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Science (American Association for the Advancement of Science), ISSN 1095-9203, 2011, Volume 334, Issue 6059, pp. 1097 - 1103
.... However, several of the recently identified PGT broadly neutralizing antibodies appear to interact directly with the HIV glycan coat... 
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
PLoS pathogens, ISSN 1553-7374, 2013, Volume 9, Issue 9, p. e1003618
...) vaccine candidate is the ability to induce broadly neutralizing antibodies (bNAbs). One approach to the problem is to create trimeric mimics of the native envelope glycoprotein (Env... 
ENVELOPE GLYCOPROTEIN TRIMERS | PROTEIN | VACCINE | GP41 | MICROBIOLOGY | GP120 | CONFORMATIONAL EPITOPE | POTENT | VIROLOGY | IMMUNODEFICIENCY-VIRUS TYPE-1 | BINDING-SITE | MONOCLONAL-ANTIBODIES | PARASITOLOGY | Protein Aggregates | Antibody Specificity | HIV Infections - prevention & control | Molecular Weight | Humans | Antibodies, Neutralizing - metabolism | env Gene Products, Human Immunodeficiency Virus - metabolism | AIDS Vaccines - therapeutic use | HIV Infections - immunology | env Gene Products, Human Immunodeficiency Virus - genetics | Immunoglobulin Fab Fragments - metabolism | env Gene Products, Human Immunodeficiency Virus - antagonists & inhibitors | Protein Stability | Mutant Proteins - antagonists & inhibitors | Peptide Fragments - genetics | env Gene Products, Human Immunodeficiency Virus - chemistry | HIV Antibodies - metabolism | Peptide Fragments - metabolism | Solubility | Antibody Affinity | Mutant Proteins - metabolism | Epitopes | Recombinant Fusion Proteins - chemistry | HIV-1 - immunology | Peptide Fragments - chemistry | Peptide Fragments - antagonists & inhibitors | Mutant Proteins - chemistry | Antibodies, Monoclonal - metabolism | Amino Acid Substitution | Physiological aspects | Genetic aspects | Research | Nucleotide sequencing | HIV (Viruses) | Gene expression | Health aspects | DNA sequencing | Medical research | AIDS | Human immunodeficiency virus | Vaccines | HIV | Acquired immune deficiency syndrome
Journal Article
Immunological Reviews, ISSN 0105-2896, 01/2017, Volume 275, Issue 1, pp. 11 - 20
Journal Article
Immunity (Cambridge, Mass.), ISSN 1074-7613, 2017, Volume 46, Issue 4, pp. 690 - 702
Broadly neutralizing antibodies (bnAbs) to HIV delineate vaccine targets and are prophylactic and therapeutic agents... 
broadly neutralizing antibody | HIV | PGT145 | trimer apex | envelope glycoprotein | cryo-electron microscopy | REFINEMENT | SYSTEM | PROTEIN | RECOGNITION | VALIDATION | IMMUNOLOGY | REVEAL | QUATERNARY | BINDING | FEATURES | REGION | Surface Plasmon Resonance | Epitopes - metabolism | env Gene Products, Human Immunodeficiency Virus - immunology | Humans | Protein Multimerization | Antibodies, Neutralizing - metabolism | Crystallography, X-Ray | env Gene Products, Human Immunodeficiency Virus - metabolism | Anions - chemistry | Epitopes - immunology | Antibodies, Neutralizing - immunology | HIV Antibodies - immunology | HEK293 Cells | Polysaccharides - chemistry | Protein Domains | env Gene Products, Human Immunodeficiency Virus - chemistry | HIV Antibodies - metabolism | Amino Acid Sequence | HIV-1 - metabolism | Protein Structure, Secondary | Models, Molecular | Polysaccharides - immunology | Protein Binding - immunology | HIV Antibodies - chemistry | Polysaccharides - metabolism | Cryoelectron Microscopy | Sequence Homology, Amino Acid | HIV-1 - immunology | Antibodies, Neutralizing - chemistry | Epitopes - chemistry | Atomic force microscopy | Residues | Immunoglobulins | Quaternary | Envelope protein | Antibodies | Pharmacology | Vaccines | Electron microscopy | Chemical compounds | Transmission electron microscopy | Human immunodeficiency virus--HIV | Neutralizing | Canopies | Atomic structure | Dismantling | Symmetry | Immune system
Journal Article
Proteins: Structure, Function, and Bioinformatics, ISSN 0887-3585, 08/2016, Volume 84, Issue 8, pp. 1162 - 1172
...‐neutralizing activity, while F8 has weak neutralizing activity. F5 buried a total of 1760 Å2 in complex with RTA and made contact with three prominent secondary structural... 
