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Showing 1–3 of 3 results
Advanced filters: Author: Rob C. Laister Clear advanced filters

  • Pirh2 is one of several ubiquitin ligases known to modify and negatively regulate p53. Solution studies reveal the structures of the three Pirh2 domains and indicate that the C-terminal domain of Pirh2 interacts with the p53 tetramerization domain. Additional data suggest that Pirh2 preferentially modifies the tetrameric, transcriptionally active form of p53 for proteasome-mediated degradation.

    • Yi Sheng
    • Rob C Laister
    • Cheryl H Arrowsmith
    Research
    Nature Structural & Molecular Biology
    Volume: 15, P: 1334-1342

  • Several rearrangements of the MLL gene are associated with acute leukemia, including the fusion of MLL with a RAS effector protein, AF6. Here the authors show that the truncated AF6 can induce AF6-MLL dimerization and drive its oncogenic activity.

    • Matthew J. Smith
    • Elizabeth Ottoni
    • Mitsuhiko Ikura
    ResearchOpen Access
    Nature Communications
    Volume: 8, P: 1-13