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Showing 1–3 of 3 results
Advanced filters: Author: Venkata R. Sabbasani Clear advanced filters

  • Here, the authors identify a small molecule degrader (XL44) for hRpn13 and solve the XL44-hRpn13 structure. XL44 induces apoptosis in myeloma cells with hRpn13 dependency and also targets KEN box proteins PCLAF and RRM2. Loss of hRpn13 and PCLAF abrogates XL44 restriction of cell viability.

    • Xiuxiu Lu
    • Monika Chandravanshi
    • Kylie J. Walters
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-18

  • Rpn13 is a substrate receptor of the 26S proteasome and an anti-cancer drug target. Here, the authors identify and characterize XL5, a lead compound that binds to the N-terminal Pru domain of human Rpn13 (hRpn13), solve the NMR structure of XL5-ligated hRpn13 Pru and develop XL5-PROTACs that preferentially target an identified hRpn13 Pru fragment present in multiple myeloma cells.

    • Xiuxiu Lu
    • Venkata R. Sabbasani
    • Kylie J. Walters
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-18

  • Bifunctional ‘MoDE-A’ molecules, which contain ligands that bind to an extracellular protein and carbohydrate residues that recruit it to the asialoglycoprotein receptor, mediate cellular uptake and lysosomal turnover of target proteins.

    • David F. Caianiello
    • Mengwen Zhang
    • David A. Spiegel
    Research
    Nature Chemical Biology
    Volume: 17, P: 947-953