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Nature, ISSN 0028-0836, 01/2018, Volume 553, Issue 7689, pp. 521 - 525
Kaposi's sarcoma-associated herpesvirus (KSHV) causes Kaposi's sarcoma(1,2), a cancer that commonly affects patients with AIDS3 and which is endemic in... 
SYSTEM | DNA-SEQUENCES | BACTERIOPHAGES | KAPOSIS-SARCOMA | VIRUS CAPSIDS | SINGLE-PARTICLE RECONSTRUCTIONS | MULTIDISCIPLINARY SCIENCES | SARCOMA-ASSOCIATED HERPESVIRUS | ELECTRON-MICROSCOPY | CRYO-EM | COMMON ANCESTRY | Disulfides - metabolism | Capsid - ultrastructure | Capsid - chemistry | Virus Replication - genetics | Protein Multimerization | Mutant Proteins - ultrastructure | Capsid Proteins - chemistry | Drug Design | Protein Domains | Herpesvirus 8, Human - chemistry | Protein Stability | Capsid - metabolism | Capsid Proteins - metabolism | Mutant Proteins - genetics | Models, Molecular | Herpesvirus 8, Human - genetics | Mutant Proteins - metabolism | Capsid Proteins - ultrastructure | Cryoelectron Microscopy | Mutagenesis | Mutant Proteins - chemistry | Herpesvirus 8, Human - ultrastructure | Hydrophobic and Hydrophilic Interactions | Protein Binding | Mutation | Herpesvirus 8, Human - growth & development | Capsid Proteins - genetics | Human herpesvirus 8 | Genetic aspects | Health aspects | Protein-protein interactions | Molecular structure | Capsid protein | Amino acids | Genomes | Hydrophobicity | Proteins | Single-cell protein | Chemical bonds | Atomic structure | Dimerization | Deoxyribonucleic acid--DNA | Antiviral agents | Disulfide bonds | Polypeptides | Sarcoma | Molecular interactions | Crosslinking | Gene expression | Electron microscopy | Capsids | Microscopy | Kaposi's sarcoma | Herpes viruses | Replication | Gene mapping | Protein interaction | Cancer | Index Medicus
Journal Article
PLoS ONE, ISSN 1932-6203, 08/2012, Volume 7, Issue 8, pp. e43519 - e43519
Mucosotropic, high-risk human papillomaviruses (HPV) are sexually transmitted viruses that are causally associated with the development of cervical cancer. The... 
MULTIDISCIPLINARY SCIENCES | HUMAN CYTOMEGALOVIRUS | SQUAMOUS-CELL CARCINOMA | INHIBITOR SLPI | VIRUS-LIKE PARTICLES | HEPARAN-SULFATE | CERVICAL-CANCER | II BINDS | MINOR CAPSID PROTEIN | COMMON NEUTRALIZATION EPITOPE | RNA, Small Interfering - genetics | Human papillomavirus 16 - physiology | Oncogene Proteins, Viral - chemistry | Humans | Protein Multimerization | Molecular Sequence Data | Substrate Specificity | Receptors, Cell Surface | S100 Proteins - immunology | S100 Proteins - chemistry | Gene Knockdown Techniques | Epitopes - immunology | Annexin A2 - chemistry | S100 Proteins - genetics | Capsid Proteins - chemistry | Protein Structure, Quaternary | Capsid Proteins - immunology | Oncogene Proteins, Viral - genetics | Annexin A2 - immunology | Oncogene Proteins, Viral - metabolism | Amino Acid Sequence | Capsid Proteins - metabolism | S100 Proteins - metabolism | Human papillomavirus 16 - metabolism | Annexin A2 - genetics | Epithelial Cells - virology | Epitopes - chemistry | Oncogene Proteins, Viral - immunology | HeLa Cells | Mutation | Annexin A2 - metabolism | Capsid Proteins - genetics | Genotype | Genetic aspects | Research | Annexins | Health aspects | Papillomavirus infections | Risk factors | Capsid protein | Peptides | Epithelial cells | Viruses | Amino acids | Infections | Biochemistry | Cell interactions | Cell surface | Nuclei | Proteins | S100 protein | Human papillomavirus | Immunology | Calcium-binding protein | Deoxyribonucleic acid--DNA | Genotypes | Immunoglobulins | Departments | Risk groups | Gynecology | Health risks | Proteinase inhibitors | Epitopes | Cervix | Obstetrics | White blood cells | Disease transmission | Neutralizing | Herpes viruses | Internalization | Nuclei (cytology) | Electron paramagnetic resonance | Molecular biology | Cervical cancer | Cancer | Index Medicus | Deoxyribonucleic acid | DNA
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 2017, Volume 292, Issue 33, pp. 13584 - 13598
Vibrio cholerae is a natural inhabitant of aquatic environments and converts to a pathogen upon infection by a filamentous phage, CTX Phi, that transmits the... 
