Article
Sites of phosphorylation in tau and factors affecting their regulation.
Biochemical Society symposium - 1 Jan 2001
Anderton B H, Betts J, Blackstock W P, Brion J P, Chapman S, Connell J, Dayanandan R, Gallo J M, Gibb G, Hanger D P, Hutton M, Kardalinou E, Leroy K, Lovestone S, Mack T, Reynolds C H, Van Slegtenhorst M
Abstract excerpt
The microtubule-associated protein, tau, is the principal component of paired helical filaments (PHFs) in Alzheimer's disease. PHF-tau is highly phosphorylated and a total of 25 sites of phosphorylation have so far been identified. Many of these sites are serine or threonine residues that are immediately followed in the sequence by proline residues, and hence are candidate phosphorylation sites for...
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