Polyglutamine expansion as a pathological epitope in Huntington's disease and four dominant cerebellar ataxias.
about
Retinitis pigmentosaNuclear localization of the spinocerebellar ataxia type 7 protein, ataxin-7Structural basis of binding of P-body-associated proteins GW182 and ataxin-2 by the Mlle domain of poly(A)-binding proteinCloning of the SCA7 gene reveals a highly unstable CAG repeat expansionpARIS-htt: an optimised expression platform to study huntingtin reveals functional domains required for vesicular traffickingCloning of the gene for spinocerebellar ataxia 2 reveals a locus with high sensitivity to expanded CAG/glutamine repeatsMapping of spinocerebellar ataxia 13 to chromosome 19q13.3-q13.4 in a family with autosomal dominant cerebellar ataxia and mental retardationMapping of a new autosomal dominant spinocerebellar ataxia to chromosome 22.Mini- and microsatellitesThe P42 peptide and Peptide-based therapies for Huntington's diseaseNeural and mesenchymal stem cells in animal models of Huntington's disease: past experiences and future challengesThe structure of a polyQ-anti-polyQ complex reveals binding according to a linear lattice modelDisease-Associated Polyglutamine Stretches in Monomeric Huntingtin Adopt a Compact StructureLinear and extended: a common polyglutamine conformation recognized by the three antibodies MW1, 1C2 and 3B5H10Conformational analysis of misfolded protein aggregation by FRET and live-cell imaging techniquesNormal huntingtin function: an alternative approach to Huntington's diseaseCommon features at the start of the neurodegeneration cascadeA Huntington's disease CAG expansion at the murine Hdh locus is unstable and associated with behavioural abnormalities in miceHuntingtin is required for neurogenesis and is not impaired by the Huntington's disease CAG expansionTargeting several CAG expansion diseases by a single antisense oligonucleotideExtended polyglutamine tracts cause aggregation and structural perturbation of an adjacent beta barrel protein.Glutamine and Asparagine Side Chain Hyperconjugation-Induced Structurally Sensitive Vibrations.Asparagine and glutamine differ in their propensities to form specific side chain-backbone hydrogen bonded motifs in proteins.Elucidating a normal function of huntingtin by functional and microarray analysis of huntingtin-null mouse embryonic fibroblasts.Monoclonal antibodies recognize distinct conformational epitopes formed by polyglutamine in a mutant huntingtin fragment.Mutant huntingtin fragments form oligomers in a polyglutamine length-dependent manner in vitro and in vivo.CTCF regulates ataxin-7 expression through promotion of a convergently transcribed, antisense noncoding RNA.PGC-1α rescues Huntington's disease proteotoxicity by preventing oxidative stress and promoting TFEB function.Familial frontotemporal dementia with neuronal intranuclear inclusions is not a polyglutamine expansion disease.Polyglutamine expansion mutation yields a pathological epitope linked to nucleation of protein aggregate: determinant of Huntington's disease onset.Molecular pathogenesis and cellular pathology of spinocerebellar ataxia type 7 neurodegenerationTricyclic pyrone compounds prevent aggregation and reverse cellular phenotypes caused by expression of mutant huntingtin protein in striatal neurons.Properties of polyglutamine expansion in vitro and in a cellular model for Huntington's disease.Evidence for both the nucleus and cytoplasm as subcellular sites of pathogenesis in Huntington's disease in cell culture and in transgenic mice expressing mutant huntingtin.CAG-polyglutamine-repeat mutations: independence from gene context.The carboxy-terminal fragment of alpha(1A) calcium channel preferentially aggregates in the cytoplasm of human spinocerebellar ataxia type 6 Purkinje cells.Full-length huntingtin levels modulate body weight by influencing insulin-like growth factor 1 expressionHuntington disease models and human neuropathology: similarities and differencesMonomeric, oligomeric and polymeric proteins in huntington disease and other diseases of polyglutamine expansionToward an understanding of polyglutamine neurodegeneration.
P2860
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P2860
Polyglutamine expansion as a pathological epitope in Huntington's disease and four dominant cerebellar ataxias.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
1995年论文
@zh
1995年论文
@zh-cn
name
Polyglutamine expansion as a p ...... r dominant cerebellar ataxias.
@en
type
label
Polyglutamine expansion as a p ...... r dominant cerebellar ataxias.
@en
prefLabel
Polyglutamine expansion as a p ...... r dominant cerebellar ataxias.
@en
P2093
P50
P356
P1433
P1476
Polyglutamine expansion as a p ...... r dominant cerebellar ataxias.
@en
P2093
P2888
P304
P356
10.1038/378403A0
P407
P577
1995-11-01T00:00:00Z
P5875
P6179
1011102548