Toward a Hepatitis C Virus Vaccine: the Structural Basis of Hepatitis C Virus Neutralization by AP33, a Broadly Neutralizing Antibody - Wikidata - awgldk - TriplyDB

Toward a Hepatitis C Virus Vaccine: the Structural Basis of Hepatitis C Virus Neutralization by AP33, a Broadly Neutralizing Antibody

Toward a Hepatitis C Virus Vaccine: the Structural Basis of Hepatitis C Virus Neutralization by AP33, a Broadly Neutralizing Antibody

http://www.wikidata.org/entity/Q27673453

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Genetic Diversity Underlying the Envelope Glycoproteins of Hepatitis C Virus: Structural and Functional Consequences and the Implications for Vaccine Design Bivalent vaccine platform based on Japanese encephalitis virus (JEV) elicits neutralizing antibodies against JEV and hepatitis C virus Structural evidence for a bifurcated mode of action in the antibody-mediated neutralization of hepatitis C virus Structural Basis of HCV Neutralization by Human Monoclonal Antibodies Resistant to Viral Neutralization Escape Immunogenicity of Leishmania-derived hepatitis B small surface antigen particles exposing highly conserved E2 epitope of hepatitis C virus Max Bergmann lecture protein epitope mimetics in the age of structural vaccinology Capitalizing on knowledge of hepatitis C virus neutralizing epitopes for rational vaccine design Optimization of peptide arrays for studying antibodies to hepatitis C virus continuous epitopes.Conformational Flexibility in the Immunoglobulin-Like Domain of the Hepatitis C Virus Glycoprotein E2.Non-random escape pathways from a broadly neutralizing human monoclonal antibody map to a highly conserved region on the hepatitis C virus E2 glycoprotein encompassing amino acids 412-423 Anatomy of β-strands at protein-protein interfaces.Fine mapping of murine antibody responses to immunization with a novel soluble form of hepatitis C virus envelope glycoprotein complex.The Humoral Immune Response to HCV: Understanding is Key to Vaccine Development.Recombinant hepatitis C virus envelope glycoprotein vaccine elicits antibodies targeting multiple epitopes on the envelope glycoproteins associated with broad cross-neutralization.Structural basis for penetration of the glycan shield of hepatitis C virus E2 glycoprotein by a broadly neutralizing human antibody.Approaching rational epitope vaccine design for hepatitis C virus with meta-server and multivalent scaffolding Monoclonal Antibodies Directed toward the Hepatitis C Virus Glycoprotein E2 Detect Antigenic Differences Modulated by the N-Terminal Hypervariable Region 1 (HVR1), HVR2, and Intergenotypic Variable Region Structural flexibility at a major conserved antibody target on hepatitis C virus E2 antigen.Global mapping of antibody recognition of the hepatitis C virus E2 glycoprotein: Implications for vaccine design.HVR1-mediated antibody evasion of highly infectious in vivo adapted HCV in humanised mice.CD81 and hepatitis C virus (HCV) infection.Structural and antigenic definition of hepatitis C virus E2 glycoprotein epitopes targeted by monoclonal antibodies.The past, present and future of neutralizing antibodies for hepatitis C virus.HCV E2 core structures and mAbs: something is still missing.Hepatitis C virus vaccines in the era of new direct-acting antivirals.Unraveling hepatitis C virus structure.Role of Conserved E2 Residue W420 in Receptor Binding and Hepatitis C Virus Infection.How human IgGs against myelin basic protein (MBP) recognize oligopeptides and MBP.Viral evasion and challenges of hepatitis C virus vaccine development.Generation and Characterization of Monoclonal Antibodies against a Cyclic Variant of Hepatitis C Virus E2 Epitope 412-422.The dynamic properties of the Hepatitis C Virus E2 envelope protein unraveled by molecular dynamics.Monoclonal anti-envelope antibody AP33 protects humanized mice against a patient-derived hepatitis C virus challenge.A Biologically-validated HCV E1E2 Heterodimer Structural Model.Structural flexibility of a conserved antigenic region in hepatitis C virus glycoprotein E2 recognized by broadly neutralizing antibodies.Structural basis of respiratory syncytial virus subtype-dependent neutralization by an antibody targeting the fusion glycoprotein.Development and characterization of a human monoclonal antibody targeting the N-terminal region of hepatitis C virus envelope glycoprotein E1.Probing the antigenicity of hepatitis C virus envelope glycoprotein complex by high-throughput mutagenesis.Designing a B Cell-Based Vaccine against a Highly Variable Hepatitis C Virus.Escape of Hepatitis C Virus from Epitope I Neutralization Increases Sensitivity of Other Neutralization Epitopes.Glycan Shielding and Modulation of Hepatitis C Virus Neutralizing Antibodies.

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Toward a Hepatitis C Virus Vaccine: the Structural Basis of Hepatitis C Virus Neutralization by AP33, a Broadly Neutralizing Antibody

http://www.wikidata.org/entity/Q27673453

description

2012 nî lūn-bûn

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2012 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2012 թվականի դեկտեմբերին 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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Toward a Hepatitis C Virus Vac ...... Broadly Neutralizing Antibody

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Toward a Hepatitis C Virus Vac ...... Broadly Neutralizing Antibody

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Toward a Hepatitis C Virus Vac ...... Broadly Neutralizing Antibody

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Toward a Hepatitis C Virus Vac ...... Broadly Neutralizing Antibody

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Toward a Hepatitis C Virus Vac ...... Broadly Neutralizing Antibody

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Journal of Virology

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Toward a hepatitis C virus vac ...... broadly neutralizing antibody

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Ania M Owsianka

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Arvind H Patel

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David J Matthews

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Jane A Potter

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Nathan Jeffery

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Patrick Lau

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Steven K H Foung

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

Zhen-Yong Keck

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

P2860

Binding of hepatitis C virus to CD81

Characterization of hepatitis C virus E2 glycoprotein interaction with a putative cellular receptor, CD81.

Human monoclonal antibodies that inhibit binding of hepatitis C virus E2 protein to CD81 and recognize conserved conformational epitopes

Role of N-linked glycans in the functions of hepatitis C virus envelope glycoproteins.

Monoclonal Antibody AP33 Defines a Broadly Neutralizing Epitope on the Hepatitis C Virus E2 Envelope Glycoprotein

Analysis of antigenicity and topology of E2 glycoprotein present on recombinant hepatitis C virus-like particles.

Neutralizing antibodies against hepatitis C virus and the emergence of neutralization escape mutant viruses

Formation and intracellular localization of hepatitis C virus envelope glycoprotein complexes expressed by recombinant vaccinia and Sindbis viruses

Humoral immune response to hypervariable region 1 of the putative envelope glycoprotein (gp70) of hepatitis C virus

Definition of a Conserved Immunodominant Domain on Hepatitis C Virus E2 Glycoprotein by Neutralizing Human Monoclonal Antibodies

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12923-12932

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scholarly article

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1296241

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10.1128/JVI.02052-12

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23

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86

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2012-09-19T00:00:00Z

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230884948

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22993159

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Hepatitis C virus

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3497650

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