Structural evidence for a bifurcated mode of action in the antibody-mediated neutralization of hepatitis C virus
about
Genetic Diversity Underlying the Envelope Glycoproteins of Hepatitis C Virus: Structural and Functional Consequences and the Implications for Vaccine DesignHepatitis C Virus E2 Envelope Glycoprotein Core StructureStructure of the core ectodomain of the hepatitis C virus envelope glycoprotein 2Discrete conformations of epitope II on the hepatitis C virus E2 protein for antibody-mediated neutralization and nonneutralizationCapitalizing on knowledge of hepatitis C virus neutralizing epitopes for rational vaccine designThe Combining Sites of Anti-lipid A Antibodies Reveal a Widely Utilized Motif Specific for Negatively Charged GroupsOptimization 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.Antibodies to an interfering epitope in hepatitis C virus E2 can mask vaccine-induced neutralizing activityStructural flexibility at a major conserved antibody target on hepatitis C virus E2 antigen.HVR1-mediated antibody evasion of highly infectious in vivo adapted HCV in humanised mice.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.A view of the E2-CD81 interface at the binding site of a neutralizing antibody against hepatitis C virus.HCV glycoprotein structures: what to expect from the unexpected.Viral evasion and challenges of hepatitis C virus vaccine development.Antibody-Mediated Catalysis in Infection and Immunity.The dynamic properties of the Hepatitis C Virus E2 envelope protein unraveled by molecular dynamics.Polyspecificity of Anti-lipid A Antibodies and Its Relevance to the Development of Autoimmunity.Structure-Based Design of Hepatitis C Virus Vaccines that Elicit Neutralizing Antibody Responses to a Conserved Epitope.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.The unexpected structures of hepatitis C virus envelope proteinsComputational Modeling of Hepatitis C Virus Envelope Glycoprotein Structure and Recognition.The Neutralizing Face of Hepatitis C Virus E2 Envelope Glycoprotein.Conformational Flexibility in the CD81-Binding Site of the Hepatitis C Virus Glycoprotein E2.HCV envelope glycoproteins in evirion assembly and entryHepatitis C Virus Envelope Glycoproteins: A Balancing Act of Order and Disorder
P2860
Q26801759-CA73CADD-1303-4241-ADB9-2D3DA7FC433DQ27680704-FEA7615B-C5F4-4BA2-803D-FCA67EA18B28Q27681839-AF20D3A8-4743-46B4-834C-A65A3A6C01E2Q27684579-052699E5-6761-4651-87E8-017C55F03A52Q30374314-72E88CDB-777C-4489-8E33-9013FC0BDBD7Q30385146-F3230EB5-29CC-4FD6-B6F5-3B2F1DCDAC95Q33563569-94E93588-924D-4A34-A858-2ABFBBE257A8Q33691856-69AA7374-00B7-4E98-A861-B3EFE28EF85CQ36378193-10C7E8DD-0483-4A9F-89C9-61F974B46F09Q37417839-D0122EAD-F92C-4DDE-A603-45A6A7F4F0F5Q37471718-EC84BB35-E0EC-4240-AB51-34977DF83B49Q38128299-07ADFA80-05B9-4C67-BDBB-37280AF4737CQ38192357-52D24619-564F-4F9B-B34A-0F8DF58C1D1DQ38244787-CDD71B99-2683-496C-9DCE-142CD5FD985DQ38262106-34FC91C6-E654-42F4-A0AB-812F405C1526Q38384140-8E151AB3-4C26-4059-B42E-12A5BF988B93Q38961608-4E3F3DED-56B6-4878-A125-E82725BC191FQ39412526-693B0ABD-AF15-4D1A-9ADD-611D9A8D0E2AQ39923648-B907727A-7549-479D-98EB-2C04697D18AFQ40059466-0566308C-9C58-407D-9D8A-EEA3F17C3065Q40088796-8A94B7F9-DC2A-4A05-BDD4-C061F7672F64Q40288437-D798772C-CAF1-466F-9B0E-C0C26C50D804Q41619358-F0EDC415-374C-4100-BB21-11CCFC1BFA83Q41672624-2C3FBCE4-6F7E-4211-B489-711C8F03E5B0Q55003572-4B802270-E2A1-4A40-88E4-F8F2FB8BCBD9Q55299977-5779637F-B0A3-4459-B147-F737757899FCQ55383950-06ADE082-1C6E-4CC0-81D8-846FC7FDD755Q56910948-E494DA75-09C8-4A3F-94C9-9FA2D95A71BDQ57265415-EFDEEBC3-2A91-4200-9108-2FAC7703D7F6
P2860
Structural evidence for a bifurcated mode of action in the antibody-mediated neutralization of hepatitis C virus
description
2013 nî lūn-bûn
@nan
2013 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
name
Structural evidence for a bifu ...... alization of hepatitis C virus
@ast
Structural evidence for a bifu ...... alization of hepatitis C virus
@en
Structural evidence for a bifu ...... alization of hepatitis C virus
@nl
type
label
Structural evidence for a bifu ...... alization of hepatitis C virus
@ast
Structural evidence for a bifu ...... alization of hepatitis C virus
@en
Structural evidence for a bifu ...... alization of hepatitis C virus
@nl
prefLabel
Structural evidence for a bifu ...... alization of hepatitis C virus
@ast
Structural evidence for a bifu ...... alization of hepatitis C virus
@en
Structural evidence for a bifu ...... alization of hepatitis C virus
@nl
P2093
P2860
P356
P1476
Structural evidence for a bifu ...... alization of hepatitis C virus
@en
P2093
Christine Harman
Evi Struble
Hailing Yan
Harvey Alter
Hongying Duan
Lilin Zhong
Maria Luisa Virata-Theimer
P2860
P304
P356
10.1073/PNAS.1305306110
P407
P577
2013-04-30T00:00:00Z