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  1. Hsp90 - Wikipedia

    Hsp90 (heat shock protein 90) is a chaperone protein that assists other proteins to fold properly, stabilizes proteins against heat stress, and aids in protein degradation. It also stabilizes a number of proteins required for tumor growth, which is why …

  2. The HSP90 chaperone machinery - Nature Reviews Molecular …

    Apr 21, 2017 · The heat shock protein 90 (HSP90) chaperone machinery is a key regulator of proteostasis under both physiological and stress conditions in eukaryotic cells.

  3. The HSP90 Family: Structure, Regulation, Function, and …

    HSP90 proteins take part in essential cellular processes and regulatory pathways like apoptosis, cell cycle control, cell viability, protein folding and degradation, and signalling events. In addition, they induce the adaptive immunity by activation of antigen presenting cells and dendritic cells.

  4. Hsp90: structure and function - PubMed

    Hsp90 is a highly abundant and ubiquitous molecular chaperone which plays an essential role in many cellular processes including cell cycle control, cell survival, hormone and other signalling pathways.

  5. Heat shock protein 90: biological functions, diseases, and …

    Heat shock protein 90 (Hsp90) is a predominant member among Heat shock proteins (HSPs), playing a central role in cellular protection and maintenance by aiding in the folding, stabilization, and modification of diverse protein substrates. It ...

  6. Structure, Function, and Regulation of the Hsp90 Machinery

    Heat shock protein 90 (Hsp90) is a molecular chaperone involved in the maturation of a plethora of substrates (“clients”), including protein kinases, transcription factors, and E3 ubiquitin ligases, positioning Hsp90 as a central regulator of ...

  7. Structural and functional complexity of HSP90 in cellular ... - Nature

    Jul 31, 2023 · We describe how these variations influence context-dependent functions of HSP90 as well as its interaction with other chaperones, co-chaperones and proteins, and how this structural complexity of...

  8. The Hsp90 molecular chaperone governs client proteins by …

    Jun 15, 2023 · The central eukaryotic molecular chaperone Hsp90 physically interacts with a large fraction of the yeast proteome by targeting select intrinsically disordered regions (IDRs) on client proteins to both regulate their cellular activities and maintain the proteostasic status of IDR-containing clients.

  9. The HSP90 Family: Structure, Regulation, Function, and ... - PubMed

    Aug 29, 2018 · The mammalian HSP90 family of proteins is a cluster of highly conserved molecules that are involved in myriad cellular processes. Their distribution in various cellular compartments underlines their essential roles in cellular homeostasis.

  10. HSP90 regulates dCK stability and inhibits ionizing radiation …

    2 days ago · HSP90 will be efficiently inhibited while IR is combined with 17-AAG treatment, which supports the HSP90-WWP1/2-NEDD4L-dCK axis’ antitumor effect (Fig. 8). As a result of our research, we have ...

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