Inactivation of the mouse Atxn3 (ataxin-3) gene increases protein ubiquitination
about
Machado-Joseph Disease: from first descriptions to new perspectives.Valosin-containing protein (VCP/p97) is an activator of wild-type ataxin-3Crystal structure of a Josephin-ubiquitin complex: evolutionary restraints on ataxin-3 deubiquitinating activityMouse models of polyglutamine diseases in therapeutic approaches: review and data table. Part II.Silencing mutant ataxin-3 rescues motor deficits and neuropathology in Machado-Joseph disease transgenic miceUbe2w and ataxin-3 coordinately regulate the ubiquitin ligase CHIPTargeting several CAG expansion diseases by a single antisense oligonucleotideTherapeutic prospects for spinocerebellar ataxia type 2 and 3.Trinucleotide repeats: a structural perspectiveAllele-specific RNA silencing of mutant ataxin-3 mediates neuroprotection in a rat model of Machado-Joseph disease.Dissociated fear and spatial learning in mice with deficiency of ataxin-2Evaluation of Antisense Oligonucleotides Targeting ATXN3 in SCA3 Mouse ModelsAtaxin-3 promotes genome integrity by stabilizing Chk1.Ataxin-3 plays a role in mouse myogenic differentiation through regulation of integrin subunit levelsSplice isoforms of the polyglutamine disease protein ataxin-3 exhibit similar enzymatic yet different aggregation properties.Absence of ataxin-3 leads to enhanced stress response in C. elegans.An optimal ubiquitin-proteasome pathway in the nervous system: the role of deubiquitinating enzymes.RNA interference mitigates motor and neuropathological deficits in a cerebellar mouse model of Machado-Joseph diseaseActivity and cellular functions of the deubiquitinating enzyme and polyglutamine disease protein ataxin-3 are regulated by ubiquitination at lysine 117.Systematic analysis of the physiological importance of deubiquitinating enzymes.Dominant negative effect of polyglutamine expansion perturbs normal function of ataxin-3 in neuronal cells.Inactivation of PNKP by mutant ATXN3 triggers apoptosis by activating the DNA damage-response pathway in SCA3Role of inositol 1,4,5-trisphosphate receptors in pathogenesis of Huntington's disease and spinocerebellar ataxiasBalancing act: deubiquitinating enzymes in the nervous system.The role of the mammalian DNA end-processing enzyme polynucleotide kinase 3'-phosphatase in spinocerebellar ataxia type 3 pathogenesis.Toward understanding Machado-Joseph diseaseThe Machado-Joseph Disease Deubiquitinase Ataxin-3 Regulates the Stability and Apoptotic Function of p53Basal and stress-induced Hsp70 are modulated by ataxin-3.The deubiquitinase ataxin-3 requires Rad23 and DnaJ-1 for its neuroprotective role in Drosophila melanogaster.Inositol 1,4,5-tripshosphate receptor, calcium signaling, and polyglutamine expansion disorders.Toward RNAi therapy for the polyglutamine disease Machado-Joseph diseaseSilencing mutant ATXN3 expression resolves molecular phenotypes in SCA3 transgenic miceEmerging pathogenic pathways in the spinocerebellar ataxias.The de-ubiquitinating enzyme ataxin-3 does not modulate disease progression in a knock-in mouse model of Huntington disease.Current understanding on the pathogenesis of polyglutamine diseases.Genetically engineered mouse models of the trinucleotide-repeat spinocerebellar ataxias.RNA therapy for polyglutamine neurodegenerative diseases.Deubiquitylases from genes to organism.Ataxin-3 protein and RNA toxicity in spinocerebellar ataxia type 3: current insights and emerging therapeutic strategies.Allele-selective suppression of mutant genes in polyglutamine diseases.
P2860
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P2860
Inactivation of the mouse Atxn3 (ataxin-3) gene increases protein ubiquitination
description
2007 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 2007
@ast
im Oktober 2007 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2007/10/26)
@sk
vědecký článek publikovaný v roce 2007
@cs
wetenschappelijk artikel (gepubliceerd op 2007/10/26)
@nl
наукова стаття, опублікована в жовтні 2007
@uk
مقالة علمية (نشرت في 26-10-2007)
@ar
name
Inactivation of the mouse Atxn3 (ataxin-3) gene increases protein ubiquitination
@ast
Inactivation of the mouse Atxn3 (ataxin-3) gene increases protein ubiquitination
@en
Inactivation of the mouse Atxn3 (ataxin-3) gene increases protein ubiquitination
@nl
type
label
Inactivation of the mouse Atxn3 (ataxin-3) gene increases protein ubiquitination
@ast
Inactivation of the mouse Atxn3 (ataxin-3) gene increases protein ubiquitination
@en
Inactivation of the mouse Atxn3 (ataxin-3) gene increases protein ubiquitination
@nl
prefLabel
Inactivation of the mouse Atxn3 (ataxin-3) gene increases protein ubiquitination
@ast
Inactivation of the mouse Atxn3 (ataxin-3) gene increases protein ubiquitination
@en
Inactivation of the mouse Atxn3 (ataxin-3) gene increases protein ubiquitination
@nl
P2093
P1476
Inactivation of the mouse Atxn3 (ataxin-3) gene increases protein ubiquitination
@en
P2093
Bernd O. Evert
Hassan Khazneh
Ina Schmitt
Marion Linden
Peter Breuer
Ullrich Wuellner
P304
P356
10.1016/J.BBRC.2007.08.062
P407
P577
2007-10-26T00:00:00Z