Overexpressed tau protein in cultured cells is phosphorylated without formation of PHF: implication of phosphoprotein phosphatase involvement-Reference-Cited by-同舟云学术

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Overexpressed tau protein in cultured cells is phosphorylated without formation of PHF: implication of phosphoprotein phosphatase involvement

Published:1995-12 Issue:1 Volume:34 Page:1-17
ISSN:0169-328X
Container-title:Molecular Brain Research
language:en
Short-container-title:Molecular Brain Research

Author:

Baum Larry,Seger Rony,Woodgett James R.,Kawabata Shigeki,Maruyama Kei,Koyama Masayasu,Silver Jack,Saitoh Tsunao

Publisher

Elsevier BV

Subject

Cellular and Molecular Neuroscience,Molecular Biology

Reference80 articles.

1. Okadaic acid induces early changes in microtubule-associated protein 2 and τ phosphorylation prior to neurodegeneration in cultured cortical neurons;Arias;J. Neurochem.,1993

2. Casein kinase II is associated with neurofibrillary tangles but is not an intrinsic component of paired helical filaments;Baum;Brain Res.,1992

3. Phosphorylation of ser262 strongly reduces binding of tau to microtubules: distinction between PHF-like immunoreactivity and microtubule binding;Biernat;Neuron,1993

4. The switch of tau protein to an Alzheimer-like state includes the phosphorylation of two serine-proline motifs upstream of the microtubule binding region;Biernat;EMBO J.,1992

5. The distribution of tau in the mammalian central nervous system;Binder;J. Cell Biol.,1985

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