POLAR LOCALIZATION | FILAMENTOUS PHAGE | 2-HYBRID SYSTEM | COLI CELL-ENVELOPE | PSEUDOMONAS-AERUGINOSA | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | C-TERMINAL DOMAIN | PAL COMPLEX | ANALYSIS WORKBENCH | OUTER-MEMBRANE INTEGRITY | Receptors, Virus - metabolism | Protein Multimerization | Vibrio cholerae - pathogenicity | Bacterial Proteins - chemistry | Crystallography, X-Ray | Receptors, Virus - genetics | Recombinant Fusion Proteins - metabolism | Cystine - chemistry | Gene Deletion | Capsid Proteins - chemistry | Protein Interaction Domains and Motifs | Viral Tropism | Binding Sites | Recombinant Proteins - metabolism | Mutagenesis, Site-Directed | Vibrio cholerae - virology | Capsid Proteins - metabolism | Bacterial Proteins - genetics | Models, Molecular | Recombinant Proteins - chemistry | Recombinant Fusion Proteins - chemistry | Static Electricity | Vibrio cholerae - metabolism | Arginine - chemistry | Point Mutation | Two-Hybrid System Techniques | Receptors, Virus - chemistry | Bacterial Proteins - metabolism | Protein Conformation | Structural Homology, Protein | Bacteriophages - physiology | Amino Acid Substitution | Capsid Proteins - genetics | Index Medicus | Life Sciences | Biochemistry, Molecular Biology | protein interaction | Microbiology | Vibrio cholerae | protein | bacterial pathogenesis | protein complex | bacteriophage | molecular motor
Journal Article
Journal of Molecular Biology, ISSN 0022-2836, 06/2014, Volume 426, Issue 13, pp. 2500 - 2519
Misfolded protein aggregates, characterized by a canonical amyloid fold, play a central role in the pathobiology of neurodegenerative diseases. Agents that... 
amyloid | gene 3 protein | amyloid remodeling | Ig fusion | FIBRIL FORMATION | MEMBRANE-FILTER ASSAY | N-TERMINAL DOMAINS | ALZHEIMERS-DISEASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | ALPHA-SYNUCLEIN | FILAMENTOUS PHAGE FD | PROLYL ISOMERIZATION | CONFORMATIONAL CONVERSION | A-BETA | Neurodegenerative Diseases - etiology | Humans | Protein Multimerization | tau Proteins - metabolism | Bacteriophage M13 - metabolism | Recombinant Fusion Proteins - metabolism | tau Proteins - chemistry | Bacteriophage M13 - genetics | Amyloid beta-Peptides - metabolism | Capsid Proteins - chemistry | Membrane Transport Proteins - metabolism | Protein Interaction Domains and Motifs | Capsid Proteins - metabolism | Bacterial Outer Membrane Proteins - chemistry | Models, Molecular | Escherichia coli Proteins - metabolism | Neurodegenerative Diseases - metabolism | Recombinant Fusion Proteins - chemistry | Protein Folding | Membrane Transport Proteins - chemistry | alpha-Synuclein - chemistry | Bacterial Outer Membrane Proteins - metabolism | Protein Binding | Recombinant Fusion Proteins - genetics | Protein Conformation | Amyloid beta-Peptides - chemistry | Kinetics | Escherichia coli Proteins - chemistry | alpha-Synuclein - metabolism | Capsid Proteins - genetics | Viral proteins | Isomerization | Protein binding | Index Medicus
Journal Article
Nature, ISSN 0028-0836, 04/2011, Volume 472, Issue 7343, pp. 361 - 365
TRIM5 is a RING domain-E3 ubiquitin ligase that restricts infection by human immunodeficiency virus (HIV)-1 and other retroviruses immediately following virus... 
