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1. Full Text Subversion of the actin cytoskeleton during viral infection
by Koyuncu, Orkide O and Enquist, Lynn W and Taylor, Matthew P
Nature Reviews Microbiology, ISSN 1740-1526, 06/2011, Volume 9, Issue 6, pp. 427 - 439
Viral infection converts the normal functions of a cell to optimize viral replication and virion production. One striking observation of this conversion is the... 
HOST-CELLS | ROUS-SARCOMA-VIRUS | MICROBIOLOGY | SRC GENE-PRODUCT | ARP2/3 COMPLEX | VACCINIA VIRUS | MEASLES-VIRUS | RHO-GTPASES | TRANSFORMED RAT-CELLS | RESPIRATORY SYNCYTIAL VIRUS | EPSTEIN-BARR-VIRUS | Rous sarcoma virus - physiology | Humans | Virion - physiology | Actins - metabolism | Cell Transformation, Viral - physiology | Adenoviridae - physiology | Virus Assembly | Hepatitis B virus - physiology | Viral Proteins - metabolism | Endocytosis - physiology | Simian virus 40 - physiology | Animals | Herpesviridae - physiology | rho GTP-Binding Proteins - metabolism | Actins - chemistry | Cytoskeleton - metabolism | Virus Replication - physiology | Physiological aspects | Research | Actin | Phagocytosis
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2. Full Text Glycoproteins gE and gI Are Required for Efficient KIF1A-Dependent Anterograde Axonal Transport of Alphaherpesvirus Particles in Neurons
by Radomir Kratchmarov and Tal Kramer and Todd M. Greco and Matthew P. Taylor and Toh Hean Ch'ng and Ileana M. Cristea and Lynn W. Enquist
Journal of Virology, ISSN 0022-538X, 09/2013, Volume 87, Issue 17, pp. 9431 - 9440
Article Usage Stats Services JVI Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley... 
CYTOPLASMIC TAIL | RAT VISUAL-SYSTEM | NERVOUS-SYSTEM | HERPES-SIMPLEX-VIRUS | II MEMBRANE-PROTEIN | VIROLOGY | PSEUDORABIES VIRUS | TO-CELL SPREAD | TRIGEMINAL GANGLIA | US9 | TRANSNEURONAL SPREAD | Lipoproteins - genetics | Recombinant Fusion Proteins - physiology | PC12 Cells | Swine | Neurons - physiology | Viral Proteins - physiology | Alphaherpesvirinae - pathogenicity | Phosphoproteins - physiology | Alphaherpesvirinae - genetics | Cell Line | Neurons - virology | Viral Envelope Proteins - physiology | Viral Envelope Proteins - genetics | Virion - physiology | Cells, Cultured | Herpesvirus 1, Suid - physiology | Rats | Viral Proteins - genetics | Axonal Transport - physiology | Herpesvirus 1, Suid - pathogenicity | Phosphoproteins - genetics | Lipoproteins - physiology | Host-Pathogen Interactions | Animals | Recombinant Fusion Proteins - genetics | Kinesin - physiology | Alphaherpesvirinae - physiology | Herpesvirus 1, Suid - genetics | Virus-Cell Interactions
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3. Full Text Monocytes Activate Natural Killer Cells via Inflammasome-Induced Interleukin 18 in Response to Hepatitis C Virus Replication
by Serti, Elisavet and Werner, Jens M and Chattergoon, Michael and Cox, Andrea L and Lohmann, Volker and Rehermann, Barbara
Gastroenterology, ISSN 0016-5085, 2014, Volume 147, Issue 1, pp. 209 - 220.e3
Background & Aims Production of interferon (IFN)-γ by natural killer (NK) cells is attenuated during chronic infection with hepatitis C virus (HCV). We... 
Gastroenterology and Hepatology | Viral Replication | Cytokine Production | Hepatocyte | Immune Response | IMMUNITY | VIRIONS | ENVELOPE PROTEIN | RELEASE | CULTURE | CD8(+) T-CELLS | INTERFERON | INHIBITION | NK CELLS | INFECTED-CELLS | GASTROENTEROLOGY & HEPATOLOGY | Hepatitis C, Chronic - pathology | Interleukin-18 - physiology | Coculture Techniques | Humans | Hepatitis C, Chronic - physiopathology | Interferon-gamma - physiology | Cell Communication - physiology | Hepatocytes - pathology | Killer Cells, Natural - pathology | Killer Cells, Natural - physiology | Inflammasomes - physiology | Liver Neoplasms - physiopathology | Monocytes - pathology | Cell Line, Tumor | Hepatocytes - virology | Hepacivirus - physiology | Liver Neoplasms - pathology | Monocytes - physiology | Virus Replication - physiology | Hepatocytes - physiology | Killer cells | Interleukins | Biological response modifiers | Hepatitis C virus | Health aspects | viral replication | cytokine production | hepatocyte | immune response
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4. Full Text Structures and organization of adenovirus cement proteins provide insights into the role of capsid maturation in virus entry and infection
by Vijay S. Reddy and Glen R. Nemerow
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 8/2014, Volume 111, Issue 32, pp. 11715 - 11720
Adenovirus cement proteins play crucial roles in virion assembly, disassembly, cell entry, and infection. Based on a refined crystal structure of the... 
