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- W2156652016 abstract "The molecular chaperone heat-shock protein of 90 kDa (Hsp90) stabilizes various proteins and occupies a central position in cellular networks. Hsp90 inhibitors are being tested in clinical trials as anticancer drugs. Recent studies have illuminated the unappreciated significance of this chaperone in chromatin transactions and this review focuses on its role in gene expression. By comparing the different mechanisms by which Hsp90 orchestrates transcriptional regulation, the review outlines the contributions of this function to the cellular and organismal phenotype. We chart exciting avenues for research to gain comprehensive insights in the chaperone's importance in cellular physiology, thereby presenting novel opportunities for therapeutic intervention. The molecular chaperone heat-shock protein of 90 kDa (Hsp90) stabilizes various proteins and occupies a central position in cellular networks. Hsp90 inhibitors are being tested in clinical trials as anticancer drugs. Recent studies have illuminated the unappreciated significance of this chaperone in chromatin transactions and this review focuses on its role in gene expression. By comparing the different mechanisms by which Hsp90 orchestrates transcriptional regulation, the review outlines the contributions of this function to the cellular and organismal phenotype. We chart exciting avenues for research to gain comprehensive insights in the chaperone's importance in cellular physiology, thereby presenting novel opportunities for therapeutic intervention." @default.
- W2156652016 created "2016-06-24" @default.
- W2156652016 creator A5033690391 @default.
- W2156652016 creator A5086283739 @default.
- W2156652016 date "2013-04-01" @default.
- W2156652016 modified "2023-10-18" @default.
- W2156652016 title "Hsp90@chromatin.nucleus: an emerging hub of a networker" @default.
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- W2156652016 doi "https://doi.org/10.1016/j.tcb.2012.11.007" @default.
- W2156652016 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/23286900" @default.