RNA-binding Protein TLS Is a Major Nuclear Aggregate-interacting Protein in Huntingtin Exon 1 with Expanded Polyglutamine-expressing Cells
Open Access
- 1 March 2008
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 283 (10), 6489-6500
- https://doi.org/10.1074/jbc.m705306200
Abstract
No abstract availableKeywords
This publication has 49 references indexed in Scilit:
- Identification of ubiquitin‐interacting proteins in purified polyglutamine aggregatesFEBS Letters, 2004
- Protein aggregation and neurodegenerative diseaseNature Medicine, 2004
- Nuclear-targeting of mutant huntingtin fragments produces Huntington's disease-like phenotypes in transgenic miceHuman Molecular Genetics, 2004
- Multiple functional domains of the oncoproteins Spi-1/PU.1 and TLS are involved in their opposite splicing effects in erythroleukemic cellsOncogene, 2004
- Pathogenesis of polyglutamine disorders: aggregation revisitedHuman Molecular Genetics, 2003
- Pro‐apoptotic protein kinase Cδ is associated with intranuclear inclusions in a transgenic model of Huntington's diseaseJournal of Neurochemistry, 2003
- Generation of prion transmission barriers by mutational control of amyloid conformationsNature, 2003
- Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseasesNature, 2002
- Altered proteasomal function due to the expression of polyglutamine-expanded truncated N-terminal huntingtin induces apoptosis by caspase activation through mitochondrial cytochrome c releaseHuman Molecular Genetics, 2001
- A huntingtin-associated protein enriched in brain with implications for pathologyNature, 1995