title: Discovery of a novel aggregation domain in the huntingtin protein: implications for the mechanisms of Htt aggregation and toxicity.
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.
authors.affiliation: Laboratory of Molecular and Chemical Biology of Neurodegeneration, Brain Mind Institute, Ecole Polytechnique Fédérale de Lausanne, Switzerland.
authors.forename: Zhe-Ming
authors.initials: ZM
authors.lastname: Wang
authors.forename: Hilal A
authors.initials: HA
authors.lastname: Lashuel
mesh_terms: D000595:Amino Acid Sequence; D006801:Humans; D000071058:Huntingtin Protein; D006816:Huntington Disease / Q000235:genetics / Q000378:metabolism*; D009419:Nerve Tissue Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D017434:Protein Structure, Tertiary
chemical_list: C086055:HTT protein, human; D000071058:Huntingtin Protein; D009419:Nerve Tissue Proteins