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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
by Liao, Hua-Xin and Lynch, Rebecca and Zhou, Tongqing and Gao, Feng and Munir Alam, S and Boyd, Scott D and Fire, Andrew Z and Roskin, Krishna M and Schramm, Chaim A and Zhang, Zhenhai and Zhu, Jiang and Shapiro, Lawrence and Mullikin, James C and Gnanakaran, S and Hraber, Peter and Wiehe, Kevin and Kelsoe, Garnett and Yang, Guang and Xia, Shi-Mao and Montefiori, David C and Parks, Robert and Lloyd, Krissey E and Scearce, Richard M and Soderberg, Kelly A and Cohen, Myron and Kamanga, Gift and Louder, Mark K and Tran, Lillian M and Chen, Yue and Cai, Fangping and Chen, Sheri and Moquin, Stephanie and Du, Xiulian and Gordon Joyce, M and Srivatsan, Sanjay and Zhang, Baoshan and Zheng, Anqi and Shaw, George M and Hahn, Beatrice H and Kepler, Thomas B and Korber, Bette T. M and Kwong, Peter D and Mascola, John R and Haynes, Barton F 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, Casandra and Mulliki, 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 Progra and NISC Comparative Sequencing Program
Nature, ISSN 0028-0836, 04/2013, Volume 496, Issue 7446, pp. 469 - 476
Current human immunodeficiency virus-1 (HIV-1) vaccines elicit strain-specific neutralizing antibodies. However, cross-reactive neutralizing antibodies arise... 
B-CELL RESPONSES | CONFORMATIONAL EPITOPE | POTENT NEUTRALIZATION | CD4 BINDING-SITE | VACCINE DESIGN | MULTIDISCIPLINARY SCIENCES | ENVELOPE GLYCOPROTEIN | HIV-1-INFECTED INDIVIDUALS | HUMAN MONOCLONAL-ANTIBODIES | SUBTYPE-B | IN-SITU PROTEOLYSIS | HIV Envelope Protein gp120 - genetics | Clone Cells - cytology | Humans | AIDS Vaccines - immunology | Molecular Sequence Data | Crystallography, X-Ray | Neutralization Tests | Phylogeny | HIV Envelope Protein gp120 - metabolism | Epitopes - immunology | HIV Envelope Protein gp120 - immunology | Antibodies, Neutralizing - immunology | HIV Antibodies - immunology | HIV-1 - chemistry | HIV Envelope Protein gp120 - chemistry | Antibodies, Monoclonal - chemistry | Antibodies, Monoclonal - immunology | Protein Structure, Tertiary | Amino Acid Sequence | CD4 Antigens - immunology | Africa | Cells, Cultured | Models, Molecular | Antibodies, Neutralizing - genetics | Cross Reactions - immunology | HIV Antibodies - chemistry | HIV-1 - classification | Antibodies, Monoclonal - genetics | Cell Lineage | HIV-1 - immunology | CD4 Antigens - chemistry | Antibodies, Neutralizing - chemistry | Epitopes - chemistry | HIV Antibodies - genetics | Mutation | Evolution, Molecular | Monoclonal antibodies | AIDS vaccines | Genetic aspects | Research | HIV (Viruses) | Properties | Proteins | Plasma | Infections | Patients | Binding sites | Crystal structure
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
Nature, ISSN 0028-0836, 12/2014, Volume 516, Issue 7531, pp. 418 - 422
Journal Article
Nature Medicine, ISSN 1078-8956, 11/2012, Volume 18, Issue 11, pp. 1688 - 1692
Journal Article
Cell, ISSN 0092-8674, 09/2016, Volume 166, Issue 6, pp. 1459 - 1470.e11
Journal Article
Science, ISSN 0036-8075, 11/2011, Volume 334, Issue 6059, pp. 1097 - 1103
The HIV envelope (Env) protein gpl20 is protected from antibody recognition by a dense glycan shield. However, several of the recently identified PGT broadly... 
Polysaccharides | HIV | Neutralizing antibodies | RESEARCH ARTICLES | Antibodies | Viruses | Trimers | Epitopes | Grants | Binding sites | Crystal structure | PANEL | TRIMERS | MULTIDISCIPLINARY SCIENCES | IMMUNOGENS | ENVELOPE GLYCOPROTEIN COMPLEX | GP120 | HUMAN-IMMUNODEFICIENCY-VIRUS | MONOCLONAL-ANTIBODIES | TYPE-1 | Antibody Specificity | Mannose - immunology | Disaccharides - metabolism | Humans | Antibodies, Neutralizing - metabolism | Crystallography, X-Ray | Disaccharides - chemistry | Mannosides - chemistry | HIV Envelope Protein gp120 - metabolism | HIV Envelope Protein gp120 - immunology | Mannose - metabolism | Antibodies, Neutralizing - immunology | HIV-1 - physiology | HIV Antibodies - immunology | Immunoglobulin Fab Fragments - metabolism | Oligosaccharides - chemistry | Polysaccharides - chemistry | HIV Envelope Protein gp120 - chemistry | Mannose - chemistry | HIV Antibodies - metabolism | Protein Structure, Tertiary | Cell Line | Models, Molecular | Antibodies, Neutralizing - genetics | Glycosylation | Polysaccharides - immunology | Oligosaccharides - metabolism | HIV Antibodies - chemistry | Polysaccharides - metabolism | HIV-1 - immunology | Hydrogen Bonding | Antibodies, Neutralizing - chemistry | Immunoglobulin Fab Fragments - chemistry | Oligosaccharides - immunology | Protein Conformation | Mannosides - metabolism | HIV Antibodies - genetics | Immunoglobulin Fab Fragments - immunology | Mutation | Binding Sites, Antibody | Carbohydrate Conformation | Viral antibodies | Physiological aspects | Development and progression | Glycoproteins | HIV (Viruses) | Health aspects | Proteins | Antigens | Immunoglobulins | Human immunodeficiency virus--HIV
Journal Article
Journal Article