The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance drug binding
The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance drug binding
About this item
Full title
Author / Creator
Woodford, Mark R. , Dunn, Diana M. , Blanden, Adam R. , Capriotti, Dante , Loiselle, David , Prodromou, Chrisostomos , Panaretou, Barry , Hughes, Philip F. , Smith, Aaron , Ackerman, Wendi , Haystead, Timothy A. , Loh, Stewart N. , Bourboulia, Dimitra , Schmidt, Laura S. , Marston Linehan, W. , Bratslavsky, Gennady and Mollapour, Mehdi
Publisher
London: Nature Publishing Group UK
Journal title
Language
English
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Publisher
London: Nature Publishing Group UK
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Contents
Heat shock protein-90 (Hsp90) is an essential molecular chaperone in eukaryotes involved in maintaining the stability and activity of numerous signalling proteins, also known as clients. Hsp90 ATPase activity is essential for its chaperone function and it is regulated by co-chaperones. Here we show that the tumour suppressor FLCN is an Hsp90 client...
Alternative Titles
Full title
The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance drug binding
Authors, Artists and Contributors
Author / Creator
Dunn, Diana M.
Blanden, Adam R.
Capriotti, Dante
Loiselle, David
Prodromou, Chrisostomos
Panaretou, Barry
Hughes, Philip F.
Smith, Aaron
Ackerman, Wendi
Haystead, Timothy A.
Loh, Stewart N.
Bourboulia, Dimitra
Schmidt, Laura S.
Marston Linehan, W.
Bratslavsky, Gennady
Mollapour, Mehdi
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Primary Identifiers
Record Identifier
TN_cdi_doaj_primary_oai_doaj_org_article_51f03ab61e4442f99c334fc8fe1d2ccd
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_51f03ab61e4442f99c334fc8fe1d2ccd
Other Identifiers
ISSN
2041-1723
E-ISSN
2041-1723
DOI
10.1038/ncomms12037
