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Times Cited: 135
Times Cited: 135
Times Cited
Times Co-cited
Similarity
A highly conserved neutralizing epitope on group 2 influenza A viruses.
Damian C Ekiert, Robert H E Friesen, Gira Bhabha, Ted Kwaks, Mandy Jongeneelen, Wenli Yu, Carla Ophorst, Freek Cox, Hans J W M Korse, Boerries Brandenburg,[...]. Science 2011
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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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Highly conserved protective epitopes on influenza B viruses.
Cyrille Dreyfus, Nick S Laursen, Ted Kwaks, David Zuijdgeest, Reza Khayat, Damian C Ekiert, Jeong Hyun Lee, Zoltan Metlagel, Miriam V Bujny, Mandy Jongeneelen,[...]. Science 2012
Cyrille Dreyfus, Nick S Laursen, Ted Kwaks, David Zuijdgeest, Reza Khayat, Damian C Ekiert, Jeong Hyun Lee, Zoltan Metlagel, Miriam V Bujny, Mandy Jongeneelen,[...]. Science 2012
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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.
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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Heterosubtypic neutralizing monoclonal antibodies cross-protective against H5N1 and H1N1 recovered from human IgM+ memory B cells.
Mark Throsby, Edward van den Brink, Mandy Jongeneelen, Leo L M Poon, Philippe Alard, Lisette Cornelissen, Arjen Bakker, Freek Cox, Els van Deventer, Yi Guan,[...]. PLoS One 2008
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Structure and Function Analysis of an Antibody Recognizing All Influenza A Subtypes.
Nicole L Kallewaard, Davide Corti, Patrick J Collins, Ursula Neu, Josephine M McAuliffe, Ebony Benjamin, Leslie Wachter-Rosati, Frances J Palmer-Hill, Andy Q Yuan, Philip A Walker,[...]. Cell 2016
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Cross-neutralization of influenza A viruses mediated by a single antibody loop.
Damian C Ekiert, Arun K Kashyap, John Steel, Adam Rubrum, Gira Bhabha, Reza Khayat, Jeong Hyun Lee, Michael A Dillon, Ryann E O'Neil, Aleksandr M Faynboym,[...]. Nature 2012
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A stable trimeric influenza hemagglutinin stem as a broadly protective immunogen.
Antonietta Impagliazzo, Fin Milder, Harmjan Kuipers, Michelle V Wagner, Xueyong Zhu, Ryan M B Hoffman, Ruud van Meersbergen, Jeroen Huizingh, Patrick Wanningen, Johan Verspuij,[...]. Science 2015
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Broadly neutralizing hemagglutinin stalk-specific antibodies require FcγR interactions for protection against influenza virus in vivo.
David J DiLillo, Gene S Tan, Peter Palese, Jeffrey V Ravetch. Nat Med 2014
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Hemagglutinin-stem nanoparticles generate heterosubtypic influenza protection.
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A common neutralizing epitope conserved between the hemagglutinins of influenza A virus H1 and H2 strains.
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Preexisting human antibodies neutralize recently emerged H7N9 influenza strains.
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An in vivo human-plasmablast enrichment technique allows rapid identification of therapeutic influenza A antibodies.
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Chimeric hemagglutinin influenza virus vaccine constructs elicit broadly protective stalk-specific antibodies.
Florian Krammer, Natalie Pica, Rong Hai, Irina Margine, Peter Palese. J Virol 2013
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Vaccine-Induced Antibodies that Neutralize Group 1 and Group 2 Influenza A Viruses.
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Heterosubtypic antibody recognition of the influenza virus hemagglutinin receptor binding site enhanced by avidity.
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Broadly neutralizing human antibody that recognizes the receptor-binding pocket of influenza virus hemagglutinin.
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Broadly neutralizing anti-influenza antibodies require Fc receptor engagement for in vivo protection.
David J DiLillo, Peter Palese, Patrick C Wilson, Jeffrey V Ravetch. J Clin Invest 2016
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Characterization of a broadly neutralizing monoclonal antibody that targets the fusion domain of group 2 influenza A virus hemagglutinin.
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Structure of a classical broadly neutralizing stem antibody in complex with a pandemic H2 influenza virus hemagglutinin.
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Cyrille Dreyfus, Damian C Ekiert, Ian A Wilson. J Virol 2013
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Heterosubtypic neutralizing antibodies are produced by individuals immunized with a seasonal influenza vaccine.
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Influenza virus vaccine based on the conserved hemagglutinin stalk domain.
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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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A potent broad-spectrum protective human monoclonal antibody crosslinking two haemagglutinin monomers of influenza A virus.
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Advances in the development of influenza virus vaccines.
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Receptor mimicry by antibody F045-092 facilitates universal binding to the H3 subtype of influenza virus.
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Hemagglutinin stalk-based universal vaccine constructs protect against group 2 influenza A viruses.
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Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution.
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Combinatorial antibody libraries from survivors of the Turkish H5N1 avian influenza outbreak reveal virus neutralization strategies.
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Immune history profoundly affects broadly protective B cell responses to influenza.
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Influenza viruses expressing chimeric hemagglutinins: globular head and stalk domains derived from different subtypes.
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Pandemic H1N1 influenza vaccine induces a recall response in humans that favors broadly cross-reactive memory B cells.
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Influenza hemagglutinin stem-fragment immunogen elicits broadly neutralizing antibodies and confers heterologous protection.
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Mechanisms of hemagglutinin targeted influenza virus neutralization.
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Cross-protective potential of a novel monoclonal antibody directed against antigenic site B of the hemagglutinin of influenza A viruses.
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Influenza virus hemagglutinin stalk-based antibodies and vaccines.
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Assessment of influenza virus hemagglutinin stalk-based immunity in ferrets.
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A recurring motif for antibody recognition of the receptor-binding site of influenza hemagglutinin.
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The antigenic structure of the influenza virus A/PR/8/34 hemagglutinin (H1 subtype).
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Antibody recognition of the pandemic H1N1 Influenza virus hemagglutinin receptor binding site.
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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.