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Understanding of the Hsp90 molecular chaperone reaches new heights

Nature Structural & Molecular Biology volume 17, pages 1400–1404 (2010)Cite this article

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Heat shock protein 90 (Hsp90) was the focus of a recent meeting in the Swiss Alps, where the Hsp90 community met to discuss the operation and functions of this ubiquitous and essential molecular chaperone.

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Figure 1: A model of Hsp90 client loading.

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Author information

Authors and Affiliations

  1. Cara K. Vaughan is at the Institute of Structural Molecular Biology, Birkbeck College, London, UK.,

    Cara K Vaughan

  2. Len Neckers is at the National Cancer Institute, Bethesda, Maryland, USA.,

    Len Neckers

  3. Peter W. Piper is at the University of Sheffield, Sheffield, UK.,

    Peter W Piper

Authors
  1. Cara K Vaughan
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  2. Len Neckers
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  3. Peter W Piper
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Corresponding author

Correspondence to Peter W Piper.

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The authors declare no competing financial interests.

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Vaughan, C., Neckers, L. & Piper, P. Understanding of the Hsp90 molecular chaperone reaches new heights. Nat Struct Mol Biol 17, 1400–1404 (2010). https://doi.org/10.1038/nsmb1210-1400

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