Depletion of interfering antibodies in chronic hepatitis C patients and vaccinated chimpanzees reveals broad cross-genotype neutralizing activity. - Wikidata - wikimedia - TriplyDB

Depletion of interfering antibodies in chronic hepatitis C patients and vaccinated chimpanzees reveals broad cross-genotype neutralizing activity.

Depletion of interfering antibodies in chronic hepatitis C patients and vaccinated chimpanzees reveals broad cross-genotype neutralizing activity.

http://www.wikidata.org/entity/Q37163082

about

A new insight into hepatitis C vaccine development Vaccination for hepatitis C virus: closing in on an evasive target 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 Hepatitis C Virus (HCV) Infection May Elicit Neutralizing Antibodies Targeting Epitopes Conserved in All Viral Genotypes Rational HIV Immunogen Design to Target Specific Germline B Cell Receptors 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 Discrete conformations of epitope II on the hepatitis C virus E2 protein for antibody-mediated neutralization and nonneutralization Human monoclonal antibodies to a novel cluster of conformational epitopes on HCV E2 with resistance to neutralization escape in a genotype 2a isolate Human monoclonal antibody HCV1 effectively prevents and treats HCV infection in chimpanzees 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 Sequential bottlenecks drive viral evolution in early acute hepatitis C virus infection.Optimization of peptide arrays for studying antibodies to hepatitis C virus continuous epitopes.Non-apical membrane antigen 1 (AMA1) IgGs from Malian children interfere with functional activity of AMA1 IgGs as judged by growth inhibition assay.Hepatitis C virus in the new era: perspectives in epidemiology, prevention, diagnostics and predictors of response to therapy.Viral entry and escape from antibody-mediated neutralization influence hepatitis C virus reinfection in liver transplantation Characterization of antibodies induced by vaccination with hepatitis C virus envelope glycoproteins.Evaluation of cross-reactive antibody response to HVR1 in chronic hepatitis C.Immune control and failure in HCV infection--tipping the balance.Folding domains within the ricin toxin A subunit as targets of protective antibodies Human broadly neutralizing antibodies to the envelope glycoprotein complex of hepatitis C virus Role of N-linked glycans in the functions of hepatitis C virus envelope proteins incorporated into infectious virions.The Humoral Immune Response to HCV: Understanding is Key to Vaccine Development.Immunogenicity of Multi-Epitope DNA and Peptide Vaccine Candidates Based on Core, E2, NS3 and NS5B HCV Epitopes in BALB/c Mice.Neutralizing antibodies in patients with chronic hepatitis C, genotype 1, against a panel of genotype 1 culture viruses: lack of correlation to treatment outcome.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.Characterization of HCV genotype 5a envelope proteins: implications for vaccine development and therapeutic entry target.Adaptive immunity to hepatitis C virus.Neutralization resistance of hepatitis C virus can be overcome by recombinant human monoclonal antibodies Immunity to ricin: fundamental insights into toxin-antibody interactions.Antibodies to an interfering epitope in hepatitis C virus E2 can mask vaccine-induced neutralizing activity Neutralizing antibodies and pathogenesis of hepatitis C virus infection.Neutralization interfering antibodies: a "novel" example of humoral immune dysfunction facilitating viral escape?Cooperativity in virus neutralization by human monoclonal antibodies to two adjacent regions located at the amino terminus of hepatitis C virus E2 glycoprotein Prevention of hepatitis C virus infection using a broad cross-neutralizing monoclonal antibody (AR4A) and epigallocatechin gallate Metabolomic analysis of key regulatory metabolites in hepatitis C virus-infected tree shrews.

