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Nature, ISSN 0028-0836, 03/2017, Volume 543, Issue 7644, pp. 248 - 251
Journal Article
Science, ISSN 0036-8075, 11/2013, Volume 342, Issue 6158, pp. 592 - 598
Journal Article
Nature, ISSN 0028-0836, 04/2015, Volume 520, Issue 7545, pp. 109 - 113
Journal Article
Nature Communications, ISSN 2041-1723, 09/2015, Volume 6, Issue 1, p. 8176
Journal Article
Cell, ISSN 0092-8674, 02/2015, Volume 160, Issue 5, pp. 904 - 912
Journal Article
Science, ISSN 0036-8075, 8/2011, Volume 333, Issue 6044, pp. 843 - 850
Current flu vaccines provide only limited coverage against seasonal strains of influenza viruses. The identification of V H 1-69 antibodies that broadly... 
Influenza A virus | RESEARCH ARTICLES | Vaccination | Cardiopulmonary resuscitation | Antibodies | Viruses | Orthomyxoviridae | Infections | Epitopes | H3N2 subtype influenza A virus | Crystal structure | FUSION | HEMAGGLUTININ | RECOGNITION | AVIAN INFLUENZA | SUBTYPES | MULTIDISCIPLINARY SCIENCES | VACCINATION | MONOCLONAL-ANTIBODIES | PEPTIDE | SEASON | Orthomyxoviridae Infections - prevention & control | Antibody Specificity | Humans | Molecular Sequence Data | Antigens, Viral - genetics | Crystallography, X-Ray | Neutralization Tests | Hemagglutinin Glycoproteins, Influenza Virus - immunology | Hemagglutinin Glycoproteins, Influenza Virus - genetics | Epitopes - immunology | Antibodies, Neutralizing - immunology | Conserved Sequence | Influenza A Virus, H7N7 Subtype - immunology | Influenza A virus - immunology | Influenza, Human - therapy | Antibodies, Monoclonal - immunology | Amino Acid Sequence | Hemagglutinin Glycoproteins, Influenza Virus - chemistry | Models, Molecular | Antigens, Viral - chemistry | Antibodies, Monoclonal - isolation & purification | Influenza A Virus, H3N2 Subtype - immunology | Antibodies, Viral - isolation & purification | Antibodies, Neutralizing - isolation & purification | Antigens, Viral - immunology | Animals | Influenza Vaccines - immunology | Antibodies, Viral - immunology | Protein Conformation | Mice | Influenza A Virus, H7N7 Subtype - genetics | Mutation | Binding Sites, Antibody | Influenza, Human - prevention & control | Orthomyxoviridae Infections - immunology | Influenza, Human - immunology | Influenza viruses | Influenza vaccines | Crystals | Monoclonal antibodies | Physiological aspects | Research | Properties | Structure | Vaccines | Influenza | Public health | Virology | fusion | peptide | avian influenza | hemagglutinin | recognition | monoclonal-antibodies | season | vaccination | subtypes
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 8/2010, 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
Nature, ISSN 0028-0836, 09/2012, Volume 489, Issue 7417, pp. 526 - 532
Immune recognition of protein antigens relies on the combined interaction of multiple antibody loops, which provide a fairly large footprint and constrain the... 
SYSTEM | POTENT NEUTRALIZATION | EPITOPE | HEMAGGLUTININ | RECOGNITION | STRUCTURAL BASIS | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | BROAD | DELETIONS | INSERTIONS | Influenza A Virus, H1N1 Subtype - immunology | Orthomyxoviridae Infections - prevention & control | Complementarity Determining Regions - genetics | Influenza A virus - chemistry | Cross Reactions - genetics | Molecular Sequence Data | Crystallography, X-Ray | Antibody Specificity - genetics | Hemagglutinin Glycoproteins, Influenza Virus - immunology | Epitopes - immunology | Antibodies, Neutralizing - immunology | Antibody Specificity - immunology | Complementarity Determining Regions - chemistry | Conserved Sequence | Influenza A virus - immunology | Binding Sites | Hemagglutinin Glycoproteins, Influenza Virus - chemistry | Enzyme-Linked Immunosorbent Assay | Models, Molecular | Antigens, Viral - chemistry | Antibodies, Neutralizing - genetics | Cross Reactions - immunology | Influenza A Virus, H3N2 Subtype - immunology | Mutation - genetics | Antigens, Viral - immunology | Animals | Influenza A Virus, H3N2 Subtype - chemistry | Influenza Vaccines - immunology | Antibodies, Neutralizing - chemistry | Antibodies, Viral - chemistry | Complementarity Determining Regions - immunology | Antibodies, Viral - immunology | Protein Conformation | Epitopes - chemistry | Influenza A Virus, H1N1 Subtype - chemistry | Mice | Influenza A virus - classification | Orthomyxoviridae Infections - virology | Antibodies, Viral - genetics | Orthomyxoviridae Infections - immunology | Influenza viruses | Agglutinins | Viruses | Complementarity-determining regions | Research | Observations | Inactivation | Proteins | Infections | Binding sites
Journal Article