Search Results - "Hugh K Haddox"

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  1. 1

    Experimental Estimation of the Effects of All Amino-Acid Mutations to HIV's Envelope Protein on Viral Replication in Cell Culture by Haddox, Hugh K, Dingens, Adam S, Bloom, Jesse D

    Published in PLoS pathogens (13-12-2016)
    “…HIV is notorious for its capacity to evade immunity and anti-viral drugs through rapid sequence evolution. Knowledge of the functional effects of mutations to…”
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  2. 2

    Comprehensive Mapping of HIV-1 Escape from a Broadly Neutralizing Antibody by Dingens, Adam S., Haddox, Hugh K., Overbaugh, Julie, Bloom, Jesse D.

    Published in Cell host & microbe (14-06-2017)
    “…Precisely defining how viral mutations affect HIV’s sensitivity to antibodies is vital to develop and evaluate vaccines and antibody immunotherapeutics…”
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  3. 3

    Mapping mutational effects along the evolutionary landscape of HIV envelope by Haddox, Hugh K, Dingens, Adam S, Hilton, Sarah K, Overbaugh, Julie, Bloom, Jesse D

    Published in eLife (28-03-2018)
    “…The immediate evolutionary space accessible to HIV is largely determined by how single amino acid mutations affect fitness. These mutational effects can shift…”
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  4. 4

    De novo design of immunoglobulin-like domains by Chidyausiku, Tamuka M., Mendes, Soraia R., Klima, Jason C., Nadal, Marta, Eckhard, Ulrich, Roel-Touris, Jorge, Houliston, Scott, Guevara, Tibisay, Haddox, Hugh K., Moyer, Adam, Arrowsmith, Cheryl H., Gomis-Rüth, F. Xavier, Baker, David, Marcos, Enrique

    Published in Nature communications (03-10-2022)
    “…Antibodies, and antibody derivatives such as nanobodies, contain immunoglobulin-like (Ig) β-sandwich scaffolds which anchor the hypervariable antigen-binding…”
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  5. 5

    Complete functional mapping of infection- and vaccine-elicited antibodies against the fusion peptide of HIV by Dingens, Adam S, Acharya, Priyamvada, Haddox, Hugh K, Rawi, Reda, Xu, Kai, Chuang, Gwo-Yu, Wei, Hui, Zhang, Baoshan, Mascola, John R, Carragher, Bridget, Potter, Clinton S, Overbaugh, Julie, Kwong, Peter D, Bloom, Jesse D

    Published in PLoS pathogens (01-07-2018)
    “…Eliciting broadly neutralizing antibodies (bnAbs) targeting envelope (Env) is a major goal of HIV vaccine development, but cross-clade breadth from…”
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    De novo design of obligate ABC-type heterotrimeric proteins by Bermeo, Sherry, Favor, Andrew, Chang, Ya-Ting, Norris, Andrew, Boyken, Scott E., Hsia, Yang, Haddox, Hugh K., Xu, Chunfu, Brunette, T. J., Wysocki, Vicki H., Bhabha, Gira, Ekiert, Damian C., Baker, David

    Published in Nature structural & molecular biology (01-12-2022)
    “…The de novo design of three protein chains that associate to form a heterotrimer (but not any of the possible two-chain heterodimers) and that can drive the…”
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  9. 9

    Deep mutational scanning reveals functional constraints and antibody-escape potential of Lassa virus glycoprotein complex by Carr, Caleb R, Crawford, Katharine H D, Murphy, Michael, Galloway, Jared G, Haddox, Hugh K, Matsen, 4th, Frederick A, Andersen, Kristian G, King, Neil P, Bloom, Jesse D

    Published in Immunity (Cambridge, Mass.) (10-09-2024)
    “…Lassa virus is estimated to cause thousands of human deaths per year, primarily due to spillovers from its natural host, Mastomys rodents. Efforts to create…”
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  10. 10

    Dissecting the stability determinants of a challenging de novo protein fold using massively parallel design and experimentation by Kim, Tae-Eun, Tsuboyama, Kotaro, Houliston, Scott, Martell, Cydney M, Phoumyvong, Claire M, Lemak, Alexander, Haddox, Hugh K, Arrowsmith, Cheryl H, Rocklin, Gabriel J

    “…Designing entirely new protein structures remains challenging because we do not fully understand the biophysical determinants of folding stability. Yet, some…”
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    The Role of Configurational Entropy in Miniprotein Stability by Estrada Pabón, Jan D, Haddox, Hugh K, Van Aken, Greg, Pendleton, Ian M, Eramian, Hamed, Singer, Jedediah M, Schrier, Joshua

    Published in The journal of physical chemistry. B (01-04-2021)
    “…Predicting protein stability is a challenge due to the many competing thermodynamic effects. Through de novo protein design, one begins with a target structure…”
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