HIV-1 | CYCLOPHILIN-A | UNANCHORED POLYUBIQUITIN CHAINS | TRIM5-ALPHA PROTEIN | RECOGNITION | HUMAN-CELLS | MULTIDISCIPLINARY SCIENCES | IMMUNODEFICIENCY-VIRUS TYPE-1 | RESISTANCE | INFECTION | RESTRICTION | Capsid - chemistry | Receptors, Pattern Recognition - immunology | Humans | Ubiquitin - metabolism | NF-kappa B - metabolism | Lipopolysaccharides - immunology | Transcription Factor AP-1 - metabolism | Receptors, Pattern Recognition - metabolism | Signal Transduction - immunology | Ubiquitin-Protein Ligases - immunology | HIV-1 - chemistry | HEK293 Cells | Carrier Proteins - immunology | Cell Line | Retroviridae - chemistry | Ubiquitin-Protein Ligases - metabolism | Retroviridae - immunology | MAP Kinase Kinase Kinases - metabolism | Transcription Factors - metabolism | Capsid - immunology | Carrier Proteins - genetics | Immunity, Innate - immunology | HIV-1 - immunology | Carrier Proteins - metabolism | Signal Transduction - drug effects | Ubiquitin-Conjugating Enzymes - metabolism | Lipopolysaccharides - pharmacology | Protein Binding | Enzyme Activation | Ubiquitin-Protein Ligases - genetics | Signal transduction | Efficiency | RNA polymerase | Pattern recognition | Kinases | Evacuations & rescues | Immune system | Index Medicus | HIV-1/immunology | Capsid/immunology | Life Sciences | MAP Kinase Kinase Kinases/metabolism | Carrier Proteins/immunology | Immunology | Transcription Factors/metabolism | Capsid/chemistry | HIV-1/chemistry | Ubiquitin/metabolism | Receptors, Pattern Recognition/immunology | Retroviridae/chemistry | Ubiquitin-Protein Ligases/immunology | Ubiquitin-Conjugating Enzymes/metabolism | HumansImmunity, Innate/immunology | Lipopolysaccharides/pharmacology | Signal Transduction/drug effects | Retroviridae/immunology | Transcription Factor AP-1/metabolism | Lipopolysaccharides/immunology | Ubiquitin-Protein Ligases/metabolism | Carrier Proteins/genetics | Signal Transduction/immunology | NF-kappa B/metabolism | Ubiquitin-Protein Ligases/genetics | Carrier Proteins/metabolism | Receptors, Pattern Recognition/metabolism
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 4/2010, Volume 107, Issue 14, pp. 6292 - 6297
Bluetongue virus (BTV) is transmitted by blood-feeding insects (Culicoides sp.) and causes hemorrhagic diseases in livestock. BTV is a nonenveloped,... 
Proteins | Capsid proteins | Double stranded RNA | Maps | Rotavirus | Viruses | Amino acids | Trimers | Infections | Bluetongue virus | Sialic acid-binding protein | dsRNA virus structure | Membrane penetration protein | Cryo-electron microscopy | CAPSID PROTEIN | RECONSTRUCTION | MULTIDISCIPLINARY SCIENCES | membrane penetration protein | HIV-1 GP41 | FUNCTIONAL-CHARACTERIZATION | RICE-DWARF-VIRUS | ATOMIC-STRUCTURE | ELECTRON CRYOMICROSCOPY | MEMBRANE-PENETRATION PROTEIN | CELL ENTRY | EXPRESSION | cryo-electron microscopy | sialic acid-binding protein | Protein Structure, Tertiary | Amino Acid Sequence | Cell Line | Cricetinae | Viral Fusion Proteins - metabolism | Protein Structure, Secondary | Capsid Proteins - metabolism | Humans | Protein Multimerization | Bluetongue virus - chemistry | Models, Molecular | Molecular Sequence Data | N-Acetylneuraminic Acid - metabolism | Capsid Proteins - ultrastructure | Cryoelectron Microscopy | N-Acetylneuraminic Acid - chemistry | Animals | Viral Fusion Proteins - chemistry | Virus Replication | Capsid Proteins - chemistry | Protein Structure, Quaternary | Viral Fusion Proteins - ultrastructure | Bluetongue virus - metabolism | Binding Sites | RNA viruses | Usage | Viral proteins | Physiological aspects | Genetic aspects | Research | Electron microscopy | Structure | Health aspects | Membranes | Genomics | Deoxyribonucleic acid--DNA | Index Medicus | Transcription | Double-stranded RNA | Amino acid sequence | Data processing | Genomes | Hemorrhagic disease | Peptide mapping | Bluetongue | Capsids | Coats | Infection | Microscopy | Influenza | Virions | Cell adhesion | Coat protein | Livestock | Fusion protein | Gene mapping | Core particles | Sugar | Biological Sciences
Journal Article
Cancer Cell, ISSN 1535-6108, 12/2004, Volume 6, Issue 6, pp. 611 - 623
ONYX-015 is an adenovirus that lacks the E1B-55K gene product for p53 degradation. Thus, ONYX-015 was conceived as an oncolytic virus that would selectively... 