Proteins | Molecules | Adenoviruses | Virions | Amino acids | Cements | Capsid | Triskelion | Vertices | Crystal structure | Cement protein scaffold | Human adenovirus | Structure-function relationships | VIRION | DNA | MULTIDISCIPLINARY SCIENCES | structure-function relationships | RESOLUTION | cement protein scaffold | human adenovirus | N-TERMINUS | MICROSCOPY | TYPE-2 | PEPTIDE | REVEALS | Viral Core Proteins - chemistry | DNA-Binding Proteins - physiology | Biophysical Phenomena | Capsid - chemistry | Viral Proteins - chemistry | Humans | Adenoviruses, Human - physiology | Models, Molecular | Capsid - physiology | Crystallography, X-Ray | Virus Assembly - physiology | Adenoviruses, Human - pathogenicity | Static Electricity | DNA-Binding Proteins - chemistry | Viral Core Proteins - physiology | Virus Internalization | Multiprotein Complexes - physiology | Multiprotein Complexes - chemistry | Capsid Proteins - physiology | Adenoviruses, Human - chemistry | Capsid Proteins - chemistry | Protein Structure, Quaternary | Viral Proteins - physiology | Protein research | Viral proteins | Host-parasite relationships | Research | Structure | Virus research | Health aspects | Index Medicus | Biological Sciences | structure–function relationships
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5. Full Text New Insights into Structure and Replication of the Hepatitis C Virus and Clinical Implications
by Poenisch, Marion and Bartenschlager, Ralf
Seminars in Liver Disease, ISSN 0272-8087, 11/2010, Volume 30, Issue 4, pp. 333 - 347
ABSTRACT With the advent of efficient systems to propagate the hepatitis C virus (HCV) in cultured cells important new discoveries have been made. For... 
NS5A protein | STAT-C | NS3 protease | NS5B RNA-dependent RNA polymerase | cyclophilin A | miR-122 | 3' NONTRANSLATED REGION | DEPENDENT RNA-POLYMERASE | NONSTRUCTURAL PROTEIN 5A | CIS-ACTING REPLICATION | HUMAN-IMMUNODEFICIENCY-VIRUS | INDUCED VIRAL CLEARANCE | LIVER-SPECIFIC MICRORNA | IN-VITRO | GASTROENTEROLOGY & HEPATOLOGY | AMPHIPATHIC ALPHA-HELIX | DENSITY-LIPOPROTEIN RECEPTOR | Humans | Virion - physiology | Protein Biosynthesis - physiology | Hepacivirus - genetics | Viral Proteins - genetics | Hepatitis C - genetics | RNA, Viral - physiology | Viral Nonstructural Proteins - physiology | Cyclophilin A - physiology | Animals | Genome, Viral - physiology | Viral Proteins - physiology | Hepacivirus - physiology | Hepatitis C - physiopathology | MicroRNAs - physiology | Virus Replication - physiology
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6. Full Text Amphipathic α-Helices in Apolipoproteins Are Crucial to the Formation of Infectious Hepatitis C Virus Particles
by Fukuhara, Takasuke and Wada, Masami and Nakamura, Shota and Ono, Chikako and Shiokawa, Mai and Yamamoto, Satomi and Motomura, Takashi and Okamoto, Toru and Okuzaki, Daisuke and Yamamoto, Masahiro and Saito, Izumu and Wakita, Takaji and Koike, Kazuhiko and Matsuura, Yoshiharu
PLoS Pathogens, ISSN 1553-7366, 12/2014, Volume 10, Issue 12, p. e1004534
Apolipoprotein B (ApoB) and ApoE have been shown to participate in the particle formation and the tissue tropism of hepatitis C virus (HCV), but their precise... 
