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Science, ISSN 0036-8075, 7/2012, Volume 337, Issue 6091, pp. 183 - 186
Journal Article
Immunity, ISSN 1074-7613, 10/2013, Volume 39, Issue 4, pp. 758 - 769
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
Nature, ISSN 0028-0836, 09/2011, Volume 477, Issue 7365, pp. 466 - 470
Journal Article
Nature, ISSN 0028-0836, 2013, Volume 503, Issue 7475, pp. 224 - 228
Journal Article
Journal Article
Science, ISSN 0036-8075, 9/2011, 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
Journal Article
Science, ISSN 0036-8075, 10/2009, Volume 326, Issue 5950, pp. 285 - 289
Journal Article