Neuronal dysfunction in a polyglutamine disease model occurs in the absence of ubiquitin–proteasome system impairment and inversely correlates with the degree of nuclear inclusion formation-Reference-Cited by-同舟云学术

Neuronal dysfunction in a polyglutamine disease model occurs in the absence of ubiquitin–proteasome system impairment and inversely correlates with the degree of nuclear inclusion formation

Published:2005-01-20 Issue:5 Volume:14 Page:679-691
ISSN:1460-2083
Container-title:Human Molecular Genetics
language:en
Short-container-title:

Author:

Bowman Aaron B.,Yoo Seung-Yun,Dantuma Nico P.,Zoghbi Huda Y.

Publisher

Oxford University Press (OUP)

Subject

Genetics(clinical),Genetics,Molecular Biology,General Medicine

Link

http://academic.oup.com/hmg/article-pdf/14/5/679/6949795/ddi064.pdf

Reference50 articles.

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2. Ross, C.A. and Poirier, M.A. ( 2004 ) Protein aggregation and neurodegenerative disease. Nat. Med. , 10 (suppl.), S10 –S17.

3. Michalik, A. and van Broeckhoven, C. ( 2003 ) Pathogenesis of polyglutamine disorders: aggregation revisited. Hum. Mol. Genet. , 12 , R173 –R186.

4. Ciechanover, A. and Brundin, P. ( 2003 ) The ubiquitin proteasome system in neurodegenerative diseases: sometimes the chicken, sometimes the egg. Neuron , 40 , 427 –446.

5. Schmidt, T., Lindenberg, K.S., Krebs, A., Schols, L., Laccone, F., Herms, J., Rechsteiner, M., Riess, O. and Landwehrmeyer, G.B. ( 2002 ) Protein surveillance machinery in brains with spinocerebellar ataxia type 3: redistribution and differential recruitment of 26S proteasome subunits and chaperones to neuronal intranuclear inclusions. Ann. Neurol. , 51 , 302 –310.

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