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Showing 1–9 of 9 results
Advanced filters: Author: Mehdi Mollapour Clear advanced filters

  • The Ninth International Conference on the Hsp90 Chaperone Machine concluded in October 2018, in Leysin, Switzerland. The program highlighted findings in various areas, including integrated insights into the molecular mechanism of Hsp90, cochaperones, and clients’ structure and function.

    • Laura J. Blair
    • Olivier Genest
    • Mehdi Mollapour
    News & Views
    Nature Structural & Molecular Biology
    Volume: 26, P: 92-95

  • Heritz et al. use an orthogonal approach to identify a selective inhibitor for HIF2α that disrupts its interaction with the molecular chaperone Hsp70. This inhibitor utilizes an alternative mechanism of action to previous HIF2α antagonists, providing a promising approach in addressing kidney cancer drug resistance.

    • Jennifer A. Heritz
    • Sarah J. Backe
    • Gennady Bratslavsky
    ResearchOpen Access
    Communications Medicine
    P: 1-13

  • Hsp90 is required for the folding, stability and activity of several drivers of oncogenesis. Here the authors show that Folliculin-interacting proteins (FNIP) 1 and 2, whose expression correlates with the cellular response to Hsp90 inhibitors, are co-chaperones of Hsp90 that function by inhibiting its ATPase activity.

    • Mark R. Woodford
    • Diana M. Dunn
    • Mehdi Mollapour
    ResearchOpen Access
    Nature Communications
    Volume: 7, P: 1-15

  • 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

  • Hsp90 is a molecular chaperone essential for the maintenance of cellular homeostasis. Now multiple approaches are used to study the deleterious effects of mutations in β-strand 8 of the N domain of Hsp90 and the role of the charged linker between N and M domains in mediating such effects.

    • Shinji Tsutsumi
    • Mehdi Mollapour
    • Len Neckers
    Research
    Nature Structural & Molecular Biology
    Volume: 16, P: 1141-1147

  • Molecular chaperones establish essential protein-protein interaction networks. Modified versions of these assemblies are generally enriched in certain maladies. A study published in Nature Communications used epichaperomics to identify unique changes occurring in chaperone-formed protein networks during mitosis in cancer cells.

    • Mark R. Woodford
    • Dimitra Bourboulia
    • Mehdi Mollapour
    Comments & OpinionOpen Access
    Nature Communications
    Volume: 14, P: 1-3

  • 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

  • Several therapeutic options for the treatment of renal cell carcinoma (RCC) are available, but challenges in the field such as drug resistance still exist. In this Perspective, Sager et. al discuss the role and the inhibition of the cyclin-dependent kinases CDK4 and CDK6 in RCC. The role of CDK4/6 at the interface between metabolic signalling pathways and cell cycle, the wide use of CDK4/6 inhibitors in cancer treatment, and promising preclinical studies testing these drugs in RCC support further investigation of CDK4/6 targeting in RCC.

    • Rebecca A. Sager
    • Sarah J. Backe
    • Mehdi Mollapour
    Reviews
    Nature Reviews Urology
    Volume: 19, P: 305-320