antibody | neutralizing | toxin | epitope | ANTIBODIES | IMMUNITY | MECHANISM | A-CHAIN | STABILITY | BIOCHEMISTRY & MOLECULAR BIOLOGY | VACCINE | RECOMBINANT RICIN | BIOPHYSICS | MICE | Protein Subunits - immunology | Epitopes, B-Lymphocyte - chemistry | Humans | Crystallography, X-Ray | Epitopes, B-Lymphocyte - immunology | Structure-Activity Relationship | Single-Chain Antibodies - genetics | Ricin - chemistry | Complementarity Determining Regions - chemistry | Cloning, Molecular | Escherichia coli - metabolism | Protein Interaction Domains and Motifs | Ricin - antagonists & inhibitors | Antibodies, Monoclonal - chemistry | Amino Acid Sequence | Gene Expression | Protein Structure, Secondary | Single-Chain Antibodies - pharmacology | Antibodies, Monoclonal - pharmacology | Recombinant Proteins - chemistry | Antibodies, Neutralizing - pharmacology | Antibodies, Neutralizing - genetics | Recombinant Proteins - genetics | Recombinant Proteins - pharmacology | B-Lymphocytes - chemistry | Ricin - immunology | Antibodies, Monoclonal - genetics | Camelids, New World | Sequence Alignment | Animals | B-Lymphocytes - immunology | Escherichia coli - genetics | Antibodies, Neutralizing - chemistry | Protein Binding | Protein Subunits - antagonists & inhibitors | Protein Subunits - chemistry | Binding Sites, Antibody | Single-Chain Antibodies - chemistry | Lectins | Enzymes | Structure | Analysis | Crystals | Antigenic determinants | BASIC BIOLOGICAL SCIENCES
Journal Article
Proceedings of the National Academy of Sciences - PNAS, ISSN 1091-6490, 2012, Volume 109, Issue 19, pp. 7439 - 7444
.... Even though infected individuals develop potent and long-lasting serotype-specific neutralizing antibodies (Abs... 
Antiserum | Virions | Dengue | Vaccination | Antibodies | Viruses | Infections | Dimers | Epitopes | Dengue virus | DOMAIN-III | PROTEIN | ENCEPHALITIS-VIRUS | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | WEST-NILE-VIRUS | ENVELOPE GLYCOPROTEIN | JAPANESE ENCEPHALITIS | INFECTION | MONOCLONAL-ANTIBODIES | TYPE-2 | Antibodies, Viral - metabolism | Epitopes - metabolism | Humans | Protein Multimerization | Antibodies, Neutralizing - metabolism | Cercopithecus aethiops | Molecular Sequence Data | Neutralization Tests | Macaca mulatta | Epitopes - immunology | Antibodies, Neutralizing - immunology | Antibody Specificity - immunology | Dengue Virus - immunology | Viral Envelope Proteins - metabolism | Dengue - immunology | Vero Cells | Antibodies, Monoclonal - immunology | Recombinant Proteins - metabolism | Virion - immunology | Amino Acid Sequence | Immune Sera - immunology | Viral Envelope Proteins - genetics | Enzyme-Linked Immunosorbent Assay | Models, Molecular | Recombinant Proteins - chemistry | Dengue - virology | Protein Binding - immunology | Sequence Homology, Amino Acid | Dengue Virus - genetics | Animals | Recombinant Proteins - immunology | Antibodies, Viral - immunology | Viral Envelope Proteins - immunology | Antibodies, Monoclonal - metabolism | Dengue Virus - metabolism | Mutation | Viral antibodies | Physiological aspects | Research | Antigenic determinants | Biological Sciences
Journal Article
Nature (London), ISSN 1476-4687, 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 unclear... 
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