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Times Cited: 327
Times Cited: 327
Times Cited
Times Co-cited
Similarity
Cross-neutralization of influenza A viruses mediated by a single antibody loop.
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Highly conserved protective epitopes on influenza B viruses.
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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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Structural and functional bases for broad-spectrum neutralization of avian and human influenza A viruses.
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Antibody recognition of a highly conserved influenza virus epitope.
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Structure and Function Analysis of an Antibody Recognizing All Influenza A Subtypes.
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A highly conserved neutralizing epitope on group 2 influenza A viruses.
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Conserved epitope on influenza-virus hemagglutinin head defined by a vaccine-induced antibody.
Donald D Raymond, Goran Bajic, Jack Ferdman, Pirada Suphaphiphat, Ethan C Settembre, M Anthony Moody, Aaron G Schmidt, Stephen C Harrison. Proc Natl Acad Sci U S A 2018
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Viral receptor-binding site antibodies with diverse germline origins.
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Receptor mimicry by antibody F045-092 facilitates universal binding to the H3 subtype of influenza virus.
Peter S Lee, Nobuko Ohshima, Robyn L Stanfield, Wenli Yu, Yoshitaka Iba, Yoshinobu Okuno, Yoshikazu Kurosawa, Ian A Wilson. Nat Commun 2014
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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 stable trimeric influenza hemagglutinin stem as a broadly protective immunogen.
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Hemagglutinin-stem nanoparticles generate heterosubtypic influenza protection.
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Vaccine-Induced Antibodies that Neutralize Group 1 and Group 2 Influenza A Viruses.
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A Site of Vulnerability on the Influenza Virus Hemagglutinin Head Domain Trimer Interface.
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Antibody recognition of the pandemic H1N1 Influenza virus hemagglutinin receptor binding site.
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Antibodies to a Conserved Influenza Head Interface Epitope Protect by an IgG Subtype-Dependent Mechanism.
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Memory B Cells that Cross-React with Group 1 and Group 2 Influenza A Viruses Are Abundant in Adult Human Repertoires.
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Preconfiguration of the antigen-binding site during affinity maturation of a broadly neutralizing influenza virus antibody.
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Heterosubtypic antibody recognition of the influenza virus hemagglutinin receptor binding site enhanced by avidity.
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Broadly cross-reactive antibodies dominate the human B cell response against 2009 pandemic H1N1 influenza virus infection.
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Rapid development of broadly influenza neutralizing antibodies through redundant mutations.
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Combinatorial antibody libraries from survivors of the Turkish H5N1 avian influenza outbreak reveal virus neutralization strategies.
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Preferential induction of cross-group influenza A hemagglutinin stem-specific memory B cells after H7N9 immunization in humans.
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Influenza Infection in Humans Induces Broadly Cross-Reactive and Protective Neuraminidase-Reactive Antibodies.
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Chimeric hemagglutinin influenza virus vaccine constructs elicit broadly protective stalk-specific antibodies.
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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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Naturally occurring antibodies in humans can neutralize a variety of influenza virus strains, including H3, H1, H2, and H5.
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An in vivo human-plasmablast enrichment technique allows rapid identification of therapeutic influenza A antibodies.
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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.