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1. Full Text Open and closed structures reveal allostery and pliability in the HIV-1 envelope spike
by Ozorowski, Gabriel and Pallesen, Jesper and De Val, Natalia and Lyumkis, Dmitry and Cottrell, Christopher A and Torres, Jonathan L and Copps, Jeffrey and Stanfield, Robyn L and Cupo, Albert and Pugach, Pavel and Moore, John P and Wilson, Ian A and Ward, Andrew B
Nature (London), ISSN 0028-0836, 07/2017, Volume 547, Issue 7663, pp. 360 - 361
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 | Viral envelopes | Allosteric proteins | Viral antibodies | Antibodies | Membrane lipids | Peptides | Binding | Carbohydrates | Antigens | CCR5 protein | Glycoprotein gp41 | 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 | Index Medicus
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2. Full Text Structure of the immature HIV-1 capsid in intact virus particles at 8.8 Å resolution
by Schur, Florian K. M and Schur, Florian K. M and Hagen, Wim J. H and Rumlová, Michaela and Ruml, Tomáš and Müller, Barbara and Kraüsslich, Hans-Georg and Briggs, John A. G
Nature (London), ISSN 0028-0836, 01/2015, Volume 517, Issue 7535, pp. 505 - 508
Capsid - ultrastructure | Capsid - chemistry | Electron Microscope Tomography | Humans | Protein Multimerization | Models, Molecular | Virion - chemistry | Mason-Pfizer monkey virus - chemistry | Virus Assembly | Capsid Proteins - ultrastructure | Cryoelectron Microscopy | Mason-Pfizer monkey virus - ultrastructure | HIV-1 - ultrastructure | HIV-1 - chemistry | Capsid Proteins - chemistry | HEK293 Cells | Virion - ultrastructure | Protein Conformation | Cell membranes | HIV (Viruses) | Proteases | Analysis | Risk factors | Proteins | Medical research | Mutation | Molecular structure | Human immunodeficiency virus--HIV | Index Medicus
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3. Full Text Cryo-EM structures and atomic model of the HIV-1 strand transfer complex intasome
by Passos, Dario Oliveira and Li, Min and Yang, Renbin and Rebensburg, Stephanie V and Ghirlando, Rodolfo and Jeon, Youngmin and Shkriabai, Nikoloz and Kvaratskhelia, Mamuka and Craigie, Robert and Lyumkis, Dmitry
Science (American Association for the Advancement of Science), ISSN 0036-8075, 01/2017, Volume 355, Issue 6320, pp. 89 - 92
Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Nucleoproteins - chemistry | Humans | Models, Molecular | Crystallography, X-Ray | HIV Integrase - chemistry | Virus Integration | Cryoelectron Microscopy | Nucleoproteins - ultrastructure | DNA, Viral - chemistry | HIV-1 - ultrastructure | HIV Integrase - ultrastructure | DNA, Viral - ultrastructure | HIV-1 - physiology | RNA, Viral - chemistry | HIV-1 - chemistry | Protein Domains | RNA, Viral - ultrastructure | Genetic aspects | Nucleotide sequencing | HIV (Viruses) | Electron microscopy | Health aspects | Methods | DNA sequencing | High resolution | Modules | Viruses | Genomes | Infections | Ribonucleic acid--RNA | Transmission electron microscopy | Human immunodeficiency virus--HIV | Life cycle engineering | Inserts | Atomic structure | Assembly | Deoxyribonucleic acid--DNA | Index Medicus | Enzymes | Deoxyribonucleic acid | Strands
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4. Full Text Mature HIV-1 capsid structure by cryo-electron microscopy and all-atom molecular dynamics
by Zhao, Gongpu and Perilla, Juan R and Yufenyuy, Ernest L and Meng, Xin and Chen, Bo and Ning, Jiying and Ahn, Jinwoo and Gronenborn, Angela M and Schulten, Klaus and Aiken, Christopher and Zhang, Peijun
