Cleavage of atrophin-1 at caspase site aspartic acid 109 modulates cytotoxicity (Q22009069)

GOA release 2020-03-11

1

L M

Ellerby

L M Ellerby

1 reference

7 February 2023

R L Andrusiak

2

R L

Andrusiak

1 reference

7 February 2023

C L Wellington

3

C L

Wellington

1 reference

7 February 2023

A S Hackam

4

A S

Hackam

1 reference

7 February 2023

S S Propp

5

S S

Propp

1 reference

7 February 2023

J D Wood

6

J D

Wood

1 reference

7 February 2023

A H Sharp

7

A H

Sharp

1 reference

7 February 2023

R L Margolis

8

R L

Margolis

1 reference

7 February 2023

C A Ross

9

C A

Ross

1 reference

7 February 2023

G S Salvesen

10

G S

Salvesen

1 reference

7 February 2023

M R Hayden

11

M R

Hayden

1 reference

7 February 2023

D E Bredesen

12

D E

Journal of Biological Chemistry

Bredesen

1 reference

7 February 2023

language of work or name

English

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publication date

26 March 1999

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published in

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volume

274

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issue

13

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page(s)

8730-6

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Cloning of the gene for spinocerebellar ataxia 2 reveals a locus with high sensitivity to expanded CAG/glutamine repeats

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Cloning of the SCA7 gene reveals a highly unstable CAG repeat expansion

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Cleavage of huntingtin by apopain, a proapoptotic cysteine protease, is modulated by the polyglutamine tract

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Caspase cleavage of gene products associated with triplet expansion disorders generates truncated fragments containing the polyglutamine tract

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Kennedy's disease: caspase cleavage of the androgen receptor is a crucial event in cytotoxicity

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Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain

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Length of huntingtin and its polyglutamine tract influences localization and frequency of intracellular aggregates

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Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation

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Huntingtin-encoded polyglutamine expansions form amyloid-like protein aggregates in vitro and in vivo

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Suppression of aggregate formation and apoptosis by transglutaminase inhibitors in cells expressing truncated DRPLA protein with an expanded polyglutamine stretch.

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Cell crawling: first the motor, now the transmission

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Truncated N-terminal fragments of huntingtin with expanded glutamine repeats form nuclear and cytoplasmic aggregates in cell culture.

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Transfecting mammalian cells: optimization of critical parameters affecting calcium-phosphate precipitate formation

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DRPLA gene (atrophin-1) sequence and mRNA expression in human brain

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The regulation of anoikis: MEKK-1 activation requires cleavage by caspases

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Molecular ordering of apoptotic mammalian CED-3/ICE-like proteases.

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Target protease specificity of the viral serpin CrmA. Analysis of five caspases

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An unusual specificity in the activation of neutrophil serine proteinase zymogens

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Atrophin-1, the DRPLA gene product, interacts with two families of WW domain-containing proteins

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Huntington disease and the related disorder, dentatorubral-pallidoluysian atrophy (DRPLA).

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Expression of dentatorubral-pallidoluysian atrophy (DRPLA) proteins in patients.

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Dentatorubral pallidoluysian atrophy (DRPLA) protein is cleaved by caspase-3 during apoptosis

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A combinatorial approach defines specificities of members of the caspase family and granzyme B. Functional relationships established for key mediators of apoptosis

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Generation of anti-apoptotic presenilin-2 polypeptides by alternative transcription, proteolysis, and caspase-3 cleavage

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Regional and cellular expression of the dentatorubral-pallidoluysian atrophy gene in brains of normal and affected individuals.

21 January 2018

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Intranuclear neuronal inclusions in Huntington's disease and dentatorubral and pallidoluysian atrophy: correlation between the density of inclusions and IT15 CAG triplet repeat length

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Intranuclear neuronal inclusions: a common pathogenic mechanism for glutamine-repeat neurodegenerative diseases?

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Ataxin-1 with an expanded glutamine tract alters nuclear matrix-associated structures

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Ataxin-1 nuclear localization and aggregation: role in polyglutamine-induced disease in SCA1 transgenic mice.

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