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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 | Human immunodeficiency virus--HIV | Virology | Index Medicus | Immunodeficiency | Vaccines | Monomers | Infection | Envelopes | N-linked glycans | Acquired immune deficiency syndrome | Virions | Glycoprotein gp120 | Biological Sciences
Journal Article
Journal Article
Science, ISSN 0036-8075, 12/2012, Volume 338, Issue 6114, pp. 1634 - 1637
The influenza viruses cause annual epidemics of respiratory disease and occasional pandemics, which constitute a major public-health issue. The segmented... 
Pandemics | RNA | Particle interactions | Virions | REPORTS | Ribonucleoproteins | Orthomyxoviridae | Viruses | Viral morphology | Atomic structure | Monomers | LOCALIZATION | NUCLEAR | REPLICATION | PARTICLES | RECONSTRUCTION | MULTIDISCIPLINARY SCIENCES | COMPLEXES | POLYMERASE | A VIRUS NUCLEOPROTEIN | OLIGOMERIZATION | Viral Core Proteins - ultrastructure | RNA Replicase - metabolism | Influenza A Virus, H1N1 Subtype - physiology | Virion - chemistry | Viral Proteins - metabolism | Influenza A Virus, H1N1 Subtype - ultrastructure | RNA Replicase - ultrastructure | Cell Nucleus - metabolism | Cell Nucleus - virology | Madin Darby Canine Kidney Cells | Viral Core Proteins - metabolism | Transcription, Genetic | RNA, Viral - metabolism | Ribonucleoproteins - chemistry | Viral Core Proteins - chemistry | Protein Structure, Secondary | Electron Microscope Tomography | Viral Proteins - chemistry | RNA-Binding Proteins - chemistry | Models, Molecular | Ribonucleoproteins - metabolism | Viral Proteins - ultrastructure | Microscopy, Electron | Cryoelectron Microscopy | RNA-Binding Proteins - ultrastructure | Animals | RNA, Viral - chemistry | Image Processing, Computer-Assisted | RNA Replicase - chemistry | Virion - ultrastructure | Protein Conformation | Influenza A Virus, H1N1 Subtype - chemistry | Ribonucleoproteins - ultrastructure | RNA-Binding Proteins - metabolism | Influenza viruses | Properties | RNA-protein interactions | Influenza | Genomics | Virology | Index Medicus | Ribonucleic acids | Mortality | Replication | Genomes | Online | Assembly
Journal Article
Journal Article
Journal Article
Nature, ISSN 0028-0836, 07/2016, Volume 535, Issue 7610, pp. 169 - 172
Ebola viruses (EBOVs) are responsible for repeated outbreaks of fatal infections, including the recent deadly epidemic in West Africa. There are currently no... 
SYSTEM | NIEMANN-PICK C1 | ENTRY | CHOLESTEROL | SMALL-MOLECULE INHIBITORS | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | ANTIBODY | RECEPTOR | INFECTION | HIV-1 VIRION FUSION | Temperature | Humans | Anti-Inflammatory Agents, Non-Steroidal - chemistry | Antiviral Agents - metabolism | Endosomes - metabolism | Protein Subunits - metabolism | Anti-Inflammatory Agents, Non-Steroidal - pharmacology | Ebolavirus - drug effects | Ibuprofen - chemistry | Antiviral Agents - chemistry | Endosomes - drug effects | Viral Envelope Proteins - metabolism | Conserved Sequence | Marburgvirus - chemistry | Anti-Inflammatory Agents, Non-Steroidal - metabolism | Binding Sites | Membrane Fusion - drug effects | Toremifene - metabolism | Toremifene - pharmacology | Cell Line | Antiviral Agents - pharmacology | Ibuprofen - pharmacology | Models, Molecular | Protein Structure, Quaternary - drug effects | Ibuprofen - metabolism | Virus Attachment - drug effects | Ebolavirus - chemistry | Viral Envelope Proteins - antagonists & inhibitors | Protein Stability - drug effects | Viral Envelope Proteins - chemistry | Hydrophobic and Hydrophilic Interactions | Protein Binding | Ligands | Protein Subunits - chemistry | Toremifene - chemistry | Ebola virus | Glycoproteins | Host-virus relationships | Observations | Health aspects | Drug interactions | Drug therapy | Binding sites | Viral infections | Crystal structure | Index Medicus
Journal Article