Discovery of a novel aggregation domain in the huntingtin protein

Implications for the mechanisms of Htt aggregation and toxicity

Zhe Ming Wang, Hilal A. Lashuel

Research output: Contribution to journalArticle

8 Citations (Scopus)

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 (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.

Original languageEnglish
Pages (from-to)562-567
Number of pages6
JournalAngewandte Chemie - International Edition
Volume52
Issue number2
DOIs
Publication statusPublished - 7 Jan 2013
Externally publishedYes

Fingerprint

Toxicity
Agglomeration
Proteins
Huntingtin Protein
polyglutamine

Keywords

  • aggregation
  • amyloid fibrils
  • Huntington's disease
  • N-terminal fragment

ASJC Scopus subject areas

  • Chemistry(all)
  • Catalysis

Cite this

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.

In: Angewandte Chemie - International Edition, Vol. 52, No. 2, 07.01.2013, p. 562-567.

Research output: Contribution to journalArticle

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