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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 | Index Medicus | ANTIBODIES | IMMUNITY | BASIC BIOLOGICAL SCIENCES | GENETICS | IMMUNOGLOBULINS | CRYSTAL STRUCTURE | CRYSTALLOGRAPHY | CHAINS | 60 APPLIED LIFE SCIENCES | FUNCTIONALS
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 | Index Medicus
Journal Article
Analytical Biochemistry, ISSN 0003-2697, 2009, Volume 392, Issue 2, pp. 145 - 154
Journal Article
Chemistry & Biology, ISSN 1074-5521, 02/2013, Volume 20, Issue 2, pp. 161 - 167
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 5/2016, Volume 113, Issue 22, pp. 6200 - 6205
Journal Article
PLoS ONE, ISSN 1932-6203, 07/2017, Volume 12, Issue 7, pp. e0181799 - e0181799
Little structural information is available so far on amyloid fibrils consisting of immunoglobulin light chains. It is not understood which features of the... 
AMIDE-ONE VIBRATION | INFRARED-SPECTRA | IN-VITRO | PROTEIN OLIGOMERS | SOLID-STATE NMR | RESONANCE INTERACTION | MULTIDISCIPLINARY SCIENCES | CROSS-POLARIZATION | VARIABLE DOMAINS | PLEATED SHEET | AGGREGATION | Recombinant Proteins - metabolism | Microscopy, Electron, Transmission | Recombinant Proteins - ultrastructure | Magnetic Resonance Spectroscopy | Protein Precursors - ultrastructure | Protein Precursors - chemistry | Humans | Immunoglobulin Variable Region - chemistry | Protein Multimerization | Immunoglobulin Variable Region - metabolism | Models, Molecular | Recombinant Proteins - chemistry | Amyloid - chemistry | Amyloid - ultrastructure | Spectroscopy, Fourier Transform Infrared | Immunoglobulin Light Chains - metabolism | Protein Precursors - metabolism | Immunoglobulin Light Chains - chemistry | Immunoglobulin Light Chains - genetics | Amyloid - metabolism | Immunoglobulin Variable Region - genetics | Protein Conformation | Kinetics | Mutation | Oligomers | Usage | Amyloid beta-protein | Monoclonal antibodies | Nuclear magnetic resonance spectroscopy | Amyloidosis | Dosage and administration | Research | Residues | Infrared spectroscopy | Fourier transformation | Fourier transforms | Immunoglobulins | Nuclear magnetic resonance--NMR | Similarity | Disease | Fibrils | Strands | Science | Amino acid sequence | Cytotoxicity | Agglomeration | Biopolymers | Proteins | Algorithms | Precursors | Spectrum analysis | Light chains | Amyloid | Index Medicus | NMR | Nuclear magnetic resonance
Journal Article