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The Lancet, ISSN 0140-6736, 03/2004, Volume 363, Issue 9413, pp. 938 - 947
Studies on the fusion-inhibitory peptides derived from the heptad repeat 1 and 2 (HR1 and HR2) regions of the HIV-1 envelope glycoprotein gp41 provided crucial... 
MEMBRANE-FUSION | MEDICINE, GENERAL & INTERNAL | GP41 CORE STRUCTURE | HIV-1 GP41 | ENVELOPE GLYCOPROTEIN | SYNTHETIC PEPTIDES | TYPE-1 GP41 | INFECTION IN-VITRO | COILED-COIL | ACUTE RESPIRATORY SYNDROME | POTENT INHIBITORS | Anti-HIV Agents - pharmacology | Surface Plasmon Resonance | Viral Envelope Proteins - pharmacology | Viral Fusion Proteins - metabolism | Membrane Glycoproteins - metabolism | Humans | Membrane Glycoproteins - chemistry | Protein Conformation - drug effects | HIV Envelope Protein gp41 - metabolism | Chromatography, High Pressure Liquid | HIV Envelope Protein gp41 - chemistry | SARS Virus - metabolism | HIV Envelope Protein gp41 - pharmacology | Viral Fusion Proteins - chemistry | HIV Envelope Protein gp41 - drug effects | Viral Envelope Proteins - metabolism | Severe Acute Respiratory Syndrome - metabolism | Circular Dichroism | Oligopeptides - chemistry | Membrane Fusion - drug effects | Electrophoresis, Polyacrylamide Gel | Membrane Glycoproteins - pharmacology | Cells, Cultured | SARS Virus - drug effects | Oligopeptides - metabolism | Severe Acute Respiratory Syndrome - drug therapy | SARS Virus - chemistry | Sequence Homology, Nucleic Acid | Spike Glycoprotein, Coronavirus | Anti-HIV Agents - chemistry | Severe Acute Respiratory Syndrome - prevention & control | Chemical Fractionation | Oligopeptides - drug effects | Viral Envelope Proteins - chemistry | Membrane Fusion - physiology | Reports | Usage | Diagnosis | Peptides | Severe acute respiratory syndrome | Pathology | Viruses | Membranes | Prophylaxis | Homology | Infections | Proteins | Hepatitis | Spectrum analysis | Human immunodeficiency virus--HIV | Dichroism | Docking | Electrophoresis | Inhibition | Sedimentation & deposition | Glycoprotein gp41 | Spike protein | Gel electrophoresis | Glycoprotein | Trimers | Liquid chromatography | Cell membranes | High-performance liquid chromatography | Sedimentation | Molecular chains | Helicity | Circular dichroism | Software | Surface plasmon resonance | Protein structure | High performance liquid chromatography
Journal Article
Nature, ISSN 0028-0836, 07/2017, Volume 547, Issue 7663, pp. 360 - 361
For many enveloped viruses, binding to a receptor(s) on a host cell acts as the first step in a series of events culminating in fusion with the host cell... 
SYSTEM | ANTIBODIES | LEGINON | IMAGES | MULTIDISCIPLINARY SCIENCES | VACCINE | CLASSIFICATION | GP120 | GLYCOPROTEIN | CRYO-EM STRUCTURE | NEUTRALIZATION | Immunoglobulin Fab Fragments - ultrastructure | env Gene Products, Human Immunodeficiency Virus - ultrastructure | HIV Envelope Protein gp41 - genetics | Antibodies - chemistry | HIV Envelope Protein gp41 - metabolism | env Gene Products, Human Immunodeficiency Virus - metabolism | HIV Envelope Protein gp41 - chemistry | Receptors, CCR5 - metabolism | env Gene Products, Human Immunodeficiency Virus - genetics | HIV-1 - chemistry | Antibodies - immunology | Binding Sites - drug effects | env Gene Products, Human Immunodeficiency Virus - chemistry | Allosteric Regulation - drug effects | HIV Envelope Protein gp41 - ultrastructure | Amino Acid Sequence | CD4 Antigens - ultrastructure | Receptors, HIV - chemistry | Antibodies - ultrastructure | Models, Molecular | Receptors, HIV - ultrastructure | Immunoglobulin Fab Fragments - pharmacology | Antibodies - pharmacology | Cryoelectron Microscopy | HIV-1 - ultrastructure | Receptors, HIV - metabolism | CD4 Antigens - chemistry | Immunoglobulin Fab Fragments - chemistry | Receptors, CCR5 - chemistry | Ligands | Immunoglobulin Fab Fragments - immunology | CD4 Antigens - metabolism | Physiological aspects | Genetic aspects | Glycoproteins | HIV (Viruses) | Structure | Binding | Carbohydrates | Antigens | CCR5 protein | Glycoprotein gp41 | Glycoprotein | Antibodies | Viruses | Glycosylation | Trimers | Cell fusion | Electron microscopy | Crystallography | CXCR4 protein | CD4 antigen | Proteins | Transmission electron microscopy | Neutralizing | Human immunodeficiency virus--HIV | Mutation | Coordination compounds | Binding sites
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 10/2008, Volume 105, Issue 42, pp. 16332 - 16337
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Journal Article
Cell, ISSN 0092-8674, 12/2015, Volume 163, Issue 7, pp. 1702 - 1715
Journal Article