Polyglutamine length-dependent interaction of Hsp40 and Hsp70 family chaperones with truncated N-terminal huntingtin: their role in suppression of aggregation and cellular toxicity

By Jana Nihar Ranjan   Tanaka Motomasa   Wang Guang-hui   Nukina Nobuyuki  

Human Molecular Genetics, Vol. 9, Iss. 13, 2000-08 ,pp. : 2009-2018

Oxford University Press

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Aggregation of N-terminal huntingtin is dependent on the length of its glutamine repeats

By Li S-H.   Li X-J.  

Human Molecular Genetics, Vol. 7, Iss. 5, 1998-05 ,pp. : 777-782

Oxford University Press

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A structure-based analysis of huntingtin mutant polyglutamine aggregation and toxicity: evidence for a compact beta-sheet structure

By Poirier Michelle A.   Jiang Haibing   Ross Christopher A.  

Human Molecular Genetics, Vol. 14, Iss. 6, 2005-03 ,pp. : 765-774

Oxford University Press

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Increased huntingtin protein length reduces the number of polyglutamine-induced gene expression changes in mouse models of Huntington's disease

By Chan Edmond Y.W.  

Human Molecular Genetics, Vol. 11, Iss. 17, 2002-06 ,pp. : 1939-1951

Oxford University Press

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Aberrant interactions of transcriptional repressor proteins with the Huntington’s disease gene product, huntingtin

By Boutell Jonathan M.   Thomas Philip   Neal James W.   Weston Victoria J.   Duce James   Harper Peter S.   Jones A. Lesley  

Human Molecular Genetics, Vol. 8, Iss. 9, 1999-09 ,pp. : 1647-1655

Oxford University Press

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