The FNIP co-chaperones decelerate the Hsp90 chaperone cycle …

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  • DOI 10.1038/ncomms12037
  • PMID https://pubmed.ncbi.nlm.nih.gov/27353360
  • OpenAlex ID W2464418635
  • Type Article
  • Language EN
  • Published 29 Jun 2016
  • Volume 7 (1)
  • Pages 12037
  • Source Nature Communications
  • Publisher Nature Portfolio
  • FWCI 3.46
  • Countries 2
  • Institutions 8
  • Added 10 Oct 2025
  • Updated 16 Oct 2026
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The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance drug binding

Article 2016 EN Gold

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 protein and its binding partners FNIP1/FNIP2 func…

76

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17

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3.46

FWCI

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Authors & Affiliations
17 authors
#AuthorInstitutionsORCID
1 Mark R. Woodford SUNY Upstate Medical Universit… (US)
2 Diana M. Dunn SUNY Upstate Medical Universit… (US)
3 Adam R. Blanden SUNY Upstate Medical Universit… (US)
4 Dante Capriotti SUNY Upstate Medical Universit… (US) —
5 David R. Loiselle Duke Medical Center (US)
6 Chrisostomos Prodromou University of Sussex (GB)
7 Barry Panaretou King's College London (GB)
8 Philip F. Hughes Duke Medical Center (US)
9 Aaron P. Smith Duke Medical Center (US)
10 Wendi Ackerman SUNY Upstate Medical Universit… (US)
11 Timothy Haystead Duke Medical Center (US)
12 Stewart N. Loh SUNY Upstate Medical Universit… (US)
13 Dimitra Bourboulia SUNY Upstate Medical Universit… (US)
14 Laura S. Schmidt Frederick National Laboratory … (US) National Cancer Institute (US) +2
15 William Marston Linehan National Cancer Institute (US) Center for Cancer Research (US)
16 Gennady Bratslavsky SUNY Upstate Medical Universit… (US)
17 Mehdi Mollapour Corresponding SUNY Upstate Medical Universit… (US)

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