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Showing 1–6 of 6 results
Advanced filters: Author: Robert J. Ragotte Clear advanced filters

  • The combination of computational design, laboratory-based screening and biophysical validation enables the de novo generation of variable heavy-chain antibody fragments and antibodies that precisely target chosen disease-related molecules.

    • Nathaniel R. Bennett
    • Joseph L. Watson
    • David Baker
    ResearchOpen Access
    Nature
    P: 1-11

  • Antibodies can have synergistic effects, but mechanisms are not well understood. Here, Ragotte et al. identify three antibodies that bind neighbouring epitopes on CyRPA, a malaria vaccine candidate, and show that lateral interactions between the antibodies slow dissociation and inhibit parasite growth synergistically.

    • Robert J. Ragotte
    • David Pulido
    • Simon J. Draper
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-12

  • Deep learning methods have been used to design proteins that can neutralize the effects of three-finger toxins found in snake venom, which could lead to the development of safer and more accessible antivenom treatments.

    • Susana Vázquez Torres
    • Melisa Benard Valle
    • David Baker
    ResearchOpen Access
    Nature
    Volume: 639, P: 225-231

  • Fine-tuning the RoseTTAFold structure prediction network on protein structure denoising tasks yields a generative model for protein design that achieves outstanding performance on a wide range of protein structure and function design challenges.

    • Joseph L. Watson
    • David Juergens
    • David Baker
    ResearchOpen Access
    Nature
    Volume: 620, P: 1089-1100

  • RH5, which is part of the trimeric RCR-complex essential for invasion, is a vaccine candidate for malaria. Here, Williams et al. show that monoclonal antibodies targeting each of the three proteins in the RCR-complex can work together to more effectively block the invasion of red blood cells by Plasmodium falciparum and design a combination vaccine candidate.

    • Barnabas G. Williams
    • Lloyd D. W. King
    • Simon J. Draper
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-16

  • Structural studies show how the PfRCR complex of Plasmodium falciparum forms a bridge between erythrocyte and parasite membranes, and how PfCyRPA-binding antibodies neutralize invasion through a steric mechanism, opening the way to new approaches in rational vaccine design.

    • Brendan Farrell
    • Nawsad Alam
    • Matthew K. Higgins
    ResearchOpen Access
    Nature
    Volume: 625, P: 578-584