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by Doria-Rose, Nicole A and Schramm, Chaim A and Gorman, Jason and Moore, Penny L and Bhiman, Jinal N and Dekosky, Brandon J and Ernandes, Michael J and Georgiev, Ivelin S and Kim, Helen J and Pancera, Marie and Staupe, Ryan P and Altae-Tran, Han R and Bailer, Robert T and Crooks, Ema T and Cupo, Albert and z, Aliaksan and Garrett, Nigel J and Hoi, Kam H and Kong, Rui and Louder, Mark K and Longo, Nancy S and McKee, Krisha and Nonyane, Molati and O'Dell, Sijy and Roark, Ryan S and Rudicell, Rebecca S and Schmidt, Stephen D and Sheward, Daniel J and Soto, Cinque and Wibmer, Constantinos Kurt and Yang, Yongping and Zhang, Zhenhai and Mullikin, James C and Binley, James M and Sanders, Rogier W and Wilson, Ian A and Moore, John P and Ward, Anew B and Georgiou, George and Williamson, Carolyn and Abdool Karim, Salim S and Morris, Lynn and Kwong, Peter D and Shapiro, Lawrence and Mascola, John R and Becker, Jesse and Benjamin, Betty and Blakesley, Robert and Bouffard, Gerry and Brooks, Shelise and Coleman, Holly and Dekhtyar, Mila and Gregory, Michael and Guan, Xiaobin and Gupta, Jyoti and Han, Joel and Hargrove, April and Ho, Shi-ling and Johnson, Taccara and Legaspi, Richelle and Lovett, Sean and Maduro, Quino and Masiello, Cathy and Maskeri, Baishali and McDowell, Jenny and Montemayor, Casana and Mullikin, James and Park, Morgan and Riebow, Nancy and Schandler, Karen and Schmidt, Brian and Sison, Christina and Stantripop, Mal and Thomas, James and Thomas, Pam and Vemulapalli, Meg and Young, Alice and NISC Comparative Sequencing and NISC Comparative Sequencing Program
Nature, ISSN 0028-0836, 2014, Volume 509, Issue 7498, pp. 55 - 62
Antibodies capable of neutralizing HIV-1 often target variable regions 1 and 2 (V1V2) of the HIV-1 envelope, but the mechanism of their elicitation has been... 
B-CELLS | MAXIMUM-LIKELIHOOD | STRUCTURAL BASIS | HIV-1-NEUTRALIZING ANTIBODIES | MULTIDISCIPLINARY SCIENCES | IMMUNODEFICIENCY-VIRUS TYPE-1 | VACCINE EFFICACY | INFECTION | BROAD | HUMAN MONOCLONAL-ANTIBODIES | ENVELOPE TRIMER | Complementarity Determining Regions - genetics | Epitope Mapping | Epitopes, B-Lymphocyte - chemistry | Humans | AIDS Vaccines - immunology | Molecular Sequence Data | Antibody Affinity - immunology | Neutralization Tests | Epitopes, B-Lymphocyte - immunology | HIV Antibodies - isolation & purification | HIV Infections - immunology | Antibodies, Neutralizing - immunology | HIV Antibodies - immunology | HIV Envelope Protein gp160 - chemistry | Complementarity Determining Regions - chemistry | HIV-1 - chemistry | Binding Sites - immunology | B-Lymphocytes - metabolism | Protein Structure, Tertiary | Amino Acid Sequence | CD4 Antigens - immunology | B-Lymphocytes - cytology | Models, Molecular | Antibody Affinity - genetics | Antibodies, Neutralizing - genetics | HIV Antibodies - chemistry | AIDS Vaccines - chemistry | Antibodies, Neutralizing - isolation & purification | Cell Lineage | HIV-1 - immunology | B-Lymphocytes - immunology | Antibodies, Neutralizing - chemistry | Complementarity Determining Regions - immunology | HIV Envelope Protein gp160 - immunology | HIV Antibodies - genetics | Somatic Hypermutation, Immunoglobulin - genetics | CD4 Antigens - metabolism | Evolution, Molecular | Viral antibodies | Antigen-antibody reactions | AIDS vaccines | AIDS (Disease) | Antibodies | Physiological aspects | Research | AIDS research | Cell culture | Genes | Human immunodeficiency virus--HIV | Phylogenetics | Amino acids | Infections | Genomes | Mutation
Journal Article
Journal Article
Science, ISSN 0036-8075, 8/2010, Volume 329, Issue 5993, pp. 856 - 861
Cross-reactive neutralizing antibodies (NAbs) are found in the sera of many HIV-1-infected individuals, but the virologie basis of their neutralization remains... 
