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Potent inhibitors of Huntingtin protein aggregation in a cell-based assay |
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| Authors: | 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 |
| Affiliation: | 1. Division of Experimental Therapeutics, Department of Medicine, Columbia University, 630 West 168th Street, New York, NY 10032, USA;2. Genome Center, Columbia University, 1150 St. Nicholas Ave., New York, NY 10032, USA;3. Scientific Computing, The Scripps Research Institute, 5353 Parkside Drive, Jupiter, FL 33458, USA;4. Department of Neurology, Columbia University, 630 West 168th Street, New York, NY 10032, USA |
| 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. |
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