SCA17, a novel autosomal dominant cerebellar ataxia caused by an expanded polyglutamine in TATA-binding protein.
about
Ataxin-2 and its Drosophila homolog, ATX2, physically assemble with polyribosomesParkin is an E3 ubiquitin-ligase for normal and mutant ataxin-2 and prevents ataxin-2-induced cell deathA mutation in the fibroblast growth factor 14 gene is associated with autosomal dominant cerebellar ataxia [corrected]UgMicroSatdb: database for mining microsatellites from unigenesSpinocerebellar ataxia type 17: report of a family with reduced penetrance of an unstable Gln49 TBP allele, haplotype analysis supporting a founder effect for unstable alleles and comparative analysis of SCA17 genotypes.Mouse models of polyglutamine diseases: review and data table. Part IIntegration of modeling with experimental and clinical findings synthesizes and refines the central role of inositol 1,4,5-trisphosphate receptor 1 in spinocerebellar ataxiaCurrent understanding of the role of microRNAs in spinocerebellar ataxiasLarge Polyglutamine Repeats Cause Muscle Degeneration in SCA17 Mice.Silencing mutant ataxin-3 rescues motor deficits and neuropathology in Machado-Joseph disease transgenic miceTriplet repeat-derived siRNAs enhance RNA-mediated toxicity in a Drosophila model for myotonic dystrophyParkinsonism in spinocerebellar ataxiaThe promise and perils of HDAC inhibitors in neurodegenerationMolecular mechanism of monoamine oxidase A gene regulation under inflammation and ischemia-like conditions: key roles of the transcription factors GATA2, Sp1 and TBPPolyglutamine expansion reduces the association of TATA-binding protein with DNA and induces DNA binding-independent neurotoxicityDeletion of the triplet repeat encoding polyglutamine within the mouse Huntington's disease gene results in subtle behavioral/motor phenotypes in vivo and elevated levels of ATP with cellular senescence in vitroRole of high mobility group box 1 (HMGB1) in SCA17 pathogenesisAtaxia and Purkinje cell degeneration in mice lacking the CAMTA1 transcription factorTargeting several CAG expansion diseases by a single antisense oligonucleotidePolyQ repeat expansions in ATXN2 associated with ALS are CAA interrupted repeatsTherapeutic prospects for spinocerebellar ataxia type 2 and 3.CAG-encoded polyglutamine length polymorphism in the human genomeHAP1 can sequester a subset of TBP in cytoplasmic inclusions via specific interaction with the conserved TBP(CORE).A role for voltage-dependent anion channel Vdac1 in polyglutamine-mediated neuronal cell death.Monomeric, oligomeric and polymeric proteins in huntington disease and other diseases of polyglutamine expansionOligonucleotide-based strategies to combat polyglutamine diseases.CAG repeats determine brain atrophy in spinocerebellar ataxia 17: a VBM study.Histone deacetylase inhibitors reduce polyglutamine toxicityExclusion of mutations in the PRNP, JPH3, TBP, ATN1, CREBBP, POU3F2 and FTL genes as a cause of disease in Portuguese patients with a Huntington-like phenotype.ZMIZ1 preferably enhances the transcriptional activity of androgen receptor with short polyglutamine tract.Role of the CCAAT-binding protein NFY in SCA17 pathogenesisBrain pathology of spinocerebellar ataxias.Indole and synthetic derivative activate chaperone expression to reduce polyQ aggregation in SCA17 neuronal cell and slice culture models.Requirement for zebrafish ataxin-7 in differentiation of photoreceptors and cerebellar neurons.Bidirectional expression of CUG and CAG expansion transcripts and intranuclear polyglutamine inclusions in spinocerebellar ataxia type 8.Pathogenic polyglutamine expansion length correlates with polarity of the flanking sequences.Neurological proteins are not enriched for repetitive sequences.Huntington's disease: revisiting the aggregation hypothesis in polyglutamine neurodegenerative diseases.Population-based study of acquired cerebellar ataxia in Al-Kharga district, New Valley, EgyptComputational neurobiology is a useful tool in translational neurology: the example of ataxia
P2860
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P2860
SCA17, a novel autosomal dominant cerebellar ataxia caused by an expanded polyglutamine in TATA-binding protein.
description
2001 nî lūn-bûn
@nan
2001 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
SCA17, a novel autosomal domin ...... amine in TATA-binding protein.
@ast
SCA17, a novel autosomal domin ...... amine in TATA-binding protein.
@en
SCA17, a novel autosomal domin ...... amine in TATA-binding protein.
@nl
type
label
SCA17, a novel autosomal domin ...... amine in TATA-binding protein.
@ast
SCA17, a novel autosomal domin ...... amine in TATA-binding protein.
@en
SCA17, a novel autosomal domin ...... amine in TATA-binding protein.
@nl
prefLabel
SCA17, a novel autosomal domin ...... amine in TATA-binding protein.
@ast
SCA17, a novel autosomal domin ...... amine in TATA-binding protein.
@en
SCA17, a novel autosomal domin ...... amine in TATA-binding protein.
@nl
P2093
P356
P1476
SCA17, a novel autosomal domin ...... amine in TATA-binding protein.
@en
P2093
Kanazawa I
Nagashima K
Nagashima T
Nakamura K
Uchihara T
P304
P356
10.1093/HMG/10.14.1441
P577
2001-07-01T00:00:00Z