Tyrosine 394 is phosphorylated in Alzheimer's paired helical filament tau and in fetal tau with c-Abl as the candidate tyrosine kinase. (Q40398116)

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30 December 2019

title

Tyrosine 394 is phosphorylated in Alzheimer's paired helical filament tau and in fetal tau with c-Abl as the candidate tyrosine kinase (English)

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Pascal Derkinderen

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author name string

Timothy M E Scales

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Kit-Yi Leung

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Helen L Byers

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Christof Lenz

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Caroline Price

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Timothy Perera

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Richard A Van Etten

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Brian H Anderton

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Stuart Kellie

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language of work or name

English

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publication date

1 July 2005

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30 December 2019

published in

Journal of Neuroscience

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volume

25

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issue

28

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30 December 2019

page(s)

6584-6593

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Cycling, stressed-out and nervous: cellular functions of c-Abl

30 December 2019

cites work

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Interaction of tau with the neural membrane cortex is regulated by phosphorylation at sites that are modified in paired helical filaments

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Cables links Cdk5 and c-Abl and facilitates Cdk5 tyrosine phosphorylation, kinase upregulation, and neurite outgrowth

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

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Abl tyrosine kinase promotes dendrogenesis by inducing actin cytoskeletal rearrangements in cooperation with Rho family small GTPases in hippocampal neurons

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Activation of the neuronal c-Abl tyrosine kinase by amyloid-beta-peptide and reactive oxygen species

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Nonmyristoylated Abl proteins transform a factor-dependent hematopoietic cell line

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Use of vanadate as protein-phosphotyrosine phosphatase inhibitor

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N-terminal mutations activate the leukemogenic potential of the myristoylated form of c-abl

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

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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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The COOH terminus of the c-Abl tyrosine kinase contains distinct F- and G-actin binding domains with bundling activity

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

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12 December 2020

Interaction of tau with the neural plasma membrane mediated by tau's amino-terminal projection domain

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Discovery of a novel, potent, and Src family-selective tyrosine kinase inhibitor. Study of Lck- and FynT-dependent T cell activation

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Recognition and specificity in protein tyrosine kinase-mediated signalling

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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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12 December 2020

10.1523/JNEUROSCI.1487-05.2005

Identifiers

DOI

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30 December 2019

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30 December 2019

PubMed publication ID

16014719

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