Antibody Recognition of the Pandemic H1N1 Influenza Virus Hemagglutinin Receptor Binding Site - Test2 - elhamkhani - TriplyDB

Antibody Recognition of the Pandemic H1N1 Influenza Virus Hemagglutinin Receptor Binding Site

Antibody Recognition of the Pandemic H1N1 Influenza Virus Hemagglutinin Receptor Binding Site

http://www.wikidata.org/entity/Q27679927

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Dynamic Viral Glycoprotein Machines: Approaches for Probing Transient States That Drive Membrane Fusion Structural characterization of viral epitopes recognized by broadly cross-reactive antibodies A common solution to group 2 influenza virus neutralization 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 Affinity maturation in an HIV broadly neutralizing B-cell lineage through reorientation of variable domains Purification and immunogenicity of hemagglutinin from highly pathogenic avian influenza virus H5N1 expressed in Nicotiana benthamiana.Influenza hemagglutinin stem-fragment immunogen elicits broadly neutralizing antibodies and confers heterologous protection 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 Analysis of B-Cell Epitopes of Influenza Virus Hemagglutinin.Influenza immunization elicits antibodies specific for an egg-adapted vaccine strain Combination of the immunization with the sequence close to the consensus sequence and two DNA prime plus one VLP boost generate H5 hemagglutinin specific broad neutralizing antibodies.Characterization of a broadly neutralizing monoclonal antibody that targets the fusion domain of group 2 influenza A virus hemagglutinin.Structure of the apo anti-influenza CH65 Fab.Structural basis for Marburg virus neutralization by a cross-reactive human antibody.OptMAVEn--a new framework for the de novo design of antibody variable region models targeting specific antigen epitopes.Design and Structure of an Engineered Disulfide-Stabilized Influenza Virus Hemagglutinin Trimer.Isolation and Characterization of Broad and Ultrapotent Human Monoclonal Antibodies with Therapeutic Activity against Chikungunya Virus.Vaccine-elicited antibody that neutralizes H5N1 influenza and variants binds the receptor site and polymorphic sites.Improving Loop Modeling of the Antibody Complementarity-Determining Region 3 Using Knowledge-Based Restraints Focused antibody response to influenza linked to antigenic drift Stabilizing the CH2 Domain of an Antibody by Engineering in an Enhanced Aromatic Sequon Use of computational and recombinant technologies for developing novel influenza vaccines.Heads, stalks and everything else: how can antibodies eradicate influenza as a human disease?A Perspective on the Structural and Functional Constraints for Immune Evasion: Insights from Influenza Virus.Comparison of the Protective Efficacy of Neutralizing Epitopes of 2009 Pandemic H1N1 Influenza Hemagglutinin.Principles of Broad and Potent Antiviral Human Antibodies: Insights for Vaccine Design.In vitro evolution of an influenza broadly neutralizing antibody is modulated by hemagglutinin receptor specificity.Viral receptor-binding site antibodies with diverse germline origins Diverse antigenic site targeting of influenza hemagglutinin in the murine antibody recall response to A(H1N1)pdm09 virus.Prospects of HA-based universal influenza vaccine.The bulky and the sweet: How neutralizing antibodies and glycan receptors compete for virus binding.Antibody 27F3 Broadly Targets Influenza A Group 1 and 2 Hemagglutinins through a Further Variation in VH1-69 Antibody Orientation on the HA Stem.Influenza A HA's conserved epitopes and broadly neutralizing antibodies: a prediction method.Structural insight into a human neutralizing antibody against influenza virus H7N9.Dissection of epitope-specific mechanisms of neutralization of influenza virus by intact IgG and Fab fragments.Structural insights into the design of novel anti-influenza therapies.An immuno-assay to quantify influenza virus hemagglutinin with correctly folded stalk domains in vaccine preparations.A small-molecule fragment that emulates binding of receptor and broadly neutralizing antibodies to influenza A hemagglutinin.

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P2860

Antibody Recognition of the Pandemic H1N1 Influenza Virus Hemagglutinin Receptor Binding Site

http://www.wikidata.org/entity/Q27679927

description

2013 nî lūn-bûn

@nan

2013 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2013 թվականի նոյեմբերին հրատարակված գիտական հոդված

@hy

2013年の論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

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2013年论文

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name

Antibody Recognition of the Pa ...... glutinin Receptor Binding Site

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Antibody Recognition of the Pa ...... glutinin Receptor Binding Site

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Antibody Recognition of the Pa ...... glutinin Receptor Binding Site

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type

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Antibody Recognition of the Pa ...... glutinin Receptor Binding Site

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Antibody Recognition of the Pa ...... glutinin Receptor Binding Site

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Antibody Recognition of the Pa ...... glutinin Receptor Binding Site

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Antibody Recognition of the Pa ...... glutinin Receptor Binding Site

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Antibody Recognition of the Pa ...... glutinin Receptor Binding Site

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Antibody Recognition of the Pa ...... glutinin Receptor Binding Site

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Journal of Virology

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Antibody Recognition of the Pa ...... glutinin Receptor Binding Site

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P2093

Andrew B Ward

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Jens C Krause

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Langzhou Song

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Lynda Tussey

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Minsun Hong

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Nick S Laursen

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Peter S Lee

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Ryan M B Hoffman

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Sung-Il Yoon

http://www.w3.org/2001/XMLSchema#string

Xueyong Zhu

http://www.w3.org/2001/XMLSchema#string

P2860

MUSCLE: multiple sequence alignment with high accuracy and high throughput

A highly conserved neutralizing epitope on group 2 influenza A viruses

MolProbity: all-atom structure validation for macromolecular crystallography

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

Structural Basis of Preexisting Immunity to the 2009 H1N1 Pandemic Influenza Virus

Structure and Receptor binding properties of a pandemic H1N1 virus hemagglutinin

The Receptor-Binding Domain of Influenza Virus Hemagglutinin Produced in Escherichia coli Folds into Its Native, Immunogenic Structure

Crystal structure of the swine-origin A (H1N1)-2009 influenza A virus hemagglutinin (HA) reveals similar antigenicity to that of the 1918 pandemic virus

Computational Design of Proteins Targeting the Conserved Stem Region of Influenza Hemagglutinin

Broadly neutralizing human antibody that recognizes the receptor-binding pocket of influenza virus hemagglutinin

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12471-80

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scholarly article

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1620393

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10.1128/JVI.01388-13

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22

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87

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James E. Crowe Jr.

Ian Andrew Wilson

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2013-11-01T00:00:00Z

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256502022

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24027321

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3807900

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