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

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Abstract

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.

Details

Title Discovery of a novel aggregation domain in the huntingtin protein: implications for the mechanisms of Htt aggregation and toxicity
Author(s) Wang, Zhe-Ming ; Lashuel, Hilal A.
Published in Angewandte Chemie (International ed. in English)
Pagination 6
Volume 52
Issue 2
Pages 562-7
Date 2012
Publisher Weinheim, Wiley-Blackwell
ISSN 1521-3773
DOI https://doi.org/10.1002/anie.201206561
Other identifier(s) View record in Web of Science
Laboratories LMNN
Record Appears in Scientific production and competences > SV - School of Life Sciences > BMI - Brain Mind Institute > LMNN - Laboratory of Molecular Neurobiology and Neuroproteomics
Work produced at EPFL
Journal Articles
Published
Record creation date 2012-09-21

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