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The Journal of Infectious Diseases, ISSN 0022-1899, 04/2019, Volume 219, Issue Supplement_1, pp. S5 - S13
Abstract The year 2018 marked the 100th anniversary of the deadliest event in human history. In 1918–1919, pandemic influenza spread globally and caused an... 
influenza | INFECTIOUS DISEASES | HOST | MICROBIOLOGY | DEATH | PATHOLOGY | IMMUNOLOGY | pandemic | PNEUMONIA | pathogenesis | vaccine | EQUINE INFLUENZA | EVOLUTION | VIRUS INFECTION
Journal Article
New England Journal of Medicine, ISSN 0028-4793, 12/2018, Volume 379, Issue 24, pp. 2285 - 2287
Journal Article
Clinical Infectious Diseases, ISSN 1058-4838, 5/2010, Volume 50, Issue 9, pp. 1252 - 1255
Pandemic 2009 H1N1 virus isolates containing the neuraminidase inhibitor resistance mutation H275Y have been reported. We describe rapid selection for the... 
H1N1 subtype influenza A virus | Pandemics | Infectious diseases | Influenza A virus | Antivirals | Viruses | Infections | Immunocompromised hosts | Inhibitory concentration 50 | Genetic mutation | BRIEF REPORTS
Journal Article
MBIO, ISSN 2150-7511, 03/2019, Volume 10, Issue 2, p. e00307-19
The effectiveness of influenza vaccines against circulating A(H1N1) pdm09 viruses was modest for several seasons despite the absence of antigenic drift of... 
influenza | IMMUNITY | ASSAY | vaccines | VACCINE | HUMANS | MICROBIOLOGY | PANDEMIC H1N1 | SERUM | neuraminidase | antigenic drift | RESISTANCE | INFECTION | MONOCLONAL-ANTIBODIES | monoclonal antibodies | EPITOPES
Journal Article
Science, ISSN 0036-8075, 7/2012, Volume 337, Issue 6091, pp. 199 - 204
Influenza A virus (IAV) infection leads to variable and imperfectly understood pathogenicity. We report that segment 3 of the virus contains a second open... 
Proteins | Messenger RNA | RNA | Lungs | RESEARCH ARTICLES | Viruses | Infections | Open reading frames | Gene expression | Codons | Genetic mutation | SYSTEM | PA SUBUNIT | ENDONUCLEASE | MULTIDISCIPLINARY SCIENCES | SIGNALS | DEGRADATION | INFECTION | SUPPRESSION | BINDING | CELL-DEATH | Humans | Influenza A virus - genetics | RNA Replicase - metabolism | Reassortant Viruses - genetics | RNA, Messenger - metabolism | Viral Proteins - metabolism | Orthomyxoviridae Infections - genetics | Base Sequence | Repressor Proteins - metabolism | Amino Acid Sequence | RNA Replicase - genetics | Viral Proteins - chemistry | Orthomyxoviridae Infections - pathology | Repressor Proteins - genetics | Viral Proteins - genetics | Proteome | Influenza A virus - metabolism | Viral Nonstructural Proteins - metabolism | Mice | Mice, Inbred BALB C | Mutation | Orthomyxoviridae Infections - virology | Open Reading Frames | Molecular Sequence Data | Influenza A Virus, H1N1 Subtype - growth & development | Lung - virology | Viral Nonstructural Proteins - chemistry | Codon | Frameshifting, Ribosomal | RNA, Viral - genetics | HEK293 Cells | Conserved Sequence | Female | Protein Interaction Domains and Motifs | RNA, Viral - metabolism | Influenza A Virus, H1N1 Subtype - genetics | Viral Proteins - biosynthesis | Cell Line | Genome, Viral | Lung - pathology | Repressor Proteins - chemistry | RNA, Messenger - genetics | Gene Expression Regulation | Viral Nonstructural Proteins - genetics | Influenza A Virus, H1N1 Subtype - pathogenicity | Animals | Virus Replication | RNA Replicase - chemistry | Orthomyxoviridae Infections - immunology | Pathology | Genetic aspects | Research | Influenza | Influenza research | Pathogenesis | Virology | Ribonucleic acids | Genes | Molecular interactions | Segments | Genomes | Constraining
Journal Article
Science, ISSN 0036-8075, 4/2006, Volume 312, Issue 5772, pp. 404 - 410
The hemagglutinin (HA) structure at 2.9 angstrom resolution, from a highly pathogenic Vietnamese H5N1 influenza virus, is more related to the 1918 and other... 
Polysaccharides | Receptors | Viruses | Ligands | Trimers | Viral morphology | Research Articles | H5N1 subtype influenza A virus | Genetic mutation | Monomers | Virology | OLIGOSACCHARIDES | EVOLUTION | FUSION | DETERMINANTS | SUBTYPES | MULTIDISCIPLINARY SCIENCES | HUMANS | SIALIC-ACID | GLYCOSYLATION | GLYCOPEPTIDES | BINDING PROPERTIES | Species Specificity | Receptors, Virus - metabolism | Humans | Virulence | Molecular Sequence Data | Crystallography, X-Ray | Influenza A Virus, H5N1 Subtype - genetics | Respiratory Mucosa - virology | Hemagglutinin Glycoproteins, Influenza Virus - immunology | Sialic Acids - chemistry | Hemagglutinin Glycoproteins, Influenza Virus - genetics | Lung - virology | Cloning, Molecular | Influenza A Virus, H5N1 Subtype - metabolism | Binding Sites | Protein Structure, Tertiary | Amino Acid Sequence | Hemagglutinin Glycoproteins, Influenza Virus - chemistry | Antigenic Variation | Sialic Acids - metabolism | Models, Molecular | Birds | Glycosylation | Hemagglutinin Glycoproteins, Influenza Virus - metabolism | Protein Folding | Polysaccharides - metabolism | Animals | Receptors, Virus - chemistry | Influenza A Virus, H5N1 Subtype - chemistry | Influenza A Virus, H5N1 Subtype - pathogenicity | Protein Conformation | Mutation | Carbohydrate Conformation | Amino Acid Substitution | Avian influenza | Agglutination tests | Research | Analysis
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