Discovery of a novel aggregation domain in the huntingtin protein: implications for the mechanisms of Htt aggregation and toxicity.
- Wang ZM Laboratory of Molecular and Chemical Biology of Neurodegeneration, Brain Mind Institute, Ecole Polytechnique Fédérale de Lausanne, Switzerland.
- Lashuel HA
- 2012-11-14
Published in:
- Angewandte Chemie (International ed. in English). - 2013
Amino Acid Sequence
Humans
Huntingtin Protein
Huntington Disease
Nerve Tissue Proteins
Protein Structure, Tertiary
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.
- Language
-
- English
- Open access status
- green
- Identifiers
-
- DOI 10.1002/anie.201206561
- PMID 23148019
- Persistent URL
- https://sonar.ch/global/documents/99396
Statistics
Document views: 19
File downloads:
- Full-text: 0