Ser-262 in human recombinant tau protein is a markedly more favorable site for phosphorylation by CaMKII than PKA or PhK. (Q48360366)

11 February 2018

title

Ser-262 in human recombinant tau protein is a markedly more favorable site for phosphorylation by CaMKII than PKA or PhK. (English)

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11 February 2018

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J J Sironi

1

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11 February 2018

S H Yen

2

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11 February 2018

J A Gondal

3

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11 February 2018

Q Wu

4

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11 February 2018

I Grundke-Iqbal

5

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11 February 2018

K Iqbal

6

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11 February 2018

language of work or name

English

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publication date

1 October 1998

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11 February 2018

published in

FEBS Letters

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11 February 2018

volume

436

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11 February 2018

issue

3

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11 February 2018

page(s)

471-475

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11 February 2018

Microtubule-associated proteins: their potential role in determining neuronal morphology

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Tau protein binds to microtubules through a flexible array of distributed weak sites

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

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Phosphorylation of Ser262 strongly reduces binding of tau to microtubules: distinction between PHF-like immunoreactivity and microtubule binding.

21 January 2018

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Microtubule-associated protein/microtubule affinity-regulating kinase (p110mark). A novel protein kinase that regulates tau-microtubule interactions and dynamic instability by phosphorylation at the Alzheimer-specific site serine 262

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Alzheimer paired helical filaments. Restoration of the biological activity by dephosphorylation

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MARK, a novel family of protein kinases that phosphorylate microtubule-associated proteins and trigger microtubule disruption

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Phosphorylation of microtubule-associated protein tau on Ser 262 by an embryonic 100 kDa protein kinase

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Phosphorylation by neuronal cdc2-like protein kinase promotes dimerization of Tau protein in vitro

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Rapid Alzheimer-like phosphorylation of tau by the synergistic actions of non-proline-dependent protein kinases and GSK-3.

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The subunit structure of rabbit-skeletal-muscle phosphorylase kinase, and the molecular basis of its activation reactions

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Detection of Phosphorylated Ser262 in Fetal Tau, Adult Tau, and Paired Helical Filament Tau

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Activation of Ca2+/calmodulin-dependent protein kinase II by stimulation with bradykinin in neuroblastoma x glioma hybrid NG108-15 cells

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Protein kinase C and calcium/calmodulin-dependent protein kinase II phosphorylate three-repeat and four-repeat tau isoforms at different rates

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Tau in paired helical filaments is functionally distinct from fetal tau: assembly incompetence of paired helical filament-tau

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Calcium/calmodulin-dependent protein kinase II phosphorylates tau at Ser-262 but only partially inhibits its binding to microtubules

21 January 2018

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Recognition of the minimal epitope of monoclonal antibody Tau-1 depends upon the presence of a phosphate group but not its location

21 January 2018

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1 Assays of protein kinase

21 January 2018

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Differential phosphorylation of tau by cyclic AMP-dependent protein kinase and Ca2+/calmodulin-dependent protein kinase II: metabolic and functional consequences

21 January 2018

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inferred from DOI database lookup

7 January 2021

based on heuristic

Identifiers

DOI

10.1016/S0014-5793(98)01185-5

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11 February 2018

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11 February 2018