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  4. Discovery of a novel aggregation domain in the huntingtin protein: implications for the mechanisms of Htt aggregation and toxicity
 
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research article

Discovery of a novel aggregation domain in the huntingtin protein: implications for the mechanisms of Htt aggregation and toxicity

Wang, Zhe-Ming
•
Lashuel, Hilal A.  
2012
Angewandte Chemie (International ed. in English)

Aggravating aggregation: an N-terminal domain that is in close proximity to the polyQ domain in the huntingtin protein, htt105-138, is shown to be highly aggregation prone. Potential cross-talk between this domain and the polyQ region may play a central role in regulating the aggregation and toxicity of Htt-N-terminal fragments.

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Type
research article
DOI
10.1002/anie.201206561
Web of Science ID

WOS:000312942900007

Author(s)
Wang, Zhe-Ming
•
Lashuel, Hilal A.  
Date Issued

2012

Publisher

Wiley-Blackwell

Published in
Angewandte Chemie (International ed. in English)
Volume

52

Issue

2

Start page

562

End page

7

Peer reviewed

NON-REVIEWED

Written at

EPFL

EPFL units
LMNN  
Available on Infoscience
September 21, 2012
Use this identifier to reference this record
https://infoscience.epfl.ch/handle/20.500.14299/85622
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