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Tau Protein and the Neurofibrillary Pathology of Alzheimer's Disease
Author(s) -
GOEDERT M.
Publication year - 1996
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1111/j.1749-6632.1996.tb34410.x
Subject(s) - senile plaques , tau protein , neurofibrillary tangle , pathology , alzheimer's disease , neuropil , chemistry , neuroscience , neurite , neurofilament , disease , biology , medicine , in vitro , biochemistry , central nervous system , immunohistochemistry
Abundant neurofibrillary tangles, neuropil threads and senile plaque neurites constitute the neurofibrillary pathology of Alzheimer's disease. They form in the nerve cells that undergo degeneration in the disease, in which their regional distribution correlates with the degree of dementia. Each lesion contains the paired helical filament (PHF) as its major component. PHFs are composed of the microtubule‐associated protein tau in a hyperphosphorylated state. PHF‐tau is hyperphosphorylated on all six adult brain isoforms. As a consequence, tau is unable to bind to microtubules and is believed to self‐assemble into the PHF. Several candidate protein kinases and protein phosphatases have been identified through in vitro experiments.