Mutations in Influenza A Virus Neuraminidase and Hemagglutinin Confer Resistance against a Broadly Neutralizing Hemagglutinin Stem Antibody

Hydration Structure and Dynamics of Inhibitor-Bound HIV-1 Protease

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How single mutations affect viral escape from broad and narrow antibodies to H1 influenza hemagglutinin

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The Combined Effect of Oseltamivir and Favipiravir on Influenza A Virus Evolution

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Dengue Virus NS2B/NS3 Protease Inhibitors Exploiting the Prime Side

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Tackling influenza with broadly neutralizing antibodies

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An experimental evaluation of drug-induced mutational meltdown as an antiviral treatment strategy

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Molecular Basis for Differential Patterns of Drug Resistance in Influenza N1 and N2 Neuraminidase

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Molecular and Dynamic Mechanism Underlying Drug Resistance in Genotype 3 Hepatitis C NS3/4A Protease

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A broadly neutralizing anti-influenza antibody reveals ongoing capacity of haemagglutinin-specific memory B cells to evolve

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Two Escape Mechanisms of Influenza A Virus to a Broadly Neutralizing Stalk-Binding Antibody

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OPLS3: A Force Field Providing Broad Coverage of Drug-like Small Molecules and Proteins

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The role of Fc–FcγR interactions in IgG-mediated microbial neutralization

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Positive Selection Drives Preferred Segment Combinations during Influenza Virus Reassortment

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Coordinated Evolution of Influenza A Surface Proteins

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Drug Resistance Conferred by Mutations Outside the Active Site through Alterations in the Dynamic and Structural Ensemble of HIV-1 Protease

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WFABC: a Wright-Fisher ABC-based approach for inferring effective population sizes and selection coefficients from time-sampled data

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Structural basis and distal effects of Gag substrate coevolution in drug resistance to HIV-1 protease

(2014) Ayşegül Özen et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Epistatic interactions between neuraminidase mutations facilitated the emergence of the oseltamivir-resistant H1N1 influenza viruses

(2014) Susu Duan et al.   Nature Communications

Influenza Virus Drug Resistance: A Time-Sampled Population Genetics Perspective

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Broadly neutralizing antibodies against influenza viruses

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Receptor binding and pH stability — How influenza A virus hemagglutinin affects host-specific virus infection

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Egg- or cell culture-derived hemagglutinin mutations impair virus stability and antigen content of inactivated influenza vaccines

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Sialylneolacto-N-tetraose c (LSTc)-bearing Liposomal Decoys Capture Influenza A Virus

(2013) Gabriel L. Hendricks et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Evolution of the Influenza A Virus Genome during Development of Oseltamivir Resistance In Vitro

(2013) N. Renzette et al.   JOURNAL OF VIROLOGY

Structure of a Classical Broadly Neutralizing Stem Antibody in Complex with a Pandemic H2 Influenza Virus Hemagglutinin

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A Mutant Influenza Virus That Uses an N1 Neuraminidase as the Receptor-Binding Protein

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A common solution to group 2 influenza virus neutralization

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Influenza-virus membrane fusion by cooperative fold-back of stochastically induced hemagglutinin intermediates

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Broadly Neutralizing Antibodies Present New Prospects to Counter Highly Antigenically Diverse Viruses

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Structural basis of influenza virus neutralization

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Structural Characterization of an Early Fusion Intermediate of Influenza Virus Hemagglutinin

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Amino Acid Changes in Hemagglutinin Contribute to the Replication of Oseltamivir-Resistant H1N1 Influenza Viruses

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Influenza A Virus Hemagglutinin Antibody Escape Promotes Neuraminidase Antigenic Variation and Drug Resistance

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Discordant antigenic drift of neuraminidase and hemagglutinin in H1N1 and H3N2 influenza viruses

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A Highly Conserved Neutralizing Epitope on Group 2 Influenza A Viruses

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Effect of receptor binding domain mutations on receptor binding and transmissibility of avian influenza H5N1 viruses

(2011) Taronna R. Maines et al.   VIROLOGY

In vitro evolution of H5N1 avian influenza virus toward human-type receptor specificity

(2011) Li-Mei Chen et al.   VIROLOGY

Acid Stability of the Hemagglutinin Protein Regulates H5N1 Influenza Virus Pathogenicity

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Amino Acid Residues in the Fusion Peptide Pocket Regulate the pH of Activation of the H5N1 Influenza Virus Hemagglutinin Protein

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Structural and functional bases for broad-spectrum neutralization of avian and human influenza A viruses

(2009) Jianhua Sui et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Structures of receptor complexes formed by hemagglutinins from the Asian Influenza pandemic of 1957

(2009) J. Liu et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Hemagglutinin Receptor Binding Avidity Drives Influenza A Virus Antigenic Drift

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Epidemiological, antigenic and genetic characteristics of seasonal influenza A(H1N1), A(H3N2) and B influenza viruses: Basis for the WHO recommendation on the composition of influenza vaccines for use in the 2009–2010 Northern Hemisphere season

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Heterosubtypic Neutralizing Monoclonal Antibodies Cross-Protective against H5N1 and H1N1 Recovered from Human IgM+ Memory B Cells

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Analysis of residues near the fusion peptide in the influenza hemagglutinin structure for roles in triggering membrane fusion

(2007) Sudha Thoennes et al.   VIROLOGY