Nature (London), ISSN 0028-0836, 05/2013, Volume 497, Issue 7451, pp. 643 - 646
Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Protein Structure, Tertiary | Capsid - ultrastructure | Capsid - chemistry | Human Immunodeficiency Virus Proteins - ultrastructure | Protein Structure, Secondary | Protein Multimerization | Capsid Proteins - ultrastructure | Molecular Dynamics Simulation | Cryoelectron Microscopy | HIV-1 - ultrastructure | Human Immunodeficiency Virus Proteins - chemistry | HIV-1 - chemistry | Capsid Proteins - chemistry | Hydrophobic and Hydrophilic Interactions | Molecular dynamics | Research | Electron microscopy | HIV (Viruses) | Properties | Methods | Proteins | Microscopy | Crystal structure | Index Medicus
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5. Full Text The structure and flexibility of conical HIV-1 capsids determined within intact virions
by Mattei, Simone and Glass, Bärbel and Hagen, Wim J.H and Kräusslich, Hans-Georg and Briggs, John A.G
Science (American Association for the Advancement of Science), ISSN 0036-8075, 12/2016, Volume 354, Issue 6318, pp. 1434 - 1437
Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Genome, Viral | Capsid - ultrastructure | Capsid - chemistry | Electron Microscope Tomography | Humans | Protein Multimerization | Virion - chemistry | gag Gene Products, Human Immunodeficiency Virus - chemistry | Capsid Proteins - ultrastructure | Cryoelectron Microscopy | gag Gene Products, Human Immunodeficiency Virus - ultrastructure | HIV-1 - ultrastructure | HIV-1 - chemistry | Capsid Proteins - chemistry | Virion - ultrastructure | Protein Conformation | Fullerenes - chemistry | Protein structure prediction | Viral proteins | HIV (Viruses) | Structure | Health aspects | Methods | Microscopy | Human immunodeficiency virus--HIV | Genomics | Crystal structure | Index Medicus | Proteins | Casing (process) | Lattices | Fullerenes | Tomography | Crosslinking | Arrays | Crystallography
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6. Full Text Exosomes and HIV Gag Bud from Endosome-like Domains of the T Cell Plasma Membrane
by Amy M. Booth and Yi Fang and Jonathan K. Fallon and Jr-Ming Yang and James E. K. Hildreth and Stephen J. Gould
The Journal of cell biology, ISSN 0021-9525, 3/2006, Volume 172, Issue 6, pp. 923 - 935
T lymphocytes | HIV | K562 cells | Microscopy | Cell lines | Antibodies | Fluorescence | Cell membranes | Exosomes | Budding | Life Sciences & Biomedicine | Science & Technology | Cell Biology | gag Gene Products, Human Immunodeficiency Virus | Humans | T-Lymphocytes - ultrastructure | Exocytosis - physiology | Endosomes - metabolism | T-Lymphocytes - virology | Antigens, CD - metabolism | T-Lymphocytes - metabolism | Platelet Membrane Glycoproteins - metabolism | Cell Membrane - metabolism | HIV-1 - metabolism | Microscopy, Electron, Transmission | Cell Surface Extensions - ultrastructure | Peptide Fragments - metabolism | Cell Surface Extensions - metabolism | Jurkat Cells | Peptide Fragments - secretion | Cell Membrane - ultrastructure | Tetraspanin 28 | Virion - metabolism | Gene Products, gag - metabolism | HIV-1 - ultrastructure | Tetraspanin 30 | Gene Products, gag - secretion | Transport Vesicles - metabolism | Membrane Lipids - metabolism | Virion - ultrastructure | Organelles - metabolism | Virus Replication - physiology | Transport Vesicles - ultrastructure | HIV Infections - metabolism | Research | T cells | Structure | Cytology | Plant cell membranes | Proteins | Plasma | Viruses | Membranes | Cellular biology | Index Medicus
