Polyglutamine Diseases
Mostrando 1-12 de 45 artigos, teses e dissertações.
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1. Occupational therapy in spinocerebellar ataxia type 3: an open-label trial
Occupational therapy (OT) is a profession concerned with promoting health and well-being through occupation, by enabling handicapped people to participate in the activities of everyday life. OT is part of the clinical rehabilitation of progressive genetic neurodegenerative diseases such as spinocerebellar ataxias; however, its effects have never been determi
Publicado em: 2011
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2. Development of an in vitro model of expanded ataxin-3 cytotoxic effects and evaluation of different therapeutic strategies to control of these effects / Desenvolvimento de um modelo in vitro dos efeitos citotóxicos da ataxina-3 expandida e avaliação de diferentes estratégias terapêuticas para o controle desses efeitos
Spinocerebellar ataxia-3 (SCA3), also known as Machado-Joseph disease (MJD), belongs to a group of neurodegenerative disorders caused by expansion of a polyglutamine stretch, called polyglutamine diseases. MJD is the most frequent inherited autosomal dominant ataxia in many countries. Clinical manifestations are varied, including abnormal motor coordination
IBICT - Instituto Brasileiro de Informação em Ciência e Tecnologia. Publicado em: 08/02/2010
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3. Machado-Joseph disease enhances genetic fitness : a comparison between affected and unaffected women and between MJD and the general population
Background: Machado-Joseph disease (MJD SCA3), a spinocerebellar ataxia related to expansion of a CAG tract, has already been related to anticipation and meiotic drift. However, fitness of MJD carriers has been little studied. Objective: To analyze genetic fitness of MJD patients, comparing them to their unaffected relatives and to the general population (GP
Publicado em: 2010
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4. Functional studies of the ataxin-3 protein / Estudos funcionais da proteina ataxina-3
Spinocerebellar ataxia type 3 (SCA 3) also known as Machado-Joseph disease (MJD) belongs to a heterogeneous group of neurodegenerative diseases of the central nervous system and is characterized by the degeneration of cerebellum and its afferent and efferent ways. The SCA3/MJD gene was mapped on chromosome 14 and was named MJD1, the causative mutation is an
Publicado em: 2007
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5. Inefficient degradation of truncated polyglutamine proteins by the proteasome
Accumulation of mutant proteins into misfolded species and aggregates is characteristic for diverse neurodegenerative diseases including the polyglutamine diseases. While several studies have suggested that polyglutamine protein aggregates impair the ubiquitin–proteasome system, the molecular mechanisms underlying the interaction between polyglutamine prot
Nature Publishing Group.
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6. Altered transcription in yeast expressing expanded polyglutamine
Expanded polyglutamine tracts are responsible for at least eight fatal neurodegenerative diseases. In mouse models, proteins with expanded polyglutamine cause transcriptional dysregulation before onset of symptoms, suggesting that this dysregulation may be an early event in polyglutamine pathogenesis. Transcriptional dysregulation and cellular toxicity may b
The National Academy of Sciences.
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7. Histone deacetylase inhibitors reduce polyglutamine toxicity
Polyglutamine diseases include at least nine neurodegenerative disorders, each caused by a CAG repeat expansion in a different gene. Accumulation of mutant polyglutamine-containing proteins occurs in patients, and evidence from cell culture and animal experiments suggests the nucleus as a site of pathogenesis. To understand the consequences of nuclear a
The National Academy of Sciences.
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8. Polyglutamine aggregates alter protein folding homeostasis in Caenorhabditis elegans
Expansion of polyglutamine repeats in several unrelated proteins causes neurodegenerative diseases with distinct but related pathologies. To provide a model system for investigating common pathogenic features, we have examined the behavior of polyglutamine expansions expressed in Caenorhabditis elegans. The expression of polyglutamine repeats as green fluore
The National Academy of Sciences.
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9. cAMP-response element-binding protein and heat-shock protein 70 additively suppress polyglutamine-mediated toxicity in Drosophila
Gene-specific expansion of polyglutamine-encoding CAG repeats can cause neurodegenerative disorders, including Huntington's disease. It is believed that part of the pathological effect of the expanded protein is due to transcriptional dysregulation. Using Drosophila as a model, we show that cAMP-response element-binding protein (CREB) is involved in expanded
National Academy of Sciences.
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10. Regulation of expanded polyglutamine protein aggregation and nuclear localization by the glucocorticoid receptor
Spinobulbar muscular atrophy and Huntington's disease are caused by polyglutamine expansion in the androgen receptor and huntingtin, respectively, and their pathogenesis has been associated with abnormal nuclear localization and aggregation of truncated forms of these proteins. Here we show, in diverse cell types, that glucocorticoids can up- or down-modulat
The National Academy of Sciences.
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11. Targeting expression of expanded polyglutamine proteins to the endoplasmic reticulum or mitochondria prevents their aggregation
Aggregation of misfolded proteins is a characteristic of several neurodegenerative diseases. The huntingtin amino-terminal fragment with extended polyglutamine repeat forms aggregates closely associated with chaperones both in the cytoplasm and the nucleus. Because each cellular compartment contains distinct chaperones and because the molecular mechanisms co
National Academy of Sciences.
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12. Transcriptional dysregulation of TrkA associates with neurodegeneration in spinocerebellar ataxia type 17
TATA binding protein (TBP), a universal transcription factor, is broadly required by nuclear RNA polymerases for the initiation of transcription. TBP contains a polymorphic polyglutamine tract in its N-terminal region, and expansion of this tract leads to spinocerebellar ataxia type 17 (SCA17), one of nine dominantly inherited neurodegenerative diseases caus
Oxford University Press.