NUCLEAR-LOCALIZATION | ADENOVIRUS REPLICATION | CHROMOSOME-TRANSLOCATION | MESSENGER-RNA | ONCOLOGY | E1B 55-KILODALTON PROTEIN | INFECTED-CELLS | TIME QUANTITATIVE PCR | SV40-TRANSFORMED CELLS | NUCLEOPORIN GENE | NECK-CANCER | Gene Expression - genetics | Virus Replication - genetics | Humans | Viral Proteins - metabolism | Cytopathogenic Effect, Viral - genetics | Caspase 3 | RNA Transport | Capsid Proteins - metabolism | HCT116 Cells | Cell Cycle Proteins - metabolism | In Situ Hybridization, Fluorescence | Caspase Inhibitors | Blotting, Western | Proto-Oncogene Proteins c-mdm2 | Models, Biological | Adenovirus E1A Proteins - genetics | Epithelial Cells - virology | Viral Nonstructural Proteins - metabolism | Adenoviruses, Human - genetics | Adenoviridae - metabolism | Mutation | Adenoviruses, Human - metabolism | Capsid Proteins - genetics | Neoplasms - metabolism | Epithelial Cells - metabolism | DNA, Viral - biosynthesis | Neoplasms - virology | Caspases - metabolism | Neoplasms - genetics | Adenovirus E1A Proteins - metabolism | Polymerase Chain Reaction | Adenoviridae - genetics | Cell Cycle Proteins - genetics | Protein Biosynthesis - genetics | RNA, Viral - metabolism | Adenovirus E1B Proteins - metabolism | Nuclear Proteins - genetics | Adenovirus E1B Proteins - genetics | Proto-Oncogene Proteins - metabolism | Epithelial Cells - radiation effects | Cyclin-Dependent Kinase Inhibitor p21 | Cells, Cultured | Tumor Suppressor Protein p53 - metabolism | Viral Nonstructural Proteins - genetics | Viral Plaque Assay | Nuclear Proteins - metabolism | Proto-Oncogene Proteins - genetics | bcl-2-Associated X Protein | Poly(ADP-ribose) Polymerases - metabolism | Viral Vaccines | Tumor Suppressor Protein p14ARF - metabolism | Proto-Oncogene Proteins c-bcl-2 - genetics | Apoptosis | Index Medicus
Journal Article
Journal of General Virology, ISSN 0022-1317, 06/2018, Volume 99, Issue 6, pp. 851 - 859
Journal Article
PLoS Pathogens, ISSN 1553-7366, 02/2012, Volume 8, Issue 2, pp. e1002549 - e1002549
Gene expression of DNA viruses requires nuclear import of the viral genome. Human Adenoviruses ( Ads), like most DNA viruses, encode factors within early... 
SIMPLEX-VIRUS TYPE-1 | UBIQUITIN-INDEPENDENT DEGRADATION | VIRAL TRANSCRIPTION | PML NUCLEAR-BODIES | CYTOMEGALOVIRUS PP71 PROTEIN | MICROBIOLOGY | PROMYELOCYTIC-LEUKEMIA-PROTEIN | ANTIVIRAL DEFENSE | VIROLOGY | EARLY GENE-EXPRESSION | CELLULAR-PROTEIN | PARASITOLOGY | DEPENDENT DEGRADATION | Transcriptional Activation - genetics | Virus Replication - genetics | Genome, Viral - genetics | Humans | Viral Proteins - metabolism | Capsid Proteins - physiology | Transfection | Capsid Proteins - chemistry | Viral Proteins - physiology | Adenoviridae - genetics | Nuclear Proteins - genetics | Transcription Factors - physiology | Capsid Proteins - metabolism | Viral Proteins - chemistry | Cells, Cultured | Mutant Proteins - genetics | Genetic Fitness - physiology | Mutant Proteins - metabolism | Mutant Proteins - physiology | Transcription Factors - genetics | Transcription Factors - metabolism | Amino Acid Motifs - physiology | Adaptor Proteins, Signal Transducing - physiology | Gene Expression Regulation, Viral | Mutant Proteins - chemistry | Adaptor Proteins, Signal Transducing - genetics | Nuclear Proteins - physiology | Amino Acid Motifs - genetics | Genes, Viral - physiology | Capsid Proteins - genetics | Viral proteins | Adenoviruses | Physiological aspects | Genetic aspects | Genetic transcription | Research | Health aspects | Proteins | Viruses | Genomes | Gene expression | Cytoplasm | Apoptosis | Index Medicus | Life Sciences | Biochemistry, Molecular Biology
Journal Article
Virus Research, ISSN 0168-1702, 2006, Volume 122, Issue 1, pp. 127 - 136
Journal Article