Oligoproline Effects on Polyglutamine Conformation and Aggregation-Reference-Cited by-同舟云学术

Oligoproline Effects on Polyglutamine Conformation and Aggregation

Published:2006-01 Issue:3 Volume:355 Page:524-535
ISSN:0022-2836
Container-title:Journal of Molecular Biology
language:en
Short-container-title:Journal of Molecular Biology

Author:

Bhattacharyya Anusri,Thakur Ashwani K.,Chellgren Veronique M.,Thiagarajan Geetha,Williams Angela D.,Chellgren Brian W.,Creamer Trevor P.,Wetzel Ronald

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference51 articles.

1. The polyglutamine diseases;Bates,2002

2. Self-assembly of polyglutamine-containing huntingtin fragments into amyloid-like fibrils: implications for Huntington's disease pathology;Scherzinger;Proc. Natl Acad. Sci. USA,1999

3. Polyglutamine aggregation behavior in vitro supports a recruitment mechanism of cytotoxicity;Chen;J. Mol. Biol.,2001

4. Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death;Arrasate;Nature,2004

5. Formation of morphologically similar globular aggregates from diverse aggregation-prone proteins in mammalian cells;Mukai;Proc. Natl Acad. Sci. USA,2005

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