Therapeutic opportunities in polyglutamine disease
Author:
Publisher
Springer Science and Business Media LLC
Subject
General Biochemistry, Genetics and Molecular Biology,General Medicine
Link
http://www.nature.com/articles/nm0401_419.pdf
Reference56 articles.
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2. Cummings, C.J. et al. Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1. Nature Genet. 19, 148–154 (1998).
3. Chai, Y., Koppenhafer, S.L., Shoesmith, S.J., Perez, M.K. & Paulson, H.L. Evidence for proteasome involvement in polyglutamine disease: localization to nuclear inclusions in SCA3/MJD and suppression of polyglutamine aggregation in vitro. Hum. Mol. Genet. 8, 673–682 (1999).
4. Stenoien, D.L. et al. Polyglutamine-expanded androgen receptors form aggregates that sequester heat shock proteins, proteasome components and SRC-1 and are suppressed by the HDJ-2 chaperone. Hum. Mol. Genet. 8, 731–741 (1999).
5. Chai, Y., Koppenhafer, S.L., Bonini, N.M. & Paulson, H.L. Analysis of the role of heat shock protein (Hsp) molecular chaperones in polyglutamine disease. J. Neurosci. 19, 10338–10347 (1999).
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