SCA17, a novel autosomal dominant cerebellar ataxia caused by an expanded polyglutamine in TATA-binding protein.

By Koichiro Nakamura, Seon‐Yong Jeong, T. Uchihara, M. Anno, K. Nagashima, T. Nagashima, S. Ikeda, S. Tsuji, I. Kanazawa. Human Molecular Genetics, 2001

617 citations recorded by the source corpus.

Subfields: Cellular and Molecular Neuroscience, Molecular Biology, Neurology

View Paper: https://www.semanticscholar.org/paper/2a06fb710191d31f6767d3cdb4a5fa08cd5a8edb

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In Molecular Biology

1. C. Chiang
2. Leslie M. Thompson
3. A. Kazantsev
4. Mary C. Thomas

Citations in the corpus

• Histone Deacetylase Inhibition by Sodium Butyrate Chemotherapy Ameliorates the Neurodegenerative Phenotype in Huntington's Disease Mice (2003, neutral): “, 2000), TATA-binding protein (Nakamura et al., 2001), mSin3a (Steffan et al.”
• Therapeutic application of histone deacetylase inhibitors for central nervous system disorders (2008, background): “For instance, an expanded repeat in the TATA-binding protein (TBP) leads to the neurodegenerative disease SCA17 (Ref”
• The General Transcription Machinery and General Cofactors (2006, background): “…imperfect Pro-Met-Thr (PMT) repeats located around amino acids 142 to 150 preceding the C-terminal core region of TBP. Expansion of the polyglutamine tract beyond 42 residues is frequently linked to human neurodegenerative diseases, such as spinocerebellar ataxia SCA17 (Nakamura et al., 2001).”