Cross-neutralization of influenza A viruses mediated by a single antibody loop - Test2 - elhamkhani - TriplyDB

Cross-neutralization of influenza A viruses mediated by a single antibody loop

Cross-neutralization of influenza A viruses mediated by a single antibody loop

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Dynamic Viral Glycoprotein Machines: Approaches for Probing Transient States That Drive Membrane Fusion Influenza Vaccination Strategies: Comparing Inactivated and Live Attenuated Influenza Vaccines Developing Universal Influenza Vaccines: Hitting the Nail, Not Just on the Head Structural characterization of viral epitopes recognized by broadly cross-reactive antibodies Universal immunity to influenza must outwit immune evasion Mechanisms of hemagglutinin targeted influenza virus neutralization Heterosubtypic antibody recognition of the influenza virus hemagglutinin receptor binding site enhanced by avidity Influenza Human Monoclonal Antibody 1F1 Interacts with Three Major Antigenic Sites and Residues Mediating Human Receptor Specificity in H1N1 Viruses A recurring motif for antibody recognition of the receptor-binding site of influenza hemagglutinin Structure of a Classical Broadly Neutralizing Stem Antibody in Complex with a Pandemic H2 Influenza Virus Hemagglutinin Structure of RSV Fusion Glycoprotein Trimer Bound to a Prefusion-Specific Neutralizing Antibody Broadly Neutralizing Antibody PGT121 Allosterically Modulates CD4 Binding via Recognition of the HIV-1 gp120 V3 Base and Multiple Surrounding Glycans Human antibodies that neutralize respiratory droplet transmissible H5N1 influenza viruses Antibody Recognition of the Pandemic H1N1 Influenza Virus Hemagglutinin Receptor Binding Site The Effects of Somatic Hypermutation on Neutralization and Binding in the PGT121 Family of Broadly Neutralizing HIV Antibodies A common solution to group 2 influenza virus neutralization Role of κ→λ light-chain constant-domain switch in the structure and functionality of A17 reactibody Receptor mimicry by antibody F045–092 facilitates universal binding to the H3 subtype of influenza virus Alternative Recognition of the Conserved Stem Epitope in Influenza A Virus Hemagglutinin by a VH3-30-Encoded Heterosubtypic Antibody Conserved Neutralizing Epitope at Globular Head of Hemagglutinin in H3N2 Influenza Viruses Two Escape Mechanisms of Influenza A Virus to a Broadly Neutralizing Stalk-Binding Antibody Anti-Hemagglutinin Antibody Derived Lead Peptides for Inhibitors of Influenza Virus Binding Modified vaccinia virus ankara (MVA) as production platform for vaccines against influenza and other viral respiratory diseases Influenza hemagglutinin stem-fragment immunogen elicits broadly neutralizing antibodies and confers heterologous protection Large-scale analysis of B-cell epitopes on influenza virus hemagglutinin - implications for cross-reactivity of neutralizing antibodies.The kinase mTOR modulates the antibody response to provide cross-protective immunity to lethal infection with influenza virus.Extreme evolutionary conservation of functionally important regions in H1N1 influenza proteome.Vaccination of monoglycosylated hemagglutinin induces cross-strain protection against influenza virus infections.Diversity of the murine antibody response targeting influenza A(H1N1pdm09) hemagglutinin In silico structural homology modelling and docking for assessment of pandemic potential of a novel H7N9 influenza virus and its ability to be neutralized by existing anti-hemagglutinin antibodies.The breadth of cross sub-type neutralisation activity of a single domain antibody to influenza hemagglutinin can be increased by antibody valency.Influenza vaccines: a moving interdisciplinary field.An anti-H5N1 influenza virus FcDART antibody is a highly efficacious therapeutic agent and prophylactic against H5N1 influenza virus infection Preexisting human antibodies neutralize recently emerged H7N9 influenza strains.Prospects for antibody-based universal influenza vaccines in the context of widespread pre-existing immunity.Serum Samples From Middle-aged Adults Vaccinated Annually with Seasonal Influenza Vaccines Cross-neutralize Some Potential Pandemic Influenza Viruses.The Analysis of B-Cell Epitopes of Influenza Virus Hemagglutinin.Glycosylation changes in the globular head of H3N2 influenza hemagglutinin modulate receptor binding without affecting virus virulence Influenza immunization elicits antibodies specific for an egg-adapted vaccine strain Structural basis of influenza virus fusion inhibition by the antiviral drug Arbidol.

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Cross-neutralization of influenza A viruses mediated by a single antibody loop

http://www.wikidata.org/entity/Q27673206

description

2012 nî lūn-bûn

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2012 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2012 թվականի սեպտեմբերին հրատարակված գիտական հոդված

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2012年の論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年论文

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name

Cross-neutralization of influenza A viruses mediated by a single antibody loop

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Cross-neutralization of influenza A viruses mediated by a single antibody loop

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Cross-neutralization of influenza A viruses mediated by a single antibody loop

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type

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Cross-neutralization of influenza A viruses mediated by a single antibody loop

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Cross-neutralization of influenza A viruses mediated by a single antibody loop

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Cross-neutralization of influenza A viruses mediated by a single antibody loop

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Cross-neutralization of influenza A viruses mediated by a single antibody loop

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Cross-neutralization of influenza A viruses mediated by a single antibody loop

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Cross-neutralization of influenza A viruses mediated by a single antibody loop

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Cross-neutralization of influenza A viruses mediated by a single antibody loop

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Adam Rubrum

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Aleksandr M Faynboym

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Andrew B Ward

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Arun K Kashyap

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John Steel

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Lawrence Horowitz

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Michael A Dillon

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Michael Horowitz

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Ramesh R Bhatt

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Reza Khayat

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P2860

Heterosubtypic neutralizing monoclonal antibodies cross-protective against H5N1 and H1N1 recovered from human IgM+ memory B cells

MUSCLE: multiple sequence alignment with high accuracy and high throughput

A highly conserved neutralizing epitope on group 2 influenza A viruses

Access of antibody molecules to the conserved coreceptor binding site on glycoprotein gp120 is sterically restricted on primary human immunodeficiency virus type 1

Hemagglutinin receptor binding avidity drives influenza A virus antigenic drift

MolProbity: all-atom structure validation for macromolecular crystallography

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

Somatic hypermutation introduces insertions and deletions into immunoglobulin V genes

PHENIX: a comprehensive Python-based system for macromolecular structure solution

Antibody recognition of a highly conserved influenza virus epitope

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526-32

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scholarly article

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454289

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10.1038/NATURE11414

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7417

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Damian C Ekiert

Ian Andrew Wilson

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2012-09-27T00:00:00Z

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1015902165

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22982990

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