(Q28574229)

31 January 2017

title

Phosphorylation of FTDP-17 mutant tau by cyclin-dependent kinase 5 complexed with p35, p25, or p39 (English)

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31 January 2017

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Fumika Sakaue

1

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31 January 2017

Taro Saito

2

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31 January 2017

Yutaka Sato

3

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31 January 2017

Akiko Asada

4

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31 January 2017

Koichi Ishiguro

5

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31 January 2017

Masato Hasegawa

6

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31 January 2017

Shin-ichi Hisanaga

7

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31 January 2017

language of work or name

English

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publication date

9 September 2005

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Journal of Biological Chemistry

31 January 2017

published in

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31 January 2017

volume

280

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31 January 2017

issue

36

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31 January 2017

page(s)

31522–31529

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The significance of tau and alpha-synuclein inclusions in neurodegenerative diseases

31 January 2017

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Tau is a candidate gene for chromosome 17 frontotemporal dementia

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

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

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New phosphorylation sites identified in hyperphosphorylated tau (paired helical filament-tau) from Alzheimer's disease brain using nanoelectrospray mass spectrometry

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Tau proteins with frontotemporal dementia-17 mutations have both altered expression levels and phosphorylation profiles in differentiated neuroblastoma cells.

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Stable expression in Chinese hamster ovary cells of mutated tau genes causing frontotemporal dementia and parkinsonism linked to chromosome 17 (FTDP-17)

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Molecular analysis of mutant and wild-type tau deposited in the brain affected by the FTDP-17 R406W mutation

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Cdk5 is a key factor in tau aggregation and tangle formation in vivo

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Aberrant Cdk5 activation by p25 triggers pathological events leading to neurodegeneration and neurofibrillary tangles

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Conversion of p35 to p25 deregulates Cdk5 activity and promotes neurodegeneration

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Neurotoxicity induces cleavage of p35 to p25 by calpain

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Deregulation of Cdk5 in a mouse model of ALS: toxicity alleviated by perikaryal neurofilament inclusions

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Truncation of CDK5 activator p35 induces intensive phosphorylation of Ser202/Thr205 of human tau.

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Tau phosphorylation by cyclin-dependent kinase 5/p39 during brain development reduces its affinity for microtubules.

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Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa

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Microtubule-stimulated phosphorylation of tau at Ser202 and Thr205 by cdk5 decreases its microtubule nucleation activity.

21 January 2018

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Mutant (R406W) human tau is hyperphosphorylated and does not efficiently bind microtubules in a neuronal cortical cell model

21 January 2018

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Processing of cdk5 Activator p35 to Its Truncated Form (p25) by Calpain in Acutely Injured Neuronal Cells

21 January 2018

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Neurobiology: p25 protein in neurodegeneration

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.M504792200

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Consolidated OpenCitations Corpus – April 2017

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Consolidated OpenCitations Corpus – April 2017

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Consolidated OpenCitations Corpus – April 2017