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Nature, ISSN 0028-0836, 10/2015, Volume 526, Issue 7572, pp. 218 - 223
HIV-1 Nef and the unrelated mouse leukaemia virus glycosylated Gag (glycoGag) strongly enhance the infectivity of HIV-1 virions produced in certain cell types... 
CYTOPLASMIC DOMAIN | CELL-SURFACE CD4 | GLYCOSYLATED-GAG | VIRION FUSION | REPLICATION | PRIMARY T-LYMPHOCYTES | MULTIDISCIPLINARY SCIENCES | IMMUNODEFICIENCY-VIRUS TYPE-1 | CD4 DOWN-REGULATION | MURINE LEUKEMIA-VIRUS | OPTIMAL VIRAL INFECTIVITY | Humans | Neoplasm Proteins - antagonists & inhibitors | Neoplasm Proteins - pharmacology | Virion - chemistry | Host-Pathogen Interactions - drug effects | Membrane Proteins - pharmacology | Neoplasm Proteins - metabolism | Receptors, Cell Surface - antagonists & inhibitors | Membrane Proteins - deficiency | HIV-1 - growth & development | HIV-1 - physiology | HIV-1 - chemistry | Gene Deletion | nef Gene Products, Human Immunodeficiency Virus - metabolism | Membrane Proteins - metabolism | Cell Line | Virus Replication - drug effects | nef Gene Products, Human Immunodeficiency Virus - deficiency | HIV-1 - drug effects | Down-Regulation | HIV Infections - virology | Virion - physiology | CD4-Positive T-Lymphocytes - metabolism | Receptors, Cell Surface - metabolism | Gene Products, gag - metabolism | Protein Transport | Virion - drug effects | Membrane Proteins - antagonists & inhibitors | Receptors, Cell Surface - deficiency | HIV Infections - drug therapy | Neoplasm Proteins - deficiency | Virion - growth & development | Leukemia Virus, Murine - chemistry | Development and progression | Genetic aspects | Virulence (Microbiology) | Viral proteins | Properties | HIV infection | Proteins | Genomes | Immunology | Mutation | Human immunodeficiency virus--HIV | Cells | Index Medicus
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 08/2013, Volume 110, Issue 32, pp. 13109 - 13113
Recent evidence indicates there is a role for small membrane vesicles, including exosomes, as vehicles for intercellular communication. Exosomes secreted by... 
Cell culture techniques | Disease transmission | Hepatocytes | RNA | Virions | Viruses | Infections | Cell membranes | Exosomes | Hepacivirus | IN-VITRO | NEUTRALIZING ANTIBODIES | RAFTS | MULTIDISCIPLINARY SCIENCES | ENVELOPE | INFECTION | SECRETION | PROTEINS | PLASMA-MEMBRANE | ESCAPE | Exosomes - metabolism | Claudin-1 - immunology | Hepacivirus - immunology | Humans | Hepacivirus - genetics | Virion - genetics | Tetraspanin 28 - immunology | Hepatitis C - immunology | Antibodies, Neutralizing - immunology | RNA, Viral - genetics | Claudin-1 - metabolism | Immunoglobulin G - immunology | Mass Spectrometry | Scavenger Receptors, Class B - immunology | Hepacivirus - physiology | RNA, Viral - metabolism | Exosomes - ultrastructure | Exosomes - virology | Microscopy, Electron, Transmission | Virion - physiology | Carcinoma, Hepatocellular - virology | Reverse Transcriptase Polymerase Chain Reaction | Host-Pathogen Interactions | Microscopy, Confocal | Carcinoma, Hepatocellular - pathology | Hepatitis C - virology | Cell Line, Tumor | Tetraspanin 28 - metabolism | Virion - ultrastructure | Scavenger Receptors, Class B - metabolism | Carcinoma, Hepatocellular - metabolism | Cell interaction | Physiological aspects | Host-parasite relationships | Research | Hepatitis C virus | Health aspects | Proteins | Hepatitis | Transmission electron microscopy | Ribonucleic acid--RNA | Mass spectrometry | Cells | Index Medicus | Biological Sciences
Journal Article
Journal Article
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
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 1/2011, Volume 108, Issue 4, pp. 1355 - 1360
Journal Article
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