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7. Full Text Crystal structure of an HIV assembly and maturation switch
by Wagner, Jonathan M and Zadrozny, Kaneil K and Chrustowicz, Jakub and Purdy, Michael D and Yeager, Mark and Ganser-Pornillos, Barbie K and Pornillos, Owen and Argonne National Lab. (ANL), Argonne, IL (United States)
eLife, ISSN 2050-084X, 07/2016, Volume 5, Issue 2016
Biology | Life Sciences & Biomedicine - Other Topics | Life Sciences & Biomedicine | Science & Technology | Capsid - ultrastructure | Protein Multimerization | Virion - genetics | Crystallography, X-Ray | gag Gene Products, Human Immunodeficiency Virus - metabolism | Proteolysis | Cloning, Molecular | Escherichia coli - metabolism | Protein Domains | gag Gene Products, Human Immunodeficiency Virus - genetics | Capsid - metabolism | Recombinant Proteins - metabolism | Amino Acid Sequence | HIV-1 - metabolism | Protein Conformation, alpha-Helical | Recombinant Proteins - ultrastructure | Capsid Proteins - metabolism | Models, Molecular | Recombinant Proteins - genetics | HIV-1 - genetics | Virion - metabolism | Virus Assembly | Capsid Proteins - ultrastructure | gag Gene Products, Human Immunodeficiency Virus - ultrastructure | HIV-1 - ultrastructure | Protein Conformation, beta-Strand | Escherichia coli - genetics | Virion - ultrastructure | Capsid Proteins - genetics | Crystallization | Genomes | Sp1 protein | Proteins | Gag protein | Mutagenesis | Microscopy | Spacer | Human immunodeficiency virus--HIV | Protein structure | Deoxyribonucleic acid--DNA | Crystal structure | Index Medicus | BASIC BIOLOGICAL SCIENCES | assembly | Biochemistry | HIV | capsid | Biophysics and Structural Biology | Other
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8. Full Text Microdomains of the C-Type Lectin DC-SIGN Are Portals for Virus Entry into Dendritic Cells
by Alessandra Cambi and Frank de Lange and Noortje M. van Maarseveen and Monique Nijhuis and Ben Joosten and Erik M. H. P. van Dijk and Bärbel I. de Bakker and Jack A. M. Fransen and Petra H. M. Bovee-Geurts and Frank N. van Leeuwen and Niek F. Van Hulst and Carl G. Figdor
The Journal of cell biology, ISSN 0021-9525, 1/2004, Volume 164, Issue 1, pp. 145 - 155
Molecules | Receptors | Dendritic cells | Rafts | Lectins | Lipids | Viruses | Ligands | Cell membranes | HIV 1 | Lectin | Multiprotein assembly | Lipid rafts | Pathogen recognition receptor | Electron microscopy | Life Sciences & Biomedicine | Science & Technology | Cell Biology | Immunohistochemistry | RNA Virus Infections - metabolism | HIV-1 - pathogenicity | Membrane Microdomains - metabolism | Receptors, Virus - metabolism | Humans | Lectins, C-Type - immunology | Monocytes - metabolism | Cell Adhesion Molecules - immunology | Membrane Microdomains - ultrastructure | HIV Infections - immunology | Lectins, C-Type - metabolism | Receptors, Cell Surface - ultrastructure | HIV-1 - physiology | Cell Membrane - metabolism | Dendritic Cells - virology | RNA Virus Infections - immunology | Dendritic Cells - metabolism | Monocytes - ultrastructure | Cells, Cultured | Receptors, Cell Surface - metabolism | Cell Membrane - ultrastructure | Microscopy, Electron | Cell Adhesion Molecules - metabolism | Receptors, Cell Surface - immunology | Receptors, Virus - ultrastructure | Endocytosis - physiology | Lectins, C-Type - ultrastructure | Monocytes - virology | Cell Adhesion Molecules - ultrastructure | Dendritic Cells - ultrastructure | Receptors, Virus - immunology | Cell Membrane - virology | HIV Infections - metabolism | Protein Structure, Tertiary - physiology | Research | Pathogens | Human immunodeficiency virus | HIV | Cellular biology | Binding sites | Index Medicus | pathogen recognition receptor; lectin; electron microscopy; multiprotein assembly; lipid rafts
