta-amyloid. The pathology in these mice is Alzheimer-like, with hyperphosphorylated tau accumulating as aggregated paired helical filaments. This pathologic tau accumulates in the cell bodies and dendrites of neurons in a spatiotemporally relevant distribution.

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