Tau cleavage and dephosphorylation in cerebellar granule neurons undergoing apoptosis (Q24312948)

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4 December 2019

title

Tau cleavage and dephosphorylation in cerebellar granule neurons undergoing apoptosis (English)

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4 December 2019

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microtubule associated protein tau

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GOA release 2020-03-11

enzyme binding

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GOA release 2020-03-11

author

Claudio Brancolini

5

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4 December 2019

author name string

N Canu

1

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4 December 2019

L Dus

2

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4 December 2019

C Barbato

3

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4 December 2019

M T Ciotti

4

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4 December 2019

A M Rinaldi

6

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M Novak

7

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4 December 2019

A Cattaneo

8

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A Bradbury

9

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P Calissano

10

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4 December 2019

language of work or name

English

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publication date

1 September 1998

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4 December 2019

published in

Journal of Neuroscience

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4 December 2019

volume

18

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issue

18

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4 December 2019

page(s)

7061-7074

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Phosphorylation affects the ability of tau protein to promote microtubule assembly.

4 December 2019

cites work

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The phosphorylation state of tau in the developing rat brain is regulated by phosphoprotein phosphatases.

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Adenosine and ADP prevent apoptosis in cultured rat cerebellar granule cells.

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Colchicine induces apoptosis in cerebellar granule cells

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Autoradiographic localization and depolarization-induced release of acidic amino acids in differentiating cerebellar granule cell cultures

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Tau protein function in living cells

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Pituitary adenylate cyclase-activating polypeptide (PACAP-38) protects cerebellar granule neurons from apoptosis by activating the mitogen-activated protein kinase (MAP kinase) pathway.

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Domains of tau protein and interactions with microtubules

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Microtubule organization and dynamics dependent on microtubule-associated proteins

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Analysis of microtubule-associated protein tau glycation in paired helical filaments.

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Evidence for apoptotic cell death in Alzheimer's disease.

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A68: a major subunit of paired helical filaments and derivatized forms of normal Tau.

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Hydrofluoric acid-treated tau PHF proteins display the same biochemical properties as normal tau

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Widespread activation of calcium-activated neutral proteinase (calpain) in the brain in Alzheimer disease: a potential molecular basis for neuronal degeneration

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Co-localization of truncated tau and DNA fragmentation in Alzheimer's disease neurones.

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Specific cleavage of alpha-fodrin during Fas- and tumor necrosis factor-induced apoptosis is mediated by an interleukin-1beta-converting enzyme/Ced-3 protease distinct from the poly(ADP-ribose) polymerase protease

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A novel pool of protein phosphatase 2A is associated with microtubules and is regulated during the cell cycle

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12 December 2020

Detection of phosphorylated Ser262 in fetal tau, adult tau, and paired helical filament tau.

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12 December 2020

Apoptosis in cerebellar granule cells is blocked by high KCl, forskolin, and IGF-1 through distinct mechanisms of action: the involvement of intracellular calcium and RNA synthesis

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Expression of separate isoforms of human tau protein: correlation with the tau pattern in brain and effects on tubulin polymerization

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Brain mu-calpain autolysis during global cerebral ischemia

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Mechanisms and genes of cellular suicide

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Calpain activation in apoptosis

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12 December 2020

Isolation of a fragment of tau derived from the core of the paired helical filament of Alzheimer disease

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Dismantling cell-cell contacts during apoptosis is coupled to a caspase-dependent proteolytic cleavage of beta-catenin.

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Difference between the tau protein of Alzheimer paired helical filament core and normal tau revealed by epitope analysis of monoclonal antibodies 423 and 7.51

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Rat monoclonal antitubulin antibodies derived by using a new nonsecreting rat cell line

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Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskeletal pathology

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Inhibition of activation-induced programmed cell death and restoration of defective immune responses of HIV+ donors by cysteine protease inhibitors

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12 December 2020

Tau consists of a set of proteins with repeated C-terminal microtubule-binding domains and variable N-terminal domains

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Molecular characterization of microtubule-associated proteins tau and MAP2.

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Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease

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12 December 2020

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12 December 2020

Phosphorylation by cAMP-dependent protein kinase inhibits the degradation of tau by calpain

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Calpain inhibitors, but not caspase inhibitors, prevent actin proteolysis and DNA fragmentation during apoptosis

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The tubulin-binding sequence of brain microtubule-associated proteins, tau and MAP-2, is also involved in actin binding

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Interaction between microtubule-associated protein tau and spectrin

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Tau in Alzheimer neurofibrillary tangles. N- and C-terminal regions are differentially associated with paired helical filaments and the location of a putative abnormal phosphorylation site

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Monoclonal antibodies with selective specificity for Alzheimer Tau are directed against phosphatase-sensitive epitopes

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Proteasomes play an essential role in thymocyte apoptosis

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Development of a method for measuring cell number: Application to CNS primary neuronal cultures

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Protein measurement with the Folin phenol reagent

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

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12 December 2020

10.1523/JNEUROSCI.18-18-07061.1998

Identifiers

DOI

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9736630%20AND%20SRC:MED&resulttype=core&format=json

OpenCitations bibliographic resource ID

4 December 2019

904246

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9736630%20AND%20SRC:MED&resulttype=core&format=json

4 December 2019

2 references

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

904246