(Q44627791)

4 December 2017

title

Pin1 colocalization with phosphorylated tau in Alzheimer's disease and other tauopathies (English)

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4 December 2017

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2

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4 December 2017

author name string

Pankajavalli Ramakrishnan

series ordinal

1

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4 December 2017

Peter Davies

series ordinal

3

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4 December 2017

language of work or name

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1 November 2003

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4 December 2017

published in

Neurobiology of Disease

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4 December 2017

volume

14

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4 December 2017

issue

2

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4 December 2017

page(s)

251-264

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New insights into progressive supranuclear palsy

4 December 2017

cites work

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Tau protein isoforms, phosphorylation and role in neurodegenerative disorders11These authors contributed equally to this work

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The mitotic peptidyl-prolyl isomerase, Pin1, interacts with Cdc25 and Plx1

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Cdc2 phosphorylation of nucleolin demarcates mitotic stages and Alzheimer's disease pathology

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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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Tau mutations in frontotemporal dementia FTDP-17 and their relevance for Alzheimer's disease

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Inverse association of Pin1 and tau accumulation in Alzheimer's disease hippocampus

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Mutation-specific functional impairments in distinct tau isoforms of hereditary FTDP-17.

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Mitotic activation: a convergent mechanism for a cohort of neurodegenerative diseases

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Association of missense and 5'-splice-site mutations in tau with the inherited dementia FTDP-17

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The endogenous and cell cycle-dependent phosphorylation of tau protein in living cells: implications for Alzheimer's disease

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

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A Conformation‐ and Phosphorylation‐Dependent Antibody Recognizing the Paired Helical Filaments of Alzheimer's Disease

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A human peptidyl-prolyl isomerase essential for regulation of mitosis

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The prolyl isomerase Pin1 restores the function of Alzheimer-associated phosphorylated tau protein

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Cell cycle-dependent phosphorylation and microtubule binding of tau protein stably transfected into Chinese hamster ovary cells.

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Mitotic phosphorylation of tau protein in neuronal cell lines resembles phosphorylation in Alzheimer's disease

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Double immunolabeling of neuropeptides in the human hypothalamus as analyzed by confocal laser scanning fluorescence microscopy

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7 January 2021

The essential mitotic peptidyl-prolyl isomerase Pin1 binds and regulates mitosis-specific phosphoproteins

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7 January 2021

The molecular genetics of the tauopathies

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7 January 2021

Aberrant expression of mitotic cdc2/cyclin B1 kinase in degenerating neurons of Alzheimer's disease brain

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7 January 2021

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Mitotic phosphoepitopes precede paired helical filaments in Alzheimer's disease

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Cloning of cDNAs for M-phase phosphoproteins recognized by the MPM2 monoclonal antibody and determination of the phosphorylated epitope

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7 January 2021

Requirement of the prolyl isomerase Pin1 for the replication checkpoint

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7 January 2021

Sequence-specific and phosphorylation-dependent proline isomerization: a potential mitotic regulatory mechanism

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7 January 2021

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

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7 January 2021

Pin1-dependent prolyl isomerization regulates dephosphorylation of Cdc25C and tau proteins

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7 January 2021

Phosphorylation-dependent prolyl isomerization: a novel signaling regulatory mechanism.

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7 January 2021

10.1016/S0969-9961(03)00109-8

Identifiers

DOI

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4 December 2017

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