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Tau Proteins and Neurofibrillary Degeneration
Author(s) -
Goedert M.,
Spillantini M. G.,
Crowther R. A.
Publication year - 1991
Publication title -
brain pathology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.986
H-Index - 132
eISSN - 1750-3639
pISSN - 1015-6305
DOI - 10.1111/j.1750-3639.1991.tb00671.x
Subject(s) - microtubule , tau protein , protein filament , biophysics , chemistry , neurofibrillary tangle , microtubule associated protein , intermediate filament , alzheimer's disease , senile plaques , biology , neuroscience , microbiology and biotechnology , cytoskeleton , pathology , biochemistry , disease , medicine , cell
The paired helical filament is the major fibrous component of neurofibrillary pathology in Alzheimer's disease. Over the last three years evidence has accumulated that the microtubule‐associated protein tau forms an important, if not the sole, constituent of the paired helical filament. Tau protein in normal brain is bound to axonal microtubules by a tandem repeat region. In Alzheimer's disease a proportion of tau protein becomes abnormally phos‐phorylated and is no longer associated with axonal microtubules but instead accumulates in paired helical filaments throughout affected nerve cells. The tandem repeat region contributes substantially to the structural core of the paired helical filament, around which the amino‐terminal half of the molecule forms a disordered coat.

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