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.

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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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Lenguaje:EN
Publicado: Nature Portfolio 2018
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Acceso en línea:https://doaj.org/article/22d6d57dbf0548efa5ef84106a4676a4
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spelling oai:doaj.org-article:22d6d57dbf0548efa5ef84106a4676a42021-12-02T16:49:38ZStructure-guided design of an Hsp90β N-terminal isoform-selective inhibitor10.1038/s41467-017-02013-12041-1723https://doaj.org/article/22d6d57dbf0548efa5ef84106a4676a42018-01-01T00:00:00Zhttps://doi.org/10.1038/s41467-017-02013-1https://doaj.org/toc/2041-1723The 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.Anuj KhandelwalCaitlin N. KentMaurie BalchShuxia PengSanket J. MishraJunpeng DengVictor W. DayWeiya LiuChitra SubramanianMark CohenJeffery M. HolzbeierleinRobert MattsBrian S. J. BlaggNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-7 (2018)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
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
Structure-guided design of an Hsp90β N-terminal isoform-selective inhibitor
description 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.
format article
author 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
author_facet 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
author_sort Anuj Khandelwal
title Structure-guided design of an Hsp90β N-terminal isoform-selective inhibitor
title_short Structure-guided design of an Hsp90β N-terminal isoform-selective inhibitor
title_full Structure-guided design of an Hsp90β N-terminal isoform-selective inhibitor
title_fullStr Structure-guided design of an Hsp90β N-terminal isoform-selective inhibitor
title_full_unstemmed Structure-guided design of an Hsp90β N-terminal isoform-selective inhibitor
title_sort structure-guided design of an hsp90β n-terminal isoform-selective inhibitor
publisher Nature Portfolio
publishDate 2018
url https://doaj.org/article/22d6d57dbf0548efa5ef84106a4676a4
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