The Aggregation-Enhancing Huntingtin N-Terminus Is Helical in Amyloid Fibrils-Reference-Cited by-同舟云学术

The Aggregation-Enhancing Huntingtin N-Terminus Is Helical in Amyloid Fibrils

Published:2011-03-07 Issue:12 Volume:133 Page:4558-4566
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Sivanandam V. N.¹,Jayaraman Murali¹,Hoop Cody L.¹,Kodali Ravindra¹,Wetzel Ronald¹,van der Wel Patrick C. A.¹

Affiliation:

1. Department of Structural Biology and ‡Pittsburgh Institute for Neurodegenerative Diseases, University of Pittsburgh School of Medicine, Biomedical Science Tower 3, 3501 Fifth Avenue, Pittsburgh, Pennsylvania 15260, United States

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

http://pubs.acs.org/doi/pdf/10.1021/ja110715f

Reference67 articles.

1. Polyglutamine Pathogenesis

2. Bates, G. P.; Benn, C.InHuntington’s Disease;Bates, G. P.; Harper, P. S.; Jones, L., Eds.Oxford University Press:Oxford, U.K. 2002; pp429−472.

3. The threshold for polyglutamine-expansion protein aggregation and cellular toxicity is dynamic and influenced by aging in Caenorhabditis elegans

4. Self-assembly of polyglutamine-containing huntingtin fragments into amyloid-like fibrils: Implications for Huntington's disease pathology

5. Polyglutamine aggregation behavior in vitro supports a recruitment mechanism of cytotoxicity

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