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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 | Ribonucleic acids | Mortality | Replication | Genomes | Online | Assembly
Journal Article
Science, ISSN 0036-8075, 12/2012, Volume 338, Issue 6114, pp. 1631 - 1634
Influenza virus ribonucleoprotein complexes (RNPs) are central to the viral life cycle and in adaptation to new host species. RNPs are composed of the viral... 
RNA | Active sites | Nucleoproteins | Virions | REPORTS | Viral genomes | Orthomyxoviridae | Viruses | Viral morphology | Genomes | Electron microscopy | A VIRUS | RIBONUCLEOPROTEIN COMPLEXES | CRYSTAL-STRUCTURE | HUMAN-CELLS | NUCLEOPROTEIN | MULTIDISCIPLINARY SCIENCES | ELECTRON-MICROSCOPY | VIRAL POLYMERASE | GENERATION | BINDING | Viral Core Proteins - ultrastructure | RNA Replicase - metabolism | Influenza A Virus, H1N1 Subtype - physiology | Crystallography, X-Ray | Viral Proteins - metabolism | Influenza A Virus, H1N1 Subtype - ultrastructure | Protein Subunits - metabolism | RNA Replicase - ultrastructure | Viral Core Proteins - metabolism | Ribonucleoproteins - genetics | Transcription, Genetic | RNA, Viral - metabolism | Ribonucleoproteins - chemistry | Nucleic Acid Conformation | Influenza A Virus, H1N1 Subtype - genetics | Genome, Viral | Viral Core Proteins - chemistry | Viral Proteins - chemistry | RNA-Binding Proteins - chemistry | Models, Molecular | Ribonucleoproteins - metabolism | Viral Proteins - ultrastructure | Microscopy, Electron | Cryoelectron Microscopy | RNA-Binding Proteins - ultrastructure | RNA, Viral - chemistry | Image Processing, Computer-Assisted | Virus Replication | RNA Replicase - chemistry | Protein Conformation | Influenza A Virus, H1N1 Subtype - chemistry | Protein Subunits - chemistry | Ribonucleoproteins - ultrastructure | RNA, Viral - ultrastructure | RNA-Binding Proteins - metabolism | Influenza viruses | Properties | Ribonucleoproteins | RNA polymerase | RNA-protein interactions | Influenza | Genomics | Virology | Ribonucleic acids | Microscopy | Mortality | Replication | Online | Assembly
Journal Article
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
Journal Article
Nature, ISSN 0028-0836, 07/2016, Volume 535, Issue 7610, pp. 173 - 177
Journal Article
Protein Science, ISSN 0961-8368, 02/2015, Volume 24, Issue 2, pp. 221 - 235
Viral proteins bind to numerous cellular and viral proteins throughout the infection cycle. However, the mechanisms by which viral proteins interact with such... 
protein–protein interactions | systems biology | host–pathogen interactions | hepatitis virus | hepatitis C virus | viral protein | virus | intrinsically disordered proteins | host-pathogen interactions | protein-protein interactions | RANDOM MUTAGENESIS | TERMINAL DOMAIN | MOLECULAR RECOGNITION FEATURES | BIOCHEMISTRY & MOLECULAR BIOLOGY | FLEXIBLE NETS | NUCLEAR-LOCALIZATION | NS5A PROTEIN | STRUCTURAL BASIS | SEQUENCE ALIGNMENT | FUZZY COMPLEXES | NUCLEOCAPSID-LIKE PARTICLES | Amino Acid Sequence | Viral Core Proteins - chemistry | Hepatitis C - metabolism | Hepatitis C - veterinary | Humans | Computational Biology | Hepacivirus - genetics | Molecular Sequence Data | Phylogeny | Hepacivirus - chemistry | Intrinsically Disordered Proteins - genetics | Protein Interaction Maps | Host-Pathogen Interactions | Animals | Intrinsically Disordered Proteins - chemistry | Viral Core Proteins - genetics | Viral Core Proteins - metabolism | Protein Binding | Hepacivirus - physiology | Intrinsically Disordered Proteins - metabolism | Proteins | Hepatitis | Binding | Yeast | Feature recognition | Biological evolution | Amino acid sequence | Viruses | Genetic screening | Conserved sequence | Mutagenesis | Core protein | Genetic analysis | Modelling | Mathematical models | Hepatitis C virus | Hepatitis C | Protein interaction | Genotypes | Index Medicus
Journal Article
Science Translational Medicine, ISSN 1946-6234, 07/2015, Volume 7, Issue 294, pp. 294ra105 - 294ra105
Journal Article
Nature, ISSN 0028-0836, 12/2006, Volume 444, Issue 7122, pp. 1078 - 1082
Journal Article