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Human combinatorial libraries yield rare antibodies that broadly neutralize hepatitis C virus

Human combinatorial libraries yield rare antibodies that broadly neutralize hepatitis C virus

http://www.wikidata.org/entity/Q27481388

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Monoclonal antibodies: Principles and applications of immmunodiagnosis and immunotherapy for hepatitis C virus Genetic Diversity Underlying the Envelope Glycoproteins of Hepatitis C Virus: Structural and Functional Consequences and the Implications for Vaccine Design The hepatitis C virus glycan shield and evasion of the humoral immune response Neutralizing antibody response to hepatitis C virus A Point Mutation Leading to Hepatitis C Virus Escape from Neutralization by a Monoclonal Antibody to a Conserved Conformational Epitope Definition of a Conserved Immunodominant Domain on Hepatitis C Virus E2 Glycoprotein by Neutralizing Human Monoclonal Antibodies In vitro selection of a neutralization-resistant hepatitis C virus escape mutant Mutations in Hepatitis C Virus E2 Located outside the CD81 Binding Sites Lead to Escape from Broadly Neutralizing Antibodies but Compromise Virus Infectivity Hepatitis C Virus (HCV) Infection May Elicit Neutralizing Antibodies Targeting Epitopes Conserved in All Viral Genotypes Identification and Characterization of Broadly Neutralizing Human Monoclonal Antibodies Directed against the E2 Envelope Glycoprotein of Hepatitis C Virus High-level secretion of recombinant monomeric murine and human single-chain Fv antibodies from Drosophila S2 cells Structural basis of hepatitis C virus neutralization by broadly neutralizing antibody HCV1 An alpaca nanobody inhibits hepatitis C virus entry and cell-to-cell transmission Human monoclonal antibodies to a novel cluster of conformational epitopes on HCV E2 with resistance to neutralization escape in a genotype 2a isolate Hepatitis C virus Broadly Neutralizing Monoclonal Antibodies Isolated 25 Years after Spontaneous Clearance Immunogenicity of Leishmania-derived hepatitis B small surface antigen particles exposing highly conserved E2 epitope of hepatitis C virus Analysis of serine codon conservation reveals diverse phenotypic constraints on hepatitis C virus glycoprotein evolution Naturally occurring antibodies that recognize linear epitopes in the amino terminus of the hepatitis C virus E2 protein confer noninterfering, additive neutralization Capitalizing on knowledge of hepatitis C virus neutralizing epitopes for rational vaccine design A Hepatitis C Virus Envelope Polymorphism Confers Resistance to Neutralization by Polyclonal Sera and Broadly Neutralizing Monoclonal Antibodies Broadly neutralizing antibodies with few somatic mutations and hepatitis C virus clearance Conformational Flexibility in the Immunoglobulin-Like Domain of the Hepatitis C Virus Glycoprotein E2.Clearance of hepatitis C infection is associated with the early appearance of broad neutralizing antibody responses Mutations within a conserved region of the hepatitis C virus E2 glycoprotein that influence virus-receptor interactions and sensitivity to neutralizing antibodies.Broadly neutralizing human monoclonal antibodies to the hepatitis C virus E2 glycoprotein.Intracytoplasmic stable expression of IgG1 antibody targeting NS3 helicase inhibits replication of highly efficient hepatitis C Virus 2a clone.Affinity maturation to improve human monoclonal antibody neutralization potency and breadth against hepatitis C virus.Structural basis for broad neutralization of hepatitis C virus quasispecies.Human broadly neutralizing antibodies to the envelope glycoprotein complex of hepatitis C virus Fine mapping of murine antibody responses to immunization with a novel soluble form of hepatitis C virus envelope glycoprotein complex.Role of N-linked glycans in the functions of hepatitis C virus envelope proteins incorporated into infectious virions.Characterization of Anti-HCV Antibodies in IL-10-Treated Patients Phage display-based strategies for cloning and optimization of monoclonal antibodies directed against human pathogens Biochemical and morphological properties of hepatitis C virus particles and determination of their lipidome.Recombinant hepatitis C virus envelope glycoprotein vaccine elicits antibodies targeting multiple epitopes on the envelope glycoproteins associated with broad cross-neutralization.Development of Norwalk virus-specific monoclonal antibodies with therapeutic potential for the treatment of Norwalk virus gastroenteritis.Determination of the human antibody response to the neutralization epitopes encompassing amino acids 313-327 and 432-443 of hepatitis C virus E1E2 glycoproteins In vivo evaluation of the cross-genotype neutralizing activity of polyclonal antibodies against hepatitis C virus.Hepatitis C patient-derived glycoproteins exhibit marked differences in susceptibility to serum neutralizing antibodies: genetic subtype defines antigenic but not neutralization serotype.Naturally selected hepatitis C virus polymorphisms confer broad neutralizing antibody resistance.

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P2860

Human combinatorial libraries yield rare antibodies that broadly neutralize hepatitis C virus

http://www.wikidata.org/entity/Q27481388

description

2007 nî lūn-bûn

@nan

2007 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2007 թվականի հոտեմբերին հրատարակված գիտական հոդված

@hy

2007年の論文

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2007年論文

@yue

2007年論文

@zh-hant

2007年論文

@zh-hk

2007年論文

@zh-mo

2007年論文

@zh-tw

2007年论文

@wuu

name

Human combinatorial libraries ...... y neutralize hepatitis C virus

@ast

Human combinatorial libraries ...... y neutralize hepatitis C virus

@en

Human combinatorial libraries ...... y neutralize hepatitis C virus

@nl

type

label

Human combinatorial libraries ...... y neutralize hepatitis C virus

@ast

Human combinatorial libraries ...... y neutralize hepatitis C virus

@en

Human combinatorial libraries ...... y neutralize hepatitis C virus

@nl

prefLabel

Human combinatorial libraries ...... y neutralize hepatitis C virus

@ast

Human combinatorial libraries ...... y neutralize hepatitis C virus

@en

Human combinatorial libraries ...... y neutralize hepatitis C virus

@nl

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Human combinatorial libraries ...... y neutralize hepatitis C virus

@en

P2093

Cécile Voisset

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

Daniel X Johansson

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

Mie Aung

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.

Infectious hepatitis C virus pseudo-particles containing functional E1-E2 envelope protein complexes

Initiation of hepatitis C virus infection is dependent on cholesterol and cooperativity between CD81 and scavenger receptor B type I

An Interplay between Hypervariable Region 1 of the Hepatitis C Virus E2 Glycoprotein, the Scavenger Receptor BI, and High-Density Lipoprotein Promotes both Enhancement of Infection and Protection against Neutralizing Antibodies

Robust hepatitis C virus infection in vitro.

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

Analysis of a Highly Flexible Conformational Immunogenic Domain A in Hepatitis C Virus E2

Subcellular localization of hepatitis C virus structural proteins in a cell culture system that efficiently replicates the virus

Recognition of native hepatitis C virus E1E2 heterodimers by a human monoclonal antibody.

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scholarly article

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10.1073/PNAS.0705522104

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41

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104

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Alexander W. Tarr

Mats A A Persson

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2007-10-09T00:00:00Z

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5934328

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17911260

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2042196

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