(Q52204170)

27 April 2018

title

In situ dephosphorylation of tau by protein phosphatase 2A and 2B in fetal rat primary cultured neurons. (English)

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27 April 2018

author name string

Saito T

1

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27 April 2018

Ishiguro K

2

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27 April 2018

Uchida T

3

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27 April 2018

Miyamoto E

4

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27 April 2018

Kishimoto T

5

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27 April 2018

Hisanaga S

6

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27 April 2018

language of work or name

English

0 references

publication date

1 December 1995

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27 April 2018

published in

FEBS Letters

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27 April 2018

volume

376

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27 April 2018

issue

3

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27 April 2018

page(s)

238-242

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27 April 2018

Purification of tau, a microtubule-associated protein that induces assembly of microtubules from purified tubulin

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Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau

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p42 map kinase phosphorylation sites in microtubule-associated protein tau are dephosphorylated by protein phosphatase 2A1Implications for Alzheimer's disease

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Biopsy-derived adult human brain tau is phosphorylated at many of the same sites as Alzheimer's disease paired helical filament tau.

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Evidence for cdk5 as a Major Activity Phosphorylating Tau Protein in Porcine Brain Extract1

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A serine/threonine proline kinase activity is included in the tau protein kinase fraction forming a paired helical filament epitope

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Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes

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Phosphorylation determines two distinct species of Tau in the central nervous system.

21 January 2018

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A novel pool of protein phosphatase 2A is associated with microtubules and is regulated during the cell cycle

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Dephosphorylation of tau factor by protein phosphatase 2A in synaptosomal cytosol fractions, and inhibition by aluminum

21 January 2018

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10.1016/0014-5793(95)01292-0

21 January 2018

Identifiers

DOI

1 reference

27 April 2018

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27 April 2018