P2860

Q21296858-8457E861-524C-426E-87E9-E8EFE3E7F13E Q22305922-66EF3A2C-88AA-46D0-9E6B-2148591D4D13 Q26801759-9DD47406-C381-4FD0-B33F-806DF73F5270 Q27023390-3A8E9FAF-1CED-4597-A8EB-C6235B21B750 Q27027484-C53AB48F-E2E4-47AC-81E4-50654C1473E7 Q27490450-5EFF9B0C-C445-41F4-B167-A8B336F62C9C Q27677104-F2461FCB-B06A-4BAE-9A78-EA3778084A07 Q27677400-1AB5A710-938B-49FF-B739-A82781EDB5F7 Q27678252-AADF64AE-3F50-46EF-823B-E93C9E48260F Q27684579-8F86A1ED-9C8C-4A5D-B860-F5CC3F8DAD8B Q28482261-F7C25614-C3A5-4BF0-98AA-D0911066FCA0 Q28483065-EFEED755-BF64-40FD-8AD6-4A52A6D0058C Q28731355-5A92B88F-EC7E-4F1B-BAB0-8BD3D44E5D7D Q30374314-C94FEF9A-9815-4D18-B1C4-70543BEEA262 Q30407004-5B9BC82D-B518-485D-ABE3-C7ADCFFD65F0 Q33563569-57B267FD-68BE-4730-952E-3FBC79419A24 Q33939405-2ECD6544-B1A5-48CA-BFFE-02517E3C9ED9 Q34008754-C4934BAE-0B44-431D-94F0-1420C0A10E50 Q34096483-596CB976-47D7-499D-A78A-4D23AD221A97 Q34097560-2A281B08-48B7-4540-A8C2-F2E0838C9B0C Q34134998-2DB08ABD-C5E9-46C3-8A04-7F9DB209EF2A Q34178628-6D674094-F955-468E-993C-5ED9200A4C22 Q34196491-FE73940E-4494-4AB2-849F-E0BF7923A709 Q34228030-998DCA8F-953B-400F-B105-12CD3CB6D49C Q34295953-704DAF8D-A5E5-4F0D-9A03-AA0F44A7B210 Q34481429-84131BDB-C048-4389-8E65-93F7B7E96B93 Q34546149-75252505-721B-4A8C-9D63-E5C7C3BA25CA Q34717544-97640049-5ACB-483E-AFCF-1B5047AE2147 Q34796179-21917E95-81A8-492F-8076-2FAE7CA8BD6B Q34816677-C5DCEB36-6E8C-478F-AA41-E06AE26F2BD1 Q34864567-B99A5E8D-F957-4566-87B9-8EED6589019C Q35259748-A9BD562E-8A6A-407A-8488-3482077EC08C Q35557495-DBC86F8B-3B0A-4B21-9F07-41738E78D24B Q35612017-B74ED784-BD67-42AE-AA3F-D4111355C444 Q36378193-2B22C9EF-E82A-40F3-A165-9256D886A0AA Q36395837-27F2A93E-7B0D-4208-8D58-5ADEE8E6CD6C Q36404194-A90E2850-1DD3-479C-82B4-9C769D6E7ED4 Q36506935-BEBB6CD7-1E5E-4162-81AC-966306936427 Q36624431-2A81F5A9-7181-4C5C-BE7E-8CF1F1884D39 Q36666366-A316DCAC-2719-4F4C-9BF4-E9944606D10C

P2860

Depletion of interfering antibodies in chronic hepatitis C patients and vaccinated chimpanzees reveals broad cross-genotype neutralizing activity.

http://www.wikidata.org/entity/Q37163082

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on 20 April 2009

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Depletion of interfering antib ...... enotype neutralizing activity.

@en

Depletion of interfering antib ...... enotype neutralizing activity.

@nl

type

label

Depletion of interfering antib ...... enotype neutralizing activity.

@en

Depletion of interfering antib ...... enotype neutralizing activity.

@nl

prefLabel

Depletion of interfering antib ...... enotype neutralizing activity.

@en

Depletion of interfering antib ...... enotype neutralizing activity.