LIFE-CYCLE | B TYPE-I | CRYSTAL-STRUCTURE | MICROBIOLOGY | CORE PROTEIN | MIR-122 | REPLICATION | VIROLOGY | MUTATIONS | A-I | ASSOCIATION | PARASITOLOGY | DENSITY-LIPOPROTEIN RECEPTOR | Liver Neoplasms - virology | Gene Expression Regulation, Viral - drug effects | Virion - pathogenicity | Humans | RNA, Small Interfering - pharmacology | Virion - physiology | Hepacivirus - pathogenicity | Apolipoproteins B - genetics | Carcinoma, Hepatocellular - virology | Apolipoproteins B - physiology | Gene Knockout Techniques | Apolipoproteins C - physiology | Apolipoproteins E - chemistry | Apolipoproteins A - physiology | Apolipoproteins E - genetics | Carcinoma, Hepatocellular - pathology | Apolipoproteins E - physiology | Cell Line, Tumor | Protein Structure, Secondary - physiology | Hepacivirus - physiology | Liver Neoplasms - pathology | Apolipoproteins B - chemistry | Virus Replication - physiology
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7. Full Text The ESCRT Machinery Is Recruited by the Viral BFRF1 Protein to the Nucleus-Associated Membrane for the Maturation of Epstein-Barr Virus
by Lee, Chung-Pei and Liu, Po-Ting and Kung, Hsiu-Ni and Su, Mei-Tzu and Chua, Huey-Huey and Chang, Yu-Hsin and Chang, Chou-Wei and Tsai, Ching-Hwa and Liu, Fu-Tong and Chen, Mei-Ru
PLoS Pathogens, ISSN 1553-7366, 09/2012, Volume 8, Issue 9, p. e1002904
The cellular endosomal sorting complex required for transport (ESCRT) machinery participates in membrane scission and cytoplasmic budding of many RNA viruses.... 
HIV-1 | CELLS | CYTOMEGALOVIRAL PROTEINS | ACTIVATION | EGRESS COMPLEX | SARCOMA-ASSOCIATED HERPESVIRUS | TRAFFICKING | MICROBIOLOGY | KINASE-C | LAMINA | VIROLOGY | ENVELOPMENT | PARASITOLOGY | Protein Binding - genetics | Herpesvirus 4, Human - genetics | Humans | Viral Proteins - metabolism | Tissue Distribution | Cell Nucleus - metabolism | Transfection | Virus Release - genetics | Membrane Proteins - physiology | Virus Assembly - genetics | Viral Proteins - physiology | Membrane Proteins - metabolism | Calcium-Binding Proteins - metabolism | Gene Expression Regulation, Viral - physiology | Membrane Proteins - genetics | Herpesvirus 4, Human - physiology | Cell Cycle Proteins - metabolism | Endosomal Sorting Complexes Required for Transport - metabolism | Viral Proteins - genetics | Virus Assembly - physiology | Protein Transport | Nuclear Envelope - metabolism | Calcium-Binding Proteins - physiology | Virus Release - physiology | Cell Line, Tumor | Herpesvirus 4, Human - metabolism | Cell Cycle Proteins - physiology | Endosomal Sorting Complexes Required for Transport - physiology | Viral proteins | Physiological aspects | Epstein-Barr virus | Virulence (Microbiology) | Research | Health aspects | Membrane proteins | Proteins | Medical research | Kinases | Plasmids
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8. Full Text Functional interchangeability of late domains, late domain cofactors and ubiquitin in viral budding
by Zhadina, Maria and Bieniasz, Paul D
PLoS Pathogens, ISSN 1553-7366, 10/2010, Volume 6, Issue 10, p. e1001153
The membrane scission event that separates nascent enveloped virions from host cell membranes often requires the ESCRT pathway, which can be engaged through... 
BINDING DOMAINS | ESCRT-III | PARTICLE RELEASE | EAP45-GLUE DOMAIN | MICROBIOLOGY | MULTIVESICULAR BODY PATHWAY | VIROLOGY | STRUCTURAL BASIS | IMMUNODEFICIENCY-VIRUS TYPE-1 | ROUS-SARCOMA-VIRUS | PROTEIN-SORTING PATHWAY | EARLY ENDOSOMES | PARASITOLOGY | Ankyrin Repeat - physiology | Protein Binding - genetics | Coenzymes - genetics | Ubiquitins - genetics | Humans | Endosomal Sorting Complexes Required for Transport - genetics | Viral Proteins - metabolism | Gene Products, gag - chemistry | Coenzymes - metabolism | Transfection | Virus Release - genetics | Viral Proteins - physiology | Cell Cycle Proteins - genetics | Spumavirus - physiology | Ubiquitins - metabolism | Calcium-Binding Proteins - metabolism | Gene Products, gag - genetics | Viral Proteins - chemistry | Cell Cycle Proteins - metabolism | Cells, Cultured | Endosomal Sorting Complexes Required for Transport - metabolism | Ubiquitin-Protein Ligases - metabolism | Viral Proteins - genetics | Spumavirus - metabolism | Protein Structure, Tertiary - genetics | Gene Products, gag - metabolism | Amino Acid Motifs - physiology | Ankyrin Repeat - genetics | Models, Biological | Calcium-Binding Proteins - physiology | Virus Release - physiology | Amino Acid Motifs - genetics | Ubiquitin-Protein Ligases - genetics | Cell Cycle Proteins - physiology | Endosomal Sorting Complexes Required for Transport - physiology | Calcium-Binding Proteins - genetics | Protein Binding - physiology | Protein Structure, Tertiary - physiology | Ubiquitin | Research | Properties | Binding proteins | Ligases | Viral genetics | Proteins | Cell division | Plasmids
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9. Full Text Norwalk virus binds to histo-blood group antigens present on gastroduodenal epithelial cells of secretor individuals
by Marionneau, Severine and Ruvoën, Nathalie and Le Moullac–Vaidye, Beatrice and Clement, Monique and Cailleau–Thomas, Anne and Ruiz–Palacois, Guillermo and Huang, Pengwei and Jiang, Xi and Le Pendu, Jacques
Gastroenterology, ISSN 0016-5085, 06/2002, Volume 122, Issue 7, pp. 1967 - 1977
Norwalk Virus (NV) is a member of the family, which causes acute epidemic gastroenteritis in humans of all ages and its cellular receptors have not yet been... 
