Structure-guided design of an Hsp90β N-terminal isoform-selective inhibitor
The molecular chaperone Hsp90 oversees the folding of many proteins associated with cancer progression but existing small-molecule inhibitors of this pathway are not isoform-selective. Here, the authors rationally design an Hsp90 inhibitor that displays high selectivity for the Hsp90β isoform.
Guardado en:
Autores principales: | Anuj Khandelwal, Caitlin N. Kent, Maurie Balch, Shuxia Peng, Sanket J. Mishra, Junpeng Deng, Victor W. Day, Weiya Liu, Chitra Subramanian, Mark Cohen, Jeffery M. Holzbeierlein, Robert Matts, Brian S. J. Blagg |
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Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2018
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Materias: | |
Acceso en línea: | https://doaj.org/article/22d6d57dbf0548efa5ef84106a4676a4 |
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