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Article

Polyglutamine domain modulates the TBP-TFIIB interaction: implications for its normal function and neurodegeneration.

Nature neuroscience - 1 Dec 2007

Friedman Meyer J, Shah Anjali G, Fang Zhi-Hui, Ward Elizabeth G, Warren Stephen T, Li Shihua, Li Xiao-Jiang

Abstract excerpt

Expansion of the polyglutamine (polyQ) tract in human TATA-box binding protein (TBP) causes the neurodegenerative disease spinocerebellar ataxia 17 (SCA17). It remains unclear how the polyQ tract regulates normal protein function and induces selective neuropathology in SCA17. We generated transge...

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Source

Identifiers

PMID: 17994014
DOI: 10.1038/nn2011

Genes

TBP
HSPB1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-17994014-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

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Polyglutamine domain modulates the TBP-TFIIB interaction: implications for its normal function and neurodegeneration.PMID 17994014Read ↗

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Phenotypic defects from the expression of wild-type and pathogenic TATA-Binding Proteins in new <i>Drosophila</i> models of Spinocerebellar Ataxia Type 17Semantic proximity Read ↗

TBP, a polyglutamine tract containing protein, accumulates in Alzheimer's disease.Semantic proximity Read ↗

Age-dependent decrease in chaperone activity impairs MANF expression, leading to Purkinje cell degeneration in inducible SCA17 mice.Semantic proximity Read ↗

Transcriptional dysregulation of TrkA associates with neurodegeneration in spinocerebellar ataxia type 17.Semantic proximity Read ↗

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