PROTEIN | ENTERIC CALICIVIRUSES | VIRAL GASTROENTERITIS | CELLULAR RECEPTOR | SIALIC-ACID | MONOCLONAL-ANTIBODIES | OUTBREAK | GASTROENTEROLOGY & HEPATOLOGY | EXPRESSION | EPIDEMIOLOGY | HEMORRHAGIC-DISEASE VIRUS | Caco-2 Cells | Duodenum - immunology | Carbohydrates - physiology | Cricetinae | Norwalk virus - physiology | Stomach - immunology | Humans | Virion - physiology | Rats | ABO Blood-Group System | Saliva - physiology | Lewis Blood-Group System - physiology | Epithelial Cells - physiology | Phenotype | Animals | Blood Group Antigens - physiology | Isoantigens - physiology | Ligands | CHO Cells | Antigens | Gastroenteritis | Communicable diseases | Transferases | Fluorescein | Albumin | Monoclonal antibodies | Cells
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10. Full Text Extracellular vesicles and viruses
: Are they close relatives?
by Esther Nolte-'t Hoen and Tom Cremer and Robert C. Gallo and Leonid B. Margolis
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 8/2016, Volume 113, Issue 33, pp. 9155 - 9161
Extracellular vesicles (EVs) released by various cells are small phospholipid membrane-enclosed entities that can carry miRNA. They are now central to research... 
PERSPECTIVE | Infection | Extracellular vesicles | Viruses | Defective viruses | Exosomes | HIV-1 | viruses | infection | extracellular vesicles | DENDRITIC CELLS | RNA | defective viruses | MULTIDISCIPLINARY SCIENCES | MICROVESICLES | MICROPARTICLES | PATHOGENESIS | BIOGENESIS | exosomes | SECRETION | EXOSOMAL TRANSFER | LYMPHOCYTES | APOBEC-3G Deaminase - physiology | Animals | Exosomes - physiology | Humans | Virion - physiology | Extracellular Vesicles - physiology | Virus Diseases - therapy | MicroRNAs - physiology | Virus Diseases - etiology | Extracellular matrix | Host-virus relationships | Observations | Health aspects | Biological Sciences
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11. Full Text HIV-1 Vpu promotes release and prevents endocytosis of nascent retrovirus particles from the plasma membrane
by Neil, Stuart J. D and Eastman, Scott W and Jouvenet, Nolwenn and Bieniasz, Paul D
PLoS Pathogens, ISSN 1553-7366, 05/2006, Volume 2, Issue 5, pp. 354 - 367
The human immunodeficiency virus (HIV) type-1 viral protein U (Vpu) protein enhances the release of diverse retroviruses from human, but not monkey, cells and... 
MICROBIOLOGY | PARASITOLOGY | VIROLOGY | Endosomes - virology | Cell Line | Retroviridae - physiology | Gene Products, gag - genetics | HeLa Cells - virology | Endosomes - physiology | Subtilisin - pharmacology | Humans | Virion - physiology | Human Immunodeficiency Virus Proteins | Green Fluorescent Proteins - genetics | Cell Membrane - physiology | Endosomes - metabolism | Endocytosis - physiology | Gene Products, gag - metabolism | Animals | HIV-1 - physiology | Leukemia Virus, Murine - metabolism | Recombinant Fusion Proteins - pharmacokinetics | Green Fluorescent Proteins - pharmacokinetics | Viral Regulatory and Accessory Proteins - physiology | Protein Structure, Tertiary - physiology | Physiological aspects | Endocytosis | Viral proteins | HIV infection | Health aspects | HIV - AIDS | Homo (human) | In Vitro | Viruses | None | Cell Biology | Virology | Proteins | Studies | HIV | Acquired immune deficiency syndrome | Atoms & subatomic particles | AIDS | Human immunodeficiency virus
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