Proteins | Reactivity | Infectious diseases | B lymphocytes | Enzyme linked immunosorbent assay | REPORTS | Antibodies | Research facilities | Viruses | Amino acids | HIV 1 | INDIVIDUALS | PANEL | IMMUNOGENICITY | VIRUS | SPECIFICITIES | MULTIDISCIPLINARY SCIENCES | HIGH-AFFINITY | GP120 | GLYCOPROTEIN | TYPE-1 INFECTION | BREADTH | Antibody Specificity | Humans | Molecular Sequence Data | Neutralization Tests | HIV Antibodies - isolation & purification | HIV Envelope Protein gp120 - metabolism | Epitopes - immunology | Genes, Immunoglobulin Heavy Chain | HIV Envelope Protein gp120 - immunology | HIV Infections - immunology | Antibodies, Neutralizing - immunology | HIV Antibodies - immunology | Drug Design | Protein Engineering | HIV Envelope Protein gp120 - chemistry | Antibodies, Monoclonal - immunology | Recombinant Proteins - metabolism | CD4 Antigens - immunology | Enzyme-Linked Immunosorbent Assay | Genes, Immunoglobulin Light Chain | HIV Infections - virology | Recombinant Proteins - chemistry | Antibodies, Monoclonal - isolation & purification | HIV-1 - genetics | Antibodies, Neutralizing - isolation & purification | Cross Reactions | HIV-1 - immunology | B-Lymphocytes - immunology | Recombinant Proteins - immunology | AIDS Vaccines | Binding Sites, Antibody | CD4 Antigens - metabolism | Monoclonal antibodies | Immunoglobulins | Research | HIV (Viruses) | Glycoproteins | Immunology | Human immunodeficiency virus--HIV
Journal Article
Science, ISSN 0036-8075, 9/2011, Volume 333, Issue 6049, pp. 1593 - 1602
Antibody VRC01 is a human immunoglobulin that neutralizes about 90% of HIV-1 isolates. To understand how such broadly neutralizing antibodies develop, we used... 
Germ cells | Neutralizing antibodies | B lymphocytes | RESEARCH ARTICLES | Genomics | Alleles | Antibodies | Phylogenetics | Epitopes | HIV 1 | High throughput nucleotide sequencing | DESIGN | DOMAIN | EPITOPE | MULTIDISCIPLINARY SCIENCES | BROAD | DIVERSITY | GLYCOPROTEIN | GP120 | MONOCLONAL-ANTIBODIES | SELECTION | BREADTH | Antibody Specificity | Complementarity Determining Regions - genetics | Humans | Immunoglobulin Heavy Chains - chemistry | Molecular Sequence Data | Crystallography, X-Ray | HIV Antibodies - isolation & purification | HIV Envelope Protein gp120 - metabolism | Genes, Immunoglobulin Heavy Chain | HIV Envelope Protein gp120 - immunology | Immunoglobulin Light Chains - chemistry | HIV Infections - immunology | Antibodies, Neutralizing - immunology | HIV Antibodies - immunology | HIV-1 - chemistry | Immunoglobulin J-Chains - genetics | Base Sequence | HIV Envelope Protein gp120 - chemistry | Binding Sites | Immunoglobulin Heavy Chains - immunology | Immunoglobulin Light Chains - immunology | Amino Acid Sequence | Models, Molecular | Antibody Affinity | Antibodies, Neutralizing - genetics | HIV Antibodies - chemistry | Sequence Analysis, DNA | Antibodies, Neutralizing - isolation & purification | HIV-1 - immunology | Antibodies, Neutralizing - chemistry | Immunoglobulin Fab Fragments - chemistry | AIDS Vaccines | High-Throughput Nucleotide Sequencing | HIV Antibodies - genetics | Immunoglobulin Fab Fragments - immunology | Mutation | Binding Sites, Antibody | CD4 Antigens - metabolism | Evolution, Molecular | Viral antibodies | X-ray crystallography | Immunoglobulins | Physiological aspects | Genetic aspects | HIV (Viruses) | Health aspects | Methods | ANTIBODIES | IMMUNITY | BASIC BIOLOGICAL SCIENCES | GENETICS | IMMUNOGLOBULINS | CRYSTAL STRUCTURE | CRYSTALLOGRAPHY | CHAINS | 60 APPLIED LIFE SCIENCES | FUNCTIONALS
Journal Article
Cell, ISSN 0092-8674, 04/2015, Volume 161, Issue 3, pp. 470 - 485
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Immunity, ISSN 1074-7613, 08/2013, Volume 39, Issue 2, pp. 245 - 258
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Cell, ISSN 0092-8674, 06/2015, Volume 161, Issue 6, pp. 1280 - 1292
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