Truncated N-terminal fragments of huntingtin with expanded glutamine repeats form nuclear and cytoplasmic aggregates in cell culture.
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Cleavage of atrophin-1 at caspase site aspartic acid 109 modulates cytotoxicityHuntingtin and huntingtin-associated protein 1 influence neuronal calcium signaling mediated by inositol-(1,4,5) triphosphate receptor type 1Ataxin 1, a SCA1 neurodegenerative disorder protein, is functionally linked to the silencing mediator of retinoid and thyroid hormone receptorsThe DNAJB6 and DNAJB8 protein chaperones prevent intracellular aggregation of polyglutamine peptidesA role for tissue transglutaminase in alpha-gliadin peptide cytotoxicityPathogenic mechanisms and therapeutic strategies in spinobulbar muscular atrophyHAP1 facilitates effects of mutant huntingtin on inositol 1,4,5-trisphosphate-induced Ca release in primary culture of striatal medium spiny neuronsNuclear localization of a non-caspase truncation product of atrophin-1, with an expanded polyglutamine repeat, increases cellular toxicityTemporal separation of aggregation and ubiquitination during early inclusion formation in transgenic mice carrying the Huntington's disease mutationAmyloid-like fibril formation by polyQ proteins: a critical balance between the polyQ length and the constraints imposed by the host proteinPlasma membrane contributes to the formation of pre-autophagosomal structuresPremature death and neurologic abnormalities in transgenic mice expressing a mutant huntingtin exon-2 fragment.Insoluble detergent-resistant aggregates form between pathological and nonpathological lengths of polyglutamine in mammalian cellsFocal distortion of the nuclear envelope by huntingtin aggregates revealed by lamin immunostainingIntracellular inclusions, pathological markers in diseases caused by expanded polyglutamine tracts?Biophysical underpinnings of the repeat length dependence of polyglutamine amyloid formationAre there multiple pathways in the pathogenesis of Huntington's disease?Polyglutamine pathogenesis.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.Monomeric, oligomeric and polymeric proteins in huntington disease and other diseases of polyglutamine expansionCaspases and neurodegeneration: on the cutting edge of new therapeutic approaches.Toward an understanding of polyglutamine neurodegeneration.Effects of intracellular expression of anti-huntingtin antibodies of various specificities on mutant huntingtin aggregation and toxicityFormation of morphologically similar globular aggregates from diverse aggregation-prone proteins in mammalian cells.Differential vulnerability of neurons in Huntington's disease: the role of cell type-specific features.Specificity in intracellular protein aggregation and inclusion body formation.Altered transcription in yeast expressing expanded polyglutamine.Nuclear localization and dominant-negative suppression by a mutant SKCa3 N-terminal channel fragment identified in a patient with schizophrenia.Wild-type huntingtin reduces the cellular toxicity of mutant huntingtin in vivoProtein aggregation and pathogenesis of Huntington's disease: mechanisms and correlations.Familial conformational diseases and dementias.Nitric oxide and nitric oxide synthase in Huntington's disease.The selective vulnerability of nerve cells in Huntington's disease.Huntingtin fragments and SOD1 mutants form soluble oligomers in the cellMolecular chaperones as modulators of polyglutamine protein aggregation and toxicityCaspases in Huntington's disease.Protein aggregates and dementia: is there a common toxicity?Electroconvulsive shock ameliorates disease processes and extends survival in huntingtin mutant mice.Analysis of proteolytic processes and enzymatic activities in the generation of huntingtin n-terminal fragments in an HEK293 cell model.
P2860
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P2860
Truncated N-terminal fragments of huntingtin with expanded glutamine repeats form nuclear and cytoplasmic aggregates in cell culture.
description
1998 nî lūn-bûn
@nan
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
1998年论文
@zh
1998年论文
@zh-cn
name
Truncated N-terminal fragments ...... ic aggregates in cell culture.
@en
type
label
Truncated N-terminal fragments ...... ic aggregates in cell culture.
@en
prefLabel
Truncated N-terminal fragments ...... ic aggregates in cell culture.
@en
P2093
P356
P1476
Truncated N-terminal fragments ...... mic aggregates in cell culture
@en
P2093
D R Borchelt
G Schilling
M F Peters
T M Dawson
V L Dawson
P304
P356
10.1093/HMG/7.5.783
P50
P577
1998-05-01T00:00:00Z