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9. Full Text Infectious HIV-1 Assembles in Late Endosomes in Primary Macrophages
by Annegret Pelchen-Matthews and Beatrice Kramer and Mark Marsh
The Journal of cell biology, ISSN 0021-9525, 8/2003, Volume 162, Issue 3, pp. 443 - 455
T lymphocytes | HIV | Virions | Antibodies | Viruses | Cell membranes | Macrophages | Vacuoles | HIV 1 | Endosomes | Multivesicular body | Virus assembly | Late endosome | Endosome | Life Sciences & Biomedicine | Science & Technology | Cell Biology | Immunohistochemistry | Virus Shedding - physiology | Intracellular Membranes - virology | HIV-1 - pathogenicity | Vacuoles - ultrastructure | Membrane Glycoproteins - metabolism | gag Gene Products, Human Immunodeficiency Virus | Humans | Retroviridae Proteins, Oncogenic - metabolism | HIV Antigens - metabolism | Monocytes - metabolism | Viral Proteins | Kangai-1 Protein | Endosomes - metabolism | Antigens, CD - metabolism | Intracellular Membranes - ultrastructure | Macrophages - virology | Endosomes - ultrastructure | Viral Envelope Proteins - metabolism | Membrane Proteins - metabolism | Proto-Oncogene Proteins | Lysosome-Associated Membrane Glycoproteins | Monocytes - ultrastructure | Endosomes - virology | HIV-1 - metabolism | Macrophages - ultrastructure | Tetraspanin 28 | Reaction Time - physiology | Microscopy, Electron | Gene Products, gag - metabolism | Cell Compartmentation - physiology | HIV-1 - ultrastructure | Monocytes - virology | Macrophages - metabolism | Vacuoles - metabolism | Virus Replication - physiology | Intracellular Membranes - metabolism | Vacuoles - virology | HIV (Viruses) | Cytology | Research | Pathology | Endocytosis | Human immunodeficiency virus | Cellular biology | Index Medicus | HIV; endosome; virus assembly; late endosome; multivesicular body
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10. Full Text 3D correlative light and electron microscopy of cultured cells using serial blockface scanning electron microscopy
by Russell, Matthew R.G and Lerner, Thomas R and Burden, Jemima J and Nkwe, David O and Pelchen-Matthews, Annegret and Domart, Marie-Charlotte and Durgan, Joanne and Weston, Anne and Jones, Martin L and Peddie, Christopher J and Carzaniga, Raffaella and Florey, Oliver and Marsh, Mark and Gutierrez, Maximiliano G and Collinson, Lucy M
Journal of cell science, ISSN 0021-9533, 2017, Volume 130, Issue 1, pp. 278 - 291
Entosis | HIV-1 | Serial blockface SEM | 3D correlative light and electron microscopy | Mycobacterium tuberculosis | Autophagy | Life Sciences & Biomedicine | Science & Technology | Cell Biology | Macrophages - ultrastructure | Cell Survival | Monocytes - cytology | Humans | Cells, Cultured | Mycobacterium tuberculosis - ultrastructure | Endothelial Cells - microbiology | Endothelial Cells - ultrastructure | HIV - ultrastructure | Macrophages - virology | Microscopy, Electron, Scanning - methods | Intracellular Space - microbiology | Imaging, Three-Dimensional | Mycobacterium tuberculosis - growth & development | Scanning electron microscopy | Cell culture | Image processing | Fluorescence | Workflow | Macrophages | Electron microscopy | Biological activity | Endothelial cells | Monocytes | Tuberculosis | Ultrastructure | Human immunodeficiency virus--HIV | Monolayers | Bacteria | Fluorescence microscopy | Tumors | Electrons | Index Medicus | Tools and Techniques
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