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

Andorfer, C; Kress, Y; Espinoza, M; de Silva, R; Tucker, KL; Barde, YA; Duff, K; (2003) Hyperphosphorylation and aggregation of tau in mice expressing normal human tau isoforms. J NEUROCHEM , 86 (3) 582 - 590. 10.1046/j.1471-4159.2003.01879.x.

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Abstract

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.

Type: Article
Title: Hyperphosphorylation and aggregation of tau in mice expressing normal human tau isoforms
DOI: 10.1046/j.1471-4159.2003.01879.x
Keywords: aggregation, Alzheimer's disease, non-mutant tau, phosphorylation, transgenic, PAIRED HELICAL FILAMENTS, PROGRESSIVE SUPRANUCLEAR PALSY, ALZHEIMERS-DISEASE, NEUROFIBRILLARY TANGLES, PICKS-DISEASE, NEURODEGENERATIVE DISORDERS, FUNCTIONAL DIFFERENCES, BASAL FOREBRAIN, SENILE DEMENTIA, NUCLEUS BASALIS
UCL classification: UCL > Provost and Vice Provost Offices
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Brain Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Brain Sciences > UCL Queen Square Institute of Neurology
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Brain Sciences > UCL Queen Square Institute of Neurology > Clinical and Movement Neurosciences
URI: http://discovery.ucl.ac.uk/id/eprint/153372
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