Polyglutamine-expanded spinocerebellar ataxia-7 protein disrupts normal SAGA and SLIK histone acetyltransferase activity.
about
Ataxin-7 associates with microtubules and stabilizes the cytoskeletal network.Comparison of an expanded ataxia interactome with patient medical records reveals a relationship between macular degeneration and ataxiaStructural basis for recognition of the third SH3 domain of full-length R85 (R85FL)/ponsin by ataxin-7PML clastosomes prevent nuclear accumulation of mutant ataxin-7 and other polyglutamine proteinsGlutamine-expanded ataxin-7 alters TFTC/STAGA recruitment and chromatin structure leading to photoreceptor dysfunction.Ubiquitin-specific peptidase 22 functions and its involvement in diseaseEpigenetics and Triplet-Repeat Neurological DiseasesCell biology of spinocerebellar ataxiaCombinatorial depletion analysis to assemble the network architecture of the SAGA and ADA chromatin remodeling complexes.Mutational uncoupling of the role of Sus1 in nuclear pore complex targeting of an mRNA export complex and histone H2B deubiquitination.SAGA-associated Sgf73p facilitates formation of the preinitiation complex assembly at the promoters either in a HAT-dependent or independent manner in vivo.Yeast Sgf73/Ataxin-7 serves to anchor the deubiquitination module into both SAGA and Slik(SALSA) HAT complexes.Yeast Ataxin-7 links histone deubiquitination with gene gating and mRNA export.Loss of Gcn5 acetyltransferase activity leads to neural tube closure defects and exencephaly in mouse embryosPoly(Q) Expansions in ATXN7 Affect Solubility but Not Activity of the SAGA Deubiquitinating ModuleProtein arginine methyltransferase 6 enhances polyglutamine-expanded androgen receptor function and toxicity in spinal and bulbar muscular atrophy.Direct inhibition of Gcn5 protein catalytic activity by polyglutamine-expanded ataxin-7.Reelin is a target of polyglutamine expanded ataxin-7 in human spinocerebellar ataxia type 7 (SCA7) astrocytes.Gcn5 loss-of-function accelerates cerebellar and retinal degeneration in a SCA7 mouse model.Native functions of the androgen receptor are essential to pathogenesis in a Drosophila model of spinobulbar muscular atrophy.Histone acetylation, acetyltransferases, and ataxia--alteration of histone acetylation and chromatin dynamics is implicated in the pathogenesis of polyglutamine-expansion disordersThe SAGA continues: expanding the cellular role of a transcriptional co-activator complex.Multi-tasking on chromatin with the SAGA coactivator complexes.CAG-encoded polyglutamine length polymorphism in the human genomeMolecular pathogenesis and cellular pathology of spinocerebellar ataxia type 7 neurodegenerationPolyglutamine-expanded ataxin-7 inhibits STAGA histone acetyltransferase activity to produce retinal degeneration.Pulling complexes out of complex diseases: Spinocerebellar Ataxia 7.Sus1p facilitates pre-initiation complex formation at the SAGA-regulated genes independently of histone H2B de-ubiquitylationDistinct regulatory mechanisms of eukaryotic transcriptional activation by SAGA and TFIID.Requirement for zebrafish ataxin-7 in differentiation of photoreceptors and cerebellar neurons.Cross-talking noncoding RNAs contribute to cell-specific neurodegeneration in SCA7The Spt-Ada-Gcn5 Acetyltransferase (SAGA) complex in Aspergillus nidulans.Aggregation of Polyglutamine-expanded Ataxin 7 Protein Specifically Sequesters Ubiquitin-specific Protease 22 and Deteriorates Its Deubiquitinating Function in the Spt-Ada-Gcn5-Acetyltransferase (SAGA) Complex.Polyglutamine (polyQ) disorders: the chromatin connection.Epigenetics in nucleotide repeat expansion disorders.Sus1 is recruited to coding regions and functions during transcription elongation in association with SAGA and TREX2.Emerging pathogenic pathways in the spinocerebellar ataxias.Decoding the epigenetic language of neuronal plasticity.Insights into SAGA function during gene expressionLoss of Drosophila Ataxin-7, a SAGA subunit, reduces H2B ubiquitination and leads to neural and retinal degeneration.
P2860
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P2860
Polyglutamine-expanded spinocerebellar ataxia-7 protein disrupts normal SAGA and SLIK histone acetyltransferase activity.
description
2005 nî lūn-bûn
@nan
2005 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Polyglutamine-expanded spinoce ...... ne acetyltransferase activity.
@ast
Polyglutamine-expanded spinoce ...... ne acetyltransferase activity.
@en
Polyglutamine-expanded spinoce ...... ne acetyltransferase activity.
@nl
type
label
Polyglutamine-expanded spinoce ...... ne acetyltransferase activity.
@ast
Polyglutamine-expanded spinoce ...... ne acetyltransferase activity.
@en
Polyglutamine-expanded spinoce ...... ne acetyltransferase activity.
@nl
prefLabel
Polyglutamine-expanded spinoce ...... ne acetyltransferase activity.
@ast
Polyglutamine-expanded spinoce ...... ne acetyltransferase activity.
@en
Polyglutamine-expanded spinoce ...... ne acetyltransferase activity.
@nl
P2093
P2860
P3181
P356
P1476
Polyglutamine-expanded spinoce ...... ne acetyltransferase activity.
@en
P2093
David Schieltz
John R Yates
Marilyn G Pray-Grant
Patrick A Grant
Stacey J McMahon
P2860
P304
P3181
P356
10.1073/PNAS.0503493102
P407
P577
2005-06-02T00:00:00Z