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article, google, scholar, cas, nature, protein, sca, access, polyglutamine, ataxia, tbp, spinocerebellar, cell, mol, transcriptional, genet, content, mice, heat, shock, neurosci, cookies, function, disease, transgenic, transcription, expression, tatabinding, hsp, privacy, data, domain, interaction, expanded, mutant, open, rev, biol, neurol, repeat, gene, nat, information, implications, neurodegeneration, expansion, polyq, human, death, tfiib,

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nature portfolio permissions reprints privacy policy author information authors advertising nature 431 nature axonal charcot-marie-tooth disease social media tata-binding protein gene caa/cag repeat oligonucleotide mutant n-terminal fragment xiao-jiang li induces cone-rod dystrophy require vertebrate-specific sequences eukaryotic protein-coding genes repetitive c-terminal domain tata-tbp-tfiib array glutamine-rich activation motif springerlink instant access spinocerebellar ataxia mutations fundamental cellular processes tata-binding protein permissions transgenic mice expressing personal data spinocerebellar ataxias trinucleotide repeat expansion progressive neurological symptoms human genetics analyzed data cag repeat expansion characterized transgenic mice data protection kainate-induced seizures polyglutamine domain modulates rna-binding proteins unstable repeat expansion privacy established transgenic mice spinocerebellar ataxia 17 plm mechanosensory neurons transcriptional activation modulated preclude transcriptional activation amino-terminal region neurological disease caused polyglutamine neurodegenerative diseases huntington disease protein shihua li issue learn

Questions {❓}

• A neurological disease caused by an expanded CAG trinucleotide repeat in the TATA-binding protein gene: a new polyglutamine disease?
• Basal components of the transcription apparatus (RNA polymerase II, TATA-binding protein) contain activation domains: is the repetitive C-terminal domain (CTD) of RNA polymerase II a “portable enhancer domain”?
• Stress granules, RNA-binding proteins and polyglutamine diseases: too much aggregation?

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