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Times Cited: 11
Times Cited: 11
Times Cited
Times Co-cited
Similarity
Exploitation of glycosylation in enveloped virus pathobiology.
Yasunori Watanabe, Thomas A Bowden, Ian A Wilson, Max Crispin. Biochim Biophys Acta Gen Subj 2019
Yasunori Watanabe, Thomas A Bowden, Ian A Wilson, Max Crispin. Biochim Biophys Acta Gen Subj 2019
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A Site of Vulnerability on the Influenza Virus Hemagglutinin Head Domain Trimer Interface.
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A highly conserved neutralizing epitope on group 2 influenza A viruses.
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Hemagglutinin-stem nanoparticles generate heterosubtypic influenza protection.
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Potent anti-influenza H7 human monoclonal antibody induces separation of hemagglutinin receptor-binding head domains.
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Site-specific glycan analysis of the SARS-CoV-2 spike.
Yasunori Watanabe, Joel D Allen, Daniel Wrapp, Jason S McLellan, Max Crispin. Science 2020
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Broad-spectrum in vitro activity and in vivo efficacy of the antiviral protein griffithsin against emerging viruses of the family Coronaviridae.
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Structure of the Lassa virus glycan shield provides a model for immunological resistance.
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N-Glycosylation of Seasonal Influenza Vaccine Hemagglutinins: Implication for Potency Testing and Immune Processing.
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Integrated Omics and Computational Glycobiology Reveal Structural Basis for Influenza A Virus Glycan Microheterogeneity and Host Interactions.
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Human lectins and their roles in viral infections.
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Diversity of Functionally Permissive Sequences in the Receptor-Binding Site of Influenza Hemagglutinin.
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A structural explanation for the low effectiveness of the seasonal influenza H3N2 vaccine.
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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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A neutralizing antibody selected from plasma cells that binds to group 1 and group 2 influenza A hemagglutinins.
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Site-specific glycosylation profile of influenza A (H1N1) hemagglutinin through tandem mass spectrometry.
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Antibodies to a Conserved Influenza Head Interface Epitope Protect by an IgG Subtype-Dependent Mechanism.
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A broadly neutralizing human monoclonal antibody that recognizes a conserved, novel epitope on the globular head of the influenza H1N1 virus hemagglutinin.
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Recent H3N2 Viruses Have Evolved Specificity for Extended, Branched Human-type Receptors, Conferring Potential for Increased Avidity.
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Major antigenic site B of human influenza H3N2 viruses has an evolving local fitness landscape.
Nicholas C Wu, Jakub Otwinowski, Andrew J Thompson, Corwin M Nycholat, Armita Nourmohammad, Ian A Wilson. Nat Commun 2020
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Human Influenza A Virus Hemagglutinin Glycan Evolution Follows a Temporal Pattern to a Glycan Limit.
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A complex epistatic network limits the mutational reversibility in the influenza hemagglutinin receptor-binding site.
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Vaccine-Induced Antibodies that Neutralize Group 1 and Group 2 Influenza A Viruses.
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18
A carbohydrate side chain on hemagglutinins of Hong Kong influenza viruses inhibits recognition by a monoclonal antibody.
J J Skehel, D J Stevens, R S Daniels, A R Douglas, M Knossow, I A Wilson, D C Wiley. Proc Natl Acad Sci U S A 1984
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Antibody recognition of a highly conserved influenza virus epitope.
Damian C Ekiert, Gira Bhabha, Marc-André Elsliger, Robert H E Friesen, Mandy Jongeneelen, Mark Throsby, Jaap Goudsmit, Ian A Wilson. Science 2009
Damian C Ekiert, Gira Bhabha, Marc-André Elsliger, Robert H E Friesen, Mandy Jongeneelen, Mark Throsby, Jaap Goudsmit, Ian A Wilson. Science 2009
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Computational design of trimeric influenza-neutralizing proteins targeting the hemagglutinin receptor binding site.
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NAction! How Can Neuraminidase-Based Immunity Contribute to Better Influenza Virus Vaccines?
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18
Highly conserved protective epitopes on influenza B viruses.
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H7N9 influenza virus neutralizing antibodies that possess few somatic mutations.
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Co-cited is the co-citation frequency, indicating how many articles cite the article together with the query article. Similarity is the co-citation as percentage of the times cited of the query article or the article in the search results, whichever is the lowest. These numbers are calculated for the last 100 citations when articles are cited more than 100 times.