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Showing 1–17 of 17 results
Advanced filters: Author: Shaun Rawson Clear advanced filters

  • An endogenous proteasome inhibitor was identified 30 years ago, but its mechanism remained unclear. Rawson et al. show that this inhibitor is present within the interior of the proteasome, where it simultaneously inhibits all six active sites.

    • Shaun Rawson
    • Richard M. Walsh Jr.
    • John Hanna
    Research
    Nature Structural & Molecular Biology
    Volume: 29, P: 791-800

  • To prevent promiscuous protein degradation, proteasomes are initially assembled as inactive complexes. Their activation is autocatalytic and coupled to assembly. Here the authors uncover key aspects of the autocatalytic activation mechanism.

    • Benjamin Velez
    • Richard M. Walsh Jr.
    • John Hanna
    Research
    Nature Structural & Molecular Biology
    Volume: 31, P: 1167-1175

  • RAF kinases are autoinhibited in the cytosol and are activated by recruitment to the plasma membrane by GTP-bound RAS. Here, the authors describe cryoEM structures of a membrane-free KRAS/BRAF/MEK/14-3-3 complex that capture a pre-activation intermediate with BRAF still in an autoinhibited state.

    • Eunyoung Park
    • Shaun Rawson
    • Michael J. Eck
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-11

  • The proteasome core particle (CP) assembles through the fusion of two half-CP precursors, yielding a complete but immature CP structure. Here the authors identify by cryogenic electron microscopy the structure of a post-fusion assembly intermediate, revealing how associated factors collaborate to chaperone CP assembly and maturation.

    • Richard M. Walsh Jr.
    • Shaun Rawson
    • John Hanna
    Research
    Nature Structural & Molecular Biology
    Volume: 30, P: 1516-1524

  • Most proteases require a catalytic triad for enzymatic function. N-terminal nucleophile enzymes such as the proteasome are unique in possessing two nucleophiles. Here the authors provide evidence that such enzymes utilize a catalytic pentad mechanism that allows for regulation of both nucleophiles.

    • Darlene Fung
    • Aida Razi
    • John Hanna
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-12

  • Precise protease positioning and gating of the proteasome core require the ordered assembly of 28 subunits. Cryo-EM structures of seven intermediates visualize five dedicated chaperones and three propeptides mediating step-by-step assembly of the human 20S proteasome.

    • Frank Adolf
    • Jiale Du
    • Brenda A. Schulman
    ResearchOpen Access
    Nature Structural & Molecular Biology
    Volume: 31, P: 1176-1188

  • A newly developed maternally selective nanobody antagonist against the angiotensin II type I receptor stabilizes the receptor in a hybrid conformation and simultaneously binds with specific small-molecule antagonists.

    • Meredith A. Skiba
    • Sarah M. Sterling
    • Andrew C. Kruse
    Research
    Nature Chemical Biology
    Volume: 20, P: 1577-1585

  • Cryo-electron microscopy structures of a folding intermediate on the BAM complex of Escherichia coli reveal how interactions between the BamA catalyst and substrate permit stable association during folding, followed by rapid turnover.

    • David Tomasek
    • Shaun Rawson
    • Daniel Kahne
    Research
    Nature
    Volume: 583, P: 473-478

  • The RXFP1 relaxin receptor is a critical mediator of physiological adaptation to pregnancy and an emerging drug target. RXFP1 activation was found to entail an unexpected mechanism of ectodomain disinhibition resulting in downstream signaling.

    • Sarah C. Erlandson
    • Shaun Rawson
    • Andrew C. Kruse
    Research
    Nature Chemical Biology
    Volume: 19, P: 1013-1021

  • Porphyromonas gingivalis, an oral anaerobe involved in the pathogenesis of periodontitis, relies on extracellular proteases to degrade proteins into peptides for growth, but how these peptides enter the cell is unknown. Here, the authors identify RagAB as the outer-membrane importer for these peptides and solve its structure, elucidating that it works via a ‘pedal bin’ mechanism of nutrient uptake.

    • Mariusz Madej
    • Joshua B. R. White
    • Bert van den Berg
    Research
    Nature Microbiology
    Volume: 5, P: 1016-1025