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Showing 1–7 of 7 results
Advanced filters: Author: Joel Quispe Clear advanced filters

  • Host antibodies can alter the glycan binding of adhesin proteins from infectious bacteria, but the antibodies’ mechanisms of action remain unclear. Here, the authors define four mechanisms of modulation, including ligand mimicry and multiple modes of allosteric interference.

    • Kelli L. Hvorecny
    • Gianluca Interlandi
    • Justin M. Kollman
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-15

  • Convergent mutations in hot spots of the spike proteins of currently circulating SARS-CoV-2 Omicron variants increase the binding affinity for the host receptor and promote more efficient fusion with host cell membranes.

    • Amin Addetia
    • Luca Piccoli
    • David Veesler
    ResearchOpen Access
    Nature
    Volume: 621, P: 592-601

  • Cryo-EM of human PRPS1 shows the nucleotide-synthesizing enzyme assembling into filaments that accommodate active and inhibited conformations. Engineered and disease mutations reveal that filament assembly stabilizes allosteric sites, enhancing catalytic activity.

    • Kelli L. Hvorecny
    • Kenzee Hargett
    • Justin M. Kollman
    Research
    Nature Structural & Molecular Biology
    Volume: 30, P: 391-402

  • A series of cryo-EM structures of human IMPDH1 variants reveal polymorphic filaments. Blindness-associated mutations in IMPDH1 are characterized and half disrupt feedback inhibition. Together, these findings are a foundation for understanding IMPDH1 in retinal function and disease.

    • Anika L. Burrell
    • Chuankai Nie
    • Justin M. Kollman
    Research
    Nature Structural & Molecular Biology
    Volume: 29, P: 47-58

  • Structural characterization of B6, a monoclonal antibody that cross-reacts with eight β-coronavirus spike proteins from three viral lineages, reveals a conserved cryptic epitope that could serve as a target for structure-guided design of a pan-β-coronavirus vaccine.

    • Maximilian M. Sauer
    • M. Alejandra Tortorici
    • David Veesler
    Research
    Nature Structural & Molecular Biology
    Volume: 28, P: 478-486