Potent inhibitors of Huntingtin protein aggregation in a cell-based assay

Alison Rinderspacher, Maria Laura Cremona, Yidong Liu, Shi Xian Deng, Yuli Xie, Gangli Gong, Nathalie Aulner, Udo Többen, Katherine Myers, Caty Chung, Monique Andersen, Dušica Vidović, Stephan Schürer, Lars Brandén, Ai Yamamoto, Donald W. Landry

Research output: Contribution to journalArticle

9 Scopus citations

Abstract

A quinazoline that decreases polyglutamine aggregate burden in a cell-based assay was identified from a high-throughput screen of a chemical-compound library, provided by the NIH Molecular Libraries Small Molecule Repository (MLSMR). A structure and activity study yielded leads with submicromolar potency.

Original languageEnglish (US)
Pages (from-to)1715-1717
Number of pages3
JournalBioorganic and Medicinal Chemistry Letters
Volume19
Issue number6
DOIs
StatePublished - Mar 15 2009
Externally publishedYes

Keywords

  • High-throughput screen
  • Huntingtin protein
  • Huntington's disease
  • Inhibitors of huntingtin protein aggregation
  • Polyglutamine aggregates
  • Quinazoline

ASJC Scopus subject areas

  • Pharmaceutical Science
  • Drug Discovery
  • Organic Chemistry
  • Molecular Medicine
  • Molecular Biology
  • Clinical Biochemistry
  • Biochemistry

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  • Cite this

    Rinderspacher, A., Cremona, M. L., Liu, Y., Deng, S. X., Xie, Y., Gong, G., Aulner, N., Többen, U., Myers, K., Chung, C., Andersen, M., Vidović, D., Schürer, S., Brandén, L., Yamamoto, A., & Landry, D. W. (2009). Potent inhibitors of Huntingtin protein aggregation in a cell-based assay. Bioorganic and Medicinal Chemistry Letters, 19(6), 1715-1717. https://doi.org/10.1016/j.bmcl.2009.01.087