Computational design of protein antigens that interact with the CDR H3 loop of HIV broadly neutralizing antibody 2F5
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William R Schief | R. Wyatt | Y. Ban | W. Schief | A. Schroeter | M. Azoitei | J. Porter | R Wyatt | J. Guenaga | M L Azoitei | Y A Ban | O Kalyuzhny | J Guenaga | A Schroeter | J Porter | O. Kalyuzhny
[1] W. Schief,et al. Design and characterization of epitope-scaffold immunogens that present the motavizumab epitope from respiratory syncytial virus. , 2011, Journal of molecular biology.
[2] K. Henrick,et al. Inference of macromolecular assemblies from crystalline state. , 2007, Journal of molecular biology.
[3] Timothy A. Whitehead,et al. Computational Design of Proteins Targeting the Conserved Stem Region of Influenza Hemagglutinin , 2011, Science.
[4] J. Mascola,et al. Relationship between Antibody 2F5 Neutralization of HIV-1 and Hydrophobicity of Its Heavy Chain Third Complementarity-Determining Region , 2009, Journal of Virology.
[5] Thomas Szyperski,et al. Computational design of a PAK1 binding protein. , 2010, Journal of molecular biology.
[6] B. Kuhlman,et al. A comparison of successful and failed protein interface designs highlights the challenges of designing buried hydrogen bonds , 2013, Protein science : a publication of the Protein Society.
[7] Steven M. Lewis,et al. Anchored Design of Protein-Protein Interfaces , 2011, PloS one.
[8] J. Recio-Rodríguez,et al. Comparison of two measuring instruments, B-pro and SphygmoCor system as reference, to evaluate central systolic blood pressure and radial augmentation index , 2012, Hypertension Research.
[9] William R Schief,et al. Advances in structure-based vaccine design. , 2013, Current opinion in virology.
[10] E. Pai,et al. Structural details of HIV-1 recognition by the broadly neutralizing monoclonal antibody 2F5: epitope conformation, antigen-recognition loop mobility, and anion-binding site. , 2008, Journal of molecular biology.
[11] K Dane Wittrup,et al. Isolating and engineering human antibodies using yeast surface display , 2006, Nature Protocols.
[12] J. Mascola,et al. HIV-1 Neutralizing Antibodies Display Dual Recognition of the Primary and Coreceptor Binding Sites and Preferential Binding to Fully Cleaved Envelope Glycoproteins , 2012, Journal of Virology.
[13] Yoshikazu Nakamura,et al. Structure of ribosomal protein L1 from Methanococcus thermolithotrophicus. Functionally important structural invariants on the L1 surface. , 2002, Acta crystallographica. Section D, Biological crystallography.
[14] E. Reinherz,et al. Antibody mechanics on a membrane-bound HIV segment essential for GP41-targeted viral neutralization , 2011, Nature Structural &Molecular Biology.
[15] D. Baker,et al. Heterologous Epitope-Scaffold Prime∶Boosting Immuno-Focuses B Cell Responses to the HIV-1 gp41 2F5 Neutralization Determinant , 2011, PloS one.
[16] Jens Meiler,et al. ROSETTA3: an object-oriented software suite for the simulation and design of macromolecules. , 2011, Methods in enzymology.
[17] T. N. Bhat,et al. The Protein Data Bank , 2000, Nucleic Acids Res..
[18] R. Wyatt,et al. Structure-guided Alterations of the gp41-directed HIV-1 Broadly Neutralizing Antibody 2F5 Reveal New Properties Regarding its Neutralizing Function , 2012, PLoS pathogens.
[19] D. Baker,et al. Computational Design of High-Affinity Epitope Scaffolds by Backbone Grafting of a Linear Epitope , 2011, Journal of Molecular Biology.
[20] F. Dyda,et al. Unexpected structural diversity in DNA recombination: the restriction endonuclease connection. , 2000, Molecular cell.
[21] David Baker,et al. Macromolecular modeling with rosetta. , 2008, Annual review of biochemistry.
[22] David Baker,et al. Proof of principle for epitope-focused vaccine design , 2014, Nature.
[23] R. Baric,et al. Increased Antibody Affinity Confers Broad In Vitro Protection against Escape Mutants of Severe Acute Respiratory Syndrome Coronavirus , 2012, Journal of Virology.
[24] Baoshan Zhang,et al. Broad and potent neutralization of HIV-1 by a gp41-specific human antibody , 2012, Nature.
[25] D. Baker,et al. Elicitation of structure-specific antibodies by epitope scaffolds , 2010, Proceedings of the National Academy of Sciences.
[26] B. Kuhlman,et al. Computational design of affinity and specificity at protein-protein interfaces. , 2009, Current opinion in structural biology.
[27] S. Koide,et al. Structural insights for engineering binding proteins based on non-antibody scaffolds. , 2012, Current opinion in structural biology.
[28] A. Kapila,et al. Picomolar affinity fibronectin domains engineered utilizing loop length diversity, recursive mutagenesis, and loop shuffling. , 2008, Journal of molecular biology.
[29] H. Liao,et al. Role of HIV membrane in neutralization by two broadly neutralizing antibodies , 2009, Proceedings of the National Academy of Sciences.
[30] Peter D. Kwong,et al. Structure and Mechanistic Analysis of the Anti-Human Immunodeficiency Virus Type 1 Antibody 2F5 in Complex with Its gp41 Epitope , 2004, Journal of Virology.
[31] Tanja Kortemme,et al. Backbone flexibility in computational protein design. , 2009, Current opinion in biotechnology.
[32] D. Baker,et al. Computation-Guided Backbone Grafting of a Discontinuous Motif onto a Protein Scaffold , 2011, Science.
[33] E. Pai,et al. Ablation of the Complementarity-Determining Region H3 Apex of the Anti-HIV-1 Broadly Neutralizing Antibody 2F5 Abrogates Neutralizing Capacity without Affecting Core Epitope Binding , 2010, Journal of Virology.
[34] L. Stamatatos,et al. Computational design of epitope-scaffolds allows induction of antibodies specific for a poorly immunogenic HIV vaccine epitope. , 2010, Structure.
[35] R. Dixon,et al. Crystal structure of isoflavone reductase from alfalfa (Medicago sativa L.). , 2006, Journal of molecular biology.
[36] T. Kepler,et al. Identification of autoantigens recognized by the 2F5 and 4E10 broadly neutralizing HIV-1 antibodies , 2013, The Journal of experimental medicine.
[37] Jeffrey J. Gray,et al. Protein-protein docking with simultaneous optimization of rigid-body displacement and side-chain conformations. , 2003, Journal of molecular biology.
[38] P. Rizkallah,et al. Crystal structure of hyaluronidase, a major allergen of bee venom. , 2000, Structure.