Ataxin-1 nuclear localization and aggregation: role in polyglutamine-induced disease in SCA1 transgenic mice.
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Identification of human proteins that modify misfolding and proteotoxicity of pathogenic ataxin-1Nuclear localization of the spinocerebellar ataxia type 7 protein, ataxin-7Cleavage of atrophin-1 at caspase site aspartic acid 109 modulates cytotoxicityThe Huntington's disease protein interacts with p53 and CREB-binding protein and represses transcriptionAtrophin-1, the dentato-rubral and pallido-luysian atrophy gene product, interacts with ETO/MTG8 in the nuclear matrix and represses transcriptionHuntingtin interacting protein 1 induces apoptosis via a novel caspase-dependent death effector domainCHIP protects from the neurotoxicity of expanded and wild-type ataxin-1 and promotes their ubiquitination and degradationAlpha-synuclein acts in the nucleus to inhibit histone acetylation and promote neurotoxicityParkin is an E3 ubiquitin-ligase for normal and mutant ataxin-2 and prevents ataxin-2-induced cell deathAtaxin 1, a SCA1 neurodegenerative disorder protein, is functionally linked to the silencing mediator of retinoid and thyroid hormone receptorsPumilio1 haploinsufficiency leads to SCA1-like neurodegeneration by increasing wild-type Ataxin1 levelsBoat, an AXH domain protein, suppresses the cytotoxicity of mutant ataxin-1.Live-cell imaging reveals divergent intracellular dynamics of polyglutamine disease proteins and supports a sequestration model of pathogenesis.Interaction of Huntington disease protein with transcriptional activator Sp1Improved activities of CREB binding protein, heterogeneous nuclear ribonucleoproteins and proteasome following downregulation of noncoding hsromega transcripts help suppress poly(Q) pathogenesis in fly modelsComparative genomics and molecular dynamics of DNA repeats in eukaryotesPathogenic mechanisms of a polyglutamine-mediated neurodegenerative disease, spinocerebellar ataxia type 1Interaction between neuronal intranuclear inclusions and promyelocytic leukemia protein nuclear and coiled bodies in CAG repeat diseasesThe localization and interactions of huntingtinProtein ligands to HuR modulate its interaction with target mRNAs in vivoEvolutionary conservation and selection of human disease gene orthologs in the rat and mouse genomesMotif co-regulation and co-operativity are common mechanisms in transcriptional, post-transcriptional and post-translational regulationCell biology of spinocerebellar ataxiaMouse models of polyglutamine diseases: review and data table. Part IPathogenic mechanisms and therapeutic strategies in spinobulbar muscular atrophyBeyond the glutamine expansion: influence of posttranslational modifications of ataxin-1 in the pathogenesis of spinocerebellar ataxia type 1The unstable repeats--three evolving faces of neurological diseasePolyglutamine neurodegeneration: expanded glutamines enhance native functionsPolyglutamine expansion accelerates the dynamics of ataxin-1 and does not result in aggregate formation.N17 Modifies mutant Huntingtin nuclear pathogenesis and severity of disease in HD BAC transgenic micedAtaxin-2 mediates expanded Ataxin-1-induced neurodegeneration in a Drosophila model of SCA1Beta conformation of polyglutamine track revealed by a crystal structure of Huntingtin N-terminal region with insertion of three histidine residuesSelf-Assembly and Conformational Heterogeneity of the AXH Domain of Ataxin-1: An Unusual Example of a Chameleon FoldDegradation-mediated protein quality control at the inner nuclear membraneDrosophila as an In Vivo Model for Human Neurodegenerative DiseaseCasein kinase II-mediated phosphorylation regulates alpha-synuclein/synphilin-1 interaction and inclusion body formationAmyloid-associated activity contributes to the severity and toxicity of a prion phenotypeOpposing effects of polyglutamine expansion on native protein complexes contribute to SCA1RNA toxicity is a component of ataxin-3 degeneration in DrosophilaSeipinopathy: a novel endoplasmic reticulum stress-associated disease
P2860
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P2860
Ataxin-1 nuclear localization and aggregation: role in polyglutamine-induced disease in SCA1 transgenic mice.
description
1998 nî lūn-bûn
@nan
1998年の論文
@ja
1998年学术文章
@wuu
1998年学术文章
@zh
1998年学术文章
@zh-cn
1998年学术文章
@zh-hans
1998年学术文章
@zh-my
1998年学术文章
@zh-sg
1998年學術文章
@yue
1998年學術文章
@zh-hant
name
Ataxin-1 nuclear localization ...... sease in SCA1 transgenic mice.
@en
Ataxin-1 nuclear localization ...... sease in SCA1 transgenic mice.
@nl
type
label
Ataxin-1 nuclear localization ...... sease in SCA1 transgenic mice.
@en
Ataxin-1 nuclear localization ...... sease in SCA1 transgenic mice.
@nl
prefLabel
Ataxin-1 nuclear localization ...... sease in SCA1 transgenic mice.
@en
Ataxin-1 nuclear localization ...... sease in SCA1 transgenic mice.
@nl
P2093
P50
P1433
P1476
Ataxin-1 nuclear localization ...... sease in SCA1 transgenic mice.
@en
P2093
P356
10.1016/S0092-8674(00)81781-X
P407
P577
1998-10-01T00:00:00Z