(Q48261325)

10 February 2018

title

The order of exposure of tau to signal transduction kinases alters the generation of "AD-like" phosphoepitopes. (English)

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10 February 2018

author name string

T B Shea

series ordinal

1

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10 February 2018

C M Cressman

series ordinal

2

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10 February 2018

publication date

1 April 1999

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10 February 2018

Cellular and Molecular Neurobiology

published in

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10 February 2018

volume

19

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10 February 2018

page(s)

223-233

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10 February 2018

issue

2

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10 February 2018

https://scigraph.springernature.com/pub.10.1023/a:1006977127422

exact match

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cites work

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Brain proline-directed protein kinase phosphorylates tau on sites that are abnormally phosphorylated in tau associated with Alzheimer's paired helical filaments.

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Potentiation of GSK-3-catalyzed Alzheimer-like phosphorylation of human tau by cdk5.

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Application of synthetic phospho- and unphospho- peptides to identify phosphorylation sites in a subregion of the tau molecule, which is modified in Alzheimer's disease.

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Phosphorylation of microtubule-associated protein tau: identification of the site for Ca2(+)-calmodulin dependent kinase and relationship with tau phosphorylation in Alzheimer tangles.

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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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p44mpk MAP kinase induces Alzheimer type alterations in tau function and in primary hippocampal neurons.

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Glycogen synthase kinase-3 and the Alzheimer-like state of microtubule-associated protein tau.

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p42 MAP kinase phosphorylation sites in microtubule-associated protein tau are dephosphorylated by protein phosphatase 2A1. Implications for Alzheimer's disease [corrected]

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Respective roles of neurofilaments, microtubules, MAP1B, and tau in neurite outgrowth and stabilization

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Proline-directed phosphorylation of human Tau protein.

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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

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Tau domains, phosphorylation, and interactions with microtubules.

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Epitope mapping of monoclonal antibodies to the paired helical filaments of Alzheimer's disease: identification of phosphorylation sites in tau protein

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Modulation of GSK-3-catalyzed phosphorylation of microtubule-associated protein tau by non-proline-dependent protein kinases.

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Implication of brain cdc2 and MAP2 kinases in the phosphorylation of tau protein in Alzheimer's disease.

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The protein kinase C activator phorbol-12-myristate-13-acetate enhances cyclic AMP accumulation in pheochromocytoma cells

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Networking with proline-directed protein kinases implicated in tau phosphorylation

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Separation of the different microtubule-associated tau protein species from bovine brain and their mode II phosphorylation by Ca2+/phospholipid-dependent protein kinase C.

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The switch of tau protein to an Alzheimer-like state includes the phosphorylation of two serine-proline motifs upstream of the microtubule binding region

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Mitogen-activated protein kinases: versatile transducers for cell signaling

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Microtubule-associated protein tau is required for axonal neurite elaboration by neuroblastoma cells.

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Opposing influences of protein kinase activities on neurite outgrowth in human neuroblastoma cells: initiation by kinase A and restriction by kinase C

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Hyperphosphorylation of the cytoskeletal protein Tau by the MAP-kinase PK40erk2: regulation by prior phosphorylation with cAMP-dependent protein kinase A.

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Proline-directed and non-proline-directed phosphorylation of PHF-tau.

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12 December 2020

Abnormal Alzheimer-like phosphorylation of tau-protein by cyclin-dependent kinases cdk2 and cdk5

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12 December 2020

The abnormal phosphorylation of tau protein at Ser-202 in Alzheimer disease recapitulates phosphorylation during development

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12 December 2020

Phospholipids alter tau conformation, phosphorylation, proteolysis, and association with microtubules: implication for tau function under normal and degenerative conditions.

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12 December 2020

Hyperphosphorylation of human TAU by brain kinase PK40erk beyond phosphorylation by cAMP-dependent PKA: relation to Alzheimer's disease.

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Regulation of the MAP kinase cascade in PC12 cells: B-Raf activates MEK-1 (MAP kinase or ERK kinase) and is inhibited by cAMP

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Calcium influx into human neuroblastoma cells induces ALZ-50 immunoreactivity: involvement of calpain-mediated hydrolysis of protein kinase C

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12 December 2020

Hyperphosphorylation of Tau and filopodial retraction following microinjection of protein kinase C catalytic subunits

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12 December 2020

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12 December 2020

A serine-->proline change in the Alzheimer's disease-associated epitope Tau 2 results in altered secondary structure, but phosphorylation overcomes the conformational gap

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12 December 2020

PHF-tau from Alzheimer's brain comprises four species on SDS-PAGE which can be mimicked by in vitro phosphorylation of human brain tau by glycogen synthase kinase-3 beta.

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12 December 2020

Phosphorylation of tau proteins to a state like that in Alzheimer's brain is catalyzed by a calcium/calmodulin-dependent kinase and modulated by phospholipids.

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12 December 2020

Phosphorylation events mediated by protein kinase C alpha and epsilon participate in regulation of tau steady-state levels and generation of certain "Alzheimer-like" phospho-epitopes.

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12 December 2020

Abnormal tau phosphorylation at Ser396 in Alzheimer's disease recapitulates development and contributes to reduced microtubule binding.

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12 December 2020

Stimulation of MAP kinase by v-raf transformation of fibroblasts fails to induce hyperphosphorylation of transfected tau.

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12 December 2020

Tau protein kinase II is involved in the regulation of the normal phosphorylation state of tau protein.

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12 December 2020

Identifiers

DOI

10.1023/A:1006977127422

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10 February 2018

Dimensions Publication ID

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10 February 2018