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Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 12/2014, Volume 111, Issue 49, pp. 17624 - 17629
Journal Article
Science, ISSN 0036-8075, 12/2013, Volume 342, Issue 6165, pp. 1477 - 1483
Journal Article
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 08/2015, Volume 290, Issue 32, pp. 19780 - 19795
The trimeric envelope spike of HIV-1 mediates virus entry into human cells. The exposed part of the trimer, gp140, consists of two noncovalently associated... 
T4 MOLECULE | IN-VITRO | GLYCOPROTEIN TRIMERS | CD4 BINDING-SITE | BROADLY NEUTRALIZING ANTIBODIES | BIOCHEMISTRY & MOLECULAR BIOLOGY | HUMAN MONOCLONAL-ANTIBODY | ENV TRIMERS | ELECTRON-MICROSCOPY | HUMAN-IMMUNODEFICIENCY-VIRUS | DEPENDENT EPITOPE | HIV Envelope Protein gp120 - genetics | HIV Envelope Protein gp41 - genetics | Antibodies - chemistry | Protein Multimerization | HIV Envelope Protein gp41 - metabolism | Molecular Sequence Data | env Gene Products, Human Immunodeficiency Virus - metabolism | HIV Envelope Protein gp41 - chemistry | HIV Envelope Protein gp120 - metabolism | Recombinant Fusion Proteins - metabolism | env Gene Products, Human Immunodeficiency Virus - genetics | HIV-1 - chemistry | Proteolysis | Escherichia coli - metabolism | Antibodies - immunology | HIV Envelope Protein gp120 - chemistry | Oligopeptides - chemistry | env Gene Products, Human Immunodeficiency Virus - chemistry | Protein Structure, Tertiary | Amino Acid Sequence | Antigens, Viral - analysis | Gene Expression | Enzyme-Linked Immunosorbent Assay | Protein Structure, Secondary | Oligopeptides - genetics | Antigens, Viral - chemistry | Glycosylation | Oligopeptides - metabolism | Recombinant Fusion Proteins - chemistry | HIV-1 - genetics | HIV-1 - immunology | Escherichia coli - genetics | Recombinant Fusion Proteins - genetics | vaccine | human immunodeficiency virus (HIV) | envelope protein | Membrane Biology | AIDS | glycosylation | recombinant protein expression | gp140 trimer
Journal Article
Immunity, ISSN 1074-7613, 04/2017, Volume 46, Issue 4, pp. 690 - 702
Broadly neutralizing antibodies (bnAbs) to HIV delineate vaccine targets and are prophylactic and therapeutic agents. Some of the most potent bnAbs target a... 
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
Structure, ISSN 0969-2126, 07/2014, Volume 22, Issue 7, pp. 974 - 984
The HIV envelope glycoprotein (Env) trimer undergoes receptor-induced conformational changes that drive fusion of the viral and cellular membranes. Env... 
ENVELOPE GLYCOPROTEIN TRIMERS | ENTRY INHIBITORS | BIOCHEMISTRY & MOLECULAR BIOLOGY | GP41 | HYDROGEN/DEUTERIUM EXCHANGE | MASS-SPECTROMETRY | CELL BIOLOGY | NEUTRALIZING ANTIBODY PG9 | BIOPHYSICS | GP120 INNER DOMAIN | IMMUNODEFICIENCY-VIRUS TYPE-1 | CONFORMATIONAL TRANSITIONS | RECEPTOR-BINDING | Oxalates - chemistry | Humans | Protein Multimerization | HIV Envelope Protein gp41 - metabolism | Piperazines - metabolism | env Gene Products, Human Immunodeficiency Virus - metabolism | Piperazines - chemistry | HIV Envelope Protein gp41 - chemistry | HIV Envelope Protein gp120 - metabolism | Deuterium Exchange Measurement | HIV-1 - physiology | Piperidines - pharmacology | Protein Binding - drug effects | HEK293 Cells | Protein Structure, Quaternary | HIV Envelope Protein gp120 - chemistry | Oxalates - pharmacology | env Gene Products, Human Immunodeficiency Virus - chemistry | HIV-1 - metabolism | Piperidines - chemistry | HIV-1 - drug effects | Piperidines - metabolism | Solubility | Models, Molecular | Glycosylation | Piperazines - pharmacology | Oxalates - metabolism | CD4 Antigens - chemistry | Mass Spectrometry - methods | CD4 Antigens - metabolism | International relief | AIDS vaccines | HIV (Viruses) | Electron microscopy | Hydrogen | NBD-556 | glycoform | CD4 | oxidative labeling | Env trimers | SOSIP | glycoprotein | gp140 | HD exchange | BMS-806 | deuterium exchange
Journal Article