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Proceedings of the National Academy of Sciences - PNAS, ISSN 1091-6490, 2010, Volume 107, Issue 31, pp. 13800 - 13805
The envelope spike of HIV is one of the most highly N-glycosylated structures found in nature. However, despite extensive research revealing essential... 
Polysaccharides | HIV | Vaccination | Cell lines | Antibodies | Viruses | Glycoproteins | Trimers | Epitopes | HIV 1 | 2G12 | gp120 | Glycosylation | Vaccine | NEUTRALIZING ANTIBODIES | MASS-SPECTROMETRIC CHARACTERIZATION | TYPE-1 ANTIBODY 2G12 | MULTIDISCIPLINARY SCIENCES | N-GLYCANS | glycosylation | LINKED OLIGOSACCHARIDES | VIRUS TYPE-1 | HIV-1 GP120 | vaccine | DC-SIGN | VACCINE DESIGN | GLYCOPROTEIN GP120 | Antigens, Viral - metabolism | Membrane Glycoproteins - metabolism | Humans | Membrane Glycoproteins - chemistry | Virion - chemistry | HIV Envelope Protein gp120 - metabolism | Simian Immunodeficiency Virus - chemistry | HIV Envelope Protein gp120 - immunology | HIV-1 - chemistry | Oligosaccharides - chemistry | Viral Envelope Proteins - metabolism | Polysaccharides - chemistry | Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization | HIV Envelope Protein gp120 - chemistry | Membrane Glycoproteins - immunology | Simian Immunodeficiency Virus - immunology | Virion - immunology | Cell Line | HIV-1 - metabolism | Antigens, Viral - chemistry | Polysaccharides - immunology | Oligosaccharides - metabolism | Virion - metabolism | Polysaccharides - metabolism | Antigens, Viral - immunology | HIV-1 - immunology | Oligosaccharides - immunology | Viral Envelope Proteins - chemistry | Golgi Apparatus - metabolism | Viral Envelope Proteins - immunology | Simian Immunodeficiency Virus - metabolism | Kinetics | Antigens | Immunological deficiency syndromes | Genetic aspects | Health aspects | Enzymes | Immunodeficiency | Vaccines | Monomers | Infection | Envelopes | N-linked glycans | Acquired immune deficiency syndrome | Virions | Glycoprotein gp120 | Biological Sciences
Journal Article
Science (American Association for the Advancement of Science), ISSN 1095-9203, 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
Nature (London), ISSN 1476-4687, 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... 
CRYSTALLIZATION | B-CELL RESPONSES | CONFORMATIONAL EPITOPE | POTENT NEUTRALIZATION | EVOLUTION | CD4 BINDING-SITE | MULTIDISCIPLINARY SCIENCES | ENVELOPE GLYCOPROTEIN | 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 (American Association for the Advancement of Science), ISSN 1095-9203, 2011, Volume 333, Issue 6049, pp. 1633 - 1637
Passive transfer of broadly neutralizing HIV antibodies can prevent infection, which suggests that vaccines that elicit such antibodies would be protective.... 
Germ cells | HIV | B lymphocytes | Neutralizing antibodies | REPORTS | Antibodies | Bone marrow | Plasma cells | Viruses | Trimers | Inhibitory concentration 50 | INDIVIDUALS | MEMORY B-CELLS | NEUTRALIZING ANTIBODIES | EPITOPE | TYPE-1 GP120 | MULTIDISCIPLINARY SCIENCES | GP41 | ENVELOPE GLYCOPROTEIN | RECEPTOR | HUMAN-IMMUNODEFICIENCY-VIRUS | HUMAN MONOCLONAL-ANTIBODIES | Consensus Sequence | Antibody Specificity | Humans | Antibodies, Neutralizing - metabolism | Immunoglobulin Heavy Chains - chemistry | Molecular Sequence Data | Crystallography, X-Ray | HIV Envelope Protein gp120 - metabolism | Genes, Immunoglobulin Heavy Chain | HIV Envelope Protein gp120 - immunology | Immunoglobulin Light Chains - chemistry | HIV Infections - immunology | Antibodies, Neutralizing - immunology | Molecular Mimicry | HIV Antibodies - immunology | Cloning, Molecular | HIV Envelope Protein gp120 - chemistry | Binding Sites | HIV Antibodies - metabolism | Amino Acid Sequence | CD4 Antigens - immunology | Antibody Affinity | HIV Antibodies - chemistry | Antibodies, Neutralizing - chemistry | Immunoglobulin Fab Fragments - chemistry | Protein Conformation | Mutation | Binding Sites, Antibody | CD4 Antigens - metabolism | HIV antibodies | Physiological aspects | Genetic aspects | Research | Nucleotide sequencing | Health aspects | Protein binding | Proteins | Immunoglobulins | Vaccines | Human immunodeficiency virus--HIV | Binding sites | Polyclonal antibodies
Journal Article
Immunity (Cambridge, Mass.), ISSN 1074-7613, 2013, Volume 38, Issue 1, pp. 176 - 186
Journal Article
Science (American Association for the Advancement of Science), ISSN 1095-9203, 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 (American Association for the Advancement of Science), ISSN 1095-9203, 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