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Showing 1–3 of 3 results
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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.

    • Cara K Vaughan
    • Len Neckers
    • Peter W Piper
    News & Views
    Nature Structural & Molecular Biology
    Volume: 17, P: 1400-1404

  • Intermediate conformations of the Hsp90 ATPase cycle have been identified in solution by fluorescence resonance energy transfer, and the impact of nucleotides and of modulatory cochaperones has been visualized in real time.

    • Len Neckers
    • Shinji Tsutsumi
    • Mehdi Mollapour
    News & Views
    Nature Structural & Molecular Biology
    Volume: 16, P: 235-236

  • Numerous oncoproteins depend on the molecular chaperone heat shock protein 90 (HSP90). However, the optimal use of HSP90-targeted therapeutics will depend on understanding the complexity of HSP90 regulation and the degree to which the chaperone participates in both neoplastic and normal cellular physiology.

    • Jane Trepel
    • Mehdi Mollapour
    • Len Neckers
    Reviews
    Nature Reviews Cancer
    Volume: 10, P: 537-549