Influenza A virus hemagglutinin trimerization completes monomer folding and antigenicity. - Wikidata - awgldk - TriplyDB

Influenza A virus hemagglutinin trimerization completes monomer folding and antigenicity.

Influenza A virus hemagglutinin trimerization completes monomer folding and antigenicity.

http://www.wikidata.org/entity/Q37123562

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The Encapsulation of Hemagglutinin in Protein Bodies Achieves a Stronger Immune Response in Mice than the Soluble Antigen Biogenesis of influenza a virus hemagglutinin cross-protective stem epitopes Radioactive Pulse-Chase Analysis and Immunoprecipitation.Novel Nonreplicating Vaccinia Virus Vector Enhances Expression of Heterologous Genes and Suppresses Synthesis of Endogenous Viral Proteins Characterization of a Prefusion-Specific Antibody That Recognizes a Quaternary, Cleavage-Dependent Epitope on the RSV Fusion Glycoprotein A Simple Flow-Cytometric Method Measuring B Cell Surface Immunoglobulin Avidity Enables Characterization of Affinity Maturation to Influenza A Virus.Broadly-Reactive Neutralizing and Non-neutralizing Antibodies Directed against the H7 Influenza Virus Hemagglutinin Reveal Divergent Mechanisms of Protection Lamprey VLRB response to influenza virus supports universal rules of immunogenicity and antigenicity Complete mapping of viral escape from neutralizing antibodies Age Dependence and Isotype Specificity of Influenza Virus Hemagglutinin Stalk-Reactive Antibodies in Humans.Zonal Sedimentation Analysis on Sucrose Gradients.IFITM3 requires an amphipathic helix for antiviral activity.Evaluation of Epic® label-free technology to quantify functional recombinant hemagglutinin Conformational modulation of influenza virus hemagglutinin: characterization and in vivo efficacy of monomeric form.Flow-Cytometric Method Measuring B Cell Surface Immunoglobulin Avidity.Influenza A virus hemagglutinin specific antibodies interfere with virion neuraminidase activity via two distinct mechanisms.Infection of Ferrets with Influenza Virus Elicits a Light Chain-Biased Antibody Response against Hemagglutinin.Eliciting unnatural immune responses by activating cryptic epitopes in viral antigens.Oligomerization of bacterially expressed H1N1 recombinant hemagglutinin contributes to protection against viral challenge

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Influenza A virus hemagglutinin trimerization completes monomer folding and antigenicity.

http://www.wikidata.org/entity/Q37123562

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on 03 July 2013

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Influenza A virus hemagglutinin trimerization completes monomer folding and antigenicity.

@en

Influenza A virus hemagglutinin trimerization completes monomer folding and antigenicity.

@nl

type

label

Influenza A virus hemagglutinin trimerization completes monomer folding and antigenicity.

@en

Influenza A virus hemagglutinin trimerization completes monomer folding and antigenicity.

@nl

prefLabel

Influenza A virus hemagglutinin trimerization completes monomer folding and antigenicity.

@en

Influenza A virus hemagglutinin trimerization completes monomer folding and antigenicity.

@nl

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Journal of Virology

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Influenza A virus hemagglutinin trimerization completes monomer folding and antigenicity.

@en

P2093

Gregory M Frank

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Hana Golding

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Jack R Bennink

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James Stevens

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Javier G Magadán

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Surender Khurana

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9742-9753

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scholarly article

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10.1128/JVI.00471-13

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17

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87

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Suman Ranjan Das

Jonathan W Yewdell

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2013-07-03T00:00:00Z

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23824811

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3754138

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