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Showing 1–6 of 6 results
Advanced filters: Author: Christopher E. Berndsen Clear advanced filters

  • Vps75 is a histone chaperone that associates with the Rtt109 acteyltransferase. The structure of Vps75 and further biochemical analysis suggest how Vps75 functions to alter histone H3K9 acetylation during S phase, and suggest a model for how it activates the histone acetyltransferase.

    • Christopher E Berndsen
    • Toshiaki Tsubota
    • John M Denu
    Research
    Nature Structural & Molecular Biology
    Volume: 15, P: 948-956

  • Ubiquitin-conjugating (E2) enzymes contain a conserved asparagine that has been proposed to stabilize an oxyanion intermediate. Structural and biochemical studies of Ubc13 suggest that this residue has a structural role in stabilizing the E2 active site.

    • Christopher E Berndsen
    • Reuven Wiener
    • Cynthia Wolberger
    Research
    Nature Chemical Biology
    Volume: 9, P: 154-156

  • Here, the authors present cryoEMPEM, a method for high-resolution structural analysis of vaccine-elicited polyclonal antibody responses. They apply cryoEMPEM in combination with standard serology experiments to characterize the polyclonal antibody (pAb) responses elicited in rhesus macaques by HIV Env trimer immunogens and were able to determine up to 8 different polyclonal antibody structures in complex with their respective antigen from a single cryoEM dataset.

    • Aleksandar Antanasijevic
    • Leigh M. Sewall
    • Andrew B. Ward
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-17

  • Nanoparticles are a promising approach to increase immunogenicity of protein antigens for vaccines. Here, Brouwer et al. design self-assembling, two-component protein NPs that present native-like SOSIP trimers of HIV envelope protein and determine immunogenicity in a small animal model.

    • Philip J. M. Brouwer
    • Aleksandar Antanasijevic
    • Rogier W. Sanders
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-17

  • Ubiquitin E3 ligases catalyze the final step of the ubiquitination cascade, promoting the transfer of ubiquitin from the E2 to the substrate target. Recent structural and biochemical studies have given insights in the catalytic mechanisms of all three E3 ligase classes, as discussed in this Review.

    • Christopher E Berndsen
    • Cynthia Wolberger
    Reviews
    Nature Structural & Molecular Biology
    Volume: 21, P: 301-307