High-content, high-throughput analysis of cell cycle perturbations induced by the HSP90 inhibitor XL888.
<h4>Background</h4>Many proteins that are dysregulated or mutated in cancer cells rely on the molecular chaperone HSP90 for their proper folding and activity, which has led to considerable interest in HSP90 as a cancer drug target. The diverse array of HSP90 client proteins encompasses o...
Guardado en:
Autores principales: | Susan K Lyman, Suzanne C Crawley, Ruoyu Gong, Joanne I Adamkewicz, Garth McGrath, Jason Y Chew, Jennifer Choi, Charles R Holst, Leanne H Goon, Scott A Detmer, Jana Vaclavikova, Mary E Gerritsen, Robert A Blake |
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Formato: | article |
Lenguaje: | EN |
Publicado: |
Public Library of Science (PLoS)
2011
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Materias: | |
Acceso en línea: | https://doaj.org/article/f3255661be8a49999d93ff431dca0903 |
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