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Discovery of a Novel Aggregation Domain in the Huntingtin Protein: Implications for the Mechanisms of Htt Aggregation and Toxicity

Authors

  • Dr. Zhe-Ming Wang,

    1. Laboratory of Molecular and Chemical Biology of Neurodegeneration, Brain Mind Institute, Ecole Polytechnique Fédérale de Lausanne (EPFL), CH-1015 Lausanne (Switzerland)
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  • Prof. Dr. Hilal A. Lashuel

    Corresponding author
    1. Laboratory of Molecular and Chemical Biology of Neurodegeneration, Brain Mind Institute, Ecole Polytechnique Fédérale de Lausanne (EPFL), CH-1015 Lausanne (Switzerland)
    • Laboratory of Molecular and Chemical Biology of Neurodegeneration, Brain Mind Institute, Ecole Polytechnique Fédérale de Lausanne (EPFL), CH-1015 Lausanne (Switzerland)
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  • We would like to express our thanks and deep appreciation to Dr. Ruth Luthi-Carter for insightful discussions and support. We thank Annalisa Ansaloni for insightful discussions and John Perrin for assistance with TEM measurements.

Abstract

original image

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 (see scheme). 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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