@nl

P1433

Q37163082-D54CB5C7-6B4A-4FE5-8C21-400AADFEA0F5

P1476

Q37163082-3CB423AC-649F-4D36-B03E-4AEEFF77A7C7

P2093

Q37163082-098315CD-60F0-400F-953A-49397ED15413

Q37163082-1D52EABD-62EF-4939-BA78-9881B5FDC326

Q37163082-22F10F6E-285A-4C98-9DE3-AD97B50F9277

Q37163082-2309374B-B838-4E17-90BD-41FDB06F1A4B

Q37163082-36B03249-AC97-4474-A1D3-120E7614AE61

Q37163082-4571280A-0776-4E4B-B8FA-69AB51621898

Q37163082-85508399-98FE-4F2F-8CB2-9117A42DE84E

Q37163082-8F2113F2-2392-4DB9-9DD3-F6067F9AAE86

Q37163082-9379CC83-A498-47E3-911F-ED73F4BEF111

Q37163082-F9C4B405-F015-42BE-A4ED-025F8532333E

P2860

Q37163082-09F41E31-2390-42FE-9A7A-1586588F2DDF

Q37163082-1922131B-216C-407A-80F2-888452F83CA5

Q37163082-34B3F5A7-71A8-4BFA-9606-0EA1EB8D4A22

Q37163082-34DE7E0A-F4CC-49D8-A789-66930BBC04A6

Q37163082-62A2A8C6-2310-4E04-BC03-88BE4C1C0DF3

Q37163082-69BF7489-7AC6-4A03-B6CD-5C00B8B94F19

Q37163082-6C0602B3-E37F-4C10-8812-4CC5FA21BCCA

Q37163082-6D14E416-C411-46BB-BF70-CD2FED25AAA9

Q37163082-6DE4220F-B2E5-4F16-9326-75B54F68A014

Q37163082-6DF469AC-7334-4406-A13E-147ADC69D905

P304

Q37163082-797FA75F-FA4E-4A4A-AE6D-EB6053AE000F

P31

Q37163082-97251152-309B-4AD6-BC16-6AF1F5218BC8

P356

Q37163082-F69C1BAE-8DA0-4195-AD67-379892A4AF97

P407

Q37163082-EF795258-4F12-4498-929C-CA2453F6B123

P433

Q37163082-FBCA7420-855A-45C0-9CD3-AA6593E89C70

P478

Q37163082-0E9B7661-F458-4226-8F93-3EDFFF4E4692

P577

Q37163082-52B08DB3-CAD1-4F9D-AFEF-9A8B18CFEABF

P5875

Q37163082-328DDF9B-5ED6-48EB-BBF7-988AA005195D

P698

Q37163082-421FB785-E8FF-4DE2-BFBC-F0C7CA42A077

P921

Q37163082-AE977B55-2025-4FF6-8D87-718EE4A4A8D4

Q37163082-E7F534B1-07FE-4C03-96B6-CE96FCA13FBC

P932

Q37163082-298007CE-EA0C-431A-861A-53C2747C52FE

P356

PNAS.0902749106

P1433

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

P1476

Depletion of interfering antib ...... enotype neutralizing activity.

@en

P2093

Alla Kachko

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

Evi Budo Struble

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

Harvey J Alter

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

Hisayoshi Watanabe

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

Kathleen Mihalik

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

Lilin Zhong

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

Maria Luisa Virata-Theimer

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

Marian Major

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

Pei Zhang

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

Stephen Feinstone

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

P2860

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

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

Identification of Conserved Residues in the E2 Envelope Glycoprotein of the Hepatitis C Virus That Are Critical for CD81 Binding

Hepatitis C virus glycoproteins mediate pH-dependent cell entry of pseudotyped retroviral particles

Hepatitis C virus epitope-specific neutralizing antibodies in Igs prepared from human plasma

Identification of a Broadly Cross-Reacting and Neutralizing Human Monoclonal Antibody Directed against the Hepatitis C Virus E2 Protein

Complete replication of hepatitis C virus in cell culture

Efficient replication of the genotype 2a hepatitis C virus subgenomic replicon

Recovery, persistence, and sequelae in hepatitis C virus infection: a perspective on long-term outcome

Characterization of the hepatitis C virus E2 epitope defined by the broadly neutralizing monoclonal antibody AP33.

P304

7537-7541

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

P31

scholarly article

P356

10.1073/PNAS.0902749106

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

P407

P433

18

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

P478

106

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

P577

2009-04-20T00:00:00Z

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

P5875

24311598

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

P698

19380744

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

P921

P932

2670884

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