Novel Phosphorylation Sites in Tau from Alzheimer Brain Support a Role for Casein Kinase 1 in Disease Pathogenesis

Tau in Alzheimer disease brain is highly phosphorylated and aggregated into paired helical filaments comprising characteristic neurofibrillary tangles. Here we have analyzed insoluble Tau (PHF-tau) extracted from Alzheimer brain by mass spectrometry and identified 11 novel phosphorylation sites, 10...

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Veröffentlicht in:	The Journal of biological chemistry 2007-08, Vol.282 (32), p.23645-23654
Hauptverfasser:	Hanger, Diane P., Byers, Helen L., Wray, Selina, Leung, Kit-Yi, Saxton, Malcolm J., Seereeram, Anjan, Reynolds, C. Hugh, Ward, Malcolm A., Anderton, Brian H.
Format:	Artikel
Sprache:	eng
Schlagworte:	Alzheimer Disease - metabolism Amino Acid Sequence Animals Brain - embryology Brain - metabolism Brain - pathology Casein Kinase Idelta - chemistry Casein Kinase Idelta - metabolism Glycogen Synthase Kinase 3 - metabolism Glycogen Synthase Kinase 3 beta Humans Models, Biological Molecular Sequence Data Neurons - metabolism Protein Binding Protein Isoforms Rats Recombinant Proteins - chemistry tau Proteins - chemistry
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