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Structural characterization of viral epitopes recognized by broadly cross-reactive antibodies
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scholarly article
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PubMed
title
Structural characterization of viral epitopes recognized by broadly cross-reactive antibodies
(English)
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stated in
PubMed
main subject
antibody
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based on heuristic
inferred from title
author name string
Peter S. Lee
series ordinal
1
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Crossref
Ian A. Wilson
series ordinal
2
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stated in
Crossref
language of work or name
English
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stated in
PubMed
publication date
2015
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stated in
PubMed
published in
Current Topics in Microbiology and Immunology
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PubMed
volume
386
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stated in
PubMed
page(s)
323-41
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stated in
PubMed
cites work
New world bats harbor diverse influenza A viruses
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A highly conserved neutralizing epitope on group 2 influenza A viruses
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Vaccination with a synthetic peptide from the influenza virus hemagglutinin provides protection against distinct viral subtypes
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Antibody recognition of a highly conserved influenza virus epitope
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Structural and functional bases for broad-spectrum neutralization of avian and human influenza A viruses
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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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Insight into Highly Conserved H1 Subtype-Specific Epitopes in Influenza Virus Hemagglutinin
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A common solution to group 2 influenza virus neutralization
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A Unique and Conserved Neutralization Epitope in H5N1 Influenza Viruses Identified by an Antibody against the A/Goose/Guangdong/1/96 Hemagglutinin
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Antibody Recognition of the Pandemic H1N1 Influenza Virus Hemagglutinin Receptor Binding Site
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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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Rational HIV Immunogen Design to Target Specific Germline B Cell Receptors
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Bat-derived influenza hemagglutinin H17 does not bind canonical avian or human receptors and most likely uses a unique entry mechanism
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A recurring motif for antibody recognition of the receptor-binding site of influenza hemagglutinin
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Hemagglutinin homologue from H17N10 bat influenza virus exhibits divergent receptor-binding and pH-dependent fusion activities
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Influenza Human Monoclonal Antibody 1F1 Interacts with Three Major Antigenic Sites and Residues Mediating Human Receptor Specificity in H1N1 Viruses
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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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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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Optimization of affinity, specificity and function of designed influenza inhibitors using deep sequencing
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Broadly neutralizing human antibody that recognizes the receptor-binding pocket of influenza virus hemagglutinin
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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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Computational Design of Proteins Targeting the Conserved Stem Region of Influenza Hemagglutinin
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Structural Basis of Preexisting Immunity to the 2009 H1N1 Pandemic Influenza Virus
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Structure of the uncleaved human H1 hemagglutinin from the extinct 1918 influenza virus
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An antibody that prevents the hemagglutinin low pH fusogenic transition
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Structural evidence for recognition of a single epitope by two distinct antibodies
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A complex of influenza hemagglutinin with a neutralizing antibody that binds outside the virus receptor binding site
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Structure of the hemagglutinin precursor cleavage site, a determinant of influenza pathogenicity and the origin of the labile conformation
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Antigen distortion allows influenza virus to escape neutralization
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Identifiers
DOI
10.1007/82_2014_413
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
454282
OpenCitations bibliographic resource ID
454282
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
454282
PMC publication ID
4358778
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
454282
PubMed publication ID
25037260
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
454282
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